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

O67740 (GCSPB_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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
Synonyms:gcsP1
Ordered Locus Names:aq_1903
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000166993

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O67740 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: D4D2BE9C407992EE

FASTA48254,973
        10         20         30         40         50         60 
MELIFEKSKK GRKGYKLPEL DVEEVNIKEY LPEEYLREEL DFPEVSELDV VRHYTNLSHL 

        70         80         90        100        110        120 
NYAVDTTMVP LGSCTMKYNP RINEELVNKK EFLNVHPLTP EEYIQPLLKL VYELKELLKE 

       130        140        150        160        170        180 
LGGFAEVSLQ PAAGAHGELL GLLLIHAYHQ DRGNKEKKVV LIPDSAHGTN PASAAICGFD 

       190        200        210        220        230        240 
IKVVKSDKKG ELDFEDFIKK LDERVAALMI TNPNTLGIFE RKIKEIAEEL HKRDALLYMD 

       250        260        270        280        290        300 
GANFNALVGR FKPGEWGVDV MHFNLHKTFS TPHGGGGPGA GPVGVSERLK PYLPVPQIEY 

       310        320        330        340        350        360 
DGKKYYLNWN IEKSVGKILA FHGHFLVWLK ALAYILTYGK DIKKVSEYAV LNARYLKHLL 

       370        380        390        400        410        420 
KGVFKDPYPE SPCMHEFVLS ATNLTKYGVR ASDVAKRILD YGFYAPTMYF PLIVREALMI 

       430        440        450        460        470        480 
EPTETENPDT LKKFALILRK IVKEAKEKPE ILKKAPHRTP VRRIKEAEAN RNLILKFKDI 


KE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07701.1.
PIRH70463.
RefSeqNP_214308.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67740.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07701; AAC07701; aq_1903.
GeneID1193545.
KEGGaae:aq_1903.
PATRIC20960746. VBIAquAeo85532_1474.

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1363-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_AQUAE
AccessionPrimary (citable) accession number: O67740
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 79 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