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Q5SKW7 (GCSPB_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TTHA0526
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 474474Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000045709

Amino acid modifications

Modified residue2661N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

................................................................................. 474
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SKW7 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A8B48175AF156C1D

FASTA47452,709
        10         20         30         40         50         60 
MSFPLIFERS RKGRRGLKLV KAVPKAEDLI PKEHLREVPP RLPEVDELTL VRHYTGLSRR 

        70         80         90        100        110        120 
QVGVDTTFYP LGSCTMKYNP KLHEEAARLF ADLHPYQDPR TAQGALRLMW ELGEYLKALT 

       130        140        150        160        170        180 
GMDAITLEPA AGAHGELTGI LIIRAYHEDR GEGRTRRVVL VPDSAHGSNP ATASMAGYQV 

       190        200        210        220        230        240 
REIPSGPEGE VDLEALKREL GPHVAALMLT NPNTLGLFER RILEISRLCK EAGVQLYYDG 

       250        260        270        280        290        300 
ANLNAIMGWA RPGDMGFDVV HLNLHKTFTV PHGGGGPGSG PVGVKAHLAP YLPVPLVERG 

       310        320        330        340        350        360 
EEGFYLDFDR PKSIGRVRSF YGNFLALVRA WAYIRTLGLE GLKKAAALAV LNARYLKELL 

       370        380        390        400        410        420 
KEKGYRVPYD GPSMHEFVAQ PPEGFRALDL AKGLLELGFH PPTVYFPLIV KEALMVEPTE 

       430        440        450        460        470 
TEAKETLEAF AEAMGALLKK PKEWLENAPY STPVRRLDEL RANKHPKLTY FDEG 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia."
Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N.
EMBO J. 24:1523-1536(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD70349.1.
RefSeqYP_143792.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYTX-ray2.40B/D1-474[»]
1WYUX-ray2.10B/D/F/H1-474[»]
1WYVX-ray2.40B/D/F/H1-474[»]
ProteinModelPortalQ5SKW7.
SMRQ5SKW7. Positions 2-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70349; BAD70349; BAD70349.
GeneID3168946.
KEGGttj:TTHA0526.
PATRIC23956027. VBITheThe93045_0524.

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.
PhylomeDBQ5SKW7.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-551-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...

Other

EvolutionaryTraceQ5SKW7.

Entry information

Entry nameGCSPB_THET8
AccessionPrimary (citable) accession number: Q5SKW7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 66 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references