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Q97C04 (GCSPB_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:TV0301
ORF Names:TVG0311358
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length472 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 – 472472Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167034

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97C04 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 92977275D2E74AE7

FASTA47252,790
        10         20         30         40         50         60 
MNFKQAYYEE PIIKDIKSSN TFSLSEQVDE SILPENLKRK DLELPEVSEY DVVRHYTRLS 

        70         80         90        100        110        120 
QMNYTVDVGI YPLGSCTMKY NPKFADRVSA IDGFRNIHPF QPENTVQGAL HVMYDLQEYL 

       130        140        150        160        170        180 
KKISDMDAVS LQPMAGADGE FTGILIVKKY FEDKGEDRTE IIIPDSAHGT NPASATMGGF 

       190        200        210        220        230        240 
DVVEVPSDDK GMVDLEALRA AVSKKTAAFM ITNPNTLGIF EQNIEEIAKI IHNAGALLYY 

       250        260        270        280        290        300 
DGANLNAIFG ITSPGLMGFD IVHFNLHKSF ATPHGGGGPG AGPVAVKSFL KDFLPVPIVD 

       310        320        330        340        350        360 
FDGNSYRLNY ELKKTIGKVS SFYGSFSILL RAWSYIIRNG DDGLKNVSAR AVLNSNYLKK 

       370        380        390        400        410        420 
KLEKYYDIPY YPLKKHEFVL STENTGKRAL DIGKYILDNG IHSPTVYFPL IVKEAMMIEP 

       430        440        450        460        470 
TETVSKADLD NYADVLIEAL KLSDEELKSR PKNTAVRRID EVKAARDLKL KW 

« Hide

References

[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000011 Genomic DNA. Translation: BAB59443.1.
RefSeqNP_110817.1. NC_002689.2.

3D structure databases

ProteinModelPortalQ97C04.
SMRQ97C04. Positions 31-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273116.TVN0298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB59443; BAB59443; BAB59443.
GeneID1440814.
KEGGtvo:TVN0298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
KOK00283.
OMAWTGLMMI.

Enzyme and pathway databases

BioCycTVOL273116:GC31-307-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_THEVO
AccessionPrimary (citable) accession number: Q97C04
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 73 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