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P11154 (PYC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate carboxylase 1

EC=6.4.1.1
Alternative name(s):
Pyruvic carboxylase 1
Short name=PCB 1
Gene names
Name:PYC1
Synonyms:PYV
Ordered Locus Names:YGL062W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1178 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Biotin.

Zinc.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Miscellaneous

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

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-14358,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11781178Pyruvate carboxylase 1
PRO_0000146824

Regions

Domain18 – 470453Biotin carboxylation
Domain140 – 337198ATP-grasp
Domain557 – 824268Carboxyltransferase
Domain1101 – 116868Biotinyl-binding
Region565 – 5695Substrate binding By similarity

Sites

Active site3121 By similarity
Metal binding5661Divalent metal cation By similarity
Metal binding7341Divalent metal cation; via carbamate group By similarity
Metal binding7641Divalent metal cation By similarity
Metal binding7661Divalent metal cation By similarity
Binding site1361ATP By similarity
Binding site2201ATP By similarity
Binding site2551ATP By similarity
Binding site6381Substrate By similarity
Binding site8981Substrate By similarity

Amino acid modifications

Modified residue7341N6-carboxylysine By similarity
Modified residue11351N6-biotinyllysine

Experimental info

Sequence conflict4621T → G in AAA34843. Ref.1
Sequence conflict4931V → D in AAA34843. Ref.1
Sequence conflict5951R → A in AAA34843. Ref.1
Sequence conflict6191E → Q in AAA34843. Ref.1
Sequence conflict6641G → S in AAA34843. Ref.1
Sequence conflict7721A → R in AAA34843. Ref.1
Sequence conflict8791E → Q in AAA34843. Ref.1
Sequence conflict9091Q → K in AAA34843. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11154 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: BC7110A8AFB23E04

FASTA1,178130,099
        10         20         30         40         50         60 
MSQRKFAGLR DNFNLLGEKN KILVANRGEI PIRIFRTAHE LSMQTVAIYS HEDRLSTHKQ 

        70         80         90        100        110        120 
KADEAYVIGE VGQYTPVGAY LAIDEIISIA QKHQVDFIHP GYGFLSENSE FADKVVKAGI 

       130        140        150        160        170        180 
TWIGPPAEVI DSVGDKVSAR NLAAKANVPT VPGTPGPIET VEEALDFVNE YGYPVIIKAA 

       190        200        210        220        230        240 
FGGGGRGMRV VREGDDVADA FQRATSEART AFGNGTCFVE RFLDKPKHIE VQLLADNHGN 

       250        260        270        280        290        300 
VVHLFERDCS VQRRHQKVVE VAPAKTLPRE VRDAILTDAV KLAKECGYRN AGTAEFLVDN 

       310        320        330        340        350        360 
QNRHYFIEIN PRIQVEHTIT EEITGIDIVA AQIQIAAGAS LPQLGLFQDK ITTRGFAIQC 

       370        380        390        400        410        420 
RITTEDPAKN FQPDTGRIEV YRSAGGNGVR LDGGNAYAGT IISPHYDSML VKCSCSGSTY 

       430        440        450        460        470        480 
EIVRRKMIRA LIEFRIRGVK TNIPFLLTLL TNPVFIEGTY WTTFIDDTPQ LFQMVSSQNR 

       490        500        510        520        530        540 
AQKLLHYLAD VAVNGSSIKG QIGLPKLKSN PSVPHLHDAQ GNVINVTKSA PPSGWRQVLL 

       550        560        570        580        590        600 
EKGPAEFARQ VRQFNGTLLM DTTWRDAHQS LLATRVRTHD LATIAPTTAH ALAGRFALEC 

       610        620        630        640        650        660 
WGGATFDVAM RFLHEDPWER LRKLRSLVPN IPFQMLLRGA NGVAYSSLPD NAIDHFVKQA 

       670        680        690        700        710        720 
KDNGVDIFRV FDALNDLEQL KVGVDAVKKA GGVVEATVCF SGDMLQPGKK YNLDYYLEIA 

       730        740        750        760        770        780 
EKIVQMGTHI LGIKDMAGTM KPAAAKLLIG SLRAKYPDLP IHVHTHDSAG TAVASMTACA 

       790        800        810        820        830        840 
LAGADVVDVA INSMSGLTSQ PSINALLASL EGNIDTGINV EHVRELDAYW AEMRLLYSCF 

       850        860        870        880        890        900 
EADLKGPDPE VYQHEIPGGQ LTNLLFQAQQ LGLGEQWAET KRAYREANYL LGDIVKVTPT 

       910        920        930        940        950        960 
SKVVGDLAQF MVSNKLTSDD VRRLANSLDF PDSVMDFFEG LIGQPYGGFP EPFRSDVLRN 

       970        980        990       1000       1010       1020 
KRRKLTCRPG LELEPFDLEK IREDLQNRFG DVDECDVASY NMYPRVYEDF QKMRETYGDL 

      1030       1040       1050       1060       1070       1080 
SVLPTRSFLS PLETDEEIEV VIEQGKTLII KLQAVGDLNK KTGEREVYFD LNGEMRKIRV 

      1090       1100       1110       1120       1130       1140 
ADRSQKVETV TKSKADMHDP LHIGAPMAGV IVEVKVHKGS LIKKGQPVAV LSAMKMEMII 

      1150       1160       1170 
SSPSDGQVKE VFVSDGENVD SSDLLVLLED QVPVETKA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and domain structure of yeast pyruvate carboxylase."
Lim F., Morris C.P., Occhiodoro F., Wallace J.C.
J. Biol. Chem. 263:11493-11497(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Yeast pyruvate carboxylase: gene isolation."
Morris C.P., Lim F., Wallace J.C.
Biochem. Biophys. Res. Commun. 145:390-396(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1003-1178.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03889 Genomic DNA. Translation: AAA34843.1.
Z72584 Genomic DNA. Translation: CAA96765.1.
BK006941 Genomic DNA. Translation: DAA08040.1.
PIRQYBYP. S64066.
RefSeqNP_011453.1. NM_001180927.1.

3D structure databases

ProteinModelPortalP11154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33185. 31 interactions.
DIPDIP-6425N.
IntActP11154. 5 interactions.
MINTMINT-700616.
STRING4932.YGL062W.

Proteomic databases

MaxQBP11154.
PeptideAtlasP11154.
PRIDEP11154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL062W; YGL062W; YGL062W.
GeneID852818.
KEGGsce:YGL062W.

Organism-specific databases

CYGDYGL062w.
SGDS000003030. PYC1.

Phylogenomic databases

GeneTreeENSGT00550000074986.
HOGENOMHOG000282801.
KOK01958.
OMAYAIQSRV.
OrthoDBEOG7GQZ41.

Enzyme and pathway databases

BioCycYEAST:YGL062W-MONOMER.
BRENDA6.4.1.1. 984.
SABIO-RKP11154.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP11154.

Family and domain databases

Gene3D1.10.10.60. 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.
InterProIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
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]
PANTHERPTHR18866:SF10. PTHR18866:SF10. 1 hit.
PfamPF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFPIRSF001594. Pyruv_carbox. 1 hit.
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01235. pyruv_carbox. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Other

NextBio972360.
PROP11154.

Entry information

Entry namePYC1_YEAST
AccessionPrimary (citable) accession number: P11154
Secondary accession number(s): D6VU79
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways