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B8FT30 (B8FT30_DESHD) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713

EC=1.4.4.2 HAMAP-Rule MF_00713
Alternative name(s):
Glycine cleavage system P-protein subunit 2 HAMAP-Rule MF_00713
Glycine decarboxylase subunit 2 HAMAP-Rule MF_00713
Glycine dehydrogenase (aminomethyl-transferring) subunit 2 HAMAP-Rule MF_00713
Gene names
Name:gcvPB HAMAP-Rule MF_00713
Ordered Locus Names:Dhaf_4036 EMBL ACL22046.1
OrganismDesulfitobacterium hafniense (strain DCB-2 / DSM 10664) [Complete proteome] [HAMAP] EMBL ACL22046.1
Taxonomic identifier272564 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

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 SAAS SAAS020580

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 SAAS SAAS020580

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713 SAAS SAAS020580

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. HAMAP-Rule MF_00713 SAAS SAAS020580

Sequence similarities

Belongs to the GcvP family. C-terminal subunit subfamily. HAMAP-Rule MF_00713

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00713

Sequences

Sequence LengthMass (Da)Tools
B8FT30 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: B946D5E95465B448

FASTA48753,961
        10         20         30         40         50         60 
MRALEPLIFE LSREGRTGVS LPSCDVPEIP LEDLIPQEFL RDKEPELPEV SEVDVVRHFT 

        70         80         90        100        110        120 
RLSSFNHGVD TGFYPLGSCT MKYNPKVNEK LARLPGFSQI HPYQPEELTQ GALGLMVELQ 

       130        140        150        160        170        180 
EELAEITGMD AFTLQPAAGA HGEMTGILII KAYHDHRQDV KRRKVIVPDS AHGTNPATGA 

       190        200        210        220        230        240 
MAGYDIVQVP SNERGGVDIE ALRQVANDEV AALMLTNPNT LGLFDENILE IAEIIHSVGG 

       250        260        270        280        290        300 
LIYYDGANAN AIMGIARPGD MGFDVVHLNL HKTFSTPHGG GGPGSGPVGV KEFLAPYLPK 

       310        320        330        340        350        360 
PVAIRTPEGR YSWDEDRPLS IGRVRAFQAN FGVLVKAYAY IRALGGEGLK AASQNAVLNA 

       370        380        390        400        410        420 
NFLMSILKEH YHLPYDRVCM HEFIITPKNL KNYGIHTLDI AKRLLDYGYH PPTIYFPLIV 

       430        440        450        460        470        480 
EEAMMIEPTE TESLETLEQF ARVMIQIAEE VKQDAEMVKN APHDTLVTRL DETGAARKPD 


LRWRKPQ 

« Hide

References

[1]"Complete sequence of Desulfitobacterium hafniense DCB-2."
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., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Madsen T., Christiansen N., Ahring B., Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DCB-2 / DSM 10664.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001336 Genomic DNA. Translation: ACL22046.1.
RefSeqYP_002460482.1. NC_011830.1.

3D structure databases

ProteinModelPortalB8FT30.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272564.Dhaf_4036.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL22046; ACL22046; Dhaf_4036.
GeneID7261056.
KEGGdhd:Dhaf_4036.
PATRIC21666081. VBIDesHaf15223_4197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDHAF272564:GCV8-4112-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 nameB8FT30_DESHD
AccessionPrimary (citable) accession number: B8FT30
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: March 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)