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Protein

Probable glycine dehydrogenase (decarboxylating) subunit 2

Gene

gcvPB

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-117-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glycine dehydrogenase (decarboxylating) subunit 2UniRule annotation (EC:1.4.4.2UniRule annotation)
Alternative name(s):
Glycine cleavage system P-protein subunit 2UniRule annotation
Glycine decarboxylase subunit 2UniRule annotation
Glycine dehydrogenase (aminomethyl-transferring) subunit 2UniRule annotation
Gene namesi
Name:gcvPBUniRule annotation
Ordered Locus Names:lpl0113
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517 Componenti: Chromosome

Organism-specific databases

LegioListilpl0113.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Probable glycine dehydrogenase (decarboxylating) subunit 2PRO_1000045696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei264 – 2641N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5X0A8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family. C-terminal subunit subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239368.
KOiK00283.
OMAiMHINLHK.
OrthoDBiEOG6HMXDX.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_00713. GcvPB.
InterProiIPR023012. GcvPB.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5X0A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIFELSKTG RQAKAQIPRA VSKNYSIPEE FQRKSRPRLP ACSELQVVRH
60 70 80 90 100
FTCLSQKNFS IDTNFYPLGS CTMKYNPRGV HKAASLPGFI NRHPLAMDNE
110 120 130 140 150
SQGFLETLYK LQNYISEITG MPGVSLTPMA GSQGEFAGVA MIKAYHQSRG
160 170 180 190 200
DTARDEILIP DAAHGTNPAS AVMCGFKVVE IATAPDGDID LDELKRKVGP
210 220 230 240 250
RTAGIMLTNP STLGLFMRQI KEIASLVHQA GGLLYYDGAN LNAILGKVRP
260 270 280 290 300
GDMGFDVMHL NLHKTFATPH GGGGPGAGPV AVGKRLIPYM PLPVVKKTDS
310 320 330 340 350
GYHWATRQDY PQSIGRLSCF MGNAGILLRA YFYMLVLGKE GLLRVSEFAT
360 370 380 390 400
LNANYLLKEL TKVGYTAAYP DRRASHEFIL TLNSEKKNYD VTAMDFAKRL
410 420 430 440 450
LDYGVHAPTT YFPLLVPECL LIEPPETESK EELDAFVAVM KTIREEASKQ
460 470 480
PDILKAAPHT LPVKRLDDVK AARELDLNYF ATHE
Length:484
Mass (Da):53,426
Last modified:November 23, 2004 - v1
Checksum:iBC2959C45F6E9A9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH14343.1.
RefSeqiWP_011214397.1. NC_006369.1.
YP_125490.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH14343; CAH14343; lpl0113.
KEGGilpf:lpl0113.
PATRICi22313663. VBILegPne33733_0182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH14343.1.
RefSeqiWP_011214397.1. NC_006369.1.
YP_125490.1. NC_006369.1.

3D structure databases

ProteinModelPortaliQ5X0A8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH14343; CAH14343; lpl0113.
KEGGilpf:lpl0113.
PATRICi22313663. VBILegPne33733_0182.

Organism-specific databases

LegioListilpl0113.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239368.
KOiK00283.
OMAiMHINLHK.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-117-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_00713. GcvPB.
InterProiIPR023012. GcvPB.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiGCSPB_LEGPL
AccessioniPrimary (citable) accession number: Q5X0A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: June 24, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.