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B1L9T8 (GCSPB_THESQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:TRQ2_0734
OrganismThermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]
Taxonomic identifier126740 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length474 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 – 474474Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132507

Amino acid modifications

Modified residue2621N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1L9T8 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 622235CEB0600A0D

FASTA47453,414
        10         20         30         40         50         60 
MTIFERSKKG RKAFRLPESD IPEYSLPDRF LRSTPPKLPE VSEPDVVRHY TDLARKNYSV 

        70         80         90        100        110        120 
DLGIYPLGSC TMKYNPKLNE KAANLEGFRE IHPYQPVETV QGSLRLMYEL KEMLCEITGM 

       130        140        150        160        170        180 
DDMTLQPAAG AHGELTGMLI VREYFKNRGD TGRKKVLVPD SAHGTNPASA SMVGFEVVEI 

       190        200        210        220        230        240 
KSKNGMVDVE DLRKLLDEEV AAVMLTNPNT LGLFEKDILK IAEMTHECGA LLYYDGANLN 

       250        260        270        280        290        300 
AIMGKVRPGD MGFDIVHLNL HKTFSTPHGM GGPGSGPVGV KKHLVDFLPF PQVKKNGELY 

       310        320        330        340        350        360 
ELFVPEKTIG RVRSFFGNFP VLVKAYTYIL TMGRDGLERV SEMAVLNANY LKKKIEKFLE 

       370        380        390        400        410        420 
IPYNGFCMHE FVASAEKVFR ETGVRTLDIA KRILDFGVHP PTVYFPLIVP EALMIEPTET 

       430        440        450        460        470 
ENKETLDKYA EILERVVKEA YENPDALKNA PHNTPVRRVN EVLASKKPVF RWRG 

« Hide

References

[1]"Complete sequence of Thermotoga sp. RQ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RQ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000969 Genomic DNA. Translation: ACB09086.1.
RefSeqYP_001738769.1. NC_010483.1.

3D structure databases

ProteinModelPortalB1L9T8.
SMRB1L9T8. Positions 2-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING126740.TRQ2_0734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB09086; ACB09086; TRQ2_0734.
GeneID6092151.
KEGGtrq:TRQ2_0734.
PATRIC23948018. VBITheSp108950_0746.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
OrthoDBEOG6HMXDX.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycTSP126740:GH49-752-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_THESQ
AccessionPrimary (citable) accession number: B1L9T8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 46 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