ID H2UM93_TAKRU Unreviewed; 502 AA.
AC H2UM93;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 40.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000038064.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000038064.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000038064.3}
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|ARBA:ARBA00004753,
CC ECO:0000256|PIRNR:PIRNR000858}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; H2UM93; -.
DR Ensembl; ENSTRUT00000038201.3; ENSTRUP00000038064.3; ENSTRUG00000014894.3.
DR GeneTree; ENSGT00390000009130; -.
DR HOGENOM; CLU_019942_1_1_1; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000005226; Chromosome 21.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IPR004163; CoA_transf_BS.
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; PS01273; COA_TRANSF_1; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR000858};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT ACT_SITE 328
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 502 AA; 54553 MW; FC87D0A2A804EE47 CRC64;
PSVYLLLHFQ TCSCYFSTSN QRSSQFYSDP FEAVKDIPNG ATVLVGGFGL CGIPENLINS
LLKTGVKDLT AVSNNAGVDD FGLGLLLQTK QIKRMVSSYV GENAEFERQY LAGELEVELT
PQGTLAERIR AGGAGVPAFF TATGYGTLIQ EGGSPIKYNK DGSIAIASEK REVKEFNGRH
YIMEKAITGD FALVKAWKAD KAGNIVFRKT ARNFNQPMCK AAKTTIVEVE EVVDVGTFAA
EDIHIPSVYV NRIVKGGSYE KRIEKRTVKK SQQTQLKPKK DSDIVRERII RRAALEFQDG
MYANLGIGIP MLASNFIKPD ITVHLQSENG ILGLGPYPTE DAVDADLINA GKETVTVLPG
AAYFSSDESF AMIRGGHINL TMLGAMQVSK YGDLANWMIP GKMVKGMGGA MDLVASAGTK
VVVTMEHSAK GGKHKILDKC SLPLTGKHCV DRIITEKAVF DVDQTKGLTL IEVWEGLTPE
DIKACTGTDF EVSPNLKTMQ QI
//