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Protein

Pyruvate carboxylase

Gene

pycA

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

biotinUniRule annotationNote: Biotin.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191ADPCombined sources
Binding sitei119 – 1191ATPCombined sources
Binding sitei161 – 1611ADPCombined sources
Binding sitei161 – 1611ATPCombined sources
Binding sitei211 – 2111ADPCombined sources
Binding sitei211 – 2111ATPCombined sources
Binding sitei278 – 2781ADPCombined sources
Binding sitei278 – 2781ATPCombined sources
Binding sitei290 – 2901ADPCombined sources
Binding sitei367 – 3671CoenzymeACombined sources
Binding sitei541 – 5411PyruvateCombined sources
Metal bindingi542 – 5421ManganeseCombined sources
Binding sitei545 – 5451PyruvateCombined sources
Binding sitei614 – 6141PyruvateCombined sources
Metal bindingi712 – 7121ManganeseCombined sources
Binding sitei712 – 7121PyruvateCombined sources
Metal bindingi741 – 7411Manganese; via tele nitrogenCombined sources
Metal bindingi743 – 7431Manganese; via tele nitrogenCombined sources
Binding sitei876 – 8761PyruvateCombined sources
Binding sitei1024 – 10241CoenzymeACombined sources
Binding sitei1049 – 10491CoenzymeACombined sources
Binding sitei1053 – 10531CoenzymeACombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1684ADPCombined sources
Nucleotide bindingi165 – 1684ATPCombined sources
Nucleotide bindingi203 – 2064ADPCombined sources
Nucleotide bindingi203 – 2064ATPCombined sources
Nucleotide bindingi235 – 2384ADPCombined sources
Nucleotide bindingi235 – 2384ATPCombined sources
Nucleotide bindingi290 – 2923ATPCombined sources

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
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingCombined sources, BiotinUniRule annotation, ManganeseCombined sources, Metal-bindingCombined sources, Nucleotide-binding, PyruvateCombined sourcesImported

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:
PDBei
RCSB PDBi
PDBji
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 bindingCombined sources
Regioni420 – 4223CoenzymeA bindingCombined sources
Regioni462 – 4654CoenzymeA bindingCombined sources

Phylogenomic databases

eggNOGiCOG1038.
KOiK01958.
OMAiPIEAYLD.
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

        10         20         30         40         50
MKQIKKLLVA NRGEIAIRIF RAAAELDIST VAIYSNEDKS SLHRYKADES
60 70 80 90 100
YLVGSDLGPA ESYLNIERII DVAKQANVDA IHPGYGFLSE NEQFARRCAE
110 120 130 140 150
EGIKFIGPHL EHLDMFGDKV KARTTAIKAD LPVIPGTDGP IKSYELAKEF
160 170 180 190 200
AEEAGFPLMI KATSGGGGKG MRIVREESEL EDAFHRAKSE AEKSFGNSEV
210 220 230 240 250
YIERYIDNPK HIEVQVIGDE HGNIVHLFER DCSVQRRHQK VVEVAPSVGL
260 270 280 290 300
SPTLRQRICD AAIQLMENIK YVNAGTVEFL VSGDEFFFIE VNPRVQVEHT
310 320 330 340 350
ITEMVTGIDI VKTQILVAAG ADLFGEEINM PQQKDITTLG YAIQCRITTE
360 370 380 390 400
DPLNDFMPDT GTIIAYRSSG GFGVRLDAGD GFQGAEISPY YDSLLVKLST
410 420 430 440 450
HAISFKQAEE KMVRSLREMR IRGVKTNIPF LINVMKNKKF TSGDYTTKFI
460 470 480 490 500
EETPELFDIQ PSLDRGTKTL EYIGNVTING FPNVEKRPKP DYELASIPTV
510 520 530 540 550
SSSKIASFSG TKQLLDEVGP KGVAEWVKKQ DDVLLTDTTF RDAHQSLLAT
560 570 580 590 600
RVRTKDMINI ASKTADVFKD GFSLEMWGGA TFDVAYNFLK ENPWERLERL
610 620 630 640 650
RKAIPNVLFQ MLLRASNAVG YKNYPDNVIH KFVQESAKAG IDVFRIFDSL
660 670 680 690 700
NWVDQMKVAN EAVQEAGKIS EGTICYTGDI LNPERSNIYT LEYYVKLAKE
710 720 730 740 750
LEREGFHILA IKDMAGLLKP KAAYELIGEL KSAVDLPIHL HTHDTSGNGL
760 770 780 790 800
LTYKQAIDAG VDIIDTAVAS MSGLTSQPSA NSLYYALNGF PRHLRTDIEG
810 820 830 840 850
MESLSHYWST VRTYYSDFES DIKSPNTEIY QHEMPGGQYS NLSQQAKSLG
860 870 880 890 900
LGERFDEVKD MYRRVNFLFG DIVKVTPSSK VVGDMALYMV QNDLDEQSVI
910 920 930 940 950
TDGYKLDFPE SVVSFFKGEI GQPVNGFNKD LQAVILKGQE ALTARPGEYL
960 970 980 990 1000
EPVDFEKVRE LLEEEQQGPV TEQDIISYVL YPKVYEQYIQ TRNQYGNLSL
1010 1020 1030 1040 1050
LDTPTFFFGM RNGETVEIEI DKGKRLIIKL ETISEPDENG NRTIYYAMNG
1060 1070 1080 1090 1100
QARRIYIKDE NVHTNANVKP KADKSNPSHI GAQMPGSVTE VKVSVGETVK
1110 1120 1130 1140 1150
ANQPLLITEA MKMETTIQAP FDGVIKQVTV NNGDTIATGD LLIEIEKATD
Length:1,150
Mass (Da):128,558
Last modified:June 1, 2001 - v1
Checksum:i2C8B9B7C1E7E3E48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57276.1.
PIRiG89881.
RefSeqiNP_371638.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-46373N.
STRINGi158878.SAV1114.

2D gel databases

World-2DPAGE0002:Q99UY8.

Proteomic databases

PRIDEiQ99UY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1038.
KOiK01958.
OMAiPIEAYLD.
OrthoDBiEOG6CVV6Z.
PhylomeDBiQ99UY8.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1133-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ99UY8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

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.