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Protein

Probable glycine dehydrogenase (decarboxylating) subunit 2

Gene

gcvPB

Organism
Desulfotomaculum reducens (strain MI-1)
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

BioCyciDRED349161:GHP6-766-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:Dred_0723
OrganismiDesulfotomaculum reducens (strain MI-1)
Taxonomic identifieri349161 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum
ProteomesiUP000001556 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Probable glycine dehydrogenase (decarboxylating) subunit 2PRO_1000072771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701N6-(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

STRINGi349161.Dred_0723.

Structurei

3D structure databases

ProteinModelPortaliA4J2F9.
SMRiA4J2F9. Positions 4-482.
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.

A4J2F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKLIFELG SPGRQGVLFP ANDVPEIPPH ELLPRDLIRE QEVPLPEVSE
60 70 80 90 100
GDAVRHFVRL SRMNFGVDVG FYPLGSCTMK YNPKVAEDAA GLSGFANIHP
110 120 130 140 150
YQPDEISQGA LQLMYETQQD LAEITGMDAF TLQPAAGAQG ELTGMLIIKA
160 170 180 190 200
YLESKGETGR NKVIVPDSAH GTNPATAALC GFKVVEVKSD QRGGVDLAAL
210 220 230 240 250
KQLLGPDVAA LMLTNPSTLG LFEDNITEIA ALVHQAGGLL YYDGANLNAI
260 270 280 290 300
MGYARPGDMG FDVVHLNLHK TFGTPHGGGG PGSGPVGVKA ELAPFLPKPV
310 320 330 340 350
IIQREGNYLP DYHRPQSIGR VKAFFANFSV IVKAYTYLRS LGGKGLKEVS
360 370 380 390 400
EHAVLNANYL MKQLSDHFRV PYQRTCMHEF VVSPPEDMKE QGIKTLDIAK
410 420 430 440 450
RLLDYGYHPP TVYFPLIVEE ALMFEPTETE SKETLDEFAH NLIKVLAEAR
460 470 480
ENPDKLRNAP YTTPIRRLDE VMAARKPLVG WFPE
Length:484
Mass (Da):53,106
Last modified:May 1, 2007 - v1
Checksum:iDF3EA3E9F8930C33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000612 Genomic DNA. Translation: ABO49262.1.
RefSeqiWP_011877098.1. NC_009253.1.
YP_001112087.1. NC_009253.1.

Genome annotation databases

EnsemblBacteriaiABO49262; ABO49262; Dred_0723.
KEGGidrm:Dred_0723.
PATRICi21727429. VBIDesRed82656_0802.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000612 Genomic DNA. Translation: ABO49262.1.
RefSeqiWP_011877098.1. NC_009253.1.
YP_001112087.1. NC_009253.1.

3D structure databases

ProteinModelPortaliA4J2F9.
SMRiA4J2F9. Positions 4-482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349161.Dred_0723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO49262; ABO49262; Dred_0723.
KEGGidrm:Dred_0723.
PATRICi21727429. VBIDesRed82656_0802.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239368.
KOiK00283.
OMAiMHINLHK.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciDRED349161:GHP6-766-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MI-1.

Entry informationi

Entry nameiGCSPB_DESRM
AccessioniPrimary (citable) accession number: A4J2F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: April 29, 2015
This is version 58 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, Reference 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.