ID A0A016RVL6_9BILA Unreviewed; 551 AA.
AC A0A016RVL6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
GN Name=Acey_s0361.g3479 {ECO:0000313|EMBL:EYB82378.1};
GN Synonyms=Acey-F02A9.4 {ECO:0000313|EMBL:EYB82378.1};
GN ORFNames=Y032_0361g3479 {ECO:0000313|EMBL:EYB82378.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB82378.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYB82378.1}.
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DR EMBL; JARK01001697; EYB82378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016RVL6; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000024635; 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:UP000024635}.
FT DOMAIN 90..347
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 350..551
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 551 AA; 59769 MW; 18AEF5675A31FAC5 CRC64;
MLGSVSQRLT SRTTSIQACR FIRARWERGY YKDLYHRRQL LGADPLIHRS SYPNCVRSHH
CFGGVAQQWS PIETAVDSSS QEYQQNYAQM KEVVDDLREK VAKITEGGGE KARALHKSRG
KMLARERINA LIDPGTSFLE LSQLAGYQSY GKEEVPAGGI ITGIGTVAGR VCIIVANDAT
VKGGTYYPIT VKKHLRAQEV ARENGLPCIY LVDSGGANLP RQADIFADRE HFGRIFYNQA
TLSSQGIPQL AVVMGSCTAG GAYVPAMSDQ AIIVKGNGTV FLGGPPLVKA ATGEEITAEE
LGGADLHCSE SGVTDYYAHS DAHALHLARN AVAGMGQPEG ALKFAEHFEE PLYPAEELFG
IVGANLKKTY DVREVIARVV DGSRFDEFKE RYGETLVTGF ANVYGQQVGI LANNGVLFSE
SAMKGAHFIE LCCQRKIPLL FLQNITGFMV GRDAEAGGIA KHGAKLVTAV ACAAVPKITV
LIGGSYGAGN YGMCGRAYSP RFLFMWPNAR ISVMGGEQAA NVLCTVQQDK RKREGLEWTK
VSRWGLDSIL L
//
