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Q5X0A8 (GCSPB_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:lpl0113
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length484 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 – 484484Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000045696

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X0A8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: BC2959C45F6E9A9C

FASTA48453,426
        10         20         30         40         50         60 
MLIFELSKTG RQAKAQIPRA VSKNYSIPEE FQRKSRPRLP ACSELQVVRH FTCLSQKNFS 

        70         80         90        100        110        120 
IDTNFYPLGS CTMKYNPRGV HKAASLPGFI NRHPLAMDNE SQGFLETLYK LQNYISEITG 

       130        140        150        160        170        180 
MPGVSLTPMA GSQGEFAGVA MIKAYHQSRG DTARDEILIP DAAHGTNPAS AVMCGFKVVE 

       190        200        210        220        230        240 
IATAPDGDID LDELKRKVGP RTAGIMLTNP STLGLFMRQI KEIASLVHQA GGLLYYDGAN 

       250        260        270        280        290        300 
LNAILGKVRP GDMGFDVMHL NLHKTFATPH GGGGPGAGPV AVGKRLIPYM PLPVVKKTDS 

       310        320        330        340        350        360 
GYHWATRQDY PQSIGRLSCF MGNAGILLRA YFYMLVLGKE GLLRVSEFAT LNANYLLKEL 

       370        380        390        400        410        420 
TKVGYTAAYP DRRASHEFIL TLNSEKKNYD VTAMDFAKRL LDYGVHAPTT YFPLLVPECL 

       430        440        450        460        470        480 
LIEPPETESK EELDAFVAVM KTIREEASKQ PDILKAAPHT LPVKRLDDVK AARELDLNYF 


ATHE 

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References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH14343.1.
RefSeqYP_125490.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5X0A8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl0113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH14343; CAH14343; lpl0113.
GeneID3114275.
KEGGlpf:lpl0113.
PATRIC22313663. VBILegPne33733_0182.

Organism-specific databases

LegioListlpl0113.
CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAKPVMHEF.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-117-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_LEGPL
AccessionPrimary (citable) accession number: Q5X0A8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 69 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