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Q99UY8

- Q99UY8_STAAM

UniProt

Q99UY8 - Q99UY8_STAAM

Protein

Pyruvate carboxylase

Gene

pycA

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Biotin.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei119 – 1191ADPImported
    Binding sitei119 – 1191ATPImported
    Binding sitei161 – 1611ADPImported
    Binding sitei161 – 1611ATPImported
    Binding sitei166 – 1661ATP; via amide nitrogen
    Binding sitei211 – 2111ADPImported
    Binding sitei211 – 2111ATPImported
    Binding sitei278 – 2781ADPImported
    Binding sitei278 – 2781ATPImported
    Binding sitei290 – 2901ADPImported
    Binding sitei367 – 3671CoenzymeAImported
    Binding sitei541 – 5411PyruvateImported
    Metal bindingi542 – 5421ManganeseImported
    Binding sitei545 – 5451PyruvateImported
    Binding sitei614 – 6141PyruvateImported
    Metal bindingi712 – 7121ManganeseImported
    Binding sitei712 – 7121PyruvateImported
    Metal bindingi741 – 7411Manganese; via tele nitrogenImported
    Metal bindingi743 – 7431Manganese; via tele nitrogenImported
    Binding sitei876 – 8761PyruvateImported
    Binding sitei1024 – 10241CoenzymeAImported
    Binding sitei1049 – 10491CoenzymeAImported
    Binding sitei1053 – 10531CoenzymeAImported

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1684ADPImported
    Nucleotide bindingi165 – 1684ATPImported
    Nucleotide bindingi203 – 2064ADPImported
    Nucleotide bindingi203 – 2064ATPImported
    Nucleotide bindingi235 – 2384ADPImported
    Nucleotide bindingi235 – 2384ATPImported
    Nucleotide bindingi290 – 2923ATPImported

    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: UniProtKB-EC

    GO - Biological processi

    1. gluconeogenesis Source: InterPro

    Keywords - Molecular functioni

    LigaseUniRule annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationImported, BiotinUniRule annotation, ManganeseImported, Metal-bindingImported, Nucleotide-binding, PyruvateImported

    Enzyme and pathway databases

    BioCyciSAUR158878:GJJ5-1133-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate carboxylaseUniRule annotation (EC:6.4.1.1UniRule annotation)
    Gene namesi
    Name:pycAImported
    Ordered Locus Names:SAV1114Imported
    OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)Imported
    Taxonomic identifieri158878 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002481: Chromosome

    PTM / Processingi

    Proteomic databases

    PRIDEiQ99UY8.

    2D gel databases

    World-2DPAGE0002:Q99UY8.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-46373N.
    STRINGi158878.SAV1114.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BG5X-ray2.80A/B/C/D1-1150[»]
    3HB9X-ray2.90A/B/C/D1-1150[»]
    3HBLX-ray2.71A/B/C/D1-1150[»]
    3HO8X-ray2.90A/B/C/D1-1150[»]
    4HNTX-ray2.80A/B/C/D1-1150[»]
    4HNUX-ray3.00A/B/C/D1-1150[»]
    4HNVX-ray2.80A/B/C/D1-1150[»]
    ProteinModelPortaliQ99UY8.
    SMRiQ99UY8. Positions 3-1146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99UY8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 507CoenzymeA bindingImported
    Regioni420 – 4223CoenzymeA bindingImported
    Regioni462 – 4654CoenzymeA bindingImported

    Phylogenomic databases

    eggNOGiCOG1038.
    KOiK01958.
    OMAiYAIQSRV.
    OrthoDBiEOG6CVV6Z.
    PhylomeDBiQ99UY8.

    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.
    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.
    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.

