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Q9K936 (GCSPB_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:BH2814
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length488 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 – 488488Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000166998

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K936 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1CBACE20B74140E6

FASTA48854,224
        10         20         30         40         50         60 
MMNKDQALIF ELSKPGRVGH SLPELDVLEQ PVETLIPAEF LREEAPELPE VSELQLMRHY 

        70         80         90        100        110        120 
TALSKRNHGV DSGFYPLGSC TMKYNPKINE DVARYPGFAN IHPYQPEAQV QGALRLMYEL 

       130        140        150        160        170        180 
QTALAEITGM DEVTLQPAAG AQGEWTGLML IRAYHEANGD TNRTKVIVPD SAHGTNPASA 

       190        200        210        220        230        240 
TVAGFESVTV RTDEDGLVDL DHLREVVGED TAALMLTNPN TLGLFEAHIV EMAAIIHEAG 

       250        260        270        280        290        300 
GKLYYDGANS NAILGIARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKKELIPYLP 

       310        320        330        340        350        360 
KPVVVKDGDS YRLDYDRPHS IGRVKPYYGN FGINVRAYTY IRTMGPEGLR TVSEYAVLNA 

       370        380        390        400        410        420 
NYMMRRLAPY FDLPYDQHCK HEFVLSGRQQ KKLGVRTLDI AKRLLDFGYH PPTIYFPLNV 

       430        440        450        460        470        480 
EECLMIEPTE TESKETLDEF IEAMIQIAKE AEETPEVVQE APHHTVIGRL DETTAARKPI 


LRYEKITQ 

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06533.1.
PIRF84001.
RefSeqNP_243680.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K936.
SMRQ9K936. Positions 7-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH2814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06533; BAB06533; BAB06533.
GeneID893342.
KEGGbha:BH2814.
PATRIC18942826. VBIBacHal18977_2924.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBHAL272558:GJC5-2900-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_BACHD
AccessionPrimary (citable) accession number: Q9K936
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 75 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