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

Q0AEQ0 (GCSPB_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Neut_1952
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

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_1000045699

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AEQ0 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: F60634E9959D10CD

FASTA48353,271
        10         20         30         40         50         60 
MLIFEHSRKN RLNYSQAPAT RPAKNNIPDN LKRKSAPLLP EVSEMDTVRH YTRLSQKNFS 

        70         80         90        100        110        120 
IDTEFYPLGS CTMKYNPRAC NALAMLPQFL SRHPLAPEDT GQGFLACMYE LQEILKDVTG 

       130        140        150        160        170        180 
MSAVSLTSMA GAQGELIGIT MIRAYHEARG DTERTEIIIP DAAHGTNPAT AVMCGYKVIE 

       190        200        210        220        230        240 
IPTDRDGDVD MEALKAAVSP RTAGLMLTNP STLGVFEKKV AEMSRVVHEA GGLLYYDGAN 

       250        260        270        280        290        300 
LNAVLGKVKP GDMGFDVIHM NLHKTFSTPH GGGGPGAAPV GVADCLLPYL PIPIVAHEQG 

       310        320        330        340        350        360 
VYRWLTEKDR PQSIGRLSAH MGNAGVLLRA YIYVRLLGAE GMFRIAEYAT LNANYLLAEL 

       370        380        390        400        410        420 
RKLGFEIAYP SRRASHEFIV TMKEIKDKTG VTAMHLAKRL LDKGFHAPTV YFPLLVPECL 

       430        440        450        460        470        480 
LIEPAETESK ETLDRFVVAM KEILDEIDTQ PEMVKTAPHN MPLRKIDDVK AARELDLVWN 


PAG 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI60182.1.
RefSeqYP_748147.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AEQ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_1952.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI60182; ABI60182; Neut_1952.
GeneID4273339.
KEGGnet:Neut_1952.
PATRIC22721458. VBINitEut7577_2375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycNEUT335283:GHT6-1991-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_NITEC
AccessionPrimary (citable) accession number: Q0AEQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 57 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