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B7GHD4 (B7GHD4_ANOFW) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 41. 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 EMBL ACJ33295.1
Ordered Locus Names:Aflv_0917 EMBL ACJ33295.1
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP] EMBL ACJ33295.1
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeAnoxybacillus

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 SAAS SAAS020581

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713 SAAS SAAS020581

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 SAAS020581

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
B7GHD4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: A14A17188D34A2A3

FASTA48453,803
        10         20         30         40         50         60 
MHKDQPLIFE LSKPGRIGYS LPKLDVPAID VAQVIPTDYI RQEAPELPEV SELDIMRHYT 

        70         80         90        100        110        120 
ALSKRNHGVD SGFYPLGSCT MKYNPKINEN VARFAGFAHI HPLQPEETVQ GALELMYDLQ 

       130        140        150        160        170        180 
EHLKEITGMD AVTLQPAAGA HGEWTGLMMI RAYHEANGDY NRTKVIVPDT AHGTNPASAT 

       190        200        210        220        230        240 
VAGFETVTVK STEEGLVDLD DLRRVVGPDT AALMLTNPNT LGLFEENILE MAEIVHAAGG 

       250        260        270        280        290        300 
KLYYDGANLN AVLSKARPGD MGFDVVHLNL HKTFTGPHGG GGPGSGPVGV KADLIPFLPK 

       310        320        330        340        350        360 
PTVEKGENGY YFDYDRPQAI GRVKPFYGNF GINVRAYTYI RSMGPDGLKA VTEYAVLNAN 

       370        380        390        400        410        420 
YMMRRLAEYY DLPYNRHCKH EFVLSGKRQK KLGVRTLDIA KRLLDFGYHP PTIYFPLIVE 

       430        440        450        460        470        480 
ECMMIEPTET ESKETLDAFI DAMIQIAKEA EETPEIVQEA PHTTVVKRLD ETTAARKPIL 


RYQK 

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References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:R161-R161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21510 / WK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000922 Genomic DNA. Translation: ACJ33295.1.
RefSeqYP_002315280.1. NC_011567.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING491915.Aflv_0917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ33295; ACJ33295; Aflv_0917.
GeneID7037175.
KEGGafl:Aflv_0917.
PATRIC20953655. VBIAnoFla45531_0937.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycAFLA491915:GHEO-993-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 2 hits.
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 nameB7GHD4_ANOFW
AccessionPrimary (citable) accession number: B7GHD4
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)