ID   Q18JE7_HALWD            Unreviewed;       579 AA.
AC   Q18JE7;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN   Name=glpA1 {ECO:0000313|EMBL:CAJ51862.1};
GN   OrderedLocusNames=HQ_1734A {ECO:0000313|EMBL:CAJ51862.1};
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51862.1, ECO:0000313|Proteomes:UP000001975};
RN   [1] {ECO:0000313|EMBL:CAJ51862.1, ECO:0000313|Proteomes:UP000001975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA   Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ51862.1; -; Genomic_DNA.
DR   RefSeq; WP_011571010.1; NC_008212.1.
DR   AlphaFoldDB; Q18JE7; -.
DR   STRING; 362976.HQ_1734A; -.
DR   GeneID; 4194052; -.
DR   KEGG; hwa:HQ_1734A; -.
DR   eggNOG; arCOG00753; Archaea.
DR   eggNOG; arCOG05746; Archaea.
DR   HOGENOM; CLU_015740_0_1_2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000001975; 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,
KW   ECO:0000313|EMBL:CAJ51862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001975}.
FT   DOMAIN          7..364
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          437..484
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   REGION          535..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  63299 MW;  48160CC6A2388342 CRC64;
     MVSKPHIVVI GGGSTGTGIV RDLAMRGVEV TLLEQGNLTH GTTGRMHGLL HSGGRYAVAD
     QASAKECMLE NRVLQDIATH CVEMTGGLFV KRPEDSEEYF QKKLQGCHEC DIPAEVLTAE
     EARAVEPHLA GDIDKAISVP DGAIDPFRLV VANAADAKEH DARIETHSTV TDLLIEDDAV
     VGVEVKHDSG TGERVHGMTG VTERIYADHV INATGAWAGH IGEMAGVDIA VRPSKGVMTV
     MNTRQVDTVI NRCRPKGDAD IVVPHETTAI LGTTDVEVDD PEDYPEKQWE VDLMIDTLSE
     LVPMLTDART IRSFWGVRPL YEPPEVGSDD PTDITRDFFL LDHQERDNLH GLTSIVGGKL
     TTYRMMAEQI TDHICERFGI EEPCRTADEP LPGSNDIRVI DDYMDEFGLR SPIGRRSADR
     LGSRVDEVLD TDEPNPTICE CEGVTRAEVQ DAISQSGSDL NAVRIRTRAT MGNCQGGICS
     HRLANELHTT YDESVVIDAW NEILQERWKG QRHALWGQQL SQAMLNYALH ATTQNRDHDP
     AADSSVDFTT FDSGEMQSDS GTTAVSVATD GGTQDGDRV
//