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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361ATPBy similarity
Binding sitei220 – 2201ATPBy similarity
Binding sitei255 – 2551ATPBy similarity
Active sitei312 – 3121By similarity
Metal bindingi566 – 5661Divalent metal cationBy similarity
Binding sitei638 – 6381SubstrateBy similarity
Metal bindingi734 – 7341Divalent metal cation; via carbamate groupBy similarity
Metal bindingi764 – 7641Divalent metal cationBy similarity
Metal bindingi766 – 7661Divalent metal cationBy similarity
Binding sitei898 – 8981SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. biotin carboxylase activity Source: InterPro
  3. DNA binding Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. pyruvate carboxylase activity Source: SGD

GO - Biological processi

  1. gluconeogenesis Source: SGD
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.
ReactomeiREACT_284110. Biotin transport and metabolism.
REACT_286539. Gluconeogenesis.
REACT_290140. Defective HLCS causes multiple carboxylase deficiency.
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
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL062w.
EuPathDBiFungiDB:YGL062W.
SGDiS000003030. PYC1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11781178Pyruvate carboxylase 1PRO_0000146824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei734 – 7341N6-carboxylysineBy similarity
Modified residuei1135 – 11351N6-biotinyllysinePROSITE-ProRule annotation1 Publication

Proteomic databases

MaxQBiP11154.
PeptideAtlasiP11154.
PRIDEiP11154.

Expressioni

Gene expression databases

GenevestigatoriP11154.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi33185. 33 interactions.
DIPiDIP-6425N.
IntActiP11154. 5 interactions.
MINTiMINT-700616.
STRINGi4932.YGL062W.

Structurei

3D structure databases

ProteinModelPortaliP11154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 470453Biotin carboxylationAdd
BLAST
Domaini140 – 337198ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini557 – 824268CarboxyltransferaseAdd
BLAST
Domaini1094 – 116976Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni565 – 5695Substrate 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

Phylogenomic databases

GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP11154.
KOiK01958.
OMAiPIEAYLD.
OrthoDBiEOG7GQZ41.

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.
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]
PfamiPF02785. 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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti462 – 4621T → G in AAA34843 (PubMed:3042770).Curated
Sequence conflicti493 – 4931V → D in AAA34843 (PubMed:3042770).Curated
Sequence conflicti595 – 5951R → A in AAA34843 (PubMed:3042770).Curated
Sequence conflicti619 – 6191E → Q in AAA34843 (PubMed:3042770).Curated
Sequence conflicti664 – 6641G → S in AAA34843 (PubMed:3042770).Curated
Sequence conflicti772 – 7721A → R in AAA34843 (PubMed:3042770).Curated
Sequence conflicti879 – 8791E → Q in AAA34843 (PubMed:3042770).Curated
Sequence conflicti909 – 9091Q → K in AAA34843 (PubMed:3042770).Curated

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33185. 33 interactions.
DIPiDIP-6425N.
IntActiP11154. 5 interactions.
MINTiMINT-700616.
STRINGi4932.YGL062W.

Proteomic databases

MaxQBiP11154.
PeptideAtlasiP11154.
PRIDEiP11154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGL062w.
EuPathDBiFungiDB:YGL062W.
SGDiS000003030. PYC1.

Phylogenomic databases

GeneTreeiENSGT00550000074986.
HOGENOMiHOG000282801.
InParanoidiP11154.
KOiK01958.
OMAiPIEAYLD.
OrthoDBiEOG7GQZ41.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciYEAST:YGL062W-MONOMER.
BRENDAi6.4.1.1. 984.
ReactomeiREACT_284110. Biotin transport and metabolism.
REACT_286539. Gluconeogenesis.
REACT_290140. Defective HLCS causes multiple carboxylase deficiency.
SABIO-RKP11154.

Miscellaneous databases

NextBioi972360.
PROiP11154.

Gene expression databases

GenevestigatoriP11154.

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.
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]
PfamiPF02785. 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]
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...

Publicationsi

« Hide 'large scale' publications
  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, BIOTINYLATION AT LYS-1135.
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1003-1178.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

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: April 29, 2015
This is version 156 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

External Data

Dasty 3

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 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.