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B2SFM4 (GCSPB_FRATM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:FTM_0566
OrganismFrancisella tularensis subsp. mediasiatica (strain FSC147) [Complete proteome] [HAMAP]
Taxonomic identifier441952 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length481 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 – 481481Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132501

Amino acid modifications

Modified residue2631N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2SFM4 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: F14F8C6591BF820A

FASTA48152,762
        10         20         30         40         50         60 
MVIFEKTRGK NSPSVMPSKK GDVSNIPTDM LRTKKPILPE QAELDVVRHY TQLSRKNFCI 

        70         80         90        100        110        120 
DTNFYPLGSC TMKYNPRAAH KYASLAGFLE RHPYASAQSV QGTLECLYDL QNLIKELTGM 

       130        140        150        160        170        180 
TGVSLAPMAG AQGEFAGVAM IKAYHHKRSD FERDEIIVPD AAHGTNPATA KVCGLKVIEI 

       190        200        210        220        230        240 
PTKKDGDIDI EALDKVLGPK TAGIMLTNPS TVGVFERNIA VIAKKVHEAG GLLYYDGANL 

       250        260        270        280        290        300 
NAIMGKARPG DMGFDVLHMN LHKTFATPHG GGGPGAGPVA VNDKLKEFLP VPMVGKKDDK 

       310        320        330        340        350        360 
FVWLEEKDVS NTIGRLSAFN GNIGVLIRAY IYGAMLGGNG LTEASEIATL NANYMMARLK 

       370        380        390        400        410        420 
EEGFTIAYPD RRASHEFIVT LKPEFLNYGV TATDFAKCLI DKGVHAPTMY FPLLVPECLL 

       430        440        450        460        470        480 
IEPTETENVD SMEKFIQAMV EIRDIAKKDP QYLKGAPYNL PARRLDDVKA AKELDIVWQP 


K 

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References

[1]"Molecular evolutionary consequences of niche restriction in Francisella tularensis, a facultative intracellular pathogen."
Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T., Keim P., Johansson A.
PLoS Pathog. 5:E1000472-E1000472(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC147.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000915 Genomic DNA. Translation: ACD30567.1.
RefSeqYP_001891345.1. NC_010677.1.

3D structure databases

ProteinModelPortalB2SFM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441952.FTM_0566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD30567; ACD30567; FTM_0566.
GeneID6291659.
KEGGftm:FTM_0566.
PATRIC17955601. VBIFraTul67519_0707.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAKPVMHEF.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycFTUL441952:GIY0-565-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_FRATM
AccessionPrimary (citable) accession number: B2SFM4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 44 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