ID   Q0VPP2_ALCBS            Unreviewed;       519 AA.
AC   Q0VPP2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CAL16856.1};
DE            EC=1.1.99.5 {ECO:0000313|EMBL:CAL16856.1};
GN   Name=glpD {ECO:0000313|EMBL:CAL16856.1};
GN   OrderedLocusNames=ABO_1408 {ECO:0000313|EMBL:CAL16856.1};
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL16856.1, ECO:0000313|Proteomes:UP000008871};
RN   [1] {ECO:0000313|EMBL:CAL16856.1, ECO:0000313|Proteomes:UP000008871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2
RC   {ECO:0000313|Proteomes:UP000008871};
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; AM286690; CAL16856.1; -; Genomic_DNA.
DR   RefSeq; WP_011588689.1; NC_008260.1.
DR   AlphaFoldDB; Q0VPP2; -.
DR   STRING; 393595.ABO_1408; -.
DR   KEGG; abo:ABO_1408; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_6; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAL16856.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008871}.
FT   DOMAIN          23..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          417..477
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          498..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  57341 MW;  7C2098C0C8AB942D CRC64;
     MLGQRRTLTE LATPTAPQAP HWDLIVIGGG ITGAGVMLEA ARRGHRVLLL EQTDFSWGTS
     SRSSKMVHGG LRYIAQGDIT LTRHSLLERE RLLNELPGLV ERAIYLFPLR KGVFPGRWPM
     KMVLWLYDFL AGIRDHRYLN RKQLLERVPA LRNQDLTGAM CYTDALTDDC RLVMRTLLEG
     ARHGGLAHNY ARVVQAERKE QGFAVAVEDR VSGERVTLNA SAVVSATGAW ADRFSGAEAR
     VRPLRGSHLF IDPAVLSVND CLTVMHPDDG RPVFVFPWEG VTCVGTTDLD HPEDMDIEAA
     ASDREVVYLL KLINTQFPGC NVTRENIYST IAGVRPVIAS GKGVDPSKER RDHAVWGDNG
     IVTVSGGKLT TFRLIALDAL LATGLIDDSE HRRSQKSKVS SFDPLENAPH AVEAFLHADQ
     SDPAFIQWVL DHESVVHLDD LMLRRTRLGL IKPTAGIAAL NGLRPQIQQT LGWDDAQWDK
     ELVRYKGIHQ RFYSVPAPAS KGDATEAVEA DGAPGQQAR
//