ID   I7CHB7_NATSJ            Unreviewed;       579 AA.
AC   I7CHB7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN   OrderedLocusNames=NJ7G_1715 {ECO:0000313|EMBL:AFO56959.1};
OS   Natrinema sp. (strain J7-2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO56959.1, ECO:0000313|Proteomes:UP000006507};
RN   [1] {ECO:0000313|EMBL:AFO56959.1, ECO:0000313|Proteomes:UP000006507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J7-2 {ECO:0000313|EMBL:AFO56959.1,
RC   ECO:0000313|Proteomes:UP000006507};
RX   PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA   Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA   Shen P., Wang L., Tang B., Tang X.F.;
RT   "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT   of growth on synthetic media without amino acid supplements.";
RL   PLoS ONE 7:E41621-E41621(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000153};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005157}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000256|ARBA:ARBA00011331}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; CP003412; AFO56959.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7CHB7; -.
DR   STRING; 406552.NJ7G_1715; -.
DR   KEGG; nat:NJ7G_1715; -.
DR   PATRIC; fig|406552.5.peg.1529; -.
DR   eggNOG; arCOG00753; Archaea.
DR   eggNOG; arCOG05746; Archaea.
DR   HOGENOM; CLU_015740_0_1_2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000006507; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR017752; G3P_DH_GlpA_su.
DR   NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
DR   PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          17..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          447..497
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   REGION          549..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  63046 MW;  31C9BE982C78EFA5 CRC64;
     MEVSVEGSDR MPRDTEVLVL GGGSTGCGIA RDLAMRGLEV TLVERGNLTD GTTGRMHGLL
     HSGGRYAVSD QASATECIEE NEILREIAGH CVEETGGLFV QRPEDSDEYF QEKLEGCREC
     GIPARVLSGT EAREVEPYLA DDVARAIEVP DGAVDPFRLC VANAIDAETH GARVETHAEV
     VDLLRDGDDI YGVEVRHESG PGKRTHATPG TTEEITADYV VNATGAWAGQ IGAMADLEIE
     VRPSKGVMTI MNVRQVDTVI NRCRPKGDAD IIVPHETTAI LGTTDEEVPD PDDYPEEQWE
     VDQMIDTLSE LVPILEEART IRSFWGVRPL YEPPGTGTQD PTDITRDFFL LDHADRDGVA
     GMSSIVGGKF TTYRAMAEEI ADHVCDKLGV TASCSTADEP LPGSENIETL EAGMDDFGLR
     SPVARRSTQR LGSRASEVLE TDDPNPVICQ CEGVTRAEIR DAISQSGSDL NAVRIRTRAS
     MGNCQGGFCC QNMANELHPT YDEETVREAL DELFQERWKG ERHALWGEQL SQAMLNYALH
     ATTMNRDRDP ASATGDIDFA AFDGGRPASD RVDGTRRAD
//