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B4S3N4 (GCSPB_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:Paes_0171
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length487 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 – 487487Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132504

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S3N4 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 9C34BE7D8D69077A

FASTA48754,093
        10         20         30         40         50         60 
MKETLIFDLS RKGRQGHRIA SLDIEPQPAI NLIPEKFLRT EPADLPEVPE SEVVRHFIRL 

        70         80         90        100        110        120 
SNLNHHVDKD MYPLGSCTMK YNPKINDQTA DIAGFTSIHP LQPAETAQGT LQLMYELGEM 

       130        140        150        160        170        180 
LREIAGMAAI TLQPAAGAHG ELTGILMIRK YHDSRASKRT KLLVVDSAHG TNPASAALVG 

       190        200        210        220        230        240 
YDILSVKSNA EGRTDIEDLK AKLDENVAAL MLTNPNTIGL FEKDIKEIEQ LVHDNGSLLY 

       250        260        270        280        290        300 
MDGANMNALM GITRPGDMGF DIVHYNLHKT FSAPHGGGGP GSGPVGVCDK LKPYLPVPVI 

       310        320        330        340        350        360 
EKHDDGNTSR YTLTTDRPLS IGRMMNFYGN FSVMVRAYTY IRMLGAEGIR RVSENAIINA 

       370        380        390        400        410        420 
NYLLSKLIDR YDLPYPKPVM HEFCLSGDRQ KKQHNVRTLD IAKRLLDLGF HAPTIYFPLI 

       430        440        450        460        470        480 
VSEALMIEPT ETETRETLDR FAEAMLQIAD ETENSPETVQ NAPQFTPVKR LDEAQASRKL 


NICCPGC 

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References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
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., Anderson I., 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 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF45230.1.
RefSeqYP_002014877.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S3N4.
SMRB4S3N4. Positions 4-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290512.Paes_0171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF45230; ACF45230; Paes_0171.
GeneID6460428.
KEGGpaa:Paes_0171.
PATRIC23039944. VBIProAes37017_0177.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAKPVMHEF.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycPAES290512:GHUT-178-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_PROA2
AccessionPrimary (citable) accession number: B4S3N4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 42 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