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A9VH10 (GCSPB_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:BcerKBAB4_4080
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [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_1000132495

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9VH10 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 736686233BD15705

FASTA49154,934
        10         20         30         40         50         60 
MKNQDQALIF EVTKEGRVGY SLPKLDVEEV KLEDVFESDY IRVEDAELPE VSELDIMRHY 

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

       130        140        150        160        170        180 
QEHLIEITGM DTVTLQPAAG AHGEWTGLML IRAYHEANGD FNRTKVIVPD SAHGTNPASA 

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

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

       310        320        330        340        350        360 
KPILEKTENG YHFNYDRPEA IGRVKPFYGN FGINVRAYTY IRSMGPDGLR AVTEYAVLNA 

       370        380        390        400        410        420 
NYMMRRLAPF YDLPFDRHCK HEFVLSGRRQ KKLGVRTLDI AKRLLDFGYH PPTIYFPLNV 

       430        440        450        460        470        480 
EECIMIEPTE TESKETLDGF IDKMIQIAKE VEENPEVVQE APHTTVIKRL DETLAARKPV 

       490 
LRYEKLAPVQ 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: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY45242.1.
RefSeqYP_001646870.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VH10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315730.BcerKBAB4_4080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY45242; ABY45242; BcerKBAB4_4080.
GeneID5844292.
KEGGbwe:BcerKBAB4_4080.
PATRIC19012803. VBIBacWei55973_4718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
OrthoDBEOG6HMXDX.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycBWEI315730:GHRU-4195-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_BACWK
AccessionPrimary (citable) accession number: A9VH10
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 49 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