TIM beta/alpha-barrel [51350] (33)
contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites
Metallo-dependent hydrolases [51556] (18) the beta-sheet barrel is similarly distorted and capped by a C-terminal helix has transition metal ions bound inside the barrel uperfamily
Aldolase [51569] (8) Common fold covers whole protein structure uperfamily
Enolase C-terminal domain-like [51604] (2) binds metal ion (magnesium or manganese) in conserved site inside barrel N-terminal alpha+beta domain is common to this superfamily uperfamily
FAD-linked oxidoreductase [51730] (2) distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation uperfamily
EAL domain-like [141868] (1) variant of the beta/alpha-barrel fold with strand 1 being antiparallel to the rest uperfamily
NAD(P)-binding Rossmann-fold domains [51734] (1)
core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456 The nucleotide-binding modes of this and the next two folds/superfamilies are similar
FAD/NAD(P)-binding domain [51904] (1)
core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
Nucleotide-binding domain [51970] (1)
3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like
Nucleotide-binding domain [51971] (3) this superfamily shares the common nucleotide-binding site with and provides a link between the Rossmann-fold NAD(P)-binding and FAD/NAD(P)-binding domains uperfamily
MurCD N-terminal domain [51983] (1)
3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; incomplete Rossmann-like fold; binds UDP group
7-stranded beta/alpha barrel [51988] (3)
variant of beta/alpha barrel; parallel beta-sheet barrel, closed, n=7, S=8; strand order 1234567; some members may have fewer strands
The "swivelling" beta/beta/alpha domain [52008] (10)
3 layers: b/b/a; the central sheet is parallel, and the other one is antiparallel; there are some variations in topology this domain is thought to be mobile in most multi-domain proteins known to contain it
MurF and HprK N-domain-like [63417] (2)
core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1234; structural similarity of the MurF and HprK extends beyond the core.
N-(deoxy)ribosyltransferase-like [52309] (3) there are similar active site architectures as well as the catalytic mechanisms of functionally characterised members uperfamily
Class I glutamine amidotransferase-like [52317] (9) conserved positions of the oxyanion hole and catalytic nucleophile; different constituent families contain different additional structures uperfamily
Adenine nucleotide alpha hydrolases-like [52402] (6) share similar mode of ligand (Adenosine group) binding can be subdivided into two group with closer relationships within each group than between the groups; the first three families form one group whereas the last two families form the other group uperfamily
Ribose/Galactose isomerase RpiB/AlsB [89622] (1)
3 layers: a/b/a, core: parallel beta-sheet of 5 strands, order 21354; topological similarity to a part of the arginase/deacetylase fold
EreA/ChaN-like [159501] (3) there are four conserved residues in the putative active site: two His and two Glu
alpha/beta knot [75216] (1)
core: 3 layers: a/b/a, parallel beta-sheet of 5 strands, order 21435; contains a deep trefoil knot
alpha/beta knot [75217] (8) known or predicted SAM-dependent methytransferases including the SPOUT 'sequence' superfamily all known members have dimeric structures uperfamily
PreATP-grasp domain [52439] (1)
3 layers: a/b/a; parallel or mixed beta-sheet of 4 to 6 strands possible rudiment form of Rossmann-fold domain
PreATP-grasp domain [52440] (8) precedes the ATP-grasp domain common to all superfamily members, can contain a substrate-binding function uperfamily
Dipeptide transport protein [63991] (1)
3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; also contains a C-terminal alpha+beta subdomain
Thiamin diphosphate-binding fold (THDP-binding) [52518] (8) there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules uperfamily
CoA-dependent acyltransferases [52776] (1)
core: 2 layers, a/b; mixed beta-sheet of 6 strands, order 324561; strands 3 & 6 are antiparallel to the rest
Rhodanese/Cell cycle control phosphatase [52821] (4) Pfam 00581 the active site structure is similar to those of the families I and II protein phosphatases; the topology can be related by a different circular permutation to the family I topology uperfamily
Thioredoxin fold [52832] (2)
core: 3 layers, a/b/a; mixed beta-sheet of 4 strands, order 4312; strand 3 is antiparallel to the rest
XCC0632-like [159594] (2) short crossover loop between strands 2 and 3; the antiparallel part of the beta-sheet (strands 3, 4 and 5) and the C-terminal helix are quite long
MTH938-like [64075] (1)
core: 3 layers, b+a/b/a ; the central mixed sheet of 5 strands: order 21534; strand 2 is antiparallel to the rest
Restriction endonuclease-like [52979] (4)
core: 3 layers, a/b/a; mixed beta-sheet of 5 strands, order 12345; strands 2 &, in some families, 5 are antiparallel to the rest
Phosphorylase/hydrolase-like [53162] (8)
core: 3 layers, a/b/a ; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops
