Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C5CF44 (GCSPB_KOSOT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 31. 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:Kole_1619
OrganismKosmotoga olearia (strain TBF 19.5.1) [Complete proteome] [HAMAP]
Taxonomic identifier521045 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeKosmotoga

Protein attributes

Sequence length483 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 – 483483Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000212671

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CF44 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: B4DF7B8A0FAAA507

FASTA48353,757
        10         20         30         40         50         60 
MTIFEKSVTG RTGYTLPEEK KDEIRPSDYI PEHLLRKELP GLPECSEIDV VRHYTELTRK 

        70         80         90        100        110        120 
NYSVDNGFYP LGSCTMKYNP KLNEKIAALE GFSLLHPYEP IEKVQGALEV MYRLQTLLSE 

       130        140        150        160        170        180 
ITGMDAFTLQ PAAGAHGELT GMLIVKKYFE VKGENQRTKV IVPDSAHGTN PASASMAGFQ 

       190        200        210        220        230        240 
VVEIKSNDNG IIDLDNLEAA LDESVAAIML TNPNTLGLFE KDIIKIAEMA HKNGTLLYYD 

       250        260        270        280        290        300 
GANLNAIMGK VRPGDMGFDI VHLNLHKTFS TPHGMGGPGS GPVGVKGHLK EFLPIPVVDL 

       310        320        330        340        350        360 
TDEGYILKTD LSHSIGRIRS FYGNFGVVVK ALAYILMLGK DGLTYASEIA VLNANYLRTR 

       370        380        390        400        410        420 
LSELIPTAYP GLCKHEFVLD GTKLVKEYGI KTLDLAKRML DYGVHPPTIY FPLIVHEALM 

       430        440        450        460        470        480 
IEPTETENKD NLDHFVEVVK KILEEAKKDP EFVKNAPYNT PIKRLDEVTA SRKPKVRWIP 


KEQ 

« Hide

References

[1]"Complete sequence of Thermotogales bacterium TBF 19.5.1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Noll K.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TBF 19.5.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001634 Genomic DNA. Translation: ACR80309.1.
RefSeqYP_002941313.1. NC_012785.1.

3D structure databases

ProteinModelPortalC5CF44.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521045.Kole_1619.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR80309; ACR80309; Kole_1619.
GeneID7967853.
KEGGkol:Kole_1619.
PATRIC22188556. VBIKosOle109242_1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycKOLE521045:GHRV-1658-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_KOSOT
AccessionPrimary (citable) accession number: C5CF44
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 31 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