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B4SB96 (GCSPB_PELPB) 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:Ppha_0179
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length482 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 – 482482Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132503

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4SB96 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: FB92B9F264D0EBEE

FASTA48252,734
        10         20         30         40         50         60 
MREKLIFELS RKGRKGYSLS GNELPEQPLE NIIPSKYLRT TPAELPEVAE SEVVRHFVRL 

        70         80         90        100        110        120 
SNLNYHVDKN MYPLGSCTMK YNPKINDYTC DLPGFSALHP LQPGETTQGA LQLMFELAEM 

       130        140        150        160        170        180 
LREIAGMAAV TLQPAAGAHG ELTGILLIKK YHESIGSKRH KLLVVDSAHG TNPASAALAG 

       190        200        210        220        230        240 
YDIISVKGNA DGRTDLDDLR SKLDGDVAAL MLTNPNTIGL FETEILAISK MVHDNGSLLY 

       250        260        270        280        290        300 
MDGANMNALL GITRPGDMGF DVVHYNLHKT FAAPHGGGGP GSGPVGVSEK LIPFLLVPVI 

       310        320        330        340        350        360 
VKEGTTYKLS YDRPESIGRM MNFYGNFAVL VRAYTYIRML GPDGLRRVSE NAIINANYLL 

       370        380        390        400        410        420 
SLLLESYDLP YPKPVMHEFC LSGDRQKKAH GVKTLDIAKR LLDYGFHAPT IYFPLIVSEA 

       430        440        450        460        470        480 
LMIEPTETES KETLDVFAQA LLSIADEAAN NPALVTSAPV TTPVKRLDDA MASRQLNICC 


SL 

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
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., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001110 Genomic DNA. Translation: ACF42517.1.
RefSeqYP_002017134.1. NC_011060.1.

3D structure databases

ProteinModelPortalB4SB96.
SMRB4SB96. Positions 4-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324925.Ppha_0179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF42517; ACF42517; Ppha_0179.
GeneID6462296.
KEGGpph:Ppha_0179.
PATRIC22900782. VBIPelPha134556_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPPHA324925:GHBF-190-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_PELPB
AccessionPrimary (citable) accession number: B4SB96
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 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