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P07633 (PCCB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Propionyl-CoA carboxylase beta chain, mitochondrial

Short name=PCCase subunit beta
EC=6.4.1.3
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit beta
Gene names
Name:Pccb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

Pathway

Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.

Subunit structure

Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the AccD/PCCB family.

Contains 1 carboxyltransferase domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion By similarity
Chain29 – 541513Propionyl-CoA carboxylase beta chain, mitochondrial
PRO_0000000296

Regions

Domain40 – 533494Carboxyltransferase
Region327 – 36034Acyl-CoA binding Potential

Amino acid modifications

Modified residue1011N6-acetyllysine; alternate By similarity
Modified residue1011N6-succinyllysine; alternate By similarity
Modified residue2501N6-succinyllysine By similarity
Modified residue4761N6-acetyllysine; alternate By similarity
Modified residue4761N6-succinyllysine; alternate By similarity
Modified residue4911N6-acetyllysine; alternate By similarity
Modified residue4911N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P07633 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 052E668E9EE23524

FASTA54158,626
        10         20         30         40         50         60 
MAAVIRIRAM AAGTRLRVLN CGLGTTIRSL CSQPVSVNER IENKRHAALL GGGQRRIDAQ 

        70         80         90        100        110        120 
HKRGKLTARE RISLLLDPGS FLESDMFVEH RCADFGMAAE KNKFPGDSVV TGRGRINGRL 

       130        140        150        160        170        180 
VYVFSQDFTV FGGSLSGAHA QKICKIMDQA ITVGAPVIGL NDSGGARIQE GVESLAGYAD 

       190        200        210        220        230        240 
IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EFVKSVTNED 

       250        260        270        280        290        300 
VTQEQLGGAK THTTVSGVAH RAFDNDVDAL CNLREFLNFL PLSNQDPASI RECHDPSDRL 

       310        320        330        340        350        360 
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPNYAK NIVIGFARMN GRTVGIVGNQ 

       370        380        390        400        410        420 
PNVASGCLDI NSSVKGARFV RFCDAFSIPL ITFVDVPGFL PGTAQEYGGI IRHGAKLLYA 

       430        440        450        460        470        480 
FAEATVPKIT VITRKAYGGA YDVMSSKHLL GDTNYAWPTA EIAVMGAKGA VEIIFKGHED 

       490        500        510        520        530        540 
VEAAQAEYVE KFANPFPAAV RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANVP 


L 

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References

[1]"Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase."
Kraus J.P., Firgaira F., Novotny J., Kalousek F., Williams K.R., Williamson C., Ohura T., Rosenberg L.E.
Proc. Natl. Acad. Sci. U.S.A. 83:8049-8053(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14634 mRNA. Translation: AAA41818.1.
PIRA25516.
UniGeneRn.9732.

3D structure databases

ProteinModelPortalP07633.
SMRP07633. Positions 39-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07633. 1 interaction.
STRING10116.ENSRNOP00000021657.

PTM databases

PhosphoSiteP07633.

Proteomic databases

PaxDbP07633.
PRIDEP07633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3265. rat.

Organism-specific databases

RGD3265. Pccb.

Phylogenomic databases

eggNOGCOG4799.
HOGENOMHOG000218693.
HOVERGENHBG003970.
InParanoidP07633.
PhylomeDBP07633.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-8607.
UniPathwayUPA00945; UER00908.

Gene expression databases

GenevestigatorP07633.

Family and domain databases

InterProIPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PROSITEPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP07633.

Entry information

Entry namePCCB_RAT
AccessionPrimary (citable) accession number: P07633
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways