ID G0LLJ6_HALWC Unreviewed; 417 AA.
AC G0LLJ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpA2 {ECO:0000313|EMBL:CCC40802.1};
GN OrderedLocusNames=Hqrw_3006 {ECO:0000313|EMBL:CCC40802.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC40802.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC40802.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
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|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
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; FR746099; CCC40802.1; -; Genomic_DNA.
DR RefSeq; WP_014556332.1; NC_017459.1.
DR AlphaFoldDB; G0LLJ6; -.
DR GeneID; 12447783; -.
DR KEGG; hwc:Hqrw_3006; -.
DR HOGENOM; CLU_015740_0_1_2; -.
DR OrthoDB; 36306at2157; -.
DR Proteomes; UP000007954; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
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 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 6..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 417 AA; 44718 MW; 861AA627DCC76EA8 CRC64;
MTIQTDVAII GGGATGAGIA RDLALRGVDV SLFERGGLGG GTSGRSHGLL HSGGRYAESD
PIGAEECIRE SRILRDIAEG CIRETGGLFV QLESDDPAYF EEKLEACNEL DIPTETISAE
EAHERVPGLT EDVERAFTVP DGVIYPSRLV VANAADAREH GASIHTHTPV ESVTTANGEI
TELHVGGEIN DTVEATQIVN ATGAWAEVMG EDLGVDVSMQ PTRGVMISVE YDGLDPVLNR
CRDPDDGDII VPHDGEVVLG TTSVAVEDPD DYEEADWEVE RSVDECAELI PDITDAPEVR
TWWGVRPLYE PDEDERDDGR GISRGFFVIN HAERNEPANL ISVVGGKLTT YRQMAEAASD
QICARLGVDA SCETDERPLH ASDDPAQLDA LIDEFDAVNP TDRDIVTTAT PAESAAD
//
