Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P11154

- PYC1_YEAST

UniProt

P11154 - PYC1_YEAST

Protein

Pyruvate carboxylase 1

Gene

PYC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Biotin.
    Zinc.

    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. protein binding Source: IntAct
    6. pyruvate carboxylase activity Source: SGD

    GO - Biological processi

    1. gluconeogenesis Source: SGD

    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_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.
    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: Chromosome VII

    Organism-specific databases

    CYGDiYGL062w.
    SGDiS000003030. PYC1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD

    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-biotinyllysine1 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. 31 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
    Domaini1101 – 116868Biotinyl-bindingAdd
    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.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    GeneTreeiENSGT00550000074986.
    HOGENOMiHOG000282801.
    KOiK01958.
    OMAiYAIQSRV.
    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]
    PANTHERiPTHR18866:SF10. PTHR18866:SF10. 1 hit.
    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

    MSQRKFAGLR DNFNLLGEKN KILVANRGEI PIRIFRTAHE LSMQTVAIYS     50
    HEDRLSTHKQ KADEAYVIGE VGQYTPVGAY LAIDEIISIA QKHQVDFIHP 100
    GYGFLSENSE FADKVVKAGI TWIGPPAEVI DSVGDKVSAR NLAAKANVPT 150
    VPGTPGPIET VEEALDFVNE YGYPVIIKAA FGGGGRGMRV VREGDDVADA 200
    FQRATSEART AFGNGTCFVE RFLDKPKHIE VQLLADNHGN VVHLFERDCS 250
    VQRRHQKVVE VAPAKTLPRE VRDAILTDAV KLAKECGYRN AGTAEFLVDN 300
    QNRHYFIEIN PRIQVEHTIT EEITGIDIVA AQIQIAAGAS LPQLGLFQDK 350
    ITTRGFAIQC RITTEDPAKN FQPDTGRIEV YRSAGGNGVR LDGGNAYAGT 400
    IISPHYDSML VKCSCSGSTY EIVRRKMIRA LIEFRIRGVK TNIPFLLTLL 450
    TNPVFIEGTY WTTFIDDTPQ LFQMVSSQNR AQKLLHYLAD VAVNGSSIKG 500
    QIGLPKLKSN PSVPHLHDAQ GNVINVTKSA PPSGWRQVLL EKGPAEFARQ 550
    VRQFNGTLLM DTTWRDAHQS LLATRVRTHD LATIAPTTAH ALAGRFALEC 600
    WGGATFDVAM RFLHEDPWER LRKLRSLVPN IPFQMLLRGA NGVAYSSLPD 650
    NAIDHFVKQA KDNGVDIFRV FDALNDLEQL KVGVDAVKKA GGVVEATVCF 700
    SGDMLQPGKK YNLDYYLEIA EKIVQMGTHI LGIKDMAGTM KPAAAKLLIG 750
    SLRAKYPDLP IHVHTHDSAG TAVASMTACA LAGADVVDVA INSMSGLTSQ 800
    PSINALLASL EGNIDTGINV EHVRELDAYW AEMRLLYSCF EADLKGPDPE 850
    VYQHEIPGGQ LTNLLFQAQQ LGLGEQWAET KRAYREANYL LGDIVKVTPT 900
    SKVVGDLAQF MVSNKLTSDD VRRLANSLDF PDSVMDFFEG LIGQPYGGFP 950
    EPFRSDVLRN KRRKLTCRPG LELEPFDLEK IREDLQNRFG DVDECDVASY 1000
    NMYPRVYEDF QKMRETYGDL SVLPTRSFLS PLETDEEIEV VIEQGKTLII 1050
    KLQAVGDLNK KTGEREVYFD LNGEMRKIRV ADRSQKVETV TKSKADMHDP 1100
    LHIGAPMAGV IVEVKVHKGS LIKKGQPVAV LSAMKMEMII SSPSDGQVKE 1150
    VFVSDGENVD SSDLLVLLED QVPVETKA 1178
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03889 Genomic DNA. Translation: AAA34843.1 .
    Z72584 Genomic DNA. Translation: CAA96765.1 .
    BK006941 Genomic DNA. Translation: DAA08040.1 .
    PIRi S64066. QYBYP.
    RefSeqi NP_011453.1. NM_001180927.1.

    3D structure databases

    ProteinModelPortali P11154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33185. 31 interactions.
    DIPi DIP-6425N.
    IntActi P11154. 5 interactions.
    MINTi MINT-700616.
    STRINGi 4932.YGL062W.

    Proteomic databases

    MaxQBi P11154.
    PeptideAtlasi P11154.
    PRIDEi P11154.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL062W ; YGL062W ; YGL062W .
    GeneIDi 852818.
    KEGGi sce:YGL062W.

    Organism-specific databases

    CYGDi YGL062w.
    SGDi S000003030. PYC1.

    Phylogenomic databases

    GeneTreei ENSGT00550000074986.
    HOGENOMi HOG000282801.
    KOi K01958.
    OMAi YAIQSRV.
    OrthoDBi EOG7GQZ41.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci YEAST:YGL062W-MONOMER.
    BRENDAi 6.4.1.1. 984.
    Reactomei REACT_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.
    SABIO-RK P11154.

    Miscellaneous databases

    NextBioi 972360.
    PROi P11154.

    Gene expression databases

    Genevestigatori P11154.

    Family and domain databases

    Gene3Di 1.10.10.60. 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.
    InterProi IPR013785. 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 ]
    PANTHERi PTHR18866:SF10. PTHR18866:SF10. 1 hit.
    Pfami PF02785. 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 ]
    PIRSFi PIRSF001594. Pyruv_carbox. 1 hit.
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01235. pyruv_carbox. 1 hit.
    PROSITEi PS50975. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 151 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