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 alpha chain, mitochondrial

Gene

Pcca

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei173ATPBy similarity1
Binding sitei257ATPBy similarity1
Binding sitei292ATPBy similarity1
Active sitei349By similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • biotin carboxylase activity Source: InterPro
  • enzyme binding Source: MGI
  • metal ion binding Source: InterPro
  • propionyl-CoA carboxylase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-71032. Propionyl-CoA catabolism.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:97499. Pcca.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
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 – 48MitochondrionBy similarityAdd BLAST48
ChainiPRO_000000283849 – 724Propionyl-CoA carboxylase alpha chain, mitochondrialAdd BLAST676

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61N6-acetyllysine; alternateCombined sources1
Modified residuei61N6-succinyllysine; alternateCombined sources1
Modified residuei115N6-succinyllysineCombined sources1
Modified residuei146N6-acetyllysine; alternateCombined sources1
Modified residuei146N6-succinyllysine; alternateCombined sources1
Modified residuei150N6-acetyllysineCombined sources1
Modified residuei184N6-succinyllysineCombined sources1
Modified residuei196N6-acetyllysine; alternateCombined sources1
Modified residuei196N6-succinyllysine; alternateCombined sources1
Modified residuei248PhosphoserineCombined sources1
Modified residuei258N6-succinyllysineCombined sources1
Modified residuei324N6-acetyllysine; alternateCombined sources1
Modified residuei324N6-succinyllysine; alternateCombined sources1
Modified residuei381N6-succinyllysineCombined sources1
Modified residuei403N6-succinyllysineCombined sources1
Modified residuei492N6-acetyllysineCombined sources1
Modified residuei498N6-succinyllysineCombined sources1
Modified residuei509N6-succinyllysineCombined sources1
Modified residuei554N6-succinyllysineCombined sources1
Modified residuei644N6-succinyllysineCombined sources1
Modified residuei690N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ91ZA3.
MaxQBiQ91ZA3.
PaxDbiQ91ZA3.
PRIDEiQ91ZA3.

2D gel databases

REPRODUCTION-2DPAGEQ91ZA3.

PTM databases

iPTMnetiQ91ZA3.
PhosphoSitePlusiQ91ZA3.
SwissPalmiQ91ZA3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000041650.
ExpressionAtlasiQ91ZA3. baseline and differential.
GenevisibleiQ91ZA3. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi225934. 1 interactor.
IntActiQ91ZA3. 4 interactors.
MINTiMINT-1844797.
STRINGi10090.ENSMUSP00000038763.

Structurei

3D structure databases

ProteinModelPortaliQ91ZA3.
SMRiQ91ZA3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 505Biotin carboxylationAdd BLAST448
Domaini177 – 374ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini645 – 724Biotinyl-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

eggNOGiKOG0238. Eukaryota.
COG4770. LUCA.
GeneTreeiENSGT00550000074675.
HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiQ91ZA3.
KOiK01965.
OMAiRAQHFQD.
OrthoDBiEOG091G06RG.
PhylomeDBiQ91ZA3.
TreeFamiTF354220.

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.

