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Q8TZJ2 (GCSPB_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:PF2000
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

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_0000167028

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TZJ2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 70BE4DC35055A565

FASTA50256,113
        10         20         30         40         50         60 
MFRQAKWDEP LIFELSRPGR VGYTLPKPIE DIKVDIPEKL RRKSKLELPE LSEPEIVKHY 

        70         80         90        100        110        120 
TRLSEMNYGV DSGIYPLGSC TMKYNPKINE EIATHPKVAY IHPYQDERTV QGALAIMWEL 

       130        140        150        160        170        180 
EQWLKEITGM DRFTLQPAAG ANGEFTGVMI IRAYHLDNGE PQRNEMLVPD SAHGTNPASA 

       190        200        210        220        230        240 
AMAGFKVIEI PSNENGTIDL EALENAVSER TAGLMLTNPN TLGIFEDEIV EIAKIIHKAG 

       250        260        270        280        290        300 
GLLYYDGANL NGILGKIRPG DMGFDIVHLN LHKTFSTPHG GGGPGAGPVG VKEFLKDYLP 

       310        320        330        340        350        360 
VPLVSYDEKS GRYYLDYNVP KSIGKVKELY GNFAVLVRAL TYLKIMGRDG LREVSEIAVL 

       370        380        390        400        410        420 
NANYLTQKLK GTRGYSLPGK ELRKHEVVFS AEPMKKETGV KALDVAKRLL DFGMHAPTIY 

       430        440        450        460        470        480 
FPLIVHEALM IEPTETVSKE ELDAYVEALK RISEEAYTNP EIVKSAPHNT AVKRVDDVLA 

       490        500 
AKKPIVTWRM YKELKEKGEV DY 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL82124.1.
RefSeqNP_579729.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8TZJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF2000.

Proteomic databases

PRIDEQ8TZJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL82124; AAL82124; PF2000.
GeneID1469884.
KEGGpfu:PF2000.

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
ProtClustDBPRK04366.

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_PYRFU
AccessionPrimary (citable) accession number: Q8TZJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 68 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