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A7X2R9 (GCSPB_STAA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase (decarboxylating) subunit 2

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P-protein subunit 2
Glycine decarboxylase subunit 2
Glycine dehydrogenase (aminomethyl-transferring) subunit 2
Gene names
Name:gcvPB
Ordered Locus Names:SAHV_1522
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein By similarity. HAMAP-Rule MF_00713

Catalytic activity

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2. HAMAP-Rule MF_00713

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713

Subunit structure

The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits By similarity.

Sequence similarities

Belongs to the GcvP family. C-terminal subunit subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000045702

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7X2R9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 6EC8CCBA16D35CBF

FASTA49054,783
        10         20         30         40         50         60 
MTSKSSPLIF ERSREGRYAY SLPKSDIKTN SVESLLDDKF IRKNKAEFPE VAELDLVRHY 

        70         80         90        100        110        120 
TELSNKNFGV DNGFYPLGSC TMKYNPKINE KVARIPGFSE SHPLQDEDQV QGSLEIIYSL 

       130        140        150        160        170        180 
QEELKEITGM DEVTLQPAAG AHGEWTALMI FKAYHENNGE GHRDEVIVPD SAHGTNPASA 

       190        200        210        220        230        240 
SFAGFKSVTV KSNERGEVDI DDLKRVVNEN TAAIMLTNPN TLGIFEKNIM EIREIVHNAG 

       250        260        270        280        290        300 
GLLYYDGANL NAIMDKVRPG DMGFDAVHLN LHKTFTGPHG GGGPGSGPVG VVKELASYLP 

       310        320        330        340        350        360 
KPMVIKDGDK FKYDNDIKNS IGRVKPFYGN FGIYLRAYTY IRTMGATGLK EVSEAAVLNA 

       370        380        390        400        410        420 
NYIKARLSEH FEIPYKQYCK HEFVLSGVRQ KEFGVRTLDM AKRLLDFGVH PPTIYFPLNV 

       430        440        450        460        470        480 
EEGMMIEPTE TESKETLDYF IDTLISIAEE AKNDPDKVLE APHTTVIDRL DEATAARKPI 

       490 
LKFENLKQEK 

« Hide

References

[1]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu3 / ATCC 700698.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009324 Genomic DNA. Translation: BAF78405.1.
RefSeqYP_001442112.1. NC_009782.1.

3D structure databases

ProteinModelPortalA7X2R9.
SMRA7X2R9. Positions 6-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418127.SAHV_1522.

Proteomic databases

PRIDEA7X2R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF78405; BAF78405; SAHV_1522.
GeneID5559123.
KEGGsaw:SAHV_1522.
PATRIC19558084. VBIStaAur127830_1559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycSAUR418127:GJP9-1539-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00713. GcvPB.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023012. GDC_P_su2.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSPB_STAA1
AccessionPrimary (citable) accession number: A7X2R9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families