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

A7HLP1 (GCSPB_FERNB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Fnod_0974
OrganismFervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1) [Complete proteome] [HAMAP]
Taxonomic identifier381764 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeFervidobacterium

Protein attributes

Sequence length477 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 – 477477Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000072772

Amino acid modifications

Modified residue2641N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HLP1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: D570DF44D8D4FD3B

FASTA47753,430
        10         20         30         40         50         60 
MTIFEKSTSG RKGYELPEYE LPSVDCGIPE HLVRKEKPLL PEVSEVDVVR HYTELASKNY 

        70         80         90        100        110        120 
SVDKGFYPLG SCTMKYNPKI NEDMAMLFTQ LHPMQPRETI QGAIDLMGHL KEMLCEITGT 

       130        140        150        160        170        180 
DDMTLQPAAG AHGELTGLLV ARAYFEDKGE LDKRRKVLVP DSAHGTNPAS AAMAGFEVVE 

       190        200        210        220        230        240 
LKSGKDGCVN LEELKAHLDE NVAVIMLTNP NTLGLFEKDI LTIAKMAHEV GALLYYDGAN 

       250        260        270        280        290        300 
LNAIMGRTRP GDMGFDIVHL NLHKTFSTPH GMGGPGSGPI GVKKHLAPYL PVPVIRKAGE 

       310        320        330        340        350        360 
KYDLDYNLPK SIGMVRSFYG NFTVMVKAYT YILTMGNKGL KHVSDMAVLN ANYLRAKLSK 

       370        380        390        400        410        420 
IYKVAYDRIC MHEFVIDNEE FVKKTGVKTL DIAKRLLDYG LHAPTVYFPL IVHEAMMIEP 

       430        440        450        460        470 
TETESKRTLD EFIDAMEKIY NEAIENPELV KKAPYKTPIR RLDDVNATKY PVFRYKK 

« Hide

References

[1]"Complete sequence of Fervidobacterium nodosum Rt17-B1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35602 / DSM 5306 / Rt17-B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000771 Genomic DNA. Translation: ABS60824.1.
RefSeqYP_001410481.1. NC_009718.1.

3D structure databases

ProteinModelPortalA7HLP1.
SMRA7HLP1. Positions 2-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381764.Fnod_0974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS60824; ABS60824; Fnod_0974.
GeneID5453161.
KEGGfno:Fnod_0974.
PATRIC21883443. VBIFerNod12464_1020.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMAIFERRIK.
OrthoDBEOG6HMXDX.

Enzyme and pathway databases

BioCycFNOD381764:GC5M-1008-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_FERNB
AccessionPrimary (citable) accession number: A7HLP1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 48 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