ID   B5EB78_CITBB            Unreviewed;       537 AA.
AC   B5EB78;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpA {ECO:0000313|EMBL:ACH40370.1};
GN   OrderedLocusNames=Gbem_3375 {ECO:0000313|EMBL:ACH40370.1};
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH40370.1, ECO:0000313|Proteomes:UP000008825};
RN   [1] {ECO:0000313|EMBL:ACH40370.1, ECO:0000313|Proteomes:UP000008825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem
RC   {ECO:0000313|Proteomes:UP000008825};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH40370.1, ECO:0000313|Proteomes:UP000008825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem
RC   {ECO:0000313|Proteomes:UP000008825};
RX   PubMed=20828392; DOI=10.1186/1471-2164-11-490;
RA   Aklujkar M., Young N.D., Holmes D., Chavan M., Risso C., Kiss H.E.,
RA   Han C.S., Land M.L., Lovley D.R.;
RT   "The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of
RT   Geobacter species that predominate in Fe(III)-reducing subsurface
RT   environments.";
RL   BMC Genomics 11:490-490(2010).
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; CP001124; ACH40370.1; -; Genomic_DNA.
DR   RefSeq; WP_012531802.1; NC_011146.1.
DR   AlphaFoldDB; B5EB78; -.
DR   STRING; 404380.Gbem_3375; -.
DR   KEGG; gbm:Gbem_3375; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_4_1_7; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000008825; 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; 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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000008825}.
FT   DOMAIN          18..380
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          402..522
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   537 AA;  58460 MW;  D11DCCF9EC6E2740 CRC64;
     MTDRKERLDR LKSGEIFDLL VVGGGATGCG IALDAASRGL KVALAERRDF AGGTSGRSTK
     LLHGGVRYLE AAVLHRDRVQ FNLVRDALHE RGVLLKIAPH LCQRLTLVTP LYRLAQVPYM
     WAGLKFYDLL ARGAGLGHSR YLSPSEMLRR FPQIKGKGLK GGVLYYDGQF NDARMNVALA
     LTALREGAAL SNYLEVVGLV REKGRVAGAL VRDPLGGASW QIRARCVVNA CGPSADLLRR
     MDDPTAAPLL RLSRGSHIVL PGKFAPADTG IMIPKTEDGR VVFILPWQGM CLVGTTEEPA
     TAGTTPVADD KDVDYLLRHL RRYFNLTVDE GDIMARWAGL RPLVHDPYTA DTAELARDHV
     ISCSPTGLIT IVGGKWTTYR KMALDTVDFA VANMGLAPSG ACRTDRIMLH GGKGFEAQGA
     TVLAKRFALP PDVALHLHGS YGTLATDVAQ LCQGELGERL VPPHPYLKGE VLYAVRNEMA
     LSPSDFLERR IPLALLDQRG AQIAAPVVLE MMAQELGWSQ VRVAHERSEL SNLLEQG
//