ID K9FLM9_PEND2 Unreviewed; 544 AA.
AC K9FLM9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=PDIG_58300 {ECO:0000313|EMBL:EKV10139.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV10139.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV10139.1}.
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DR EMBL; AKCT01000232; EKV10139.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FLM9; -.
DR STRING; 1170229.K9FLM9; -.
DR eggNOG; KOG3822; Eukaryota.
DR HOGENOM; CLU_019942_1_1_1; -.
DR InParanoid; K9FLM9; -.
DR OMA; VKVWVQS; -.
DR OrthoDB; 177109at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000009882; Unassembled WGS sequence.
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; 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; TIGR02428; pcaJ_scoB_fam; 1.
DR PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR PANTHER; PTHR13707:SF60; 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:UP000009882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 370
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 544 AA; 57935 MW; 1623F90E23622A12 CRC64;
MTTLRISTTL SRKALTVCRP RLFIGVRASV HPLQPFSTST SARYSRPAPL QSLAPKIERG
GSKLFKDADA AVADIKSGST ILSSGFGLCG VAETLINAMH RRGVDQLHSL TAISNNAGSA
GQGGLSTLSQ NGQIDRLILS YLGNNKSLEK KYLTGRIAIE LCPQGTLAER LRAGGAGIPA
FFTPTGVHTF IQEGKIPVRM DESGHVLESG KPRETREFNG KTYLMEEALT GDVAILRAWK
VDEAGNCVFR YTTKAFGPIM AKAATLTIVE AENIVPVGSI DPNDVDLPGI FVDRIVPATD
DKHIENRKLR SSEATAAGSA KDAAQMQREL IGRRAAKELK PGFYVNLGVG IPTLAPSFLP
KDVKVWIQSE NGILGMGDYP TEKELDPDII NAGKETVTLV PGAATFDSTE SFGMIRGGHV
DVSILGALQV SANGDLANYM IPGKVFKGMG GAMDLISNPD KTKIVVATSH VAKDGSPKIV
QKCSLPLTGA NVVSTIITDL CVFQVNRATG ELTLTELAPG VEVEEVQSKT DAKFTIADTL
EMME
//
