ID   A8LYN4_SALAI            Unreviewed;       603 AA.
AC   A8LYN4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Sare_0315 {ECO:0000313|EMBL:ABV96245.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV96245.1};
RN   [1] {ECO:0000313|EMBL:ABV96245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV96245.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) 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|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; CP000850; ABV96245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8LYN4; -.
DR   STRING; 391037.Sare_0315; -.
DR   KEGG; saq:Sare_0315; -.
DR   PATRIC; fig|391037.6.peg.322; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
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; 1.10.8.870; Alpha-glycerophosphate oxidase, cap 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; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 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          27..379
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          422..545
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          565..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  64712 MW;  3E4AF016FACE68B1 CRC64;
     MSRANASQLS PLRRAADLRR LATEHFDVLI IGGGVTGAGA ALDAASRGLK VALVEARDYA
     AGTSSRSSKL IHGGLRYLEQ LEFHLVHEAL TERGLLATRL APHLVRPVPF LVPLLGGGLR
     DLPARMLRRS YYGAGVAAYD VFAGVFGGGR GMPLHRHLTR EGARRTFPSL KAEGLAGAIR
     YFDGQVDDAR LVVTLARTAA SLGATVVSSA RAVGLIRQAR EVTGVRVRDL EAPADSPDAE
     FEVRARTVIA ATGVWSDDMS RMLDDVGLRP RVRVRASKGV HLVVPRSAIT GETGLLLRTA
     TSVLFVIPWG GHWIIGTTDT DWRLDRSHPA ASARDIDYLL AQVNTVLDRP LTTADIEGVY
     AGLRPLLAGE ADSTSKLSRE HAVIEPMLGL LLVAGGKYTT YRVMASDVVD RAARRLGAVR
     PSRTADLPLL GADGYSAMWR DRADLARRHG VPVGVVEHLL ERYGSLTLDL LALIGADPLL
     GSPLAGAPEY LAAEVTYATR AEGALHLEDV LTRRTRISIE TAHRGLESAE HTAELMGAVL
     GWNAEVRARE VAHYRARVAA ERNSQLMPDD ATADTARLGA PDVRGFPADR GDDDPVESAS
     PSR
//