ID   A0AI94_LISW6            Unreviewed;       558 AA.
AC   A0AI94;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   02-SEP-2026, entry version 96.
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:CAK20726.1};
GN   OrderedLocusNames=lwe1308 {ECO:0000313|EMBL:CAK20726.1};
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CCUG 15529
OS   / CIP 8149 / NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Listeriaceae;
OC   Listeria.
OX   NCBI_TaxID=386043 {ECO:0000313|EMBL:CAK20726.1, ECO:0000313|Proteomes:UP000000779};
RN   [1] {ECO:0000313|EMBL:CAK20726.1, ECO:0000313|Proteomes:UP000000779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CCUG 15529 / CIP 8149 / NCTC 11857 /
RC   SLCC 5334 / V8 {ECO:0000313|Proteomes:UP000000779};
RX   PubMed=16936040; DOI=10.1128/JB.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + a quinol; 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:ARBA00049055,
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; AM263198; CAK20726.1; -; Genomic_DNA.
DR   RefSeq; WP_011702115.1; NC_008555.1.
DR   AlphaFoldDB; A0AI94; -.
DR   STRING; 386043.lwe1308; -.
DR   PaxDb; 386043-lwe1308; -.
DR   GeneID; 61189185; -.
DR   KEGG; lwe:lwe1308; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OrthoDB; 9766796at2; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000000779; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase (FAD) complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:TreeGrafter.
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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 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:UP000000779}.
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;  63364 MW;  1838B17EEF3F2D00 CRC64;
     MVQLFSAFDR ETIERNLQEE KFDLVIVGGG ITGAGIALDA TTRGMNVALV EMGDFASGTS
     SRSTKLVHGG LRYLQQFEIK EVADLGKERA IVYENGPHVT TPEWMMLPFH KGGNMGKTTA
     SFGIRLYDYL AGVKKNERRK ILSAKETLAK NPFVKKDGLK GSGYYVEYRT DDARLTIEVM
     KKAVELGANA INYTKAEHFL YDDNKQVVGV TVTDRLTGKA YDIKGHRVIN AAGPWVDKVR
     KLDYATNNKH LRLTKGIHLV IDKKKFPMEQ AVYFDTPDGR MVFAIPRDKK VYVGTTDTVY
     DEAVINPKAL ESDHNYVIKA INYMFPDVHI TEKDIESSWA GVRPLIYEEG KDPSEISRKD
     EVWFSESGLI TMAGGKLTGY RKMAEKLLDD VSKTLTKETG KKYKPVQTKH LPISGGDIGG
     SEQLESFLSK KAKEGNNRFG WTLEEGREIA KRYGSNIDQL FTYAQEHKEQ EESTLPNSLY
     AELRYSIQHE AVTTPIDFLL RRTGYLLFDM PYLLEWKDAV IDEMAKQFHW SDEVKQTYIE
     ELDIQINDAR EPADWHDR
//