ID   GLPD1_MYCTU             Reviewed;         516 AA.
AC   P9WN81; L0T922; P64182; Q10502;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1;
DE            EC=1.1.5.3;
GN   Name=glpD1; Synonyms=glpD; OrderedLocusNames=Rv2249c; ORFNames=MTCY427.31c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP45029.1; -; Genomic_DNA.
DR   PIR; E70779; E70779.
DR   RefSeq; NP_216765.1; NC_000962.3.
DR   RefSeq; WP_003411591.1; NZ_NVQJ01000008.1.
DR   AlphaFoldDB; P9WN81; -.
DR   SMR; P9WN81; -.
DR   STRING; 83332.Rv2249c; -.
DR   PaxDb; P9WN81; -.
DR   DNASU; 887276; -.
DR   GeneID; 887276; -.
DR   KEGG; mtu:Rv2249c; -.
DR   PATRIC; fig|83332.111.peg.2503; -.
DR   TubercuList; Rv2249c; -.
DR   eggNOG; COG0578; Bacteria.
DR   OMA; GVMTIMN; -.
DR   PhylomeDB; P9WN81; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
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:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..516
FT                   /note="Glycerol-3-phosphate dehydrogenase 1"
FT                   /id="PRO_0000126100"
FT   BINDING         28..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  54176 MW;  164A136FEEB402E6 CRC64;
     MLMPHSAALN AARRSADLTA LADGGALDVI VIGGGITGVG IALDAATRGL TVALVEKHDL
     AFGTSRWSSK LVHGGLRYLA SGNVGIARRS AVERGILMTR NAPHLVHAMP QLVPLLPSMG
     HTKRALVRAG FLAGDALRVL AGTPAATLPR SRRIPASRVV EIAPTVRRDG LDGGLLAYDG
     QLIDDARLVM AVARTAAQHG ARILTYVGAS NVTGTSVELT DRRTRQSFAL SARAVINAAG
     VWAGEIDPSL RLRPSRGTHL VFDAKSFANP TAALTIPIPG ELNRFVFAMP EQLGRIYLGL
     TDEDAPGPIP DVPQPSSEEI TFLLDTVNTA LGTAVGTKDV IGAYAGLRPL IDTGGAGVQG
     RTADVSRDHA VFESPSGVIS VVGGKLTEYR YMAEDVLNRA ITLRHLRAAK CRTRNLPLIG
     APANPGPAPG SGAGLPESLV ARYGAEAANV AAAATCERPT EPVADGIDVT RAEFEYAVTH
     EGALDVDDIL DRRTRIGLVP RDRERVVAVA KEFLSR