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A6LP69 (GCSPB_THEM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Tmel_1887
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP]
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length481 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 – 481481Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000045707

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LP69 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: E620A2A7190D3AF9

FASTA48154,036
        10         20         30         40         50         60 
MTIFELSKEG RKAYNLPKNN IKDYGFDFPN HLMRGKEPRL PQVSELDIVR HYTNLAAKNY 

        70         80         90        100        110        120 
AVDVGFYPLG SCTMKYNPKI NEKLASLEGF TMIHPCQPRE VTQGALQLMY ELKEMLCEIS 

       130        140        150        160        170        180 
GMDDMTLIPS AGAHGELTGM LIARAYHLSR GDTKRKKAIV PDSAHGTNPA SAMMAGFEVV 

       190        200        210        220        230        240 
ELKSGKDGRI DLEELEKHLD DEVAVLLLTN PNTLGLFEKD IIKIAETVHK HGALLYYDGA 

       250        260        270        280        290        300 
NLNAILGRTR PGDMGFDIVH LNLHKTFSTP HGMGGPGSGP VGVKKHLAKF LPIPEIIKES 

       310        320        330        340        350        360 
DVYKFNYNKS ESIGFIRSFY GNFSVLVRAY VYIKTMGNDG LKKVGQMAVL NANYLRKKVS 

       370        380        390        400        410        420 
KIMDIAYPDM CMHEFVATCE KLTKETGVKA LDIAKRLLDY GIHAPTMYFP LIVHEDFMIE 

       430        440        450        460        470        480 
PTETESKDTL DEFTKILEKI FIEAKENPEL VKNAPYTTPV RRLDEASASR KPIVKYNFEE 


E 

« Hide

References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR31720.1.
RefSeqYP_001307105.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LP69.
SMRA6LP69. Positions 2-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_1887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR31720; ABR31720; Tmel_1887.
GeneID5297775.
KEGGtme:Tmel_1887.
PATRIC23925089. VBITheMel19269_1957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-1950-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_THEM4
AccessionPrimary (citable) accession number: A6LP69
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 50 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