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Protein

Probable glycine dehydrogenase (decarboxylating) subunit 2

Gene

gcvPB

Organism
Bacillus cereus subsp. cytotoxis (strain NVH 391-98)
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

  1. glycine dehydrogenase (decarboxylating) activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glycine decarboxylation via glycine cleavage system Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBCYT315749:GH2A-3021-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:Bcer98_2913
OrganismiBacillus cereus subsp. cytotoxis (strain NVH 391-98)
Taxonomic identifieri315749 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002300: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Probable glycine dehydrogenase (decarboxylating) subunit 2PRO_1000083227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731N6-(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

Protein-protein interaction databases

STRINGi315749.Bcer98_2913.

Structurei

3D structure databases

ProteinModelPortaliA7GSN6.
SMRiA7GSN6. Positions 7-485.
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.
InterProiIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023012. GDC_P_su2.
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.

A7GSN6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNQDQALIF EMSKEGRVGY SLPQLDVEEV KLEDVFESNY IRAEDAELPE
60 70 80 90 100
VSELDIMRHY TALSNRNHGV DSGFYPLGSC TMKYNPKINE NVARFPGFAN
110 120 130 140 150
IHPLQDEKTV QGAMELMYDL QEHLVEITGM DAVTLQPAAG AHGEWTGLML
160 170 180 190 200
IRAYHEANGD HNRTKVIVPD SAHGTNPASA TVAGFETITV KSNEHGLVDL
210 220 230 240 250
EDLKRVVNEE TAALMLTNPN TLGLFEENIL EMAEIVHNAG GKLYYDGANL
260 270 280 290 300
NAVLSQARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKEDLIPFLP
310 320 330 340 350
KPILEKTENG YHFNYDRPQA IGRVKPFYGN FGINVRAYTY IRSMGPDGLR
360 370 380 390 400
AVTENAVLNA NYMMRRLAPY YDLPFDRHCK HEFVLSGRCQ KKLGVRTLDI
410 420 430 440 450
AKRLLDFGYH PPTIYFPLNV EECIMIEPTE TESKETLDGF IDKMIQIAKE
460 470 480 490
AKENPEIVQE APHTTVITRL DETMAARKPI LRYQKPTPVQ V
Length:491
Mass (Da):54,867
Last modified:September 11, 2007 - v1
Checksum:i6C31F335795C2718
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS23144.1.
RefSeqiYP_001376139.1. NC_009674.1.

Genome annotation databases

EnsemblBacteriaiABS23144; ABS23144; Bcer98_2913.
GeneIDi5347262.
KEGGibcy:Bcer98_2913.
PATRICi18934440. VBIBacCyt128034_3064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS23144.1.
RefSeqiYP_001376139.1. NC_009674.1.

3D structure databases

ProteinModelPortaliA7GSN6.
SMRiA7GSN6. Positions 7-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315749.Bcer98_2913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS23144; ABS23144; Bcer98_2913.
GeneIDi5347262.
KEGGibcy:Bcer98_2913.
PATRICi18934440. VBIBacCyt128034_3064.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239368.
KOiK00283.
OMAiMHINLHK.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciBCYT315749:GH2A-3021-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
HAMAPiMF_00713. GcvPB.
InterProiIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023012. GDC_P_su2.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NVH 391-98.

Entry informationi

Entry nameiGCSPB_BACCN
AccessioniPrimary (citable) accession number: A7GSN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: January 7, 2015
This is version 57 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.