ID A0A084VDM8_ANOSI Unreviewed; 523 AA.
AC A0A084VDM8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 24.
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=ZHAS_00003102 {ECO:0000313|EMBL:KFB36072.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB36072.1};
RN [1] {ECO:0000313|EMBL:KFB36072.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC003102-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; ATLV01011630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01011631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524705; KFB36072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084VDM8; -.
DR STRING; 74873.A0A084VDM8; -.
DR EnsemblMetazoa; ASIC003102-RA; ASIC003102-PA; ASIC003102.
DR VEuPathDB; VectorBase:ASIC003102; -.
DR VEuPathDB; VectorBase:ASIS024450; -.
DR OMA; VKTMGQI; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000030765; Unassembled WGS sequence.
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:UP000030765};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT ACT_SITE 346
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 523 AA; 56232 MW; F38A98BC04032229 CRC64;
MALSLCSKQV LGTTGRFSSR ILSWEISKVL ACRYSTEKKR SKIYASADEA IADIPDGSKL
LVGGFGLCGI PENLIGALVK KRAKDLTVVS NNAGVDTFGL GLLLKEKLIR RMIASYVGEN
AEFERQYLSG ELELELTPQG TLAERIRAGG AGIPAFFTPT AYGTLVHEGG SPIKYGPGGT
IEIASEPRPM QLFGGKPYIM EEAITGDYAL VKAHVADEAG NLIFNKSARN FNPPMCKAAK
VTIVEVEEIV PVGSLDPDQV HMPSVFVHRI VKGPSYEKRI ERLRVRDAKR SGSVVSSTPA
AKMRERIVKR VAMEYRDGMH INLGIGIPVL SSNFIPAGMN VLLQSENGIL GLGPFPEKHE
VDPDLINAGK ETVTVLPGAS YFSSDDSFAM IRGGHIDITV LGAMEVSQYG DLANWMIPGK
LVKGMGGAMD LVAAPGTKVI VTMEHNAKDG SHKILSNCNL PVTGRNCVDM IVTEKAVFNV
DKDTGLTLME LAEDCSVEEV ITSTGCDFSV SPDLKKMGQV DEV
//
