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A5IKK7 (GCSPB_THEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Tpet_0710
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length474 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 – 474474Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000045708

Amino acid modifications

Modified residue2621N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IKK7 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 909C0B921F7CD7DF

FASTA47453,530
        10         20         30         40         50         60 
MTIFERSKKG RKAFRLPESD IPEYSLPNRF LRRTPPELPE VSEPDVVRHY TDLARKNYSV 

        70         80         90        100        110        120 
DRGIYPLGSC TMKYNPKLNE KVANLEGFRE IHPYQPAETV QGSLRLMYEL KEMLCEITGM 

       130        140        150        160        170        180 
DDMTLQPAAG AHGELTGMLI VREYFKSRGD TGRKKVLVPD SAHGTNPASA SMVGFEVVEI 

       190        200        210        220        230        240 
KSKNGMVDVE DLKKLLDEEV AAVMLTNPNT LGLFEKDILK IAEMTHECGA LLYYDGANLN 

       250        260        270        280        290        300 
AVMGKVRPGD MGFDIVHLNL HKTFSTPHGM GGPGSGPVGV KKHLVDFLPF PQVRKNGELY 

       310        320        330        340        350        360 
ELFVPEKTIG RVRSFFGNFP VLVKAYTYIL TMGRDGLERV SEMAVLNANY LKKKIEKFLE 

       370        380        390        400        410        420 
IPYNGFCMHE FVASAEKVFR ETGVRTLDIA KRILDFGVHP PTVYFPLIVL EALMIEPTET 

       430        440        450        460        470 
ENKETLDKYA EILERVVKEA YENPDVLKNA PHNTPVRRVD EVLASKKPVF RWRG 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ46730.1.
RefSeqYP_001244306.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5IKK7.
SMRA5IKK7. Positions 2-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_0710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ46730; ABQ46730; Tpet_0710.
GeneID5170610.
KEGGtpt:Tpet_0710.
PATRIC23944184. VBIThePet65348_0717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycTPET390874:GHJI-726-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_THEP1
AccessionPrimary (citable) accession number: A5IKK7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 51 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