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

Q9HII2 (GCSPB_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:Ta1357
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length472 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_0000167033

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HII2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F964E65C0517D872

FASTA47252,839
        10         20         30         40         50         60 
MEFRQAYYDE PLIKDIKSDT SFKLSEDVDE NLLPQDMRRT DLKLPQVSEV DVVRHYTRLS 

        70         80         90        100        110        120 
QMNYTVDVGI YPLGSCTMKY NPKYADRIAS FAEFRNIHPF QPESTVQGTL QIMYELQEFL 

       130        140        150        160        170        180 
KKISDMDAVT LQPMAGADGE FTGILIIKKY FEDLHEDRTE IIVPDSAHGT NPASATMGGF 

       190        200        210        220        230        240 
DVVEIPSNSE GMVDLNALKA AISKKTAALM ITNPNTLGIF EQNITEIAKI LHDAGALLYY 

       250        260        270        280        290        300 
DGANLNAIFG ITSPGLMGFD IVHFNLHKSF ATPHGGGGPG AGPVAVKSFL SDFLPVPVVG 

       310        320        330        340        350        360 
YDGKRYFLDY GKKKSIGRVS SFYGSFSILL RAWSYVIRNG DDGLKNATIR AVLNSNYLKK 

       370        380        390        400        410        420 
KVEGYYEVPY YPLKKHEFVL STEKTGRRAL DIGKYLLDFG IHSPTVYFPL IVKEAMMIEP 

       430        440        450        460        470 
TETVSKDDLD RYADVLISAL KVPEDDLKSR PRNTAVSRID EVKAARDLKV RW 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445067 Genomic DNA. Translation: CAC12478.1.
RefSeqNP_394813.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HII2.
SMRQ9HII2. Positions 11-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta1357.

Proteomic databases

PRIDEQ9HII2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12478; CAC12478; CAC12478.
GeneID1456828.
KEGGtac:Ta1357.

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAMHINLHK.
ProtClustDBPRK04366.

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_THEAC
AccessionPrimary (citable) accession number: Q9HII2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 72 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