ID E9AHQ2_LEIIN Unreviewed; 489 AA.
AC E9AHQ2; A0A2K4Z411; A0A381MSR6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=LINJ_33_2470 {ECO:0000313|EMBL:CBZ08952.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CBZ08952.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CBZ08952.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CBZ08952.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CBZ08952.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CBZ08952.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JPCM5;
RA Hilley J.D., Rogers M., Wilkes J., Dickens N.J., Bates P., Depledge D.P.,
RA Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., Saad W., Seeger K.,
RA Berriman M., Smith D.F., Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow genomic structural
RT differences between species and strains of Leishmania.";
RL Submitted (FEB-2011) 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|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 EMBL; FR796465; CBZ08952.1; -; Genomic_DNA.
DR RefSeq; XP_003392753.1; XM_003392705.1.
DR AlphaFoldDB; E9AHQ2; -.
DR SMR; E9AHQ2; -.
DR STRING; 5671.E9AHQ2; -.
DR GeneID; 10966223; -.
DR KEGG; lif:LINJ_33_2470; -.
DR VEuPathDB; TriTrypDB:LINF_330032400; -.
DR eggNOG; KOG3822; Eukaryota.
DR InParanoid; E9AHQ2; -.
DR OMA; VKVWVQS; -.
DR OrthoDB; 177109at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000008153; Chromosome 33.
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; 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; 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:UP000008153};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT ACT_SITE 313
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 489 AA; 52630 MW; 15F4E537F90D4C6E CRC64;
MLRRNFWRLV GLNKVQSLEE AVADMTDGIS VAVGGFGCSG VPDAVISAMC KKGVKEMILY
TDSAGIDGFG LARLIETKQV RRMCCSFVGM NKIFKRRYLE GDVELEFVPQ GTLAERMRAG
GAGIPAFYTA TAYGTQRQTG GQIIRYDKNG VPCVISEPKE TRQFGNRWYV LEKTIRPDYA
IVKALKADKS GNLVFRGTAR NFNIPAAQCG RRVIAEVEQV VENGEIHPDD VHLPGVYVHR
VVQASYEVPI EKRTVSGSGA EPSSVNPNDD RQKIARRAAL EFADGMYANL GIGIPTEAAN
YMPAGVTVTL HSENGLLGMG PFPTADKVSA DWINAGKQTI SFLPGAACFD SATSFAMIRG
GHMNLTMLGA LEVSSNGDLA NWGIPGKLVN GPGGAMDLVA SGSRVVVTMS HCNKRGDSKL
VERCSLPVTG LHCVTRIITE KAVFDVIDKH LVLKEVAEGL TVDDIKKCTA AHFEVDKVKP
IAYAAPVSG
//
