Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Propionyl-CoA carboxylase beta chain, mitochondrial

Gene

Pccb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathwayi: propanoyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Propionyl-CoA carboxylase alpha chain, mitochondrial (Pcca), Propionyl-CoA carboxylase beta chain, mitochondrial (Pccb)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • propionyl-CoA carboxylase activity Source: RGD

GO - Biological processi

  • cellular amino acid catabolic process Source: RGD
  • fatty acid catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8607.
UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

Protein namesi
Recommended name:
Propionyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.3)
Short name:
PCCase subunit beta
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:Pccb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3265. Pccb.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionBy similarityAdd BLAST28
ChainiPRO_000000029629 – 541Propionyl-CoA carboxylase beta chain, mitochondrialAdd BLAST513

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73PhosphoserineBy similarity1
Modified residuei101N6-acetyllysine; alternateBy similarity1
Modified residuei101N6-succinyllysine; alternateBy similarity1
Modified residuei250N6-succinyllysineBy similarity1
Modified residuei476N6-acetyllysine; alternateBy similarity1
Modified residuei476N6-succinyllysine; alternateBy similarity1
Modified residuei491N6-acetyllysine; alternateBy similarity1
Modified residuei491N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07633.
PRIDEiP07633.

PTM databases

iPTMnetiP07633.
PhosphoSitePlusiP07633.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP07633. 1 interactor.
STRINGi10116.ENSRNOP00000021657.

Structurei

3D structure databases

ProteinModelPortaliP07633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 292CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST259
Domaini296 – 535CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST240

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 535CarboxyltransferasePROSITE-ProRule annotationAdd BLAST502
Regioni327 – 360Acyl-CoA bindingSequence analysisAdd BLAST34

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiP07633.
PhylomeDBiP07633.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVIRIRAM AAGTRLRVLN CGLGTTIRSL CSQPVSVNER IENKRHAALL
60 70 80 90 100
GGGQRRIDAQ HKRGKLTARE RISLLLDPGS FLESDMFVEH RCADFGMAAE
110 120 130 140 150
KNKFPGDSVV TGRGRINGRL VYVFSQDFTV FGGSLSGAHA QKICKIMDQA
160 170 180 190 200
ITVGAPVIGL NDSGGARIQE GVESLAGYAD IFLRNVTASG VIPQISLIMG
210 220 230 240 250
PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EFVKSVTNED VTQEQLGGAK
260 270 280 290 300
THTTVSGVAH RAFDNDVDAL CNLREFLNFL PLSNQDPASI RECHDPSDRL
310 320 330 340 350
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPNYAK NIVIGFARMN
360 370 380 390 400
GRTVGIVGNQ PNVASGCLDI NSSVKGARFV RFCDAFSIPL ITFVDVPGFL
410 420 430 440 450
PGTAQEYGGI IRHGAKLLYA FAEATVPKIT VITRKAYGGA YDVMSSKHLL
460 470 480 490 500
GDTNYAWPTA EIAVMGAKGA VEIIFKGHED VEAAQAEYVE KFANPFPAAV
510 520 530 540
RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANVP L
Length:541
Mass (Da):58,626
Last modified:April 1, 1988 - v1
Checksum:i052E668E9EE23524
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14634 mRNA. Translation: AAA41818.1.
PIRiA25516.
UniGeneiRn.9732.

Genome annotation databases

UCSCiRGD:3265. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14634 mRNA. Translation: AAA41818.1.
PIRiA25516.
UniGeneiRn.9732.

3D structure databases

ProteinModelPortaliP07633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07633. 1 interactor.
STRINGi10116.ENSRNOP00000021657.

PTM databases

iPTMnetiP07633.
PhosphoSitePlusiP07633.

Proteomic databases

PaxDbiP07633.
PRIDEiP07633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3265. rat.

Organism-specific databases

RGDi3265. Pccb.

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiP07633.
PhylomeDBiP07633.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.
BioCyciMetaCyc:MONOMER-8607.

Miscellaneous databases

PROiP07633.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCCB_RAT
AccessioniPrimary (citable) accession number: P07633
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.