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B6J4T8 (GCSPB_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:CbuK_0295
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length491 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 – 491491Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132498

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J4T8 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 7BCD7C9D7CCD45AF

FASTA49154,647
        10         20         30         40         50         60 
MLIFEKSRKN RRTLAHAIAD KMDANDIPAN LLRHDAPRLP ELSELEVVRH FTRLSTQNFS 

        70         80         90        100        110        120 
IDTHFYPLGS CTMKYNPRAA NRLASLPGYL KRHPLSPAPQ SQAFLQCLYE LQTMLTEITG 

       130        140        150        160        170        180 
MEKISLTSMA GAQGEFAGVA MIKAYHESRG DYDRTEMIVP DAAHGTNPAS AAMCGFTVKE 

       190        200        210        220        230        240 
ISTTKDGDID LEKLRQMVGA KTAGIMLTNP STLGVFERQI SEVAKIIHNA GGLLYYDGAN 

       250        260        270        280        290        300 
LNAILGKYRP GDMGFDVMHL NLHKTFATPH GGGGPGAGPV AAGPRLSKFL PVPMVGKNKE 

       310        320        330        340        350        360 
GYDWLTEKEC PKSIGRLSAF MGNSGVLLRA YIYLRLLGKE GLSRVAEFST LNANYLMKRL 

       370        380        390        400        410        420 
EQLGFTLAFP NRRASHEFII TLKPLTRAYG VTALDIAKRL LDYGFHAPTI YFPLLVPECL 

       430        440        450        460        470        480 
LIEPTETESK QTLDHFIEAM EKILTEIKTT PDLLRNAPHQ QLINRLDEVK AARELDLRWY 

       490 
PIAKETEIFI Q 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ19603.1.
RefSeqYP_002304748.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J4T8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434924.CbuK_0295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ19603; ACJ19603; CbuK_0295.
GeneID7014809.
KEGGcbc:CbuK_0295.
PATRIC17916001. VBICoxBur77120_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycCBUR434924:GHWU-294-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_COXB1
AccessionPrimary (citable) accession number: B6J4T8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 37 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