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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731ATPBy similarity
Binding sitei257 – 2571ATPBy similarity
Binding sitei292 – 2921ATPBy similarity
Active sitei349 – 3491By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848MitochondrionBy similarityAdd
BLAST
Chaini49 – 724676Propionyl-CoA carboxylase alpha chain, mitochondrialPRO_0000002838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternateCombined sources
Modified residuei61 – 611N6-succinyllysine; alternateCombined sources
Modified residuei115 – 1151N6-succinyllysineCombined sources
Modified residuei146 – 1461N6-acetyllysine; alternateCombined sources
Modified residuei146 – 1461N6-succinyllysine; alternateCombined sources
Modified residuei150 – 1501N6-acetyllysineCombined sources
Modified residuei184 – 1841N6-succinyllysineCombined sources
Modified residuei196 – 1961N6-acetyllysine; alternateCombined sources
Modified residuei196 – 1961N6-succinyllysine; alternateCombined sources
Modified residuei248 – 2481PhosphoserineCombined sources
Modified residuei258 – 2581N6-succinyllysineCombined sources
Modified residuei324 – 3241N6-acetyllysine; alternateCombined sources
Modified residuei324 – 3241N6-succinyllysine; alternateCombined sources
Modified residuei381 – 3811N6-succinyllysineCombined sources
Modified residuei403 – 4031N6-succinyllysineCombined sources
Modified residuei492 – 4921N6-acetyllysineCombined sources
Modified residuei498 – 4981N6-succinyllysineCombined sources
Modified residuei509 – 5091N6-succinyllysineCombined sources
Modified residuei554 – 5541N6-succinyllysineCombined sources
Modified residuei644 – 6441N6-succinyllysineCombined sources
Modified residuei690 – 6901N6-biotinyllysinePROSITE-ProRule annotationBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ91ZA3.
MaxQBiQ91ZA3.
PaxDbiQ91ZA3.
PRIDEiQ91ZA3.

2D gel databases

REPRODUCTION-2DPAGEQ91ZA3.

PTM databases

iPTMnetiQ91ZA3.
PhosphoSiteiQ91ZA3.
SwissPalmiQ91ZA3.

Expressioni

Gene expression databases

BgeeiQ91ZA3.
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

IntActiQ91ZA3. 4 interactions.
MINTiMINT-1844797.
STRINGi10090.ENSMUSP00000038763.

Structurei

3D structure databases

ProteinModelPortaliQ91ZA3.
SMRiQ91ZA3. Positions 59-724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 505448Biotin carboxylationAdd
BLAST
Domaini177 – 374198ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini645 – 72480Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

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.
OMAiSSTWNLA.
OrthoDBiEOG7RZ5PH.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti497 – 4971T → A in AAL02364 (PubMed:11461925).Curated
Sequence conflicti542 – 5421H → R in AAH06915 (PubMed:15489334).Curated
Sequence conflicti555 – 5617WELSVKL → VGALGKV in AAL02364 (PubMed:11461925).Curated

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. Positions 59-724.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91ZA3. 4 interactions.
MINTiMINT-1844797.
STRINGi10090.ENSMUSP00000038763.

PTM databases

iPTMnetiQ91ZA3.
PhosphoSiteiQ91ZA3.
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.
OMAiSSTWNLA.
OrthoDBiEOG7RZ5PH.
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.
NextBioi364725.
PROiQ91ZA3.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZA3.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Fatal propionic acidemia in mice lacking propionyl-CoA carboxylase and its rescue by postnatal, liver-specific supplementation via a transgene."
    Miyazaki T., Ohura T., Kobayashi M., Shigematsu Y., Yamaguchi S., Suzuki Y., Hata I., Aoki Y., Yang X., Minjares C., Haruta I., Uto H., Ito Y., Muller U.
    J. Biol. Chem. 276:35995-35999(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Embryo and Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-115; LYS-146; LYS-184; LYS-196; LYS-258; LYS-324; LYS-381; LYS-403; LYS-498; LYS-509; LYS-554 AND LYS-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-146; LYS-150; LYS-196; LYS-324 AND LYS-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: May 11, 2016
This is version 119 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.