Comparing 3609500 FitnessBrowser__Dino:3609500 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AFG6 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; EC 2.3.1.61 from Escherichia coli (strain K12) (see 3 papers)
52% identity, 79% coverage: 103:496/496 of query aligns to 3:405/405 of P0AFG6
Sites not aligning to the query:
P11179 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; EC 2.3.1.61 from Bos taurus (Bovine) (see paper)
54% identity, 51% coverage: 242:496/496 of query aligns to 198:455/455 of P11179
Sites not aligning to the query:
Q9N0F1 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; E2o; PE2o; EC 2.3.1.61 from Sus scrofa (Pig) (see paper)
54% identity, 52% coverage: 241:496/496 of query aligns to 196:455/455 of Q9N0F1
P36957 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; EC 2.3.1.61 from Homo sapiens (Human) (see 5 papers)
54% identity, 50% coverage: 247:496/496 of query aligns to 200:453/453 of P36957
Sites not aligning to the query:
P11961 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; EC 2.3.1.12 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 2 papers)
36% identity, 79% coverage: 103:495/496 of query aligns to 2:427/428 of P11961
Sites not aligning to the query:
P21883 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; S complex, 48 kDa subunit; EC 2.3.1.12 from Bacillus subtilis (strain 168) (see paper)
34% identity, 78% coverage: 108:495/496 of query aligns to 7:441/442 of P21883
P06959 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; EC 2.3.1.12 from Escherichia coli (strain K12) (see 6 papers)
32% identity, 99% coverage: 4:494/496 of query aligns to 107:630/630 of P06959
Sites not aligning to the query:
P10515 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial; 70 kDa mitochondrial autoantigen of primary biliary cirrhosis; PBC; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; M2 antigen complex 70 kDa subunit; Pyruvate dehydrogenase complex component E2; PDC-E2; PDCE2; EC 2.3.1.12 from Homo sapiens (Human) (see 4 papers)
29% identity, 99% coverage: 4:494/496 of query aligns to 93:647/647 of P10515
Sites not aligning to the query:
Q8NNJ2 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2; PDH component E2; EC 2.3.1.12 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
41% identity, 57% coverage: 207:487/496 of query aligns to 375:665/675 of Q8NNJ2
Sites not aligning to the query:
6zzkB Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
43% identity, 44% coverage: 271:487/496 of query aligns to 9:231/241 of 6zzkB
6zzkA Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
43% identity, 44% coverage: 271:487/496 of query aligns to 8:230/240 of 6zzkA
6zzjA Crystal structure of the catalytic domain of corynebacterium glutamicum acetyltransferase acef (e2p) in complex with oxidized coa. (see paper)
43% identity, 44% coverage: 271:487/496 of query aligns to 8:230/240 of 6zzjA
6zzmB Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (e2p). (see paper)
41% identity, 44% coverage: 271:487/496 of query aligns to 6:228/238 of 6zzmB
P11181 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 from Bos taurus (Bovine) (see 2 papers)
30% identity, 80% coverage: 101:496/496 of query aligns to 62:481/482 of P11181
P11182 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; 52 kDa mitochondrial autoantigen of primary biliary cirrhosis; Branched chain 2-oxo-acid dehydrogenase complex component E2; BCOADC-E2; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; BCKDH-E2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 from Homo sapiens (Human) (see 3 papers)
28% identity, 80% coverage: 101:496/496 of query aligns to 62:481/482 of P11182
P11180 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2; PDC-E2; PDCE2; EC 2.3.1.12 from Bos taurus (Bovine) (see paper)
34% identity, 58% coverage: 206:494/496 of query aligns to 358:647/647 of P11180
Sites not aligning to the query:
O00330 Pyruvate dehydrogenase protein X component, mitochondrial; Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex; E3-binding protein; E3BP; Lipoyl-containing pyruvate dehydrogenase complex component X; proX from Homo sapiens (Human) (see 5 papers)
26% identity, 79% coverage: 101:492/496 of query aligns to 54:500/501 of O00330
Sites not aligning to the query:
A0A0D2Y5A7 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial; FoDLAT; DLAT; EC 2.3.1.12 from Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato) (see paper)
27% identity, 78% coverage: 106:494/496 of query aligns to 39:457/457 of A0A0D2Y5A7
1eafA Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex (see paper)
38% identity, 48% coverage: 255:494/496 of query aligns to 3:243/243 of 1eafA
G0S4X6 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; MRP3; Pyruvate dehydrogenase complex component E2; PDC-E2; PDCE2; EC 2.3.1.12 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) (see paper)
29% identity, 78% coverage: 106:494/496 of query aligns to 37:459/459 of G0S4X6
>3609500 FitnessBrowser__Dino:3609500
MSVEVRVPTLGESVTEATVATWFKKPGDTVAVDEMLCELETDKVTVEVPSPAAGTLAEIV
AAEGSTVGVDALLASIGEGSGAAAAEAAPAAPKAAPAESGGESVDVMVPTLGESVTEATV
STWFKKVGDTVVQDEMLCELETDKVSVEVPAPAAGVLTEILAPEGATVEASAKLAVLGGA
GAVAAPSEPAPAPAAPTAQGKDVEDAPSAKKLMAENNLASGDVQGTGRDGRVMKGDVLAA
LAAPKAAAPAPSAAPRAPVAAEDAAREERVKMTKLRQTIAKRLKDSQNTAAMLTTYNEVD
MTETMALRKEYKDLFEKKHGVRLGFMSFFTKACCHALKEVPEVNAEIDGTDIVYKNFVHM
GIAAGTPQGLVVPVIRDADRMSFAEIEAAIAEKGRRARDGKLSMAEMQGGTFTISNGGVY
GSLMSSPILNPPQSGILGMHKIQDRPMVINGEIKIRPMMYLALSYDHRIVDGKGAVTFLV
RVKEALEDPRRLLMDL
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory