Comparing WP_025274975.1 NCBI__GCF_000527155.1:WP_025274975.1 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)
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)
52% identity, 100% coverage: 3:562/562 of query aligns to 122:675/675 of Q8NNJ2
Sites not aligning to the query:
6zzkA Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
52% identity, 43% coverage: 323:562/562 of query aligns to 2:240/240 of 6zzkA
6zzjA Crystal structure of the catalytic domain of corynebacterium glutamicum acetyltransferase acef (e2p) in complex with oxidized coa. (see paper)
52% identity, 43% coverage: 323:562/562 of query aligns to 2:240/240 of 6zzjA
6zzkB Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
52% identity, 43% coverage: 323:562/562 of query aligns to 3:241/241 of 6zzkB
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)
38% identity, 76% coverage: 126:553/562 of query aligns to 5:397/405 of P0AFG6
Sites not aligning to the query:
6zzmB Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (e2p). (see paper)
48% identity, 42% coverage: 325:562/562 of query aligns to 2:238/238 of 6zzmB
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)
37% identity, 76% coverage: 126:553/562 of query aligns to 4:420/428 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)
33% identity, 76% coverage: 126:553/562 of query aligns to 4:434/442 of P21883
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)
44% identity, 44% coverage: 305:553/562 of query aligns to 197:447/455 of Q9N0F1
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)
46% identity, 40% coverage: 328:553/562 of query aligns to 227:447/455 of P11179
Sites not aligning to the query:
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)
44% identity, 40% coverage: 328:553/562 of query aligns to 225:445/453 of P36957
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)
30% identity, 98% coverage: 5:553/562 of query aligns to 108:624/630 of P06959
Sites not aligning to the query:
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)
32% identity, 80% coverage: 110:556/562 of query aligns to 50:476/482 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)
32% identity, 77% coverage: 122:556/562 of query aligns to 62:476/482 of P11182
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)
32% identity, 98% coverage: 5:553/562 of query aligns to 94:641/647 of P10515
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)
32% identity, 98% coverage: 5:553/562 of query aligns to 94:641/647 of P11180
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, 77% coverage: 122:553/562 of query aligns to 54:496/501 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)
41% identity, 35% coverage: 356:553/562 of query aligns to 33:225/234 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)
41% identity, 35% coverage: 356:553/562 of query aligns to 33:225/234 of 2ii4A
2ii3A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), oxidized coenzyme a-bound form (see paper)
41% identity, 35% coverage: 356:553/562 of query aligns to 33:225/234 of 2ii3A
>WP_025274975.1 NCBI__GCF_000527155.1:WP_025274975.1
MPTSVTMPALGESVTEGTVTQWLKQEGDTVEVDEPLLEVSTDKVDTEVPSPVAGTLIKIV
AAEDAEVEVGGELAVVGEAGEAAGSPTPAPAEAPAEETPAEKPVEDTPAPVASAEAPASG
GGEGTDVTLPELGESVTEGTVTQWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGTLQD
IRVPEDETANVGDVLAVIGTGAAPAADTPQESPAPQPAAPAEPKPEPSEKPEPAAAAPQP
AAPAAPATTPPAAPTNKPTEVSYVTPLVRKLANENDVDLSQVTGTGVGGRIRKQDVQEVI
DRQKSSAPAPSAQPSAPVEPSPLRGRVEKMTRLRQVAAKALHDSLQSQAQLTTVVEVDLT
KVMNLRAAKKDEFLARHGVKLSPLPFMVVAAIEALQQYPIVNASMNMEEKTITYPEAENV
GVAVDTEKGLIVPVIKNAGDLNIPGIARHTAELAEKARSGGLTPDDLSGGTFTVTNTGSR
GALFDTPIVNAPQSAILGTGALVKRPVIVDDPELGEVVAPRQMMYLALSYDHRLIDGADA
ARFLQSVKGRLEEGNFEGALGL
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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