Q91ZA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGQWVRTVA LLAARRHWRR SSQQQLLGTL KHAPVYSYQC LVVSRSLSSV
60 70 80 90 100
EYEPKEKTFD KILIANRGEI ACRVIKTCKK MGIKTVAIHS DVDASSVHVK
110 120 130 140 150
MADEAVCVGP APTSKSYLNM DAIMEAIKKT RAQAVHPGYG FLSENKEFAK
160 170 180 190 200
RLAAEDVTFI GPDTHAIQAM GDKIESKLLA KRAKVNTIPG FDGVVKDADE
210 220 230 240 250
AVRIAREIGY PVMIKASAGG GGKGMRIAWD DEETRDGFRF SSQEAASSFG
260 270 280 290 300
DDRLLIEKFI DNPRHIEIQV LGDKHGNALW LNERECSIQR RNQKVVEEAP
310 320 330 340 350
SIFLDPETRQ AMGEQAVALA KAVKYSSAGT VEFLVDSQKN FYFLEMNTRL
360 370 380 390 400
QVEHPVTECI TGLDLVQEMI LVAKGYPLRH KQEDIPISGW AVECRVYAED
410 420 430 440 450
PYKSFGLPSI GRLSQYQEPI HLPGVRVDSG IQPGSDISIY YDPMISKLVT
460 470 480 490 500
YGSDRAEALK RMEDALDNYV IRGVTHNIPL LREVIINTRF VKGDISTKFL
510 520 530 540 550
SDVYPDGFKG HTLTLSERNQ LLAIASSVFV ASQLRAQRFQ EHSRVPVIRP
560 570 580 590 600
DVAKWELSVK LHDEDHTVVA SNNGPAFTVE VDGSKLNVTS TWNLASPLLS
610 620 630 640 650
VNVDGTQRTV QCLSREAGGN MSIQFLGTVY KVHILTKLAA ELNKFMLEKV
660 670 680 690 700
PKDTSSTLCS PMPGVVVAVS VKPGDMVAEG QEICVIEAMK MQNSMTAGKM
710 720
GKVKLVHCKA GDTVGEGDLL VELE
Length:724
Mass (Da):79,922
Last modified:May 24, 2005 - v2
Checksum:i249189EDF9F99274
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti497T → A in AAL02364 (PubMed:11461925).Curated1
Sequence conflicti542H → R in AAH06915 (PubMed:15489334).Curated1
Sequence conflicti555 – 561WELSVKL → VGALGKV in AAL02364 (PubMed:11461925).Curated7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046947 mRNA. Translation: AAL02364.1.
BC006915 mRNA. Translation: AAH06915.1.
BC049802 mRNA. Translation: AAH49802.1.
CCDSiCCDS27350.1.
RefSeqiNP_659093.2. NM_144844.2.
UniGeneiMm.23876.

Genome annotation databases

EnsembliENSMUST00000038374; ENSMUSP00000038763; ENSMUSG00000041650.
GeneIDi110821.
KEGGimmu:110821.
UCSCiuc007vbe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046947 mRNA. Translation: AAL02364.1.
BC006915 mRNA. Translation: AAH06915.1.
BC049802 mRNA. Translation: AAH49802.1.
CCDSiCCDS27350.1.
RefSeqiNP_659093.2. NM_144844.2.
UniGeneiMm.23876.

3D structure databases

ProteinModelPortaliQ91ZA3.
SMRiQ91ZA3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225934. 1 interactor.
IntActiQ91ZA3. 4 interactors.
MINTiMINT-1844797.
STRINGi10090.ENSMUSP00000038763.

PTM databases

iPTMnetiQ91ZA3.
PhosphoSitePlusiQ91ZA3.
SwissPalmiQ91ZA3.

2D gel databases

REPRODUCTION-2DPAGEQ91ZA3.

Proteomic databases

EPDiQ91ZA3.
MaxQBiQ91ZA3.
PaxDbiQ91ZA3.
PRIDEiQ91ZA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038374; ENSMUSP00000038763; ENSMUSG00000041650.
GeneIDi110821.
KEGGimmu:110821.
UCSCiuc007vbe.2. mouse.

Organism-specific databases

CTDi5095.
MGIiMGI:97499. Pcca.

Phylogenomic databases

eggNOGiKOG0238. Eukaryota.
COG4770. LUCA.
GeneTreeiENSGT00550000074675.
HOGENOMiHOG000008989.
HOVERGENiHBG000555.
InParanoidiQ91ZA3.
KOiK01965.
OMAiRAQHFQD.
OrthoDBiEOG091G06RG.
PhylomeDBiQ91ZA3.
TreeFamiTF354220.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.
ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-71032. Propionyl-CoA catabolism.

Miscellaneous databases

ChiTaRSiPcca. mouse.
PROiQ91ZA3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000041650.
ExpressionAtlasiQ91ZA3. baseline and differential.
GenevisibleiQ91ZA3. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q91ZA3
Secondary accession number(s): Q80VU5, Q922N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 24, 2005
Last modified: November 2, 2016
This is version 123 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.