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

Pyruvate carboxylase 1

Gene

PYC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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 sitei136ATPBy similarity1
Binding sitei220ATPBy similarity1
Binding sitei255ATPBy similarity1
Active sitei312By similarity1
Metal bindingi566Divalent metal cationBy similarity1
Binding sitei638SubstrateBy similarity1
Metal bindingi734Divalent metal cation; via carbamate groupBy similarity1
Metal bindingi764Divalent metal cationBy similarity1
Metal bindingi766Divalent metal cationBy similarity1
Binding sitei898SubstrateBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • biotin binding Source: InterPro
  • biotin carboxylase activity Source: InterPro
  • DNA binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • pyruvate carboxylase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: SGD
  • pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Biotin, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YGL062W-MONOMER.
BRENDAi6.4.1.1. 984.
ReactomeiR-SCE-196780. Biotin transport and metabolism.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP11154.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase 1 (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase 1
Short name:
PCB 1
Gene namesi
Name:PYC1
Synonyms:PYV
Ordered Locus Names:YGL062W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL062W.
SGDiS000003030. PYC1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001468241 – 1178Pyruvate carboxylase 1Add BLAST1178

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei734N6-carboxylysineBy similarity1
Modified residuei1135N6-biotinyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

MaxQBiP11154.
PRIDEiP11154.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-14358,EBI-16219

Protein-protein interaction databases

BioGridi33185. 35 interactors.
DIPiDIP-6425N.
IntActiP11154. 5 interactors.
MINTiMINT-700616.

Structurei

3D structure databases

ProteinModelPortaliP11154.
SMRiP11154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 470Biotin carboxylationAdd BLAST453
Domaini140 – 337ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini557 – 824Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST268
Domaini1094 – 1169Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni565 – 569Substrate bindingBy similarity5

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 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP11154.
KOiK01958.
OMAiYYLDFVD.
OrthoDBiEOG092C0BFY.

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.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQRKFAGLR DNFNLLGEKN KILVANRGEI PIRIFRTAHE LSMQTVAIYS
60 70 80 90 100
HEDRLSTHKQ KADEAYVIGE VGQYTPVGAY LAIDEIISIA QKHQVDFIHP
110 120 130 140 150
GYGFLSENSE FADKVVKAGI TWIGPPAEVI DSVGDKVSAR NLAAKANVPT
160 170 180 190 200
VPGTPGPIET VEEALDFVNE YGYPVIIKAA FGGGGRGMRV VREGDDVADA
210 220 230 240 250
FQRATSEART AFGNGTCFVE RFLDKPKHIE VQLLADNHGN VVHLFERDCS
260 270 280 290 300
VQRRHQKVVE VAPAKTLPRE VRDAILTDAV KLAKECGYRN AGTAEFLVDN
310 320 330 340 350
QNRHYFIEIN PRIQVEHTIT EEITGIDIVA AQIQIAAGAS LPQLGLFQDK
360 370 380 390 400
ITTRGFAIQC RITTEDPAKN FQPDTGRIEV YRSAGGNGVR LDGGNAYAGT
410 420 430 440 450
IISPHYDSML VKCSCSGSTY EIVRRKMIRA LIEFRIRGVK TNIPFLLTLL
460 470 480 490 500
TNPVFIEGTY WTTFIDDTPQ LFQMVSSQNR AQKLLHYLAD VAVNGSSIKG
510 520 530 540 550
QIGLPKLKSN PSVPHLHDAQ GNVINVTKSA PPSGWRQVLL EKGPAEFARQ
560 570 580 590 600
VRQFNGTLLM DTTWRDAHQS LLATRVRTHD LATIAPTTAH ALAGRFALEC
610 620 630 640 650
WGGATFDVAM RFLHEDPWER LRKLRSLVPN IPFQMLLRGA NGVAYSSLPD
660 670 680 690 700
NAIDHFVKQA KDNGVDIFRV FDALNDLEQL KVGVDAVKKA GGVVEATVCF
710 720 730 740 750
SGDMLQPGKK YNLDYYLEIA EKIVQMGTHI LGIKDMAGTM KPAAAKLLIG
760 770 780 790 800
SLRAKYPDLP IHVHTHDSAG TAVASMTACA LAGADVVDVA INSMSGLTSQ
810 820 830 840 850
PSINALLASL EGNIDTGINV EHVRELDAYW AEMRLLYSCF EADLKGPDPE
860 870 880 890 900
VYQHEIPGGQ LTNLLFQAQQ LGLGEQWAET KRAYREANYL LGDIVKVTPT
910 920 930 940 950
SKVVGDLAQF MVSNKLTSDD VRRLANSLDF PDSVMDFFEG LIGQPYGGFP
960 970 980 990 1000
EPFRSDVLRN KRRKLTCRPG LELEPFDLEK IREDLQNRFG DVDECDVASY
1010 1020 1030 1040 1050
NMYPRVYEDF QKMRETYGDL SVLPTRSFLS PLETDEEIEV VIEQGKTLII
1060 1070 1080 1090 1100
KLQAVGDLNK KTGEREVYFD LNGEMRKIRV ADRSQKVETV TKSKADMHDP
1110 1120 1130 1140 1150
LHIGAPMAGV IVEVKVHKGS LIKKGQPVAV LSAMKMEMII SSPSDGQVKE
1160 1170
VFVSDGENVD SSDLLVLLED QVPVETKA
Length:1,178
Mass (Da):130,099
Last modified:October 1, 1996 - v2
Checksum:iBC7110A8AFB23E04
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti462T → G in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti493V → D in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti595R → A in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti619E → Q in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti664G → S in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti772A → R in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti879E → Q in AAA34843 (PubMed:3042770).Curated1
Sequence conflicti909Q → K in AAA34843 (PubMed:3042770).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03889 Genomic DNA. Translation: AAA34843.1.
Z72584 Genomic DNA. Translation: CAA96765.1.
BK006941 Genomic DNA. Translation: DAA08040.1.
PIRiS64066. QYBYP.
RefSeqiNP_011453.1. NM_001180927.1.

Genome annotation databases

EnsemblFungiiYGL062W; YGL062W; YGL062W.
GeneIDi852818.
KEGGisce:YGL062W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03889 Genomic DNA. Translation: AAA34843.1.
Z72584 Genomic DNA. Translation: CAA96765.1.
BK006941 Genomic DNA. Translation: DAA08040.1.
PIRiS64066. QYBYP.
RefSeqiNP_011453.1. NM_001180927.1.

3D structure databases

ProteinModelPortaliP11154.
SMRiP11154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33185. 35 interactors.
DIPiDIP-6425N.
IntActiP11154. 5 interactors.
MINTiMINT-700616.

Proteomic databases

MaxQBiP11154.
PRIDEiP11154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL062W; YGL062W; YGL062W.
GeneIDi852818.
KEGGisce:YGL062W.

Organism-specific databases

EuPathDBiFungiDB:YGL062W.
SGDiS000003030. PYC1.

Phylogenomic databases

GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP11154.
KOiK01958.
OMAiYYLDFVD.
OrthoDBiEOG092C0BFY.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciYEAST:YGL062W-MONOMER.
BRENDAi6.4.1.1. 984.
ReactomeiR-SCE-196780. Biotin transport and metabolism.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP11154.

Miscellaneous databases

PROiP11154.

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.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYC1_YEAST
AccessioniPrimary (citable) accession number: P11154
Secondary accession number(s): D6VU79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12500 molecules/cell in log phase SD medium.1 Publication

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.