SitesBLAST

Q29551 Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial; SCOT; 3-oxoacid CoA-transferase 1; Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; SCOT-s; Succinate-coenzyme A transferase; Succinyl-CoA:3-oxoacid CoA transferase; EC 2.8.3.5 from Sus scrofa (Pig) (see 3 papers)
57% identity, 95% coverage: 5:203/209 of query aligns to 302:502/520 of Q29551

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Q29551

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E344 (= E47) active site, 5-glutamyl coenzyme A thioester intermediate

Sites not aligning to the query:

1:39 modified: transit peptide, Mitochondrion
67 C→A: Decreases KM for acetoacetyl-CoA 3-fold. No effect on KM for acetoacetate, succinyl-CoA and succinate.; C→S: Decreases KM for acetoacetate and acetoacetyl-CoA 2-fold. Increases KM for succinate 2-fold. Decreases KM for succinyl-CoA nearly 4-fold. Strongly reduces catalytic activity.
235 C→S: Similar specific activity to wild-type.

3k6mC Dynamic domains of succinyl-coa:3-ketoacid-coenzyme a transferase from pig heart. (see paper)
57% identity, 95% coverage: 5:203/209 of query aligns to 249:449/466 of 3k6mC

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3k6mC

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binding glycerol: I270 (= I26), E291 (= E47), A313 (= A69), V377 (= V133), A380 (≠ V136), T382 (vs. gap), C412 (≠ V167), N414 (≠ D169)

Sites not aligning to the query:

binding glycerol: 25, 52, 76, 99

3oxoE Succinyl-coa:3-ketoacid coa transferase from pig heart covalently bound to coa (see paper)
56% identity, 95% coverage: 6:203/209 of query aligns to 246:445/462 of 3oxoE

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3oxoE

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binding coenzyme a: I266 (= I26), G267 (= G27), I268 (= I28), E287 (= E47), G343 (= G103), M345 (= M105), N355 (= N115), I358 (= I118), M366 (= M126), A369 (= A129), K389 (= K148)

Query Sequence

>GFF606 FitnessBrowser__Phaeo:GFF606
MAWDRNQMAARAAQELQDGWYVNLGIGIPTLVSNHIPEGVNVTLQSENGMLGMGPFPVEG
EEDADLINAGKQTITELPQTAYFDSAQSFAMIRGGKIAMAILGAMEVAENGDLANWMIPG
KLVKGMGGAMDLVAGVGRVVVVMDHTNKHGDSKVLTDCTLPLTGKGVVDRIITNLGVLDV
VDGGLKIVETAEGVSEDELRAATQATIIN

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SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory