ID M1Y0P2_NATM8 Unreviewed; 409 AA.
AC M1Y0P2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CCQ36039.1};
GN OrderedLocusNames=Nmlp_1851 {ECO:0000313|EMBL:CCQ36039.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ36039.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ36039.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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; HF582854; CCQ36039.1; -; Genomic_DNA.
DR RefSeq; WP_015408864.1; NC_020388.1.
DR AlphaFoldDB; M1Y0P2; -.
DR STRING; 268739.Nmlp_1851; -.
DR GeneID; 14652598; -.
DR KEGG; nmo:Nmlp_1851; -.
DR eggNOG; arCOG00753; Archaea.
DR HOGENOM; CLU_015740_0_1_2; -.
DR OrthoDB; 36306at2157; -.
DR Proteomes; UP000011867; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT DOMAIN 7..336
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 409 AA; 42463 MW; 8D194141D1517BF0 CRC64;
MSADPTVLVI GGGATGTGIA RDLALRGVDV TLVERGGLGS GTSGRSHGLL HSGARYAESD
ASGAAECLAE SRTLREIAGA CVRETGGLFV RLEGDDAAYF ETKLAACEET GIETERLDGD
AARDLVDGLS DAVVEAFRVP DGVVYPSRLV AANAADAAAH GADVHPHAPV EAIETGADGI
TAVDVGGSVD EHIEPTHVVN ATGAWADRIA EMAGCTVGMA PSRGVMVSLE YDGLGPVLNR
CRDPDDGDIV LPHEGEVVVG TTSVPVSTPE TYETAEWEIE RSIEECAAML PAVAEAPERR
TWWGVRPLYE PDEAAADRRG ISRGFTILDH GDEGVSNLHS VVGGKLTTYR EMAEVTADRV
CERLGVAEPC RTAEEPLVGA DDPSRLDALV EQYGGPNPTD AGVVGTDGG
//