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Database: UniProt
Entry: Q2QMG2
LinkDB: Q2QMG2
Original site: Q2QMG2 
ID   MCCA_ORYSJ              Reviewed;         737 AA.
AC   Q2QMG2; A0A0P0YC98; Q0IM20; Q2QMG3; Q2QMG4; Q8W2G0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   16-JAN-2019, entry version 104.
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; OrderedLocusNames=Os12g0605800, LOC_Os12g41250;
GN   ORFNames=OsJ_36794;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease
RT   resistance genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 535-737, AND INDUCTION.
RC   STRAIN=cv. Tainung 67; TISSUE=Leaf;
RX   PubMed=11432928; DOI=10.1093/jexbot/52.358.1117;
RA   Lee R.-H., Wang C.-H., Huang L.-T., Chen S.-C.G.;
RT   "Leaf senescence in rice plants: cloning and characterization of
RT   senescence up-regulated genes.";
RL   J. Exp. Bot. 52:1117-1121(2001).
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-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
CC         H(+) + phosphate + trans-3-methylglutaconyl-CoA;
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-
CC       hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC   -!- SUBUNIT: Probably a heterodimer composed of biotin-containing
CC       alpha subunits and beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- INDUCTION: Induced during senescence.
CC       {ECO:0000269|PubMed:11432928}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA99832.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DP000011; ABA99831.2; -; Genomic_DNA.
DR   EMBL; DP000011; ABA99832.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008218; BAF30245.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT17984.1; -; Genomic_DNA.
DR   EMBL; CM000149; EEE53566.1; -; Genomic_DNA.
DR   EMBL; AK121511; BAH00526.1; -; mRNA.
DR   EMBL; AF251074; AAL65397.1; -; mRNA.
DR   RefSeq; XP_015620588.1; XM_015765102.1.
DR   UniGene; Os.19628; -.
DR   ProteinModelPortal; Q2QMG2; -.
DR   SMR; Q2QMG2; -.
DR   STRING; 39947.LOC_Os12g41250.1; -.
DR   CarbonylDB; Q2QMG2; -.
DR   PaxDb; Q2QMG2; -.
DR   PRIDE; Q2QMG2; -.
DR   EnsemblPlants; Os12t0605800-01; Os12t0605800-01; Os12g0605800.
DR   GeneID; 4352741; -.
DR   Gramene; Os12t0605800-01; Os12t0605800-01; Os12g0605800.
DR   KEGG; osa:4352741; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; COG4770; LUCA.
DR   InParanoid; Q2QMG2; -.
DR   KO; K01968; -.
DR   OMA; MEFELDR; -.
DR   OrthoDB; 254436at2759; -.
DR   Reactome; R-OSA-196780; Biotin transport and metabolism.
DR   Reactome; R-OSA-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000059680; Chromosome 12.
DR   ExpressionAtlas; Q2QMG2; differential.
DR   Genevisible; Q2QMG2; OS.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; 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   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   2: Evidence at transcript level;
KW   ATP-binding; Biotin; Complete proteome; Ligase; Manganese;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     33       Mitochondrion. {ECO:0000255}.
FT   CHAIN        34    737       Methylcrotonoyl-CoA carboxylase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000247483.
FT   DOMAIN       38    485       Biotin carboxylation.
FT   DOMAIN      157    355       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      656    732       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   NP_BIND     185    246       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   COMPBIAS    624    635       His-rich.
FT   ACT_SITE    330    330       {ECO:0000250}.
FT   METAL       312    312       Manganese 1. {ECO:0000250}.
FT   METAL       326    326       Manganese 1. {ECO:0000250}.
FT   METAL       326    326       Manganese 2. {ECO:0000250}.
FT   METAL       328    328       Manganese 2. {ECO:0000250}.
FT   BINDING     153    153       ATP. {ECO:0000250}.
FT   BINDING     237    237       ATP. {ECO:0000250}.
FT   BINDING     272    272       ATP. {ECO:0000250}.
FT   MOD_RES     698    698       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   737 AA;  80284 MW;  0CD85579D649AF8B CRC64;
     MASRLLLLPR RRSRHGGASL LLARLLSSSS SEAGGGGAVE KVLVANRGEI ACRVMRTARR
     LGIPTVAVYS DADRGALHVR AADEAVRLGP PPARESYLNA SAIVDAALRT GAKAIHPGYG
     FLSESADFAQ LCKAEGLTFI GPPPSAIRDM GDKSASKRIM GAAGVPLVPG YHGAEQDIEL
     LKLEANKIGY PVLIKPTHGG GGKGMRIVQR PEDFVDSVLS AQREAAASFG INTLLVEKYI
     TQPRHIEVQI FGDQHGNVIH LYERDCSLQR RHQKIIEEAP APNVTAQFRS HIGEAAVSAA
     KAVGYYSAGT VEFIVDTLSG EFYFMEMNTR LQVEHPVTEM IVGQDLVEWQ IRIANGECLP
     LSQEQVPLNG HAFEARIYAE NVPRGFLPAT GTLHHYRPVP STATVRVETG VEEGDTVSMH
     YDPMIAKLVV WGESRNAALV KLKNSLSNFQ IAGLPTNVGF LQELAGHSAF EKGLVDTHFI
     ERYQNDLLST STQALSGSHE AEELGAILAA ACICKKDHVS SEVSLHDKKL SMWYAHPPFR
     MHHFAKRLME FELDRELGGS SDDLLKLSVT YRSDGTYFVE TEDGSSPGLD VKVDSRGDHD
     FRVDVGGLQT DVTLAFYSKD NCNHIHIWHG KHHHHYRQTL RAEQSPDDSS QPSASSEARS
     HPKGSVLAPM AGLVVKVLLK DGARVEEGQP VMVMEAMKME HVVKAPCAGY VEGLKATAGQ
     QVFDSSVLFT VKENKPN
//
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