ID A0A0K0EJW4_STRER Unreviewed; 585 AA.
AC A0A0K0EJW4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=methylcrotonoyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00026116};
DE EC=6.4.1.4 {ECO:0000256|ARBA:ARBA00026116};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2 {ECO:0000256|ARBA:ARBA00031404};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit {ECO:0000256|ARBA:ARBA00031109};
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000975500.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000975500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00029358};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC {ECO:0000256|ARBA:ARBA00025711}.
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DR AlphaFoldDB; A0A0K0EJW4; -.
DR STRING; 6248.A0A0K0EJW4; -.
DR WBParaSite; SSTP_0000975500.1; SSTP_0000975500.1; SSTP_0000975500.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT DOMAIN 71..328
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 328..577
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 585 AA; 63687 MW; A388158F4165361C CRC64;
MKKILLLKEC VNISNLRYLN KNIIKEHEGK SFIRKLQTSV FLSGSVTHKW SPITSEIDDS
SETYIQNKKE MEEVVKDLKK TVGKHVNGGD PKAIEKHKKR GKLLARERIE YLLDSGSSFL
EVGQLAGHEL YGKEEVPSGS IVTGIGKVSG RLCLIAANDA TVKGGTYYPI TVKKHLRGQE
IARENKLPCI YLVDSGGANL PRQANIFADR DHFGRIFYNQ ATMSAEGIPQ IAVVMGSCTA
GGAYVPAMAD QSIIVRKNGT VFLGGPPLVK AATGEVISAE ELGGADLHCG TSGVTDYYAV
NDEHALTMAR NVVAGLPEQK SAININQDVE EPLYSAEELY GIVGTNLKKT YDVREIIARI
VDGSRFDEFK KMFGETLVTG FSTIYGIPVG IIGNNGVLFG ESAQKGAHFI QLCCQRKIPL
LFLQNITGFM VGREAEASGI AKHGAKMVTA VACANVPKIT VVVGGSYGAG NYGMCGRAYS
PRFMYMWPNA RISVMGGEQA ANVLAQIQRD RAEATGSVWN DELENKLKKP IIETFEKEGH
PYFASGHLWD DGIIDPIDTR KVVGMSLKVS LNAPIPDAKF GIFRM
//
