ID B7G2E2_PHATC Unreviewed; 557 AA.
AC B7G2E2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=PHATRDRAFT_21350 {ECO:0000313|EMBL:EEC47286.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC47286.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC47286.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC47286.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CM000614; EEC47286.1; -; Genomic_DNA.
DR RefSeq; XP_002181363.1; XM_002181327.1.
DR AlphaFoldDB; B7G2E2; -.
DR STRING; 556484.B7G2E2; -.
DR PaxDb; 2850-Phatr21350; -.
DR EnsemblProtists; Phatr3_J21350.t1; Phatr3_J21350.p1; Phatr3_J21350.
DR GeneID; 7202164; -.
DR KEGG; pti:PHATRDRAFT_21350; -.
DR eggNOG; KOG3822; Eukaryota.
DR HOGENOM; CLU_026774_4_0_1; -.
DR InParanoid; B7G2E2; -.
DR OMA; YQFTTEH; -.
DR OrthoDB; 5486183at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000000759; Chromosome 12.
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; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR43293; ACETATE COA-TRANSFERASE YDIF; 1.
DR PANTHER; PTHR43293:SF1; ACETATE COA-TRANSFERASE YDIF; 1.
DR Pfam; PF01144; CoA_trans; 1.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 1.
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:UP000000759};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 405
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 557 AA; 60459 MW; EFB45FA1024976A4 CRC64;
MASVVWRRPC TRLLSTVQYT LSASRVYRRS AVYLSVSTIQ LSVRSFSDKH DLESPKKRLH
YEIPQRVRQK VVSASDAVAL VRDGDTVSCS GFVAQGVAEA VLKALGERYD RTGHPNNLTL
LFGGGPGDWD SRGLNHLGKY SEDSSKPHML RRTIGSHYGQ TPKVAHMALQ NMVEAWTLPL
GSVSRMIRAQ ATHSPGHITE VGIGTYIDPD ISGGATNETA LESPLHSKLV QKLDIDGRPN
LMYKALPIHV AIIRGTTGDC RGNISIEEES VICDQKILAA AAKNSGGIVI AQVKRLAADG
TIPCRSVAIP GPLVDAVVVV DEKDHDSLHP MSYVERNNPS LTGQIKTPQD EVQKMPLDVR
KLIARRAFFK LSPDQIVNLG IGLPEGIASV AAEEDMLQYI TLSTEVGVFG GLPASGHNFG
PAYNATAMVE MNQMFDFYDG GGLDICFLGA AQIGKNGDVN VSRMSKDRLT GPGGFIDITQ
STRRIGFVMA FTAKGLEVDI PGDGKLGIKQ EGRVKKLVSS VFEKTFSGDE AVRRGQEVTY
ITERAVFRRT GKFDVQN
//