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Q49XX9 (GCSPB_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:SSP1220
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length492 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 – 492492Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167020

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49XX9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: CFD1C854A95D2812

FASTA49255,035
        10         20         30         40         50         60 
MVVSKSSPLI FERSKKGRYA YSLPKKEIDN GAVEKLLDDK FIRKNKAELP EVAELDLVRH 

        70         80         90        100        110        120 
YTELSNKNFG VDSGFYPLGS CTMKYNPKIN EKIARIPGFA ESHPLQDESQ VQGSLEIIHS 

       130        140        150        160        170        180 
LQEELKEITG MDEVTLQPAA GAHGEWTALM IFKAFHQKNG EGHRDEVIVP DSAHGTNPAS 

       190        200        210        220        230        240 
AAFAGFKAVT VKSNERGEVD IDDLKRVVNE NTAAIMLTNP NTLGIFEKNI MDIRNIVHEA 

       250        260        270        280        290        300 
GGLLYYDGAN LNAIMDKVRP GDMGFDAVHL NLHKTFTGPH GGGGPGSGPV GVKKELASFL 

       310        320        330        340        350        360 
PKPMVVKEDD VYKYDNDIEN SIGRVKPFYG NFGIYLRAYT YIRTMGNKGL EEVSEAAVLN 

       370        380        390        400        410        420 
ANYIKARLKD HFEIPYPQYC KHEFVLSGSK QKEHGVRTLD MAKRLLDFGV HPPTIYFPLN 

       430        440        450        460        470        480 
VEEGMMIEPT ETESKETLDY FCDKMIEIAN EAKEDPDKVL EAPHTTIIDR LDETKAARQP 

       490 
VLKFENLRSE KE 

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References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18365.1.
RefSeqYP_301310.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49XX9.
SMRQ49XX9. Positions 6-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP1220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18365; BAE18365; SSP1220.
GeneID3616987.
KEGGssp:SSP1220.
PATRIC19624024. VBIStaSap90642_1219.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
OrthoDBEOG6HMXDX.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-1279-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_STAS1
AccessionPrimary (citable) accession number: Q49XX9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 59 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