ID A2Q843_ASPNC Unreviewed; 504 AA.
AC A2Q843;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Succinyl-CoA:3-ketoacid-coenzyme A transferase {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.5 {ECO:0000256|PIRNR:PIRNR000858};
GN ORFNames=An01g03000 {ECO:0000313|EMBL:CAK43666.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK43666.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK43666.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA
CC moiety from succinate to acetoacetate. Formation of the enzyme-CoA
CC intermediate proceeds via an unstable anhydride species formed between
CC the carboxylate groups of the enzyme and substrate.
CC {ECO:0000256|PIRNR:PIRNR000858}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate;
CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5;
CC Evidence={ECO:0000256|PIRNR:PIRNR000858};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000256|PIRNR:PIRNR000858}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000256|ARBA:ARBA00007154, ECO:0000256|PIRNR:PIRNR000858}.
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DR EMBL; AM269955; CAK43666.1; -; Genomic_DNA.
DR RefSeq; XP_001388734.1; XM_001388697.2.
DR AlphaFoldDB; A2Q843; -.
DR SMR; A2Q843; -.
DR EnsemblFungi; CAK43666; CAK43666; An01g03000.
DR GeneID; 4977961; -.
DR KEGG; ang:An01g03000; -.
DR VEuPathDB; FungiDB:An01g03000; -.
DR HOGENOM; CLU_019942_1_1_1; -.
DR OrthoDB; 177109at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008260; F:succinyl-CoA:3-oxo-acid CoA-transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR02429; pcaI_scoA_fam; 1.
DR NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR PANTHER; PTHR13707:SF58; SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE; 1.
DR Pfam; PF01144; CoA_trans; 2.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 2.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000858};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 332
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 504 AA; 54458 MW; CCABFBCA02EEBD4D CRC64;
MSRPVPAVFR PIWRRNFSVS TAKRAIDKLC PSAQEAIKDM KGSSTLLVGG FGFAGVPTTL
IDAVRDRPDI KDLTVVSNNA GMPGVGLGQL LESKQISKMI ASFIGENKVF EKMYLTGDLS
LELTPQGTIA EKCAAGAAGV PAFYTPAAYG TIVQSGELPV RYNKDGSVAI KNAPKEEREF
NGKKYILEES IFGDYALVKV HKADKLGNCQ FRKSMNNFNE AMAKNAKYTI VEADHIVEVG
EIDPESIHLQ GIYVNKVIQS TGEKKIEKLT FAKDPNEMLQ AGSGDATARR ERIVKRAAKE
FKDGMYVNLG IGMPLIAPSY VEEGVEVVLQ AENGILGLGG YPKPGEEDPD LINPGKETVT
LGRGASVFGS HESFGMIRSG RIDLTMLGAL QVSQYGDLAN FMLPGKVKGM GGAMDLVSNP
EKTKVVVTME HTDKKGNPKI LPECSFPLTG PRCVWKIITD LAVFEVSPTE GLTLAEYAEG
VTVEEIRSKT AAPFKVSADL KPML
//
