ID A0A2R4WZH3_9EURY Unreviewed; 570 AA.
AC A0A2R4WZH3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN Name=glpA {ECO:0000313|EMBL:AWB26924.1};
GN ORFNames=HARCEL1_03955 {ECO:0000313|EMBL:AWB26924.1};
OS Halococcoides cellulosivorans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halococcoides.
OX NCBI_TaxID=1679096 {ECO:0000313|EMBL:AWB26924.1, ECO:0000313|Proteomes:UP000244727};
RN [1] {ECO:0000313|EMBL:AWB26924.1, ECO:0000313|Proteomes:UP000244727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HArcel1 {ECO:0000313|EMBL:AWB26924.1,
RC ECO:0000313|Proteomes:UP000244727};
RA Sorokin D.Y., Toshchakov S.V., Samarov N.I., Korzhenkov A., Kublanov I.V.;
RT "Halococcoides cellulosivorans gen. nov., sp. nov., an extremely halophilic
RT cellulose-utilizing haloarchaeon from hypersaline lakes.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
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,
CC ECO:0000256|RuleBase:RU361217}.
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DR EMBL; CP028858; AWB26924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4WZH3; -.
DR KEGG; harc:HARCEL1_03955; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000244727; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000244727}.
FT DOMAIN 7..360
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 433..480
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT REGION 532..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 61075 MW; 8C18E29997D9EE29 CRC64;
MPSPPHVLVV GGGSTGTGIA RDAAMRGFEV TLLERGTLTA GTSGRMHGLL HSGGRYAVSD
RESARECIAE NRVLRSIADH CIEDTHGLFV ARPEDDDAYF ERKRAGLDAC DIPATELTGR
EARQREPELA DDVARALAVP DAAIDPFRLC VANAVSAEAH GARIETHTPV TDLIVEDSRV
VGARVDRDGP GTATIRADHV VNATGAWAGD LAARAGVDVP VTPSKGAMTV TNVRPVDTVI
NRCRPKGDAD ILVPHETTAI LGTTDERVAD PDDYAEERWE RDLLVEELSE LVPALESARM
LRSFWGVRPL YEPSDGPVDG ESAAAEDPSD VSRGFSVLDH ADEGRPGLTT IVGGKLTTYR
LMAEAVVDHL ADRFGIGAAC RTAERALPGS EHPADLDRAM ERFELRSPVA RRSAERLGSR
TEAVLDTDGP NPVVCSCEAV TRAEVRDAIE QAPDLDAVRI RTRAGMGTCQ GGFCGHRLAS
ELARTTGPDR ARDALAAFRD ERWAGQRHEL RGEQLEQAAI TYAMHAMTMH HDGDPIETGS
TAFDAFDAGP PDTIGGPPTN DHDREGQDGD
//
