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A8F8M6 (GCSPB_THELT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:Tlet_1956
OrganismThermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO) [Complete proteome] [HAMAP]
Taxonomic identifier416591 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length479 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 – 479479Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000062081

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8F8M6 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0E9F5B51925C8736

FASTA47953,612
        10         20         30         40         50         60 
MIIFEKSVPG RKAYRLPDEE LQRIDPVFPE HLKRTRPLRL PELSEPDVVR HYTALAEKNY 

        70         80         90        100        110        120 
SVDKGFYPLG SCTMKYNPKL NEYVAGLEGF TDIHPYQPWE SVQGALQVMY ELKEFLCEIT 

       130        140        150        160        170        180 
GMDEMTLQPA AGAHGELTGM LIVRAYHLSR NDKKRHVALV PDSAHGTNPA SAAMAGFDVV 

       190        200        210        220        230        240 
EIKSTEDGLV DLEQLENHLN DEIAVLMLTN PNTLGLFEKD IVKIAEKVHQ AGALLYYDGA 

       250        260        270        280        290        300 
NLNAIMGKIK PGEMGFDIVH LNLHKTFSAP HGMGGPGSGP VGVKAFLSEF LPIPIIRKDG 

       310        320        330        340        350        360 
DKYYPDFKLP NSIGRTRSFY GNFLVLLKAY VYILSMGKDG LTRASEMAVL NANYLRSLIS 

       370        380        390        400        410        420 
KFLKIASPGI CMHEFVVDGS QFVKETGVKI LDVAKRILDY GLHAPTVYFP LIVHEDMMIE 

       430        440        450        460        470 
PTETENKNTL DYFAKVLEKI VEEAKKTPEV VKTAPHTTPV KRLDDITATK KPVYRYRLS 

« Hide

References

[1]"Complete sequence of Thermotoga lettingae TMO."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-301 / DSM 14385 / TMO.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000812 Genomic DNA. Translation: ABV34510.1.
RefSeqYP_001471574.1. NC_009828.1.

3D structure databases

ProteinModelPortalA8F8M6.
SMRA8F8M6. Positions 2-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416591.Tlet_1956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV34510; ABV34510; Tlet_1956.
GeneID5608229.
KEGGtle:Tlet_1956.
PATRIC23934635. VBITheLet125395_2046.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTLET416591:GI64-2009-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_THELT
AccessionPrimary (citable) accession number: A8F8M6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 47 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