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Protein

Pyruvate carboxylase, mitochondrial

Gene

Pc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.

Miscellaneous

This enzyme performs an important anaplerotic function in replenishing citric acid cycle intermediates that exit the mitochondrion for consumption in various pathways.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarity
  • 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)DescriptionActionsGraphical viewLength
Binding sitei152ATPBy similarity1
Binding sitei236ATPBy similarity1
Binding sitei271ATPBy similarity1
Active sitei328By similarity1
Metal bindingi572ManganeseBy similarity1
Binding sitei644SubstrateBy similarity1
Metal bindingi741Manganese; via carbamate groupBy similarity1
Metal bindingi771ManganeseBy similarity1
Metal bindingi773ManganeseBy similarity1
Binding sitei908SubstrateBy similarity1

GO - Molecular functioni

  • ATP binding Source: RGD
  • biotin binding Source: RGD
  • carboxylic acid binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • pyruvate carboxylase activity Source: RGD

GO - Biological processi

  • gluconeogenesis Source: RGD
  • lipid metabolic process Source: UniProtKB-KW
  • oxaloacetate metabolic process Source: RGD
  • positive regulation of phospholipid biosynthetic process Source: CACAO
  • pyruvate metabolic process Source: RGD

Keywordsi

Molecular functionLigase, Multifunctional enzyme
Biological processGluconeogenesis, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding, Pyruvate

Enzyme and pathway databases

BRENDAi6.4.1.1 5301
ReactomeiR-RNO-196780 Biotin transport and metabolism
R-RNO-70263 Gluconeogenesis
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3262 Pc

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 20MitochondrionSequence analysisAdd BLAST20
ChainiPRO_000000284221 – 1178Pyruvate carboxylase, mitochondrialAdd BLAST1158

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35N6-acetyllysineBy similarity1
Modified residuei39N6-acetyllysineBy similarity1
Modified residuei79N6-acetyllysine; alternateBy similarity1
Modified residuei79N6-succinyllysine; alternateBy similarity1
Modified residuei148N6-acetyllysineBy similarity1
Modified residuei152N6-acetyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei297N6-acetyllysineBy similarity1
Modified residuei316N6-acetyllysineBy similarity1
Modified residuei319N6-acetyllysineBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei442N6-succinyllysineBy similarity1
Modified residuei589N6-acetyllysineBy similarity1
Modified residuei661N6-acetyllysineBy similarity1
Modified residuei717N6-acetyllysineBy similarity1
Modified residuei741N6-carboxylysineBy similarity1
Modified residuei748N6-acetyllysineBy similarity1
Modified residuei892N6-acetyllysineBy similarity1
Modified residuei969N6-acetyllysineBy similarity1
Modified residuei988N6-acetyllysine; alternateBy similarity1
Modified residuei988N6-succinyllysine; alternateBy similarity1
Modified residuei992N6-acetyllysineBy similarity1
Modified residuei1003PhosphothreonineCombined sources1
Modified residuei1061N6-acetyllysineBy similarity1
Modified residuei1090N6-acetyllysineBy similarity1
Modified residuei1124N6-acetyllysineBy similarity1
Modified residuei1144N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Post-translational modificationi

Acetylation of Lys-748 might play a role in catalytic activity regulation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP52873
PRIDEiP52873

2D gel databases

World-2DPAGE0004:P52873

PTM databases

CarbonylDBiP52873
iPTMnetiP52873
PhosphoSitePlusiP52873

Expressioni

Gene expression databases

BgeeiENSRNOG00000019372
ExpressionAtlasiP52873 baseline and differential
GenevisibleiP52873 RN

Interactioni

Subunit structurei

Homotetramer. Interacts (via the biotin carboxylation domain) with SIRT4.By similarity

Protein-protein interaction databases

BioGridi247176, 2 interactors
IntActiP52873, 1 interactor
MINTiP52873
STRINGi10116.ENSRNOP00000026316

Structurei

3D structure databases

ProteinModelPortaliP52873
SMRiP52873
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 486Biotin carboxylationAdd BLAST451
Domaini156 – 353ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini563 – 832Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST270
Domaini1109 – 1178Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni571 – 575Substrate bindingBy similarity5

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IU5D Eukaryota
COG1038 LUCA
GeneTreeiENSGT00900000141164
HOGENOMiHOG000282801
HOVERGENiHBG008340
InParanoidiP52873
KOiK01958
PhylomeDBiP52873
TreeFamiTF300535

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR011761 ATP-grasp
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
IPR016185 PreATP-grasp_dom_sf
IPR000891 PYR_CT
IPR005930 Pyruv_COase
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF02785 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
PIRSFiPIRSF001594 Pyruv_carbox, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
TIGRFAMsiTIGR01235 pyruv_carbox, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50991 PYR_CT, 1 hit

Sequencei

Sequence statusi: Complete.

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

P52873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKFQTVRGG LRLLGVRRSS TAPVASPNVR 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 NSPINSLHEA HEFSNTYGFP 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 FLAGIVDTQF IDENPELFQL RPAQNRAQKL
510 520 530 540 550
LHYLGHVMVN GPTTPIPVKV SPSPVDPIVP VVPIGPPPAG FRDILLREGP
560 570 580 590 600
EGFARAVRNH QGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFNN
610 620 630 640 650
LFSIENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG
660 670 680 690 700
YTNYPDNVVF KFCEVAKENG MDVFRIFDSL NYLPNMLLGM EAAGSAGGVV
710 720 730 740 750
EAAISYTGDV ADPSRTKYSL EYYMGLAEEL VRAGTHILCI KDMAGLLKPA
760 770 780 790 800
ACTMLVSSLR DRFPDLPLHI HTHDTSGSGV 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 IDVKVAAGAK VVKGQPLCVL SAMKMETVVT
1160 1170
SPMEGTIRKV HVTKDMTLEG DDLILEIE
Length:1,178
Mass (Da):129,777
Last modified:May 1, 2007 - v2
Checksum:i782CDFEF3380DB2D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21 – 22TA → SG AA sequence (PubMed:3178228).Curated2
Sequence conflicti26 – 27SP → PL AA sequence (PubMed:3178228).Curated2
Sequence conflicti30 – 31RR → LL AA sequence (PubMed:3178228).Curated2
Sequence conflicti35K → P AA sequence (PubMed:3178228).Curated1
Sequence conflicti222S → P in AAA96256 (PubMed:8522203).Curated1
Sequence conflicti866I → D in AAA96256 (PubMed:8522203).Curated1
Sequence conflicti977R → G in AAA96256 (PubMed:8522203).Curated1
Sequence conflicti1135Q → A AA sequence (PubMed:3178228).Curated1
Sequence conflicti1153M → T AA sequence (PubMed:3178228).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32314 mRNA Translation: AAA96256.1
U36585 mRNA Translation: AAC52668.1
BC085680 mRNA Translation: AAH85680.1
PIRiS68252 JC4391
RefSeqiNP_036876.2, NM_012744.2
XP_006230754.1, XM_006230692.3
XP_006230755.1, XM_006230693.2
XP_006230756.1, XM_006230694.3
UniGeneiRn.11094

Genome annotation databases

EnsembliENSRNOT00000026316; ENSRNOP00000026316; ENSRNOG00000019372
ENSRNOT00000082388; ENSRNOP00000075317; ENSRNOG00000019372
GeneIDi25104
KEGGirno:25104
UCSCiRGD:3262 rat

Similar proteinsi

Entry informationi

Entry nameiPYC_RAT
AccessioniPrimary (citable) accession number: P52873
Secondary accession number(s): Q5RKM0, Q64555
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: May 23, 2018
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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