ID   Q8Y7I4_LISMO            Unreviewed;       558 AA.
AC   Q8Y7I4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpD {ECO:0000313|EMBL:CAC99371.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99371.1, ECO:0000313|Proteomes:UP000000817};
RN   [1] {ECO:0000313|EMBL:CAC99371.1, ECO:0000313|Proteomes:UP000000817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA   Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA   Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA   Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA   Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA   Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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; AL591978; CAC99371.1; -; Genomic_DNA.
DR   PIR; AE1236; AE1236.
DR   RefSeq; NP_464818.1; NC_003210.1.
DR   RefSeq; WP_003723738.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y7I4; -.
DR   STRING; 169963.gene:17593950; -.
DR   PaxDb; 169963-lmo1293; -.
DR   EnsemblBacteria; CAC99371; CAC99371; CAC99371.
DR   GeneID; 985350; -.
DR   KEGG; lmo:lmo1293; -.
DR   PATRIC; fig|169963.11.peg.1328; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OrthoDB; 9766796at2; -.
DR   PhylomeDB; Q8Y7I4; -.
DR   BioCyc; LMON169963:LMO1293-MONOMER; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000817; 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; IBA:GO_Central.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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; 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   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000817}.
FT   DOMAIN          23..378
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          407..533
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   558 AA;  63239 MW;  B3683A6C96AB8D04 CRC64;
     MVQLFSAFDR ETIERNLQEE KFDLVIVGGG ITGAGIALDA TSRGMSVALV EMGDFASGTS
     SRSTKLVHGG LRYLQQFEIK EVADLGKERA IVYENGPHVT TPEWMMLPFH KGGNMGKTTA
     SFGIRLYDYL AGVKKNERRK ILSAKETLAK NPFVKKDGLK GSGYYVEYRT DDARLTIEVM
     KKAVELGANA INYTKAEHFL YDDNKQVVGV TVTDRLSGKA YDIKGHRVIN AAGPWVDKVR
     KLDYATNNKH LRLTKGIHLV IDKQKFPMEQ AVYFDTPDGR MVFAIPRDKK VYVGTTDTVY
     DEAVINPKAL ESDHNYVIKA INYMFPDVHI TEKDIESSWA GVRPLIYEEG KDPSEISRKD
     EVWFSESGLI TMAGGKLTGY RKMAEKLLDD VSKTLAKETG KKYKTVQTKH LPISGGDIGG
     SEQLEAFLSK KAKEGNNRFG WTLEEGREMA KRFGSNIDQL FTYAQEHKEQ NETTLPNSLY
     AELRYSIQHE AVTTPIDFLL RRTGYLLFDM PYLLEWKDAV VDEMAKQFHW SDDVKQTYIE
     ELNIQINDAR EPADWHDR
//