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A7Z6M2 (GCSPB_BACA2) 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:RBAM_022870
OrganismBacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC 10A6 / FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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_1000045686

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z6M2 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 94EB4C294AD4A3A8

FASTA49154,699
        10         20         30         40         50         60 
MNNQDQALIF EMSREGRIGY SLPELDVPET ELESLLPGDY IRDEDAKLPE VSELDIMRHY 

        70         80         90        100        110        120 
TALSKRNHGV DSGFYPLGSC TMKYNPKLNE KIARIAGFSA IHPLQDEDTV QGALELLYDL 

       130        140        150        160        170        180 
SGHLEEITGM DEVTLQPAAG AHGEWTGLMM IRAYHEARGD FGRTKVIVPD SAHGTNPASA 

       190        200        210        220        230        240 
TVAGFETITV KSNEHGLVDI EDLKRAVNEE TAALMLTNPN TLGLFEENIT EMAEIVHQAG 

       250        260        270        280        290        300 
GKLYYDGANL NAVLSKARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKKEFIPYLP 

       310        320        330        340        350        360 
KPVLTKKEGR LTFDYDRPQS IGRVKPYYGN FGINVRAYTY IRSMGPDGLK AVTENAVLNA 

       370        380        390        400        410        420 
NYMMRRLAPY YDLPYDRHCK HEFVLSGRRQ KKLGVRTLDI AKRLLDFGYH PPTVYFPLNV 

       430        440        450        460        470        480 
EESIMIEPTE TESKETLDAF IDAMIQIARE AEESPEIVQE APHTTVVKRM DETKAARKPV 

       490 
LKYERTLDGS R 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 23117 / BGSC 10A6 / FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74648.1.
RefSeqYP_001421879.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z6M2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326423.RBAM_022870.

Proteomic databases

PRIDEA7Z6M2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS74648; ABS74648; RBAM_022870.
GeneID5461360.
KEGGbay:RBAM_022870.
PATRIC18749666. VBIBacAmy31356_2309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycBAMY326423:GCM4-2285-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_BACA2
AccessionPrimary (citable) accession number: A7Z6M2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
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