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B1YLN8 (GCSPB_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:Exig_0891
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length492 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 – 492492Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000132500

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YLN8 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 96ECCA89C1577794

FASTA49253,845
        10         20         30         40         50         60 
MHKTSEQTLI FEISKAGRVA YSLPLPTVDE VAAEELLPAH LLRQEDVELP EVSELDLVRH 

        70         80         90        100        110        120 
YTALSNRNHG VDSGFYPLGS CTMKYNPKIN EDMARLPGFA HIHPLQPVES VQGALGLMYD 

       130        140        150        160        170        180 
LQEKLAVITG MDEVTLQPAA GAHGEWTGLM LIKAYHHARG DFKRTKVLVP DSAHGTNPAS 

       190        200        210        220        230        240 
ASVAGFDTVT VLSDERGLVD LADLKSKVGE DTAALMLTNP NTLGLFESDI VEIAKAVHEA 

       250        260        270        280        290        300 
GGKLYYDGAN SNAIMGIARP GDMGFDVVHL NLHKTFTGPH GGGGPGSGPV GVKKDLIPYL 

       310        320        330        340        350        360 
PKPIVAKTAE GFVLDYDRPE SIGRVKPFYG NFGINVRAYS YIRTMGGAGL ARVSKEAVLN 

       370        380        390        400        410        420 
ANYMLARLKG AYDAPYDVYC KHEFVLSGRR QKALGVRTLD IAKRLLDFGY HPPTIYFPLN 

       430        440        450        460        470        480 
VEECIMIEPT ETESKETLDD FCDAMLQIAK EVEETPDVVL NAPHTTVVKR MDETLAARKP 

       490 
ILRYQPKQEV HV 

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001022 Genomic DNA. Translation: ACB60371.1.
RefSeqYP_001813388.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YLN8.
SMRB1YLN8. Positions 8-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262543.Exig_0891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB60371; ACB60371; Exig_0891.
GeneID6172913.
KEGGesi:Exig_0891.
PATRIC32135363. VBIExiSib53410_0907.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycESIB262543:GHBP-967-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00713. GcvPB.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020581. GDC_P.
IPR023012. GDC_P_su2.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSPB_EXIS2
AccessionPrimary (citable) accession number: B1YLN8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 42 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