    Q99UY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQIKKLLVA NRGEIAIRIF RAAAELDIST VAIYSNEDKS SLHRYKADES     50
    YLVGSDLGPA ESYLNIERII DVAKQANVDA IHPGYGFLSE NEQFARRCAE 100
    EGIKFIGPHL EHLDMFGDKV KARTTAIKAD LPVIPGTDGP IKSYELAKEF 150
    AEEAGFPLMI KATSGGGGKG MRIVREESEL EDAFHRAKSE AEKSFGNSEV 200
    YIERYIDNPK HIEVQVIGDE HGNIVHLFER DCSVQRRHQK VVEVAPSVGL 250
    SPTLRQRICD AAIQLMENIK YVNAGTVEFL VSGDEFFFIE VNPRVQVEHT 300
    ITEMVTGIDI VKTQILVAAG ADLFGEEINM PQQKDITTLG YAIQCRITTE 350
    DPLNDFMPDT GTIIAYRSSG GFGVRLDAGD GFQGAEISPY YDSLLVKLST 400
    HAISFKQAEE KMVRSLREMR IRGVKTNIPF LINVMKNKKF TSGDYTTKFI 450
    EETPELFDIQ PSLDRGTKTL EYIGNVTING FPNVEKRPKP DYELASIPTV 500
    SSSKIASFSG TKQLLDEVGP KGVAEWVKKQ DDVLLTDTTF RDAHQSLLAT 550
    RVRTKDMINI ASKTADVFKD GFSLEMWGGA TFDVAYNFLK ENPWERLERL 600
    RKAIPNVLFQ MLLRASNAVG YKNYPDNVIH KFVQESAKAG IDVFRIFDSL 650
    NWVDQMKVAN EAVQEAGKIS EGTICYTGDI LNPERSNIYT LEYYVKLAKE 700
    LEREGFHILA IKDMAGLLKP KAAYELIGEL KSAVDLPIHL HTHDTSGNGL 750
    LTYKQAIDAG VDIIDTAVAS MSGLTSQPSA NSLYYALNGF PRHLRTDIEG 800
    MESLSHYWST VRTYYSDFES DIKSPNTEIY QHEMPGGQYS NLSQQAKSLG 850
    LGERFDEVKD MYRRVNFLFG DIVKVTPSSK VVGDMALYMV QNDLDEQSVI 900
    TDGYKLDFPE SVVSFFKGEI GQPVNGFNKD LQAVILKGQE ALTARPGEYL 950
    EPVDFEKVRE LLEEEQQGPV TEQDIISYVL YPKVYEQYIQ TRNQYGNLSL 1000
    LDTPTFFFGM RNGETVEIEI DKGKRLIIKL ETISEPDENG NRTIYYAMNG 1050
    QARRIYIKDE NVHTNANVKP KADKSNPSHI GAQMPGSVTE VKVSVGETVK 1100
    ANQPLLITEA MKMETTIQAP FDGVIKQVTV NNGDTIATGD LLIEIEKATD 1150
    Length:1,150
    Mass (Da):128,558
    Last modified:June 1, 2001 - v1
    Checksum:i2C8B9B7C1E7E3E48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57276.1.
    PIRiG89881.
    RefSeqiNP_371638.1. NC_002758.2.

    Genome annotation databases

    EnsemblBacteriaiBAB57276; BAB57276; SAV1114.
    GeneIDi1121091.
    KEGGisav:SAV1114.
    PATRICi19562927. VBIStaAur52173_1142.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57276.1 .
    PIRi G89881.
    RefSeqi NP_371638.1. NC_002758.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BG5 X-ray 2.80 A/B/C/D 1-1150 [» ]
    3HB9 X-ray 2.90 A/B/C/D 1-1150 [» ]
    3HBL X-ray 2.71 A/B/C/D 1-1150 [» ]
    3HO8 X-ray 2.90 A/B/C/D 1-1150 [» ]
    4HNT X-ray 2.80 A/B/C/D 1-1150 [» ]
    4HNU X-ray 3.00 A/B/C/D 1-1150 [» ]
    4HNV X-ray 2.80 A/B/C/D 1-1150 [» ]
    ProteinModelPortali Q99UY8.
    SMRi Q99UY8. Positions 3-1146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46373N.
    STRINGi 158878.SAV1114.

    2D gel databases

    World-2DPAGE 0002:Q99UY8.

    Proteomic databases

    PRIDEi Q99UY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB57276 ; BAB57276 ; SAV1114 .
    GeneIDi 1121091.
    KEGGi sav:SAV1114.
    PATRICi 19562927. VBIStaAur52173_1142.

    Phylogenomic databases

    eggNOGi COG1038.
    KOi K01958.
    OMAi YAIQSRV.
    OrthoDBi EOG6CVV6Z.
    PhylomeDBi Q99UY8.

    Enzyme and pathway databases

    BioCyci SAUR158878:GJJ5-1133-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q99UY8.

    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.
    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.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mu50 / ATCC 700699Imported.
    2. "Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction."
      Xiang S., Tong L.
      Nat. Struct. Mol. Biol. 15:295-302(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP; MANGANESE AND PYRUVATE.
    3. "A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A."
      Yu L.P., Xiang S., Lasso G., Gil D., Valle M., Tong L.
      Structure 17:823-832(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH ADP; COENZYMEA AND MANGANESE.
    4. "Characterizing the importance of the biotin carboxylase domain dimer for Staphylococcus aureus pyruvate carboxylase catalysis."
      Yu L.P., Chou C.Y., Choi P.H., Tong L.
      Biochemistry 52:488-496(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ADP; ATP AND MANGANESE.

    Entry informationi

    Entry nameiQ99UY8_STAAM
    AccessioniPrimary (citable) accession number: Q99UY8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 1, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteomeImported

    External Data

    Dasty 3