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

B8GN14 (GCSPB_THISH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:Tgr7_2755
OrganismThioalkalivibrio sp. (strain HL-EbGR7) [Complete proteome] [HAMAP]
Taxonomic identifier396588 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio

Protein attributes

Sequence length496 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 – 496496Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000148002

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8GN14 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 23D25911406EF20B

FASTA49654,429
        10         20         30         40         50         60 
MLIFERSRPG RGATAQAPLR EATVSGLPER FRRGTRAPLP ELSELDVVRH YTRLSQKNFS 

        70         80         90        100        110        120 
IDTQFYPLGS CTMKYNPRAC NSLAMLPGFL GRHPHAPDTH SQGFLACMFE LQEMLRDVTG 

       130        140        150        160        170        180 
MKGGVSLTPM AGAQGEFAGV AMIRAYHDAR KDTARTEILV PDAAHGTNPA TATMCGYTVK 

       190        200        210        220        230        240 
EIPTDDSGDV DMEALKAALG PHTAGIMLTN PSTLGVFERR IKEIADLVHQ AGGLLYYDGA 

       250        260        270        280        290        300 
NLNAILGKVR PGDMGFDVIH MNLHKTFSTP HGGGGPGAGA VGVSERLRPF MPIPVVAKEG 

       310        320        330        340        350        360 
ERYRFMTEKD LPQSIGRLSA FAGNAGVLLR AYVYMRMLGR AGMPRVAEFS TLNANYVMAR 

       370        380        390        400        410        420 
LREKGFELAF PGRRATHEFI VTLKRLAKDT EVTAMDVAKR LLDFNYHAPT TYFPLLVPEC 

       430        440        450        460        470        480 
LLIEPTETES KETLDGFVEA MAEILEEART SPDKVKGAPY TQPNRRFDEV RAARELDVAW 

       490 
RPGAALDEVA EQGRTD 

« Hide

References

[1]"Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7."
Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.
Stand. Genomic Sci. 4:23-35(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HL-EbGR7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001339 Genomic DNA. Translation: ACL73829.1.
RefSeqYP_002514816.1. NC_011901.1.

3D structure databases

ProteinModelPortalB8GN14.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396588.Tgr7_2755.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL73829; ACL73829; Tgr7_2755.
GeneID7316917.
KEGGtgr:Tgr7_2755.
PATRIC23965014. VBIThiSp19295_2728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
KOK00283.
OMAMHINLHK.
OrthoDBEOG6HMXDX.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycTSUL396588:GH5B-2799-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_THISH
AccessionPrimary (citable) accession number: B8GN14
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 37 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