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A7GSN6 (GCSPB_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Bcer98_2913
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

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_1000083227

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GSN6 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 6C31F335795C2718

FASTA49154,867
        10         20         30         40         50         60 
MKNQDQALIF EMSKEGRVGY SLPQLDVEEV KLEDVFESNY IRAEDAELPE VSELDIMRHY 

        70         80         90        100        110        120 
TALSNRNHGV DSGFYPLGSC TMKYNPKINE NVARFPGFAN IHPLQDEKTV QGAMELMYDL 

       130        140        150        160        170        180 
QEHLVEITGM DAVTLQPAAG AHGEWTGLML IRAYHEANGD HNRTKVIVPD SAHGTNPASA 

       190        200        210        220        230        240 
TVAGFETITV KSNEHGLVDL EDLKRVVNEE TAALMLTNPN TLGLFEENIL EMAEIVHNAG 

       250        260        270        280        290        300 
GKLYYDGANL NAVLSQARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKEDLIPFLP 

       310        320        330        340        350        360 
KPILEKTENG YHFNYDRPQA IGRVKPFYGN FGINVRAYTY IRSMGPDGLR AVTENAVLNA 

       370        380        390        400        410        420 
NYMMRRLAPY YDLPFDRHCK HEFVLSGRCQ KKLGVRTLDI AKRLLDFGYH PPTIYFPLNV 

       430        440        450        460        470        480 
EECIMIEPTE TESKETLDGF IDKMIQIAKE AKENPEIVQE APHTTVITRL DETMAARKPI 

       490 
LRYQKPTPVQ V 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23144.1.
RefSeqYP_001376139.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GSN6.
SMRA7GSN6. Positions 7-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315749.Bcer98_2913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS23144; ABS23144; Bcer98_2913.
GeneID5347262.
KEGGbcy:Bcer98_2913.
PATRIC18934440. VBIBacCyt128034_3064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycBCYT315749:GH2A-3021-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_BACCN
AccessionPrimary (citable) accession number: A7GSN6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 54 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