ID A0A074W4L8_9PEZI Unreviewed; 517 AA.
AC A0A074W4L8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=M437DRAFT_71578 {ECO:0000313|EMBL:KEQ67793.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ67793.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ67793.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ67793.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584824; KEQ67793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W4L8; -.
DR STRING; 1043003.A0A074W4L8; -.
DR HOGENOM; CLU_019942_1_2_1; -.
DR OrthoDB; 177109at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000030672; 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; 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:UP000030672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 344
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 517 AA; 55264 MW; 2FC652C3682DEB56 CRC64;
MPSITLSLRT VGHLARNGSK PHNLLRTFAS SAKRSEINKV YSSAEEAISD VKGDSTLLCG
GFGLCGVPDT LINAVKNKPS IKGLTAVSNN AGIVGSGLGL LLESKQVKKM IASYVGENKV
FEKMYLTGEI ELELTPQGTL AERCRAGGAG IPAFFTPAAF GTVVQTGELP TVHNSDGSVA
QYSTPRDVKV FDGKSYVMEE AIKGDYAFIK AWKADKLGNL MFRFAAQNFN GAMARNAKVT
IVEAEHIVEV GEIDPAAVHV PGIYVDRVIQ STEPKNIEKV VNAKDPAEAL NALGSGDAAS
KRERIVRRAA KEFKNGMYAN LGIGMPMMAP AFVDDSIEVQ LQSENGILGL GAYPQKGQED
PDLINAGKET VTLRPGAAVF GSDESFAMIR AGRIHMTMLG AMQVSARGDL ANFAMPGKIK
GMGGAMDLVS NPEKTRVVVT MEHTDKKGGP KIMKMCEFPL TGKACVSRII TELAVFDVDF
TTGLTLIEHA EGVTVEEIRS KTEAPFKVSE SLQVMQQ
//
