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A9KC20 (GCSPB_COXBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:CBUD_0293
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [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_1000083228

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KC20 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D7D0E3A1859A98F7

FASTA49154,619
        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 LEKLRQMAGA 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: Dugway 5J108-111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS78325.1.
RefSeqYP_001423715.1. NC_009727.1.

3D structure databases

ProteinModelPortalA9KC20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434922.CBUD_0293.

Proteomic databases

PRIDEA9KC20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS78325; ABS78325; CBUD_0293.
GeneID5458581.
KEGGcbd:CBUD_0293.
PATRIC17920432. VBICoxBur32972_0339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycCBUR434922:GJTP-312-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_COXBN
AccessionPrimary (citable) accession number: A9KC20
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 50 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