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Q99UY8 (Q99UY8_STAAM) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 91. Feed History...

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

Names and origin

Protein attributes

Sequence length1150 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. PIRNR PIRNR001594

Catalytic activity

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate. PIRNR PIRNR001594

Cofactor

Biotin By similarity. PIRNR PIRNR001594

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding165 – 1684ADP PDB 3HB9 PDB 3HBL
Nucleotide binding165 – 1684ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Nucleotide binding203 – 2064ADP PDB 3HB9 PDB 3HBL PDB 4HNT PDB 4HNU PDB 4HNV
Nucleotide binding203 – 2064ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Nucleotide binding235 – 2384ADP PDB 3HB9 PDB 3HBL PDB 4HNT PDB 4HNU PDB 4HNV
Nucleotide binding235 – 2384ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Nucleotide binding290 – 2923ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Region44 – 507Coenzyme A binding PDB 3HO8
Region420 – 4223Coenzyme A binding PDB 3HO8
Region462 – 4654Coenzyme A binding PDB 3HO8

Sites

Metal binding5421Manganese PDB 3HO8 PDB 3HB9 PDB 3HBL PDB 3BG5 PDB 4HNT PDB 4HNU PDB 4HNV
Metal binding7121Manganese PDB 3HO8 PDB 3HB9 PDB 3HBL PDB 3BG5 PDB 4HNT PDB 4HNU PDB 4HNV
Metal binding7411Manganese; via tele nitrogen PDB 3HO8 PDB 3HB9 PDB 3HBL PDB 3BG5 PDB 4HNT PDB 4HNU PDB 4HNV
Metal binding7431Manganese; via tele nitrogen PDB 3HO8 PDB 3HB9 PDB 3HBL PDB 3BG5 PDB 4HNT PDB 4HNU PDB 4HNV
Binding site1191ADP PDB 3HB9 PDB 3HBL PDB 4HNV
Binding site1191ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Binding site1611ADP PDB 3HB9 PDB 4HNT PDB 4HNV
Binding site1611ATP PDB 3BG5
Binding site1661ATP; via amide nitrogen
Binding site2111ADP PDB 3HB9 PDB 3HBL PDB 4HNT PDB 4HNU PDB 4HNV
Binding site2111ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Binding site2781ADP PDB 3HB9 PDB 3HBL
Binding site2781ATP PDB 3BG5 PDB 4HNT PDB 4HNV
Binding site2901ADP PDB 3HB9 PDB 3HBL PDB 4HNT PDB 4HNU PDB 4HNV
Binding site3671Coenzyme A PDB 3HO8
Binding site5411Pyruvate PDB 3BG5
Binding site5451Pyruvate PDB 3BG5
Binding site6141Pyruvate PDB 3BG5
Binding site7121Pyruvate PDB 3BG5
Binding site8761Pyruvate PDB 3BG5
Binding site10241Coenzyme A PDB 3HO8
Binding site10491Coenzyme A PDB 3HO8
Binding site10531Coenzyme A PDB 3HO8

Sequences

Sequence LengthMass (Da)Tools
Q99UY8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2C8B9B7C1E7E3E48

FASTA1,150128,558
        10         20         30         40         50         60 
MKQIKKLLVA NRGEIAIRIF RAAAELDIST VAIYSNEDKS SLHRYKADES YLVGSDLGPA 

        70         80         90        100        110        120 
ESYLNIERII DVAKQANVDA IHPGYGFLSE NEQFARRCAE EGIKFIGPHL EHLDMFGDKV 

       130        140        150        160        170        180 
KARTTAIKAD LPVIPGTDGP IKSYELAKEF AEEAGFPLMI KATSGGGGKG MRIVREESEL 

       190        200        210        220        230        240 
EDAFHRAKSE AEKSFGNSEV YIERYIDNPK HIEVQVIGDE HGNIVHLFER DCSVQRRHQK 

       250        260        270        280        290        300 
VVEVAPSVGL SPTLRQRICD AAIQLMENIK YVNAGTVEFL VSGDEFFFIE VNPRVQVEHT 

       310        320        330        340        350        360 
ITEMVTGIDI VKTQILVAAG ADLFGEEINM PQQKDITTLG YAIQCRITTE DPLNDFMPDT 

       370        380        390        400        410        420 
GTIIAYRSSG GFGVRLDAGD GFQGAEISPY YDSLLVKLST HAISFKQAEE KMVRSLREMR 

       430        440        450        460        470        480 
IRGVKTNIPF LINVMKNKKF TSGDYTTKFI EETPELFDIQ PSLDRGTKTL EYIGNVTING 

       490        500        510        520        530        540 
FPNVEKRPKP DYELASIPTV SSSKIASFSG TKQLLDEVGP KGVAEWVKKQ DDVLLTDTTF 

       550        560        570        580        590        600 
RDAHQSLLAT RVRTKDMINI ASKTADVFKD GFSLEMWGGA TFDVAYNFLK ENPWERLERL 

       610        620        630        640        650        660 
RKAIPNVLFQ MLLRASNAVG YKNYPDNVIH KFVQESAKAG IDVFRIFDSL NWVDQMKVAN 

       670        680        690        700        710        720 
EAVQEAGKIS EGTICYTGDI LNPERSNIYT LEYYVKLAKE LEREGFHILA IKDMAGLLKP 

       730        740        750        760        770        780 
KAAYELIGEL KSAVDLPIHL HTHDTSGNGL LTYKQAIDAG VDIIDTAVAS MSGLTSQPSA 

       790        800        810        820        830        840 
NSLYYALNGF PRHLRTDIEG MESLSHYWST VRTYYSDFES DIKSPNTEIY QHEMPGGQYS 

       850        860        870        880        890        900 
NLSQQAKSLG LGERFDEVKD MYRRVNFLFG DIVKVTPSSK VVGDMALYMV QNDLDEQSVI 

       910        920        930        940        950        960 
TDGYKLDFPE SVVSFFKGEI GQPVNGFNKD LQAVILKGQE ALTARPGEYL EPVDFEKVRE 

       970        980        990       1000       1010       1020 
LLEEEQQGPV TEQDIISYVL YPKVYEQYIQ TRNQYGNLSL LDTPTFFFGM RNGETVEIEI 

      1030       1040       1050       1060       1070       1080 
DKGKRLIIKL ETISEPDENG NRTIYYAMNG QARRIYIKDE NVHTNANVKP KADKSNPSHI 

      1090       1100       1110       1120       1130       1140 
GAQMPGSVTE VKVSVGETVK ANQPLLITEA MKMETTIQAP FDGVIKQVTV NNGDTIATGD 

      1150 
LLIEIEKATD 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB57276.1.
PIRG89881.
RefSeqNP_371638.1. NC_002758.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ99UY8.
SMRQ99UY8. Positions 3-1146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46373N.
STRING158878.SAV1114.

2D gel databases

World-2DPAGE0002:Q99UY8.

Proteomic databases

PRIDEQ99UY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB57276; BAB57276; SAV1114.
GeneID1121091.
KEGGsav:SAV1114.
PATRIC19562927. VBIStaAur52173_1142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1038.
KOK01958.
OMAYAIQSRV.
OrthoDBEOG6CVV6Z.
PhylomeDBQ99UY8.

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-1133-MONOMER.

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.
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.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ99UY8.

Entry information

Entry nameQ99UY8_STAAM
AccessionPrimary (citable) accession number: Q99UY8
Entry history
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 statusUnreviewed (UniProtKB/TrEMBL)