Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5HP13 (GCSPA_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 1

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P-protein subunit 1
Glycine decarboxylase subunit 1
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
Gene names
Name:gcvPA
Ordered Locus Names:SERP1101
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length448 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_00712

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_00712

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. N-terminal subunit subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Probable glycine dehydrogenase (decarboxylating) subunit 1 HAMAP-Rule MF_00712
PRO_0000166977

Sequences

Sequence LengthMass (Da)Tools
Q5HP13 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 18461D6535BE06CD

FASTA44849,962
        10         20         30         40         50         60 
MSHRYIPLTE QDKNEMLNSI GAKSISELFD DIPTDILLKR NLNIAESEAE TILLRRLNRL 

        70         80         90        100        110        120 
AAKNTTKETH ATFLGAGVYD HYTPAVVDAM ISRSEFYTAY TPYQPEISQG ELQAIFEFQT 

       130        140        150        160        170        180 
LICELTDMDV ANSSMYDGMT SFAEACILAL SHTKKNKIVV SSGLHYQALQ ILHTYAKTRD 

       190        200        210        220        230        240 
EFEIIEVDLK GTITDLEKLE QLIDDNTAAV AVQYPNFYGS IEDLEQINNY IKDKKALFIV 

       250        260        270        280        290        300 
YANPLSLGLL TPPGTFGADI VVGDTQPFGI PTQFGGPHCG YFATTKKLMR KVPGRLVGQT 

       310        320        330        340        350        360 
QDDEGNRGFV LTLQAREQHI RRDKATSNIC SNQALNALAS SIAMSALGKQ GIYEIAVQNL 

       370        380        390        400        410        420 
KNANYAKNKF EEHGFEVLKA QSFNEFVVKF NQPIKNINLK LAEYGYIGGF DLGEVSDDFK 

       430        440 
NHMLVAVTEL RSKDEIDDFV TKAGELND 

« 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: AAW54492.1.
RefSeqYP_188677.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HP13.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP1101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54492; AAW54492; SERP1101.
GeneID3240950.
KEGGser:SERP1101.
PATRIC19613059. VBIStaEpi130894_1072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0403.
HOGENOMHOG000132025.
KOK00282.
OMASMYDGST.
OrthoDBEOG6XWV3B.
ProtClustDBPRK00451.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-1128-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00712. GcvPA.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023010. GDC_P_su1.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 1 hit.
[Graphical view]
PIRSFPIRSF006815. GcvPA. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSPA_STAEQ
AccessionPrimary (citable) accession number: Q5HP13
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