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Database: UniProt
Entry: G3NUV3_GASAC
LinkDB: G3NUV3_GASAC
Original site: G3NUV3_GASAC 
ID   G3NUV3_GASAC            Unreviewed;       517 AA.
AC   G3NUV3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Succinyl-CoA:3-ketoacid-coenzyme A transferase {ECO:0000256|PIRNR:PIRNR000858};
DE            EC=2.8.3.5 {ECO:0000256|PIRNR:PIRNR000858};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000009122.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000009122.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000009122.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; G3NUV3; -.
DR   Ensembl; ENSGACT00000009142.1; ENSGACP00000009122.1; ENSGACG00000006876.1.
DR   GeneTree; ENSGT00390000009130; -.
DR   UniPathway; UPA00929; UER00894.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000006876; Expressed in muscle tissue and 12 other cell types or tissues.
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; IPR004164; CoA_transf_AS.
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:SF23; 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.
DR   PROSITE; PS01274; COA_TRANSF_2; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000858};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT   ACT_SITE        342
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   517 AA;  56099 MW;  DA19229DBA821DFD CRC64;
     SSNIWQLASG REIVKCQRAC RASLTSGCYF STSSQRRSLF YADPTEAVKD IPSGATILVG
     GFGLCGIPEN LINSLLKTGV NGLTAVSNNA GVDNFGLGLL LKTKQIKRMI SSYVGENAEF
     ERQYLTGELE VELTPQGTLA ERIRAGGAGV PAFFTATGYG TLIQEGGSPI KYNKDGSIAI
     ASEKREVREF NGRHYIMEKA ITGDFALIKA WKADKAGNII FRKTARNFNQ PMCKAATTTI
     VEVEEVVDVG TFAEEDIHIP SIYVQRVVQG ASYEKRIEKR TVKRSQEEKP KPKKDADIVR
     ERIIRRAALE FEDGMYANLG IGIPMLASNF IKPDITVNLQ SENGILGLGP YPTEDAVDAD
     LINAGKETVT VLPGAAYFSS DESFSMIRGG HINLTMLGAM QVSKHGDLAN WMIPGKMVKG
     MGGAMDLVAS AGTKVVVTTN YSVSQGGKHK ILDKCSLPLT GKQCVDRIIT EKAVFDVDET
     KGLTLIEVWE GLTPEDIKAC TGTDFQVSPN LRSMQQI
//
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