MCCA_SOYBN
ID MCCA_SOYBN Reviewed; 731 AA.
AC Q42777; Q42778;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
DE Short=MCCase subunit alpha;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
DE Flags: Precursor;
GN Name=MCCA;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF
RP N-TERMINUS.
RC STRAIN=cv. Corsoy 79; TISSUE=Cotyledon;
RX PubMed=8016064; DOI=10.1073/pnas.91.13.5779;
RA Song J., Wurtele E.S., Nikolau B.J.;
RT "Molecular cloning and characterization of the cDNA coding for the biotin-
RT containing subunit of 3-methylcrotonoyl-CoA carboxylase: identification of
RT the biotin carboxylase and biotin-carrier domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5779-5783(1994).
CC -!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
CC carboxylase, an enzyme that catalyzes the conversion of 3-
CC methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC leucine and isovaleric acid catabolism. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBUNIT: Probably a heterodimer composed of biotin-containing alpha
CC subunits and beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: In leaves, cotyledons and stems.
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DR EMBL; U08469; AAA53140.1; -; mRNA.
DR EMBL; U08846; AAA53141.1; -; Genomic_DNA.
DR PIR; T06361; T06360.
DR AlphaFoldDB; Q42777; -.
DR SMR; Q42777; -.
DR STRING; 3847.GLYMA02G16390.1; -.
DR eggNOG; KOG0238; Eukaryota.
DR InParanoid; Q42777; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IDA:CACAO.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR045774; MCCA_BT_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF19331; MCCA_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; Direct protein sequencing; Ligase; Manganese;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8016064"
FT CHAIN 23..731
FT /note="Methylcrotonoyl-CoA carboxylase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000002836"
FT DOMAIN 32..478
FT /note="Biotin carboxylation"
FT DOMAIN 151..349
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 653..729
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 324
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 695
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 68
FT /note="R -> K (in Ref. 1; AAA53141)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> S (in Ref. 1; AAA53141)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="E -> K (in Ref. 1; AAA53141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 80620 MW; C4D5A94F8123A9B4 CRC64;
MASLALLRRT TLSHSHVRAR AFSEGKSSNR HRIEKILVAN RGEIACRITR TARRLGIQTV
AVYSDADRDS LHVATADEAI RIGPPPARLS YLNGASIVDA AIRSGAQAIH PGYGFLSESA
DFAKLCEESG LTFIGPPASA IRDMGDKSAS KRIMGAAGVP LVPGYHGYDQ DIEKMKLEAD
RIGYPVLIKP THGGGGKGMR IVHTPDEFVE SFLAAQREAA ASFGVNTILL EKYITRPRHI
EVQIFGDKHG NVLHLYERDC SVQRRHQKII EEAPAPNISA DFRAQLGVAA VSAAKAVNYY
NAGTVEFIVD TVSDEFYFME MNTRLQVEHP VTEMIVGQDL VEWQILVANG EALPLSQSQV
PLSGHAFEAR IYAENVQKGF LPATGVLHHY HVPVSSAVRV ETGVKEGDKV SMHYDPMIAK
LVVWGENRAA ALVKLKDSLS KFQVAGLPTN VNFLQKLANH RAFAIGNVET HFIDNYKEDL
FVDANNSVSV KEAYEAARLN ASLVAACLIE KEHFILARNP PGGSSLLPIW YSSPPFRIHH
QAKRRMELEW DNEYGSGSSK IMKLTITYQP DGRYLIETEQ NGSPVLEVKS TYVKDNYFRV
EAAGVINDVN VAVYSKDQIR HIHIWQGSCH HYFREKLGLE LSEDEESQHK PKVETSANPQ
GTVVAPMAGL VVKVLVENKT RVEEGQPVLV LEAMKMEHVV KAPSSGYVHG LQLMVGEQVS
DGSVLFSVKD Q
