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

C3MUU9 (GCSPB_SULIM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. 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:M1425_1304
OrganismSulfolobus islandicus (strain M.14.25 / Kamchatka #1) [Complete proteome] [HAMAP]
Taxonomic identifier427317 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length509 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 – 509509Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000212676

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C3MUU9 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 2181A9B4FA39ABD2

FASTA50956,584
        10         20         30         40         50         60 
MVWRQAKWDE PLIFELNNSG ANRQGLLINK DDEIRSEIKE MKIPKNLLRE NGPNLPSLSE 

        70         80         90        100        110        120 
LEVVRHFIRL SQMNFGVDVG IMPLGSCTMK YNPKIEEKAT AITESHHPLE DEDHVQGILE 

       130        140        150        160        170        180 
MIYELQNWFS EITGMDECSL QVPAGSAGEF AGVLMIKKYH EDHNRNYKDT MLVADTAHGT 

       190        200        210        220        230        240 
NPASAAMAGY KVMYVKSNGE GLVDMDILRE IVNDKTAGFM LTNPNTLGLF EENILEISKI 

       250        260        270        280        290        300 
IHSANAILYY DGANLNGVLG IARPGDMGFD IVHLNLHKTF AVPHGGGGPG AGAICAKGEL 

       310        320        330        340        350        360 
VNYLPYPMVE KVNGKYRLSK IPKNSVGKIA TFYGNVGNLA RSFAYLLGLG PQGVQMVGKM 

       370        380        390        400        410        420 
STLATNYLIA KLRDIKELEL IAPNRHRKHE VVFSVKQLME NYGVSANDVA KALLDSGFYA 

       430        440        450        460        470        480 
PTIYFPPIIE EALMIEPTET ESKETLDMFA EALKKIVEDA KRNPEQLLKS PSNTSIARLD 

       490        500 
QAYANHPSTI TPTYRVLKLR RMGKINYLK 

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M.14.25 / Kamchatka #1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001400 Genomic DNA. Translation: ACP38059.1.
RefSeqYP_002829357.1. NC_012588.1.

3D structure databases

ProteinModelPortalC3MUU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING427317.M1425_1304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP38059; ACP38059; M1425_1304.
GeneID7793742.
KEGGsia:M1425_1304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycSISL427317:GI7C-1339-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_SULIM
AccessionPrimary (citable) accession number: C3MUU9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 31 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