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
//
