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C5A7J0 (GCSPB_THEGJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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:TGAM_1700
OrganismThermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3) [Complete proteome] [HAMAP]
Taxonomic identifier593117 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length502 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 – 502502Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000212679

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C5A7J0 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: AFA1836BFAA7BF8F

FASTA50256,100
        10         20         30         40         50         60 
MFRQAKWDEP LIFELSREGR VGYTLPKPIE DLEVEIPEKI RRKSKLDLPE LSEPEIVKHY 

        70         80         90        100        110        120 
TRLSEMNYGV DSGIYPLGSC TMKYNPKINE EMAAHPGVAY IHPYQDERTV QGALKIMWEL 

       130        140        150        160        170        180 
EQWLKEITGM DRFTLQPAAG ANGEFTGVSI IRTYHIDNGE PQRDEMLVPD SAHGTNPASA 

       190        200        210        220        230        240 
AMAGFKVIEI PSNENGTVDL EALENAVGER TAGLMLTNPN TLGIFEDEIL EIAKIVHKAG 

       250        260        270        280        290        300 
GLLYYDGANL NAVLGKVRPG DMGFDIVHLN LHKTFSTPHG GGGPGSGPVG VKDFLKDYLP 

       310        320        330        340        350        360 
VPLVGYDEEN DRYYLDYNVP KSIGKVKELY GNFAVMVRAL VYLKVMGRDG LKNASEIAVL 

       370        380        390        400        410        420 
NANYLTRKLL GTRGYELPGK KLRKHETVFS AEPMKKETGV TAMDVAKRLL DFGMHAPTVY 

       430        440        450        460        470        480 
FPLIVHEALM IEPTETVSKE ELDAYVEALK RISDEAYTNP EVVKSAPHNT AVRRVDDVMA 

       490        500 
VKKPVISWRM YLELKEKGEI NY 

« Hide

References

[1]"Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea."
Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.
Genome Biol. 10:R70.1-R70.23(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15229 / JCM 11827 / EJ3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001398 Genomic DNA. Translation: ACS34202.1.
RefSeqYP_002960066.1. NC_012804.1.

3D structure databases

ProteinModelPortalC5A7J0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING593117.TGAM_1700.

Proteomic databases

PaxDbC5A7J0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS34202; ACS34202; TGAM_1700.
GeneID7987419.
KEGGtga:TGAM_1700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycTGAM593117:GHFT-1731-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_THEGJ
AccessionPrimary (citable) accession number: C5A7J0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 32 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