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Protein

Pyruvate carboxylase, mitochondrial

Gene

Pc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Protein has several cofactor binding sites:
  • biotin
  • Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521ATPBy similarity
Binding sitei236 – 2361ATPBy similarity
Binding sitei271 – 2711ATPBy similarity
Active sitei328 – 3281By similarity
Metal bindingi572 – 5721ManganeseBy similarity
Binding sitei644 – 6441SubstrateBy similarity
Metal bindingi741 – 7411Manganese; via carbamate groupBy similarity
Metal bindingi771 – 7711ManganeseBy similarity
Metal bindingi773 – 7731ManganeseBy similarity
Binding sitei908 – 9081SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase, mitochondrial (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase
Short name:
PCB
Gene namesi
Name:Pc
Synonyms:Pcx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97520. Pcx.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionSequence analysisAdd
BLAST
Chaini21 – 11781158Pyruvate carboxylase, mitochondrialPRO_0000002841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei79 – 791N6-acetyllysine; alternateCombined sources
Modified residuei79 – 791N6-succinyllysine; alternateCombined sources
Modified residuei297 – 2971N6-acetyllysineCombined sources
Modified residuei316 – 3161N6-acetyllysineCombined sources
Modified residuei319 – 3191N6-acetyllysineCombined sources
Modified residuei434 – 4341N6-acetyllysineCombined sources
Modified residuei442 – 4421N6-succinyllysineCombined sources
Modified residuei661 – 6611N6-acetyllysineCombined sources
Modified residuei741 – 7411N6-carboxylysineBy similarity
Modified residuei748 – 7481N6-acetyllysineCombined sources
Modified residuei988 – 9881N6-acetyllysine; alternateCombined sources
Modified residuei988 – 9881N6-succinyllysine; alternateCombined sources
Modified residuei992 – 9921N6-acetyllysineCombined sources
Modified residuei1003 – 10031PhosphothreonineBy similarity
Modified residuei1061 – 10611N6-acetyllysineCombined sources
Modified residuei1090 – 10901N6-acetyllysineCombined sources
Modified residuei1124 – 11241N6-acetyllysineCombined sources
Modified residuei1144 – 11441N6-biotinyllysinePROSITE-ProRule annotationBy similarity

Post-translational modificationi

Acetylation of Lys-316 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ05920.
MaxQBiQ05920.
PaxDbiQ05920.
PRIDEiQ05920.

2D gel databases

REPRODUCTION-2DPAGEQ05920.
SWISS-2DPAGEQ05920.

PTM databases

iPTMnetiQ05920.
PhosphoSiteiQ05920.
SwissPalmiQ05920.

Expressioni

Tissue specificityi

Liver, kidney, adipose tissue, liver and brain.

Gene expression databases

CleanExiMM_PCX.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiQ05920. 8 interactions.
MINTiMINT-1841846.
STRINGi10090.ENSMUSP00000063825.

