ID A0A1H5T657_9EURY Unreviewed; 450 AA.
AC A0A1H5T657;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase subunit B {ECO:0000313|EMBL:SEF58342.1};
DE SubName: Full=Glycerol-3-phosphate dehydrogenase subunit GlpB {ECO:0000313|EMBL:QCC47392.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:QCC47392.1};
GN ORFNames=DV707_06795 {ECO:0000313|EMBL:QCC47392.1}, SAMN04488133_0189
GN {ECO:0000313|EMBL:SEF58342.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEF58342.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEF58342.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEF58342.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC47392.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC47392.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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DR EMBL; CP031311; QCC47392.1; -; Genomic_DNA.
DR EMBL; FNVN01000001; SEF58342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5T657; -.
DR KEGG; hlm:DV707_06795; -.
DR OrthoDB; 197288at2157; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; Chromosome.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009158; G3P_DH_GlpB_su.
DR Pfam; PF00890; FAD_binding_2; 2.
DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:QCC47392.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236740}.
FT DOMAIN 6..60
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 88..431
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT REGION 52..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 46371 MW; 6AFA99D18B39CC2C CRC64;
MAIREDVLVV GGGIAGATAA LAAAESGATV RLLSHKKSTL RQASGLIDVL GAIPRDGSSD
GADPAGDRSP GDRTEPAGGG STGESELVAD PFEAIGRLPE AHPYRVVGGG AIRDGLELFD
DAVGGAYEGA HTDRNALVIT HGGTVKPTAR YPESVAPGLA SAERDTLLVG FAGLTDFDAP
AAAAHLDAAG VPFAVDGATV EFPVRFRDDA LTTRFAKALD TDESNARRRL ADAVRDADAD
LDGYDRVGFP AMLGDDEGEA VRTDLEDRLG ASVFQIPTGP PSLLGTQLED LLFDALDAAG
VRLASGNPAV GYEASDGRID SVLVDRRGRE VPYAAEEFVL ATGGLVGKGI DSDRESVTEP
VFGCHVPHPE DRYDWSEPEA FGGHAFARFG VVPDDDLRPA GESGEPEFEN LRAAGGVLGG
ADTAREKSAA GVSLATGAYA GRRAGEEATR
//
