SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99UY8

- Q99UY8_STAAM

UniProt

Q99UY8 - Q99UY8_STAAM

(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)

Protein
Pyruvate carboxylase
Gene
pycA, SAV1114
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Unreviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Biotin By similarity.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 – 3671Coenzyme AImported
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 – 10241Coenzyme AImported
Binding sitei1049 – 10491Coenzyme AImported
Binding sitei1053 – 10531Coenzyme AImported

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. DNA binding Source: InterPro
  3. biotin carboxylase activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. pyruvate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. gluconeogenesis Source: InterPro
Complete GO annotation...

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.

Miscellaneous databases

EvolutionaryTraceiQ99UY8.

Family & Domainsi

Region

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  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; COENZYME A 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: June 11, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

Similar proteinsi