Comparing 201485 FitnessBrowser__MR1:201485 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)
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)
44% identity, 83% coverage: 91:535/535 of query aligns to 44:482/482 of P11182
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)
46% identity, 83% coverage: 92:535/535 of query aligns to 45:482/482 of P11181
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)
55% identity, 44% coverage: 303:535/535 of query aligns to 3:234/234 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)
55% identity, 44% coverage: 303:535/535 of query aligns to 3:234/234 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)
55% identity, 44% coverage: 303:535/535 of query aligns to 3:234/234 of 2ii3A
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)
37% identity, 79% coverage: 111:532/535 of query aligns to 4:440/442 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)
35% identity, 79% coverage: 111:532/535 of query aligns to 4:426/428 of P11961
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)
32% identity, 99% coverage: 4:532/535 of query aligns to 107:630/630 of P06959
Sites not aligning to the query:
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)
26% identity, 80% coverage: 107:532/535 of query aligns to 2:403/405 of P0AFG6
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)
31% identity, 55% coverage: 230:525/535 of query aligns to 374:665/675 of Q8NNJ2
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)
25% identity, 98% coverage: 7:532/535 of query aligns to 96:647/647 of P11180
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)
25% identity, 98% coverage: 7:532/535 of query aligns to 96:647/647 of P10515
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)
33% identity, 41% coverage: 306:525/535 of query aligns to 8:231/241 of 6zzkB
6zzkA Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
33% identity, 41% coverage: 306:525/535 of query aligns to 7:230/240 of 6zzkA
6zzjA Crystal structure of the catalytic domain of corynebacterium glutamicum acetyltransferase acef (e2p) in complex with oxidized coa. (see paper)
33% identity, 41% coverage: 306:525/535 of query aligns to 7:230/240 of 6zzjA
6zzmB Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (e2p). (see paper)
33% identity, 41% coverage: 308:525/535 of query aligns to 7:228/238 of 6zzmB
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, 78% coverage: 111:527/535 of query aligns to 58:497/501 of O00330
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, 78% coverage: 114:532/535 of query aligns to 39:459/459 of G0S4X6
1eafA Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex (see paper)
35% identity, 42% coverage: 307:532/535 of query aligns to 19:243/243 of 1eafA
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)
29% identity, 57% coverage: 230:532/535 of query aligns to 181:457/457 of A0A0D2Y5A7
Sites not aligning to the query:
>201485 FitnessBrowser__MR1:201485
MIKDFILPDIGEGVVECELVEWLVKEGDTIVEDQPIADVMTDKALVQIPAPFAGVVTKLY
YAKGDIAKVHAPLYAVQIEAEEPSSQVAPQTVEHSAPNQAAISAASSSIEQFLLPDIGEG
IVECELVEWLVQEGDIVVEDQPIADVMTDKALVQIPAIKAGKIVKLHYRKGQLAKVHAPL
YAIEVEGGVIPAVSAHETTNVAVANTATSAACATASVSQEPARQGKALASPAVRRMARAL
DIDLSRVPGSGKHGRVYKEDISRFQAQGSATPVVAPVATASTQQSSVTQSAVPITVASAA
RADIVEPIRGVKAVMAKLMVESVSTIPHFTYCEEFDLTDLVALRESMKAKYSSDEVKLTM
MPFFMKAMSLALTQFPVLNSQVNADCTEITYKARHNIGMAVDSKVGLLVPNVKDVQDKSI
LEVAAEITRLTNAARSGRVAPADLKEGTISISNIGALGGTVATPIINKPEVAIVALGKLQ
TLPRFNAKGEVEARQIMQVSWSGDHRVIDGGTIARFCNLWKQYLEQPQDMLLAMR
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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