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Q8RCW2 (GCSPB_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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
Synonyms:gcvP
Ordered Locus Names:TTE0293
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobacter

Protein attributes

Sequence length485 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 – 485485Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167022

Amino acid modifications

Modified residue2731N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RCW2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B53EB282A21B93CB

FASTA48553,938
        10         20         30         40         50         60 
MLKEYNSLIF ELSKEGKKAY TLPPLDVEEK PLEDMLPKEM LREKEVDLPE VSEVDVIRHY 

        70         80         90        100        110        120 
TLLSQKNYGV DIGFYPLGSC TMKYNPKINE DMASLPGFTE LHPYQPEETV QGALKLMYEL 

       130        140        150        160        170        180 
EKALCEITGM DRFSLHPAAG AHGELTGLMI IKAYHEHRND KKRKKIIVPD SAHGTNPASA 

       190        200        210        220        230        240 
AVAGFDVIEI KSNKEGAIDL EALKAVLNDE VAGLMLTNPS TLGLFEENIV EIARLVHEAG 

       250        260        270        280        290        300 
GLLYYDGANL NAIMGISRPG DMGFDVVHLN LHKTFSTPHG GGGPGSGPVG VKKELADFLP 

       310        320        330        340        350        360 
VPTVEEKDGR YFLDYDRPLS IGKVRSFYGN FNVMIKAYSY ILTMGAEGLK RASELAVLNA 

       370        380        390        400        410        420 
NYLKEKLKGY YKVAVDKTCM HEFVLAGLAE KSGDVRTLDV AKRLIDYGFH PPTIYFPLIV 

       430        440        450        460        470        480 
EEALMIEPTE TETKETLDAF AETLIKIAKE AKENPELLKE APHNTPVRRL DEVLAARNPV 


IRWTK 

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References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM23589.1.
RefSeqNP_621985.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8RCW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273068.TTE0293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM23589; AAM23589; TTE0293.
GeneID996270.
KEGGtte:TTE0293.
PATRIC23895223. VBITheTen82880_0287.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
OrthoDBEOG6HMXDX.
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_THETN
AccessionPrimary (citable) accession number: Q8RCW2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 69 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