Comparing WP_015799638.1 NCBI__GCF_000022745.1:WP_015799638.1 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)
6cerD Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
56% identity, 69% coverage: 136:455/461 of query aligns to 3:326/331 of 6cerD
6cfoB Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
56% identity, 69% coverage: 136:455/461 of query aligns to 2:325/330 of 6cfoB
P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; EC 1.2.4.1 from Homo sapiens (Human) (see 8 papers)
56% identity, 69% coverage: 136:455/461 of query aligns to 31:354/359 of P11177
Sites not aligning to the query:
Q5SLR3 2-oxoisovalerate dehydrogenase subunit beta; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDH E1-beta; EC 1.2.4.4 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
43% identity, 70% coverage: 135:455/461 of query aligns to 1:319/324 of Q5SLR3
1umdD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
44% identity, 69% coverage: 138:455/461 of query aligns to 3:318/323 of 1umdD
1umcD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
44% identity, 69% coverage: 138:455/461 of query aligns to 3:318/323 of 1umcD
1umbD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
44% identity, 69% coverage: 138:455/461 of query aligns to 3:318/323 of 1umbD
3dv0D Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 70% coverage: 137:457/461 of query aligns to 2:321/324 of 3dv0D
3dv0B Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 70% coverage: 137:457/461 of query aligns to 2:321/324 of 3dv0B
3dufD Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 70% coverage: 137:457/461 of query aligns to 2:321/324 of 3dufD
1w85B The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
40% identity, 70% coverage: 137:457/461 of query aligns to 2:321/324 of 1w85B
1qs0B Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
38% identity, 70% coverage: 137:457/461 of query aligns to 4:335/338 of 1qs0B
P21953 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDE1B; BCKDH E1-beta; EC 1.2.4.4 from Homo sapiens (Human) (see 2 papers)
34% identity, 72% coverage: 126:455/461 of query aligns to 59:387/392 of P21953
1dtwB Human branched-chain alpha-keto acid dehydrogenase (see paper)
35% identity, 69% coverage: 138:455/461 of query aligns to 5:321/326 of 1dtwB
2j9fD Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase e1b (see paper)
35% identity, 69% coverage: 138:455/461 of query aligns to 8:324/329 of 2j9fD
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)
51% identity, 18% coverage: 2:82/461 of query aligns to 56:136/501 of O00330
Sites not aligning to the query:
G0S5Q0 Pyruvate dehydrogenase complex protein X component, mitochondrial; Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex; E3-binding protein; Pyruvate dehydrogenase complex component E3BP from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) (see paper)
51% identity, 17% coverage: 4:82/461 of query aligns to 39:117/442 of G0S5Q0
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)
47% identity, 19% coverage: 3:89/461 of query aligns to 219:302/647 of P10515
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)
53% identity, 17% coverage: 5:81/461 of query aligns to 39:115/457 of A0A0D2Y5A7
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)
47% identity, 18% coverage: 3:87/461 of query aligns to 219:300/647 of P11180
Sites not aligning to the query:
>WP_015799638.1 NCBI__GCF_000022745.1:WP_015799638.1
MPIEILMPALSPTMEEGKLSKWLKKEGDKVTSGDVIAEIETDKATMEVEAVDEGTIGKLL
VDEGTEGVKVNTPIAVLLGDGESAADIGSAPAAKAEAAKEEPKAEENKADAVPAAPKAPA
VEVASDPDIPAGTEMVSMTVREALRDAMAEEMRRDPDVFIMGEEVAQYQGAYKITQGLLD
EFGPKRVVDTPITEHGFAGVGVGAAFAGLKPIVEFMTFNFAMQAIDQIVNSAAKTLYVSG
GQMGAPMVFRGPSGAAARVAAQHSQCYAAWYSHIPGLKVVMPYTAADAKGLLKAAIRDPN
PVIFLENEILYGHHFDVPKLDDFVLPIGKARIHKQGKDATIVSFGIGMTYAVKAAEELAG
QGIDVEIIDLRTIRPMDIPTVVESVKKTGRLVTVEEGFPQSSVGTEIATRVMQQAFDYLD
APILTIAGKDVPMPYAANLEKLALPSVAEVVEAVKAVTYTA
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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