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B3EEC8 (GCSPB_CHLL2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Clim_0163
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length486 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 – 486486Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132496

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EEC8 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: DF6C9ED29002A2E3

FASTA48653,191
        10         20         30         40         50         60 
MIEKLIFDLS REGRKGYSLS GNDIPELSIE TVLPAKFLRT EPADLPEVPE SEVVRHFIRL 

        70         80         90        100        110        120 
SNMNYHVDKN MYPLGSCTMK YNPKVNDAAC DLAGFSELHP LQPEKTVQGA LQMMYELSGM 

       130        140        150        160        170        180 
LAEIAGMSAV TLQPAAGAHG ELTGILLIKK YHEARGSKRS KLLVVDSAHG TNPASAAIAG 

       190        200        210        220        230        240 
YEIISVSSNA DGRTDLGDLK AKLDGEVAAL MLTNPNTIGL FEKDILTIAQ MVHENGSLLY 

       250        260        270        280        290        300 
MDGANMNALL GITRPGDMGF DVVHYNLHKS FSAPHGGGGP GSGPVGVCEK LIPYLPVPVI 

       310        320        330        340        350        360 
ERIETPEGSS FRLNTDHPES IGRMMNFYGN FSVLIRAYTY IRMLGATGLR RVSENAIINA 

       370        380        390        400        410        420 
NYLLSRLDSR YDLPYPKPVL HEFCLSGDRQ KKAHGVKTLD IAKRLLDYGY HAPTIYFPLI 

       430        440        450        460        470        480 
VSEALMIEPT ETETRETLDL FAEALLCIAD EAENSPDLLR SAPVNTPVKR LDEAQASRQL 


NICCQG 

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001097 Genomic DNA. Translation: ACD89262.1.
RefSeqYP_001942241.1. NC_010803.1.

3D structure databases

ProteinModelPortalB3EEC8.
SMRB3EEC8. Positions 4-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290315.Clim_0163.

Proteomic databases

PRIDEB3EEC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD89262; ACD89262; Clim_0163.
GeneID6356133.
KEGGcli:Clim_0163.
PATRIC21372253. VBIChlLim118737_0185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCLIM290315:GHUH-175-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_CHLL2
AccessionPrimary (citable) accession number: B3EEC8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 40 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