HybD-like [53163] (2) the HybD fold coincides with the consensus core structure uperfamily
Purine and uridine phosphorylases [53167] (1) complex architecture; contains mixed beta-sheet of 8 strands, order 23415867, strands 3, 6 & 7 are antiparallel to the rest; and barrel, closed; n=5, S=8 uperfamily
Molybdenum cofactor biosynthesis proteins [53217] (1)
3 layers: a/b/a; mixed beta-sheet of 5 strands; order: 21354, strand 5 is antiparallel to the rest; permutation of the Phosphorylase/hydrolase-like fold
CobE/GbiG C-terminal domain-like [159663] (1)
3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32154; strand 5 is antiparallel to the rest
CobE/GbiG C-terminal domain-like [159664] (1) probably involved in deacylation steps in both anaerobic and aerobic pathways of cobalamin biosynthesis
CbiG N-terminal domain-like [159671] (1)
3 layers: a/b/a; mixed beta-sheet of 6 strands, order 213456, strand 5 is antiparallel to the rest
CbiG N-terminal domain-like [159672] (1) probable biological unit is a homodimer; putative active site is formed by residues from both subunits
Bacterial fluorinating enzyme, N-terminal domain [102521] (1)
3 layers: a/b/a; mixed beta-sheet of 6 strands; order: 213546, strand 5 is antiparallel to the rest; topological similarity to the MogA-like family fold
L-sulfolactate dehydrogenase-like [89732] (1)
core: 3 layers, a/b/a; mixed sheet of 7 strands, order 1237456; strands 1, 6 and 7 are antiparallel to the rest
LmbE-like [102587] (1)
3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest; topological similarity to SAM-dependent methyltransferases
PLP-dependent transferase-like [53382] (3)
main domain: 3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest
RibA-like [142694] (1)
3 layers: a/b/a; mixed beta-sheet of 7 strands, order 1235467, strands 1 and 3 are antiparallel to the rest; partial topological similarity to some alpha/beta hydrolases (scop_cf 53473)
Activating enzymes of the ubiquitin-like proteins [69572] (2) transfer adenylyl group to the C-terminal carboxyl group of the ubiquitin and MoaD/ThiS-related proteins the ATP nucleotide-binding site is similar to that of the NAD-binding Rossmann-folds uperfamily
alpha/beta-Hydrolases [53473] (1)
core: 3 layers, a/b/a; mixed beta-sheet of 8 strands, order 12435678, strand 2 is antiparallel to the rest
alpha/beta-Hydrolases [53474] (41) many members have left-handed crossover connection between strand 8 and additional strand 9 uperfamily
Nucleoside hydrolase [53589] (1)
core: 3 layers, a/b/a ; mixed beta-sheet of 8 strands, order 32145687; strand 7 is antiparallel to the rest
Ribokinase-like [53612] (3)
core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest potential superfamily: members of this fold have similar functions but different ATP-binding sites
CoaB-like [102645] (1) combination of the Rossmann-like and Ribokinase-like topologies; mixed beta-sheet of 8 strands, order 32145678, strand 7 is antiparallel to the rest uperfamily
YjeF N-terminal domain-like [64152] (1)
3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 32145678; strand 8 is antiparallel to the rest
Carbamate kinase-like [53632] (1)
3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 34215786; strand 8 is antiparallel to the rest
Carbamate kinase-like [53633] (3) the sheet topology is similar to those of undecaprenyl diphosphate synthase and the N-terminal domain of phosphoglycerate kinase uperfamily
Glycerol-3-phosphate (1)-acyltransferase [69592] (1)
3 layers: a/b/a; mixed beta-sheet of 9 strands, order 918736452; strands 1, 2 and 8 are antiparallel to the rest
SurE-like [64166] (1)
3 layers: a/b/a; mixed beta-sheet of 9 strands, order 342156798; strands 3, 8 and 9 are antiparallel to the rest; left-handed crossover connection between strands 6 and 7
SurE-like [64167] (1) some topological similarity to the N-terminal domain of Glutaminase/Asparaginase family uperfamily
YerB-like [159773] (1)
3 layers: b/b/a; central mixed beta-sheet of 9 strands, order 541329678; strands 3 and 7 are antiparallel to the rest; an unusual "over the other end" connection between strands 3 and 4
Isocitrate/Isopropylmalate dehydrogenase-like [53658] (1)
consists of two intertwined (sub)domains related by pseudo dyad; duplication 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213A945867 (A=10); strands from 5 to 9 are antiparallel to the rest
Amidase signature (AS) enzymes [75303] (1)
possible duplication: the topologies of N- and C-terminal halves are similar; 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213549A867 (A=10); strands from 5 to 9 are antiparallel to the rest
ATC-like [53670] (2)
consists of two similar domains related by pseudo dyad; duplication core: 3 layers, a/b/a, parallel beta-sheet of 4 strands, order 2134
Formate dehydrogenase/DMSO reductase, domains 1-3 [53705] (1)
contains of two similar intertwined domains related by pseudo dyad; duplication core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
ALDH-like [53719] (1)
consists of two similar domains with 3 layers (a/b/a) each; duplication core: parallel beta-sheet of 5 strands, order 32145
ALDH-like [53720] (2) binds NAD differently from other NAD(P)-dependent oxidoreductases uperfamily
