ID   GLPD2_MYCTO             Reviewed;         585 AA.
AC   P9WN78; L0TDR3; O07168; P64184;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 2;
DE            EC=1.1.5.3;
GN   Name=glpD2; OrderedLocusNames=MT3401;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47744.1; -; Genomic_DNA.
DR   PIR; H70533; H70533.
DR   RefSeq; WP_003417217.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN78; -.
DR   SMR; P9WN78; -.
DR   EnsemblBacteria; AAK47744; AAK47744; MT3401.
DR   KEGG; mtc:MT3401; -.
DR   PATRIC; fig|83331.31.peg.3660; -.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase.
FT   CHAIN           1..585
FT                   /note="Glycerol-3-phosphate dehydrogenase 2"
FT                   /id="PRO_0000427174"
FT   BINDING         37..65
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   585 AA;  62778 MW;  760C15F7E75BB69F CRC64;
     MSNPIQAPDG GQGWPAAALG PAQRAVAWKR LGTEQFDVVV IGGGVVGSGC ALDAATRGLK
     VALVEARDLA SGTSSRSSKM FHGGLRYLEQ LEFGLVREAL YERELSLTTL APHLVKPLPF
     LFPLTKRWWE RPYIAAGIFL YDRLGGAKSV PAQRHFTRAG ALRLSPGLKR SSLIGGIRYY
     DTVVDDARHT MTVARTAAHY GAVVRCSTQV VALLREGDRV IGVGVRDSEN GAVAEVRGHV
     VVNATGVWTD EIQALSKQRG RFQVRASKGV HVVVPRDRIV SDVAMILRTE KSVMFVIPWG
     SHWIIGTTDT DWNLDLAHPA ATKADIDYIL GTVNAVLATP LTHADIDGVY AGLRPLLAGE
     SDDTSKLSRE HAVAVPAAGL VAIAGGKYTT YRVMAADAID AAVQFIPARV APSITEKVSL
     LGADGYFALV NQAEHVGALQ GLHPYRVRHL LDRYGSLISD VLAMAASDPS LLSPITEAPG
     YLKVEAAYAA AAEGALHLED ILARRMRISI EYPHRGVDCA REVAEVVAPV LGWTAADIDR
     EVANYMARVE AEVLSQAQPD DVSADMLRAS APEARAEILE PVPLD