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Reviewed, UniProtKB/Swiss-Prot Q42777 (MCCA_SOYBN)

Last modified February 9, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

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Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Tissue specificity

In leaves, cotyledons and stems.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

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Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Biotin
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion
Chain23 – 731709Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
PRO_0000002836

Regions

Domain32 – 478447Biotin carboxylation
Domain151 – 349199ATP-grasp
Domain661 – 72868Biotinyl-binding

Sites

Active site3241 By similarity
Metal binding3061Manganese 1 By similarity
Metal binding3201Manganese 1 By similarity
Metal binding3201Manganese 2 By similarity
Metal binding3221Manganese 2 By similarity
Binding site1471ATP By similarity
Binding site2311ATP By similarity
Binding site2661ATP By similarity

Amino acid modifications

Modified residue6951N6-biotinyllysine By similarity

Experimental info

Sequence conflict681R → K in AAA53141. Ref.1
Sequence conflict751T → S in AAA53141. Ref.1
Sequence conflict781E → K in AAA53141. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q42777-1 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: C4D5A94F8123A9B4

FASTA73180,620
        10         20         30         40         50         60 
MASLALLRRT TLSHSHVRAR AFSEGKSSNR HRIEKILVAN RGEIACRITR TARRLGIQTV 

        70         80         90        100        110        120 
AVYSDADRDS LHVATADEAI RIGPPPARLS YLNGASIVDA AIRSGAQAIH PGYGFLSESA 

       130        140        150        160        170        180 
DFAKLCEESG LTFIGPPASA IRDMGDKSAS KRIMGAAGVP LVPGYHGYDQ DIEKMKLEAD 

       190        200        210        220        230        240 
RIGYPVLIKP THGGGGKGMR IVHTPDEFVE SFLAAQREAA ASFGVNTILL EKYITRPRHI 

       250        260        270        280        290        300 
EVQIFGDKHG NVLHLYERDC SVQRRHQKII EEAPAPNISA DFRAQLGVAA VSAAKAVNYY 

       310        320        330        340        350        360 
NAGTVEFIVD TVSDEFYFME MNTRLQVEHP VTEMIVGQDL VEWQILVANG EALPLSQSQV 

       370        380        390        400        410        420 
PLSGHAFEAR IYAENVQKGF LPATGVLHHY HVPVSSAVRV ETGVKEGDKV SMHYDPMIAK 

       430        440        450        460        470        480 
LVVWGENRAA ALVKLKDSLS KFQVAGLPTN VNFLQKLANH RAFAIGNVET HFIDNYKEDL 

       490        500        510        520        530        540 
FVDANNSVSV KEAYEAARLN ASLVAACLIE KEHFILARNP PGGSSLLPIW YSSPPFRIHH 

       550        560        570        580        590        600 
QAKRRMELEW DNEYGSGSSK IMKLTITYQP DGRYLIETEQ NGSPVLEVKS TYVKDNYFRV 

       610        620        630        640        650        660 
EAAGVINDVN VAVYSKDQIR HIHIWQGSCH HYFREKLGLE LSEDEESQHK PKVETSANPQ 

       670        680        690        700        710        720 
GTVVAPMAGL VVKVLVENKT RVEEGQPVLV LEAMKMEHVV KAPSSGYVHG LQLMVGEQVS 

       730 
DGSVLFSVKD Q

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References

[1]"Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of 3-methylcrotonoyl-CoA carboxylase: identification of the biotin carboxylase and biotin-carrier domains."
Song J., Wurtele E.S., Nikolau B.J.
Proc. Natl. Acad. Sci. U.S.A. 91:5779-5783(1994) [PubMed: 8016064] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS.
Strain: cv. Corsoy 79.
Tissue: Cotyledon.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U08469 mRNA. Translation: AAA53140.1.
U08846 Genomic DNA. Translation: AAA53141.1.
PIRT06360. T06361.
UniGeneGma.6752

3D structure databases

SMRQ42777. Positions 33-481, 661-729.
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.4.1.4. 299.

Gene expression databases

GenevestigatorQ42777.

Family and domain databases

InterProIPR011761. 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]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
PfamPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
PROSITEPS50975. 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]
ProtoNetSearch...

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Entry information

Entry nameMCCA_SOYBN
AccessionPrimary (citable) accession number: Q42777
Secondary accession number(s): Q42778
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: February 9, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents