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Q5HP14 (GCSPB_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:SERP1100
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length502 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 – 502502Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167018

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HP14 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F2862E1B1281806C

FASTA50256,404
        10         20         30         40         50         60 
MISKSSPLIF ERSKKDRYAY SLPQNDIENI SIASLLDDKY IRKHKAEFPE VSELDLVRHY 

        70         80         90        100        110        120 
TELSNKNFGV DTGFYPLGSC TMKYNPKINE KVARISGFSE SHPLQEEEHV QGSLEIIYSL 

       130        140        150        160        170        180 
QEELKEITGM DEVTLQPAAG AHGEWTALMI FKAYHEKNGQ SHRDEVIVPD SAHGTNPASA 

       190        200        210        220        230        240 
SFAGFKSVTV KSNQRGEVDI EDLKRVVNDN TAAIMLTNPN TLGIFEQDII EIGKIVHEAG 

       250        260        270        280        290        300 
GLLYYDGANL NAILDKVRPG DMGFDAVHLN LHKTFTGPHG GGGPGSGPVG VVEKLASYLP 

       310        320        330        340        350        360 
KPMVIKDNDR YKYDNDIPNS IGRVKPFYGN FGIYLRAYTY IRSMGANGLK EVSEAAVLNA 

       370        380        390        400        410        420 
NYIKSRLKNH FEIPFNQYCK HEFVLSGTLQ KQYGVRTLDM AKRLLDFGVH PPTIYFPLNV 

       430        440        450        460        470        480 
EEGMMIEPTE TESKETLDYF IDAMIQIADE TKNDPDKVLE APHTTIIDRL DETTAARKPI 

       490        500 
LKFEELKDEK YKEHTNIDSE DN 

« 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: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54491.1.
RefSeqYP_188676.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HP14.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP1100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54491; AAW54491; SERP1100.
GeneID3240949.
KEGGser:SERP1100.
PATRIC19613057. VBIStaEpi130894_1071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSEPI176279:GJJB-1127-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_STAEQ
AccessionPrimary (citable) accession number: Q5HP14
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 63 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