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Protein

Propionyl-CoA carboxylase alpha chain, mitochondrial

Gene

Pcca

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

Functioni

Catalytic activityi

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

Cofactori

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei186ATPBy similarity1
Binding sitei270ATPBy similarity1
Binding sitei305ATPBy similarity1
Active sitei362By similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • biotin carboxylase activity Source: InterPro
  • metal ion binding Source: InterPro
  • 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, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8606.
BRENDAi6.4.1.3. 5301.
UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

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

Organism-specific databases

RGDi3264. Pcca.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Propionic acidemia due to recessively inherited deficiency of PCCase activity often causes life-threatening ketosis and acidosis.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 61MitochondrionBy similarityAdd BLAST61
ChainiPRO_000000283962 – 737Propionyl-CoA carboxylase alpha chain, mitochondrialAdd BLAST676

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74N6-acetyllysine; alternateBy similarity1
Modified residuei74N6-succinyllysine; alternateBy similarity1
Modified residuei128N6-succinyllysineBy similarity1
Modified residuei159N6-acetyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysine; alternateBy similarity1
Modified residuei163N6-acetyllysineBy similarity1
Modified residuei197N6-succinyllysineBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1
Modified residuei261PhosphoserineCombined sources1
Modified residuei271N6-succinyllysineBy similarity1
Modified residuei337N6-acetyllysine; alternateBy similarity1
Modified residuei337N6-succinyllysine; alternateBy similarity1
Modified residuei394N6-succinyllysineBy similarity1
Modified residuei416N6-succinyllysineBy similarity1
Modified residuei505N6-acetyllysineBy similarity1
Modified residuei511N6-succinyllysineBy similarity1
Modified residuei522N6-succinyllysineBy similarity1
Modified residuei567N6-succinyllysineBy similarity1
Modified residuei657N6-succinyllysineBy similarity1
Modified residuei703N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP14882.

PTM databases

iPTMnetiP14882.
PhosphoSitePlusiP14882.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP14882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 518Biotin carboxylationAdd BLAST448
Domaini190 – 387ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini658 – 737Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST80

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiP14882.
KOiK01965.
PhylomeDBiP14882.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. 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]

Sequencei

Sequence statusi: Complete.

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

P14882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLWVRTVA LLAARRHWRR SSQQLLWTLK RAPRSSQQLL WTLKRAPVYS
60 70 80 90 100
QQCLVVSRSL SSVEYEPKEK TFDKILIANR GEIACRVIKT CRKMGIRTVA
110 120 130 140 150
IHSDVDASSV HVKMADEAVC VGPAPTSKSY LNMDAIMEAI KKTGAQAVHP
160 170 180 190 200
GYGFLSENKE FAKCLAAEDV TFIGPDTHAI QAMGDKIESK LLAKRAKVNT
210 220 230 240 250
IPGFDGVLKD ADEAVRIARE IGYPVMIKAS AGGGGKGMRI PWDDEETRDG
260 270 280 290 300
FRFSSQEAAS SFGDDRLLIE KFIDNPRHIE IQVLGDKHGN ALWLNERECS
310 320 330 340 350
IQRRNQKVVE EAPSIFLDPE TRRAMGEQAV AWPKAVKYSS AGTVEFLVDS
360 370 380 390 400
QKNFYFLEMN TRLQVEHPVT ECITGLDLVQ EMILVAKGYP LRHKQEDIPI
410 420 430 440 450
SGWAVECRVY AEDPYKSFGL PSIGRLSQYQ EPIHLPGVRV DSGIQPGSDI
460 470 480 490 500
SIYHDPMISK LVTYGSDRAE ALKRMEDALD SYVIRGVTHN IPLLREVIIN
510 520 530 540 550
TRFVKGDIST KFLSDVYPDG FKGHMLTPSE RDQLLAIASS LFVASQLRAQ
560 570 580 590 600
RFQEHSRVPV IRPDVAKWEL SVKLHDEDHT VVASNNGPTF NVEVDGSKLN
610 620 630 640 650
VTSTWNLASP LLSVNVDGTQ RTVQCLSPDA GGNMSIQFLG TVYKVHILTK
660 670 680 690 700
LAAELNKFML EKVPKDTSSV LRSPKPGVVV AVSVKPGDMV AEGQEICVIE
710 720 730
AMKMQNSMTA GKMGKVKLVH CKAGDTVGEG DLLVELE
Length:737
Mass (Da):81,623
Last modified:November 30, 2010 - v3
Checksum:i58D13E5033A1D024
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CK228512 mRNA. No translation available.
M22631 mRNA. Translation: AAA88512.1. Sequence problems.
PIRiA34337.
RefSeqiNP_062203.1. NM_019330.1.
UniGeneiRn.6033.

Genome annotation databases

GeneIDi687008.
KEGGirno:687008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CK228512 mRNA. No translation available.
M22631 mRNA. Translation: AAA88512.1. Sequence problems.
PIRiA34337.
RefSeqiNP_062203.1. NM_019330.1.
UniGeneiRn.6033.

3D structure databases

ProteinModelPortaliP14882.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP14882.
PhosphoSitePlusiP14882.

Proteomic databases

PRIDEiP14882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi687008.
KEGGirno:687008.

Organism-specific databases

CTDi5095.
RGDi3264. Pcca.

Phylogenomic databases

HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiP14882.
KOiK01965.
PhylomeDBiP14882.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.
BioCyciMetaCyc:MONOMER-8606.
BRENDAi6.4.1.3. 5301.

Miscellaneous databases

PROiP14882.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPCCA_RAT
AccessioniPrimary (citable) accession number: P14882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 30, 2010
Last modified: November 2, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.