Structurei

3D structure databases

ProteinModelPortaliQ05920.
SMRiQ05920. Positions 494-1178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 486451Biotin carboxylationAdd
BLAST
Domaini156 – 353198ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini563 – 832270CarboxyltransferaseAdd
BLAST
Domaini1109 – 117870Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni571 – 5755Substrate bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IU5D. Eukaryota.
COG1038. LUCA.
HOVERGENiHBG008340.
InParanoidiQ05920.
PhylomeDBiQ05920.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. 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.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
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.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKFQTVRGG LRLLGVRRSS SAPVASPNVR RLEYKPIKKV MVANRGEIAI
60 70 80 90 100
RVFRACTELG IRTVAVYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP
110 120 130 140 150
DIIKVAKENG VDAVHPGYGF LSERADFAQA CQDAGVRFIG PSPEVVRKMG
160 170 180 190 200
DKVEARAIAI AAGVPVVPGT DSPISSLHEA HEFSNTFGFP IIFKAAYGGG
210 220 230 240 250
GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE KPRHIEVQIL
260 270 280 290 300
GDQYGNILHL YERDCSIQRR HQKVVEIAPA THLDPQLRSR LTSDSVKLAK
310 320 330 340 350
QVGYENAGTV EFLVDKHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH
360 370 380 390 400
VSEGRSLPDL GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG
410 420 430 440 450
EGMGIRLDNA SAFQGAVISP HYDSLLVKVI AHGKDHPTAA TKMSRALAEF
460 470 480 490 500
RVRGVKTNIP FLQNVLNNQQ FLAGTVDTQF IDENPELFQL RPAQNRAQKL
510 520 530 540 550
LHYLGHVMVN GPTTPIPVNV SPSPVDPAVP VVPIGPPPAG FRDILLREGP
560 570 580 590 600
EGFARAVRNH QGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFNK
610 620 630 640 650
LFSMENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG
660 670 680 690 700
YTNYPDNVVF KFCEVAKENG MDVFRVFDSL NYLPNMLLGM EAAGSAGGVV
710 720 730 740 750
EAAISYTGDV ADPSRTKYSL EYYMGLAEEL VRAGTHILCI KDMAGLLKPA
760 770 780 790 800
ACTMLVSSLR DRFPDLPLHI HTHDTSGAGV AAMLACAQAG ADVVDVAVDS
810 820 830 840 850
MSGMTSQPSM GALVACTKGT PLDTEVPLER VFDYSEYWEG ARGLYAAFDC
860 870 880 890 900
TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM
910 920 930 940 950
LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG
960 970 980 990 1000
YIGIPHGGFP EPFRSKVLKD LPRIEGRPGA SLPPLNLKEL EKDLIDRHGE
1010 1020 1030 1040 1050
EVTPEDVLSA AMYPDVFAQF KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV
1060 1070 1080 1090 1100
ELERGKTLHI KALAVSDLNR AGQRQVFFEL NGQLRSILVK DTQAMKEMHF
1110 1120 1130 1140 1150
HPKALKDVKG QIGAPMPGKV IDIKVAAGDK VAKGQPLCVL SAMKMETVVT
1160 1170
SPMEGTIRKV HVTKDMTLEG DDLILEIE
Length:1,178
Mass (Da):129,685
Last modified:February 1, 1994 - v1
Checksum:i14CEA0F9DA8B8127
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09192 mRNA. Translation: AAA39737.1.
BC055030 mRNA. Translation: AAH55030.1.
CCDSiCCDS29430.1.
PIRiA47255.
UniGeneiMm.1845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09192 mRNA. Translation: AAA39737.1.
BC055030 mRNA. Translation: AAH55030.1.
CCDSiCCDS29430.1.
PIRiA47255.
UniGeneiMm.1845.

3D structure databases

ProteinModelPortaliQ05920.
SMRiQ05920. Positions 494-1178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ05920. 8 interactions.
MINTiMINT-1841846.
STRINGi10090.ENSMUSP00000063825.

PTM databases

iPTMnetiQ05920.
PhosphoSiteiQ05920.
SwissPalmiQ05920.

2D gel databases

REPRODUCTION-2DPAGEQ05920.
SWISS-2DPAGEQ05920.

Proteomic databases

EPDiQ05920.
MaxQBiQ05920.
PaxDbiQ05920.
PRIDEiQ05920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:97520. Pcx.

Phylogenomic databases

eggNOGiENOG410IU5D. Eukaryota.
COG1038. LUCA.
HOVERGENiHBG008340.
InParanoidiQ05920.
PhylomeDBiQ05920.

Enzyme and pathway databases

UniPathwayiUPA00138.

Miscellaneous databases

PROiQ05920.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PCX.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. 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.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
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.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Adipose pyruvate carboxylase: amino acid sequence and domain structure deduced from cDNA sequencing."
    Zhang J., Xia W.L., Brew K., Ahmad F.
    Proc. Natl. Acad. Sci. U.S.A. 90:1766-1770(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipocyte.
  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: Liver.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: 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-79; LYS-442 AND LYS-988, 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-79; LYS-297; LYS-316; LYS-319; LYS-434; LYS-661; LYS-748; LYS-988; LYS-992; LYS-1061; LYS-1090 AND LYS-1124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPYC_MOUSE
AccessioniPrimary (citable) accession number: Q05920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 144 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, Multifunctional enzyme, 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.