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Q8XD33 (GCSP_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:
Glycine dehydrogenase (decarboxylating)

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P-protein
Glycine decarboxylase
Glycine dehydrogenase (aminomethyl-transferring)
Gene names
Name:gcvP
Ordered Locus Names:Z4240, ECs3774
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length957 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_00711

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_00711

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00711

Subunit structure

The glycine cleavage system is composed of four proteins: P, T, L and H By similarity.

Sequence similarities

Belongs to the GcvP family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 957956Glycine dehydrogenase (decarboxylating) HAMAP-Rule MF_00711
PRO_0000166915

Amino acid modifications

Modified residue7081N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XD33 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 026A17DFFA1C150D

FASTA957104,347
        10         20         30         40         50         60 
MTQTLSQLEN SGAFIERHIG PDAAQQQEML NAVGAQSLNA LTGQIVPKDI QLATPPQVGA 

        70         80         90        100        110        120 
PATEYAALAE LKAIASRNKR FTSYIGMGYT AVQLPPVILR NMLENPGWYT AYTPYQPEVS 

       130        140        150        160        170        180 
QGRLEALLNF QQVTLDLTGL DMASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVASDVH 

       190        200        210        220        230        240 
PQTLDVVRTR AETFGFEVIV DDAQKVLDHQ DIFGVLLQQV GTTGEIHDYT ALISELKSRK 

       250        260        270        280        290        300 
IVVSVAADIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEYKRSMPGR 

       310        320        330        340        350        360 
IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPIGLKRI 

       370        380        390        400        410        420 
ANRIHRLTDI LAAGLQQKGL KLRHAHYFDT LCVEVADKAG VLARAEAAEI NLRSDILNAV 

       430        440        450        460        470        480 
GITLDETTTR ENVMQLFSVL LGDNHGLDID TLDKDVAHDS RSIQPAMLRD DEILTHPVFN 

       490        500        510        520        530        540 
RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE 

       550        560        570        580        590        600 
QAEGYQQMIA QLADWLVKLT GYDAVCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI 

       610        620        630        640        650        660 
PASAHGTNPA SAHMAGMQVV VVACDKNGNI DLTDLRAKAE QAGDNLSCIM VTYPSTHGVY 

       670        680        690        700        710        720 
EETIREVCEV VHQFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG 

       730        740        750        760        770        780 
MGPIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAEGLKK 

       790        800        810        820        830        840 
ASQVAILNAN YIASRLQDAF PVLYTGRDGR VAHECILDIR PLKEETGISE LDIAKRLIDY 

       850        860        870        880        890        900 
GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIDQVKAGVW PLEDNPLVNA 

       910        920        930        940        950 
PHIQSELVAE WAHPYSREVA VFPAGVADKY WPTVKRLDDV YGDRNLFCSC VPISEYQ 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58030.1.
BA000007 Genomic DNA. Translation: BAB37197.1.
PIRB85946.
F91100.
RefSeqNP_289471.1. NC_002655.2.
NP_311801.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8XD33.
SMRQ8XD33. Positions 17-441, 461-952.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58030; AAG58030; Z4240.
BAB37197; BAB37197; BAB37197.
GeneID916407.
961098.
KEGGece:Z4240.
ecs:ECs3774.
PATRIC18357035. VBIEscCol44059_3696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239369.
KOK00281.
OMAFDSRPYS.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3742-MONOMER.
ECOO157:GCVP-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 2 hits.
HAMAPMF_00711. GcvP.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMSSF53383. SSF53383. 3 hits.
TIGRFAMsTIGR00461. gcvP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSP_ECO57
AccessionPrimary (citable) accession number: Q8XD33
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 75 of the entry and version 3 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