GLPD1_MYCTO
ID GLPD1_MYCTO Reviewed; 516 AA.
AC P9WN80; 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 37.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase 1;
DE EC=1.1.5.3;
GN Name=glpD1; Synonyms=glpD; OrderedLocusNames=MT2309;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK46593.1; Type=Erroneous initiation; Evidence={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; AE000516; AAK46593.1; ALT_INIT; Genomic_DNA.
DR PIR; E70779; E70779.
DR RefSeq; WP_003411591.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN80; -.
DR SMR; P9WN80; -.
DR EnsemblBacteria; AAK46593; AAK46593; MT2309.
DR KEGG; mtc:MT2309; -.
DR PATRIC; fig|83331.31.peg.2486; -.
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..516
FT /note="Glycerol-3-phosphate dehydrogenase 1"
FT /id="PRO_0000427173"
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