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Q5JGX6 (GCSPB_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:TK1379
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167030

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JGX6 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: AFE4AC2931468554

FASTA50255,991
        10         20         30         40         50         60 
MFHQAKWDEP TIFELSRPGR IGYTLPKPIE DVDVDIPEKL RRKSPLNLPE LSEPEVVKHY 

        70         80         90        100        110        120 
TRLSEMNYGV DSGIYPLGSC TMKYNPKINE EIASHPGVAY VHPYQDEGTV QGALKIMWEL 

       130        140        150        160        170        180 
EQWLKEITGM DRFTLQPAAG ANGEFTGVSI IRAYHIDRGE TQRTEMLVPD SAHGTNPASA 

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

       250        260        270        280        290        300 
GLLYYDGANL NAVLGKIRPG DMGFDVVHLN LHKTFSTPHG GGGPGSGPVG VKDFLKDYLP 

       310        320        330        340        350        360 
VPLVSYDAEN DRYYLDYNVP RSIGKVKELY GNFAVIVRAL TYLKIMGREG LKEVSEVAVL 

       370        380        390        400        410        420 
NANYLTQKLK GTRGYELPGK ELRKHETVFS AEPMKKETGV KALDVAKRLL DFCMHAPTIY 

       430        440        450        460        470        480 
FPLIVHEALM IEPTETVSKE ELDAYVEALK RISEEAYSNP EVVTSAPHNT AVRRVDDVLA 

       490        500 
AKKPVITWRM YRELKERGEI DY 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD85568.1.
RefSeqYP_183792.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JGX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5JGX6. 1 interaction.
MINTMINT-8376968.
STRING69014.TK1379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85568; BAD85568; TK1379.
GeneID3235783.
KEGGtko:TK1379.

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1400-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_THEKO
AccessionPrimary (citable) accession number: Q5JGX6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 63 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