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Q9UXT1 (GCSPB_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:PYRAB17770
ORF Names:PAB1172
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167027

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UXT1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F8E8C9CFA27EBD3B

FASTA50256,288
        10         20         30         40         50         60 
MYRQAKWDEP LIFELSRPGR VGYTLPKPIE DVDVEIPEKL KRKSPLNLPE VSEPEVVKHY 

        70         80         90        100        110        120 
TRLSEMNYGV DSGIYPLGSC TMKYNPKINE ELAGHPKVAY IHPYQDERTV QGALRIMWEL 

       130        140        150        160        170        180 
EQWLKEITGM DRFTLQPAAG ANGEFTGVMI IKAYHLDRGE TQRNEMLVPD SAHGTNPASA 

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

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

       310        320        330        340        350        360 
VPLVSYDEEN DRYYLDYDVP KSIGKVKELF GNFAVLVRAL TYLKVMGKDG LREVSEVAVL 

       370        380        390        400        410        420 
NANYLARKLK GTRGYELPHK ELRKHEVVFS AEPMKRETGV RTLDVAKRLL DFGMHAPTIY 

       430        440        450        460        470        480 
FPLIVHEALM IEPTETVSKE ELDAYVEAMK KISEEAYTNP EVVKSAPHNT AVRRVDDVLA 

       490        500 
SKKPIITWKM YKELKEKGEV DY 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50682.1.
HE613800 Genomic DNA. Translation: CCE71251.1.
PIRD75030.
RefSeqNP_127453.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UXT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50682; CAB50682; PAB1172.
GeneID1496080.
KEGGpab:PAB1172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.

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_PYRAB
AccessionPrimary (citable) accession number: Q9UXT1
Secondary accession number(s): G8ZKW0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 81 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