ID   GLPD2_MYCBO             Reviewed;         585 AA.
AC   P64185; A0A1R3Y3R5; O07168; X2BMT2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 2;
DE            EC=1.1.5.3;
GN   Name=glpD2; OrderedLocusNames=BQ2027_MB3330C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU01959.1; -; Genomic_DNA.
DR   RefSeq; NP_856975.1; NC_002945.3.
DR   RefSeq; WP_003417217.1; NC_002945.4.
DR   AlphaFoldDB; P64185; -.
DR   SMR; P64185; -.
DR   PATRIC; fig|233413.5.peg.3660; -.
DR   Proteomes; UP000001419; 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: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; 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; 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   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..585
FT                   /note="Glycerol-3-phosphate dehydrogenase 2"
FT                   /id="PRO_0000126103"
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
//