Comparing WP_009781680.1 NCBI__GCF_000152985.1:WP_009781680.1 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)
45% identity, 98% coverage: 2:402/411 of query aligns to 3:404/405 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)
40% identity, 97% coverage: 3:402/411 of query aligns to 72:454/455 of P11179
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)
52% identity, 59% coverage: 159:402/411 of query aligns to 207:454/455 of Q9N0F1
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, 98% coverage: 1:402/411 of query aligns to 1:441/442 of P21883
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)
34% identity, 98% coverage: 1:402/411 of query aligns to 1:427/428 of P11961
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 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
36% identity, 66% coverage: 126:395/411 of query aligns to 374:666/675 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)
40% identity, 55% coverage: 170:394/411 of query aligns to 1:231/241 of 6zzkB
6zzkA Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
41% identity, 54% coverage: 172:394/411 of query aligns to 3:230/240 of 6zzkA
6zzjA Crystal structure of the catalytic domain of corynebacterium glutamicum acetyltransferase acef (e2p) in complex with oxidized coa. (see paper)
41% identity, 54% coverage: 172:394/411 of query aligns to 3:230/240 of 6zzjA
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, 97% coverage: 3:402/411 of query aligns to 65:480/482 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 7 papers)
30% identity, 98% coverage: 2:402/411 of query aligns to 64:480/482 of P11182
6zzmB Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (e2p). (see paper)
38% identity, 54% coverage: 175:394/411 of query aligns to 3:228/238 of 6zzmB
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)
28% identity, 97% coverage: 5:401/411 of query aligns to 39:457/457 of A0A0D2Y5A7
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)
28% identity, 97% coverage: 3:401/411 of query aligns to 219:647/647 of P10515
Sites not aligning to the query:
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)
28% identity, 97% coverage: 4:401/411 of query aligns to 208:630/630 of P06959
Sites not aligning to the query:
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)
33% identity, 67% coverage: 126:401/411 of query aligns to 358:647/647 of P11180
Sites not aligning to the query:
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)
27% identity, 97% coverage: 5:401/411 of query aligns to 37:459/459 of G0S4X6
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)
27% identity, 97% coverage: 3:399/411 of query aligns to 57:500/501 of O00330
Sites not aligning to the query:
2ii5A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), isobutyryl-coenzyme a-bound form (see paper)
35% identity, 48% coverage: 204:402/411 of query aligns to 32:232/234 of 2ii5A
2ii4A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), coenzyme a-bound form (see paper)
35% identity, 48% coverage: 204:402/411 of query aligns to 32:232/234 of 2ii4A
>WP_009781680.1 NCBI__GCF_000152985.1:WP_009781680.1
MALEMKVPSPGESITEVEIAQWLVEDGDYVEKDQAIAEVDSDKATLELPAEASGIITLKA
EEGDAVAVGEVVCLIDTDAAKPEGDSSGDKEEQKEEKAEPKKEAPSKSSTPEQAQDKKTY
ASGSPSPAAKKTLDEKGIDAKDVKGTGRDGRITKEDAVNAQPSMGTPGTGSRGESRSKMS
MLRRKVAERLVSVKNETAMLTTFNEVDMTPIFDLRSKYKEDFKAKHGVSLGFMSFFTLAC
VRALEMYPAVNSMIDGKEMVSYDFKDISIAVSGPKGLMVPVIRNAENLSFRGVESEVKRL
ALRARDGQITVDEMTGGTFTITNGGVFGSMLSTPIINPPQSAILGMHNIVERPIVRDGGI
AIAPIMYVALSYDHRIIDGKESVGFLVAVKEALENPEELLMDNNVLKALEL
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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