NadA-like [142753] (1)
duplication; consists of three similar domains related by pseudo threefold symmetry; 3 layers, a/b/a; parallel beta sheet, order: 2134
Aconitase iron-sulfur domain [53731] (1)
consists of three similar domains with 3 layers (a/b/a) each; duplication core: parallel beta-sheet of 5 strands, order 32145
Phosphoglucomutase, first 3 domains [53737] (1)
consists of three similar domains with 3 layers (a/b/a) each; duplication core: mixed beta-sheet of 4 strands, order 2134, strand 4 is antiparallel to the rest
FucI/AraA N-terminal and middle domains [53742] (1)
consists of two domains of similar topology, 3 layers (a/b/a) each Domain 1 (1-173) has parallel beta-sheet of 5 strands, order 21345 Domain 2 (174-355) has parallel beta-sheet of 4 strands, order 2134
YgbK-like [142763] (1)
consists of two domains with partial topological similarity to the P-loop kinases but without the P-loop motif; the domain association results in the formation of a single mixed beta-sheet of 15 strands
Phosphoglycerate kinase [53747] (1)
consists of two non-similar domains, 3 layers (a/b/a) each Domain 1 has parallel beta-sheet of 6 strands, order 342156 Domain 2 has parallel beta-sheet of 6 strands, order 321456
UDP-Glycosyltransferase/glycogen phosphorylase [53755] (1)
consists of two non-similar domains with 3 layers (a/b/a) each domain 1: parallel beta-sheet of 7 strands, order 3214567 domain 2: parallel beta-sheet of 6 strands, order 321456
Glutaminase/Asparaginase [53773] (1)
consists of two non-similar alpha/beta domains, 3 layers (a/b/a) each Domain 1 has mixed beta-sheet of 6 strands, order 213456, strand 6 is antiparallel to the rest; left-handed crossover connection between strands 4 and 5 Domain 2 has parallel beta-sheet of 4 strands, order 1234
Phosphofructokinase [53783] (1)
consists of two non-similar domains, 3 layers (a/b/a) each Domain 1 has mixed sheet of 7 strands, order 3214567; strands 3 & 7 are antiparallel to the rest Domain 2 has parallel sheet of 4 strands, order 2314
Tetrapyrrole methylase [53789] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 5 strands, order 32415 Domain 2 has mixed sheet of 5 strands, order 12534; strands 4 & 5 are antiparallel to the rest
GckA/TtuD-like [82543] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 6 strands, order 321456, Rossmann-like topology Domain 2 has mixed sheet of 6 strands, order 126345; strands 5 and 6 are antiparallel to the rest; some similarity to CbiF Domain 2
DAK1/DegV-like [82548] (1)
2 different domains; d1: [core: 3 layers, a/b/a; parallel sheet of 5 strands, order: 2134]; D2: [2 layers, a/b; mixed sheet of 6 strands, order 321645; strands 2 and 6 are antiparallel to the rest]
DAK1/DegV-like [82549] (2) domain folds and architecture show some similarity to the tubulin-like GTPases; the nucleotide-binding sites of the Dihydroxyacetone kinase and tubulin families are different uperfamily
DHH phosphoesterases [64181] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 6 strands, order 321456 Domain 2 has mixed sheet of 5 strands, order 12345; strands 1 & 4 are antiparallel to the rest
DHH phosphoesterases [64182] (2) constituent families have similar domain organization with variable interdomain linker and spatial arrangement of the domains uperfamily
Glycerate kinase I [110737] (1)
consists of two different alpha/beta domains; (1) of the Flavodoxin-like fold (scop_cf 52171); (2) similar to the Restriction endonuclease-like fold (scop_cf 52979), inserted into domain 1
PEP carboxykinase-like [53794] (1)
contains a P-loop NTP-binding motif; mixed beta-sheet folds into a barrel-like structure with helices packed on one side
CAC2185-like [142794] (1)
consists of two non-similar domains, 3 layers (a/b/a) each; d1 has parallel sheet of 4 strands, order 2134; d2 has parallel sheet of 5 strands, order 21345, and antiparallel meander sheet of 3 strands
Periplasmic binding protein-like I [53821] (1)
consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication parallel beta-sheet of 6 strands, order 213456
Periplasmic binding protein-like II [53849] (1)
consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest
Thiolase-like [53900] (1)
consists of two similar domains related by pseudo dyad; duplication 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32451; strand 5 is antiparallel to the rest
NIF3 (NGG1p interacting factor 3)-like [102704] (1)
consist of two intertwined domains; duplication: contains two structural repeats of alpha-beta-(beta-alpha)3 motif with mixed beta-sheet, order: 1432, strand 1 is antiparallel to the rest
ComB-like [142822] (1)
contains of two similar intertwined domains related by pseudo dyad; duplication; core: 3 layers: a/b/a; parallel beta-sheet of 4 strands, order 1423
CoA-transferase family III (CaiB/BaiF) [89795] (1)
consist of two different alpha/beta domains; N-terminal domain has a SurE-like topology with a left-handed beta-alpha-beta unit
Cytidine deaminase-like [53926] (2)
core: alpha-beta(2)-(alpha-beta)2; 3 layers (a/b/a); mixed beta-sheet of 4 strands, order 2134; strand 1 is antiparallel to the rest