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

A4J2F9 (GCSPB_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Dred_0723
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length484 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 – 484484Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000072771

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4J2F9 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: DF3EA3E9F8930C33

FASTA48453,106
        10         20         30         40         50         60 
MTEKLIFELG SPGRQGVLFP ANDVPEIPPH ELLPRDLIRE QEVPLPEVSE GDAVRHFVRL 

        70         80         90        100        110        120 
SRMNFGVDVG FYPLGSCTMK YNPKVAEDAA GLSGFANIHP YQPDEISQGA LQLMYETQQD 

       130        140        150        160        170        180 
LAEITGMDAF TLQPAAGAQG ELTGMLIIKA YLESKGETGR NKVIVPDSAH GTNPATAALC 

       190        200        210        220        230        240 
GFKVVEVKSD QRGGVDLAAL KQLLGPDVAA LMLTNPSTLG LFEDNITEIA ALVHQAGGLL 

       250        260        270        280        290        300 
YYDGANLNAI MGYARPGDMG FDVVHLNLHK TFGTPHGGGG PGSGPVGVKA ELAPFLPKPV 

       310        320        330        340        350        360 
IIQREGNYLP DYHRPQSIGR VKAFFANFSV IVKAYTYLRS LGGKGLKEVS EHAVLNANYL 

       370        380        390        400        410        420 
MKQLSDHFRV PYQRTCMHEF VVSPPEDMKE QGIKTLDIAK RLLDYGYHPP TVYFPLIVEE 

       430        440        450        460        470        480 
ALMFEPTETE SKETLDEFAH NLIKVLAEAR ENPDKLRNAP YTTPIRRLDE VMAARKPLVG 


WFPE 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO49262.1.
RefSeqYP_001112087.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J2F9.
SMRA4J2F9. Positions 4-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349161.Dred_0723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO49262; ABO49262; Dred_0723.
GeneID4957321.
KEGGdrm:Dred_0723.
PATRIC21727429. VBIDesRed82656_0802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycDRED349161:GHP6-766-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_DESRM
AccessionPrimary (citable) accession number: A4J2F9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 50 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