(data stored in SCRATCH zone)

SWISSPROT: A2Q7C6_ASPNC

ID   A2Q7C6_ASPNC            Unreviewed;       485 AA.
AC   A2Q7C6;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 60.
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=An01g00200 {ECO:0000313|EMBL:CAK36870.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36870.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {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|PIRNR:PIRNR000858}.
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DR   EMBL; AM269949; CAK36870.1; -; Genomic_DNA.
DR   PaxDb; A2Q7C6; -.
DR   EnsemblFungi; CAK36870; CAK36870; An01g00200.
DR   HOGENOM; HOG000221244; -.
DR   UniPathway; UPA00929; UER00894.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
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   PANTHER; PTHR13707; PTHR13707; 1.
DR   Pfam; PF01144; CoA_trans; 2.
DR   PIRSF; PIRSF000858; SCOT-t; 1.
DR   SMART; SM00882; CoA_trans; 2.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7C6.
DR   SWISS-2DPAGE; A2Q7C6.
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000858};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000858, ECO:0000313|EMBL:CAK36870.1}.
FT   ACT_SITE        311
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   485 AA;  51737 MW;  DCB713C9C26259A8 CRC64;
     MLSTVATFSE PVKIFLVLPD NTTSLLTHES IAETLISAIH RRGADNLHSL TAVSNNAGLA
     GKGGLSTLTQ AGQVNRLILS YLGNNKALEK KYLTGNIAIE LCPQGSLAER LRAGGAGIPA
     FYTPTGVHTL LQKGEIPVRV DESGKVLERG KPRETREFNG KTYMMETALN GDVAILRAWK
     VDAAGNCVFR YTTKAFGPIM AKAAALTIVE AENIVPVGSI DPNDVDLPGI FVDRIVPATD
     EKHIEIKKLR SDKGDDANKK AEDAATVLRN RIAKRAAREL KQGYYVNLGV GIPTLAPSFL
     PEDVKVWIQS ENGILGMGPY PTEEEVDADI INAGKETVTL VPGAATFDSS ESFGMIRGGH
     VDVSILGALQ VSANGDLANY MIPGKVFKGM GGAMDLISNP EKTKIVVATS HTAKDGSPKI
     VDQCSLPLTG ANCVSTIITE LCVFQVDRTK GELLLTELAP GVEVEEIQDK TGAKFSVAEN
     LEIME
//

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