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Protein

Glycine dehydrogenase (decarboxylating)

Gene

gcvP

Organism
Stenotrophomonas maltophilia (strain K279a)
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

BioCyciSMAL522373:GJE8-3461-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine dehydrogenase (decarboxylating)UniRule annotation (EC:1.4.4.2UniRule annotation)
Alternative name(s):
Glycine cleavage system P-proteinUniRule annotation
Glycine decarboxylaseUniRule annotation
Glycine dehydrogenase (aminomethyl-transferring)UniRule annotation
Gene namesi
Name:gcvPUniRule annotation
Ordered Locus Names:Smlt3579
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 955955Glycine dehydrogenase (decarboxylating)PRO_1000132460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei702 – 7021N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

The glycine cleavage system is composed of four proteins: P, T, L and H.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt3579.

Structurei

3D structure databases

ProteinModelPortaliB2FQE7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiPHYKTLY.
OrthoDBiEOG6HMXDX.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR003437. GcvP.
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. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.

Sequencei

Sequence statusi: Complete.

B2FQE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNTPSLRE LEHHNAFVER HIGPNDAEIA QMLDVVGHAS LDAMTDAIVP
60 70 80 90 100
AKIKSPAPLA LPESMTEVQA LAKIRAIADK NTVLRSFIGQ GYYGTHTPNV
110 120 130 140 150
ILRNILENPA WYTAYTPYQA EISQGRMEAL INFQTLCADL TGMEIANASL
160 170 180 190 200
LDEATAAAEA MTLAKRSAKS KSDTFFVHDA VHPQTLELLR TRAEPMGIVL
210 220 230 240 250
RVGTPAEALE AEAFGLLLQY PDTFGQVGDY KALVDAVHAR GGLVAVATDL
260 270 280 290 300
LALTLLAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
310 320 330 340 350
RLIGVSIDAQ GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA
360 370 380 390 400
VYHGPEGLTR IARRTHRLAS ILAAALRNAG VQVGGDFFDT LHVTGVHADE
410 420 430 440 450
IHAKARAAGY NLRAIDSDSV GISLDETTTR ADIVAVAAVF GASLDVDALD
460 470 480 490 500
ASTADALPAG LLRQSAFLTH PVFNTHHSEH ELLRYLRSLA DKDLAMDRTM
510 520 530 540 550
IPLGSCTMKL NATAEMIPVT WPEFSQIHPL VPADQALGYK ELIDTLEAML
560 570 580 590 600
VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEGHRD ICLIPDSAHG
610 620 630 640 650
TNPASAQMCG MKVVVTKTDA NGNVDVEDIR LNAEKYSDRL AAIMMTYPST
660 670 680 690 700
HGVFEEEVVE ICEIIHKHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL
710 720 730 740 750
HKTFCIPHGG GGPGVGPCAV KEHLAPFLPG KLGDNGPVGM VSAASFGSAS
760 770 780 790 800
ILPISWMYIA MMGREGLRKA TQVAQLNANY IAKRLAPHFK TLYTGRNGLV
810 820 830 840 850
AHECILDVRP LEKTSGIGAE DVAKRLIDFG FHAPTLSFPV AGTLMVEPTE
860 870 880 890 900
SESLHELDRF IDAMIQIREE ITAIEDGRLD REDNPLKNAP HTATAVTASE
910 920 930 940 950
WTHAYPRELA AFPLASLKQS KYWPPVARVD NVYGDKNVMC ACIPVDAYKD

DEVEA
Length:955
Mass (Da):102,998
Last modified:June 10, 2008 - v1
Checksum:i9AF7C403FAA3C8FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA. Translation: CAQ46996.1.
RefSeqiYP_001973285.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ46996; CAQ46996; Smlt3579.
KEGGisml:Smlt3579.
PATRICi23702617. VBISteMal45202_3361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA. Translation: CAQ46996.1.
RefSeqiYP_001973285.1. NC_010943.1.

3D structure databases

ProteinModelPortaliB2FQE7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi522373.Smlt3579.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ46996; CAQ46996; Smlt3579.
KEGGisml:Smlt3579.
PATRICi23702617. VBISteMal45202_3361.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiPHYKTLY.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciSMAL522373:GJE8-3461-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR003437. GcvP.
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. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279a.

Entry informationi

Entry nameiGCSP_STRMK
AccessioniPrimary (citable) accession number: B2FQE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: April 29, 2015
This is version 55 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.