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Protein

Pyruvate carboxylase, mitochondrial

Gene

Pc

Organism
Rattus norvegicus (Rat)
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:
  • 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)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

  • ATP binding Source: RGD
  • biotin binding Source: RGD
  • biotin carboxylase activity Source: InterPro
  • carboxylic acid binding Source: RGD
  • DNA binding Source: InterPro
  • 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
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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3262. Pc.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
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_0000002842Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP52873.
PRIDEiP52873.

2D gel databases

World-2DPAGE0004:P52873.

PTM databases

iPTMnetiP52873.
PhosphoSiteiP52873.

Expressioni

Gene expression databases

ExpressionAtlasiP52873. baseline and differential.
GenevisibleiP52873. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi247176. 1 interaction.
IntActiP52873. 1 interaction.
MINTiMINT-4592965.
STRINGi10116.ENSRNOP00000026316.

Structurei

3D structure databases

ProteinModelPortaliP52873.
SMRiP52873. Positions 35-490, 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.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
HOVERGENiHBG008340.
InParanoidiP52873.
KOiK01958.
OMAiYAIQSRV.
OrthoDBiEOG7WT40F.
PhylomeDBiP52873.
TreeFamiTF300535.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 222TA → SG AA sequence (PubMed:3178228).Curated
Sequence conflicti26 – 272SP → PL AA sequence (PubMed:3178228).Curated
Sequence conflicti30 – 312RR → LL AA sequence (PubMed:3178228).Curated
Sequence conflicti35 – 351K → P AA sequence (PubMed:3178228).Curated
Sequence conflicti222 – 2221S → P in AAA96256 (PubMed:8522203).Curated
Sequence conflicti866 – 8661I → D in AAA96256 (PubMed:8522203).Curated
Sequence conflicti977 – 9771R → G in AAA96256 (PubMed:8522203).Curated
Sequence conflicti1135 – 11351Q → A AA sequence (PubMed:3178228).Curated
Sequence conflicti1153 – 11531M → T AA sequence (PubMed:3178228).Curated

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_006230753.1. XM_006230691.2.
XP_006230754.1. XM_006230692.2.
XP_006230755.1. XM_006230693.2.
XP_006230756.1. XM_006230694.2.
XP_008758309.1. XM_008760087.1.
UniGeneiRn.11094.

Genome annotation databases

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

Cross-referencesi

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_006230753.1. XM_006230691.2.
XP_006230754.1. XM_006230692.2.
XP_006230755.1. XM_006230693.2.
XP_006230756.1. XM_006230694.2.
XP_008758309.1. XM_008760087.1.
UniGeneiRn.11094.

3D structure databases

ProteinModelPortaliP52873.
SMRiP52873. Positions 35-490, 494-1178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247176. 1 interaction.
IntActiP52873. 1 interaction.
MINTiMINT-4592965.
STRINGi10116.ENSRNOP00000026316.

PTM databases

iPTMnetiP52873.
PhosphoSiteiP52873.

2D gel databases

World-2DPAGE0004:P52873.

Proteomic databases

PaxDbiP52873.
PRIDEiP52873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5091.
RGDi3262. Pc.

Phylogenomic databases

eggNOGiENOG410IU5D. Eukaryota.
COG1038. LUCA.
GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
HOVERGENiHBG008340.
InParanoidiP52873.
KOiK01958.
OMAiYAIQSRV.
OrthoDBiEOG7WT40F.
PhylomeDBiP52873.
TreeFamiTF300535.

Enzyme and pathway databases

UniPathwayiUPA00138.
BRENDAi6.4.1.1. 5301.
ReactomeiR-RNO-196780. Biotin transport and metabolism.
R-RNO-70263. Gluconeogenesis.

Miscellaneous databases

PROiP52873.

Gene expression databases

ExpressionAtlasiP52873. baseline and differential.
GenevisibleiP52873. RN.

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. "The sequence of the rat pyruvate carboxylase-encoding cDNA."
    Lehn D.A., Moran S.M., Macdonald M.J.
    Gene 165:331-332(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Cloning, sequencing and expression of rat liver pyruvate carboxylase."
    Jitrapakdee S., Booker G.W., Cassady A.I., Wallace J.C.
    Biochem. J. 316:631-637(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  3. "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].
    Tissue: Kidney.
  4. "A rapid purification method for rat liver pyruvate carboxylase and amino acid sequence analyses of NH2-terminal and biotin peptide."
    Thampy K.G., Huang W.Y., Wakil S.J.
    Arch. Biochem. Biophys. 266:270-276(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-35; 1134-1137 AND 1139-1158.
    Tissue: Liver.
  5. Lubec G., Afjehi-Sadat L.
    Submitted (DEC-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 244-263; 329-355; 407-428 AND 943-964, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYC_RAT
AccessioniPrimary (citable) accession number: P52873
Secondary accession number(s): Q5RKM0, Q64555
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: June 8, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, 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.