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B1KWD8 (B1KWD8_CLOBM) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713

EC=1.4.4.2 HAMAP-Rule MF_00713
Alternative name(s):
Glycine cleavage system P-protein subunit 2 HAMAP-Rule MF_00713
Glycine decarboxylase subunit 2 HAMAP-Rule MF_00713
Glycine dehydrogenase (aminomethyl-transferring) subunit 2 HAMAP-Rule MF_00713
Gene names
Name:gcvPB HAMAP-Rule MF_00713 EMBL ACA56785.1
Ordered Locus Names:CLK_0100 EMBL ACA56785.1
OrganismClostridium botulinum (strain Loch Maree / Type A3) [Complete proteome] [HAMAP] EMBL ACA56785.1
Taxonomic identifier498214 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length484 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 SAAS SAAS020580

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 SAAS SAAS020580

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713 SAAS SAAS020580

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. HAMAP-Rule MF_00713 SAAS SAAS020580

Sequence similarities

Belongs to the GcvP family. C-terminal subunit subfamily. HAMAP-Rule MF_00713

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00713

Sequences

Sequence LengthMass (Da)Tools
B1KWD8 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 858671CD922F0D66

FASTA48453,762
        10         20         30         40         50         60 
MKDYNKVIFE LSSEGRKGYR LPDLDVPEVE LSKLLPKNLL REDEIELPEV SEVDVVRHYT 

        70         80         90        100        110        120 
ALSNKNYTVD NGFYPLGSCT MKYNPKINED IVALSGFSKI HPLQDENISQ GALELMYDLK 

       130        140        150        160        170        180 
GKLCEITGLD DFTLQPAAGA HGEYTGLLII KAYHEKRGDT KRTKIIVPDS AHGTNPASAS 

       190        200        210        220        230        240 
VAGFDIVEIK SGEDGRVSIE ELKKVLNDEI AGLMLTNPST LGLFEKDIKL ISELVHEAGG 

       250        260        270        280        290        300 
LLYYDGANLN AIMGIARPGD MGFDVCHLNM HKTFSTPHGG GGPGSGPVGV KKHLAKFLPV 

       310        320        330        340        350        360 
PTVEKENDKF ILDYNREDSL GKIRSLYGNF GVMVKAYTYI LTMGKEGLKS ASENAVLNAN 

       370        380        390        400        410        420 
YIKESLRDYY NIGKDDICKH EVILSTLKEN PHHIATLDIA KRLIDYGVHP PTVYFPLIIE 

       430        440        450        460        470        480 
EALMIEPTES ESKETVDEFI DAMKKIAVEA KENPELLHEA PVKAPVRRLD QVKAARKPIL 


RWQK 

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References

[1]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Loch Maree / Type A3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000962 Genomic DNA. Translation: ACA56785.1.
RefSeqYP_001786051.1. NC_010520.1.

3D structure databases

ProteinModelPortalB1KWD8.
SMRB1KWD8. Positions 6-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498214.CLK_0100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA56785; ACA56785; CLK_0100.
GeneID6152085.
KEGGcbl:CLK_0100.
PATRIC19386837. VBICloBot822_1032.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCBOT498214:GH05-763-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 nameB1KWD8_CLOBM
AccessionPrimary (citable) accession number: B1KWD8
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: March 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)