Reviewed, UniProtKB/Swiss-Prot Q2QMG2 (MCCA_ORYSJ)

Names and origin

Protein names

Recommended name:
    Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
      Short name=MCCase subunit alpha
    EC=6.4.1.4
Alternative name(s):
    3-methylcrotonyl-CoA carboxylase 1
    3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha

Gene names

Name:	MCCA
Ordered Locus Names:	Os12g0605800, LOC_Os12g41250

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.
Cofactor	Biotin. Binds 2 manganese ions per subunit By similarity.
Pathway	Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
Subunit structure	Probably a heterodimer composed of biotin-containing alpha subunits and beta subunits By similarity.
Subcellular location	Mitochondrion matrix Probable.
Induction	Induced during senescence. Ref.3
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain.
Sequence caution	The sequence ABA99832.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylcrotonoyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion Potential
	Chain	34 – 737	704	Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial		PRO_0000247483
Regions
	Domain	38 – 485	448	Biotin carboxylation
	Domain	157 – 355	199	ATP-grasp
	Domain	664 – 731	68	Biotinyl-binding
	Nucleotide binding	185 – 246	62	ATP By similarity
	Compositional bias	624 – 635	12	His-rich
Sites
	Active site	330	1	By similarity
	Metal binding	312	1	Manganese 1 By similarity
	Metal binding	326	1	Manganese 1 By similarity
	Metal binding	326	1	Manganese 2 By similarity
	Metal binding	328	1	Manganese 2 By similarity
	Binding site	153	1	ATP By similarity
	Binding site	237	1	ATP By similarity
	Binding site	272	1	ATP By similarity
Amino acid modifications
	Modified residue	698	1	N6-biotinyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2QMG2-1 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 0CD85579D649AF8B	FASTA	737	80,284
	10 20 30 40 50 60 MASRLLLLPR RRSRHGGASL LLARLLSSSS SEAGGGGAVE KVLVANRGEI ACRVMRTARR 70 80 90 100 110 120 LGIPTVAVYS DADRGALHVR AADEAVRLGP PPARESYLNA SAIVDAALRT GAKAIHPGYG 130 140 150 160 170 180 FLSESADFAQ LCKAEGLTFI GPPPSAIRDM GDKSASKRIM GAAGVPLVPG YHGAEQDIEL 190 200 210 220 230 240 LKLEANKIGY PVLIKPTHGG GGKGMRIVQR PEDFVDSVLS AQREAAASFG INTLLVEKYI 250 260 270 280 290 300 TQPRHIEVQI FGDQHGNVIH LYERDCSLQR RHQKIIEEAP APNVTAQFRS HIGEAAVSAA 310 320 330 340 350 360 KAVGYYSAGT VEFIVDTLSG EFYFMEMNTR LQVEHPVTEM IVGQDLVEWQ IRIANGECLP 370 380 390 400 410 420 LSQEQVPLNG HAFEARIYAE NVPRGFLPAT GTLHHYRPVP STATVRVETG VEEGDTVSMH 430 440 450 460 470 480 YDPMIAKLVV WGESRNAALV KLKNSLSNFQ IAGLPTNVGF LQELAGHSAF EKGLVDTHFI 490 500 510 520 530 540 ERYQNDLLST STQALSGSHE AEELGAILAA ACICKKDHVS SEVSLHDKKL SMWYAHPPFR 550 560 570 580 590 600 MHHFAKRLME FELDRELGGS SDDLLKLSVT YRSDGTYFVE TEDGSSPGLD VKVDSRGDHD 610 620 630 640 650 660 FRVDVGGLQT DVTLAFYSKD NCNHIHIWHG KHHHHYRQTL RAEQSPDDSS QPSASSEARS 670 680 690 700 710 720 HPKGSVLAPM AGLVVKVLLK DGARVEEGQP VMVMEAMKME HVVKAPCAGY VEGLKATAGQ 730 QVFDSSVLFT VKENKPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[2]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
[3]	"Leaf senescence in rice plants: cloning and characterization of senescence up-regulated genes." Lee R.-H., Wang C.-H., Huang L.-T., Chen S.-C.G. J. Exp. Bot. 52:1117-1121(2001) [PubMed: 11432928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 535-737, INDUCTION. Strain: cv. Tainung 67. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DP000011 Genomic DNA. Translation: ABA99831.2. DP000011 Genomic DNA. Translation: ABA99832.2. Sequence problems. DP000011 Genomic DNA. Translation: ABA99833.1. AK121511 mRNA. No translation available. AF251074 mRNA. Translation: AAL65397.1.
RefSeq	NP_001067226.1.
UniGene	Os.19628
3D structure databases
SMR	Q2QMG2. Positions 39-488, 664-731.
ModBase	Search...
Genome annotation databases
GeneID	4352741.
KEGG	osa:4352741.
Organism-specific databases
Gramene	Q8W2G0.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCCA_ORYSJ

Accession

Primary (citable) accession number: Q2QMG2
Secondary accession number(s): Q2QMG3, Q2QMG4, Q8W2G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 11, 2006
Last modified:	January 19, 2010
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)