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Q5HFM4 (GCSPB_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:SACOL1593
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [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_0000167011

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HFM4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 5D01D5D7A35E07D7

FASTA49054,781
        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 KSNERGEVNI 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 
NYIKARLSKH FEIPYKQYCK HEFVLSGVRQ KEFGVRTLDM AKRLLDFGVH PPTIYFPLNV 

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

       490 
LKFENLKQEK 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW38209.1.
RefSeqYP_186433.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HFM4.
SMRQ5HFM4. Positions 5-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL1593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW38209; AAW38209; SACOL1593.
GeneID3238025.
KEGGsac:SACOL1593.
PATRIC19529385. VBIStaAur112458_1547.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-1559-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_STAAC
AccessionPrimary (citable) accession number: Q5HFM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 62 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