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Protein

Glycerol-3-phosphate dehydrogenase

Gene

glpD

Organism
Xenorhabdus bovienii (strain SS-2004)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.UniRule annotation

Cofactori

FADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

FlavoproteinUniRule annotation

Enzyme and pathway databases

BioCyciXBOV406818:GHLH-135-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenaseUniRule annotation (EC:1.1.5.3UniRule annotationImported)
Gene namesi
Name:glpDImported
Ordered Locus Names:XBJ1_0138Imported
OrganismiXenorhabdus bovienii (strain SS-2004)Imported
Taxonomic identifieri406818 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeXenorhabdus
ProteomesiUP000002045 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi406818.XBJ1_0138.

Structurei

3D structure databases

ProteinModelPortaliD3UYB1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000004811.
KOiK00111.
OMAiARMVVLN.

Family and domain databases

InterProiIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3UYB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METKDLIVIG GGINGAGIAA DAAGRGLSVL LLEGQDLASA TSSASSKLIH
60 70 80 90 100
GGLRYLEHYE FRLVSEALAE REVLLKLAPH IAFPMRFRLP HQPHLRPAWM
110 120 130 140 150
IRIGLFLYDN LGKRVSLPSS KGLKFGANSV LKPSIRRGFE YSDCWVDDAR
160 170 180 190 200
LVVLNAQEVQ KHGGEVRTRT QVTRAWREKG YWMVEAKDLT TGKTDTWRAK
210 220 230 240 250
GLVNATGPWV KNFFDDGLKL KSPYGIRLIK GSHIVVPRAH DEPQAYILQN
260 270 280 290 300
EDNRIVFVIP WNDEFSIIGT TDVEYKGDPK EVKIDDQEIG YLLKVYNNHF
310 320 330 340 350
KKQLNRSDVV WTYSGVRPLC DDESDSPQAI TRDYTLDVQD EQGQMPLLSV
360 370 380 390 400
FGGKLTTYRK LAEHALEKLV QYYPNAGKAW TKNGKLPGGE LEGHDRDGYA
410 420 430 440 450
RLLRQRHNWL PEGVAQRYAR TYGSNCQIIL KGAEALTDLG EFFGHGLYEA
460 470 480 490 500
ELRYLVEHEW VTQLDDAIWR RTKLGMWLTD EQKQRVADWL AQNVQSSQAQ

S
Length:501
Mass (Da):56,778
Last modified:April 20, 2010 - v1
Checksum:i523749DF9902C0F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN667741 Genomic DNA. Translation: CBJ79289.1.
RefSeqiWP_012986756.1. NC_013892.1.

Genome annotation databases

EnsemblBacteriaiCBJ79289; CBJ79289; XBJ1_0138.
GeneIDi8829762.
KEGGixbo:XBJ1_0138.
PATRICi35295465. VBIXenBov95754_0126.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN667741 Genomic DNA. Translation: CBJ79289.1.
RefSeqiWP_012986756.1. NC_013892.1.

3D structure databases

ProteinModelPortaliD3UYB1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406818.XBJ1_0138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBJ79289; CBJ79289; XBJ1_0138.
GeneIDi8829762.
KEGGixbo:XBJ1_0138.
PATRICi35295465. VBIXenBov95754_0126.

Phylogenomic databases

HOGENOMiHOG000004811.
KOiK00111.
OMAiARMVVLN.

Enzyme and pathway databases

BioCyciXBOV406818:GHLH-135-MONOMER.

Family and domain databases

InterProiIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."
    Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., Suen G.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SS-2004Imported.
  2. "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus: convergent lifestyles from divergent genomes."
    Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E., Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.
    , Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.
    PLoS ONE 6:e27909-e27909(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SS-2004Imported.

Entry informationi

Entry nameiD3UYB1_XENBS
AccessioniPrimary (citable) accession number: D3UYB1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: July 22, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.