GLPD_MYCLE
ID GLPD_MYCLE Reviewed; 585 AA.
AC P53435;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase;
DE EC=1.1.5.3;
GN Name=glpD; OrderedLocusNames=ML0713; ORFNames=L308_C1_179;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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;
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; U00022; AAA17328.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30222.1; -; Genomic_DNA.
DR PIR; S73029; S73029.
DR RefSeq; NP_301564.1; NC_002677.1.
DR RefSeq; WP_010907888.1; NC_002677.1.
DR AlphaFoldDB; P53435; -.
DR SMR; P53435; -.
DR STRING; 272631.ML0713; -.
DR EnsemblBacteria; CAC30222; CAC30222; CAC30222.
DR KEGG; mle:ML0713; -.
DR PATRIC; fig|272631.5.peg.1287; -.
DR Leproma; ML0713; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OMA; CIVNAAG; -.
DR Proteomes; UP000000806; 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;
KW Reference proteome.
FT CHAIN 1..585
FT /note="Glycerol-3-phosphate dehydrogenase"
FT /id="PRO_0000126099"
FT BINDING 37..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 585 AA; 63373 MW; 4B468DD09C1C70F8 CRC64;
MTDLIQAPES EQTWPASALG PQQRAAAWER FGTEQFDVVV IGGGVVGSGC ALDAATRGLK
VALVEARDLA SGTSSRSSKM FHGGLRYLEQ LEFGLVREAL YERELSLTTL APHLVKPLPF
LFPLTKRWWE RPYIAAGIFL YDRLGGAKSV PAQKHLTRAG ALRLSPGLKR SSLIGGIRYY
DTVVDDARHT LTVARTAAHY GAVVRCSTQV VALLREGDRV IGVRVRDSED GAVTEIRGHV
VVNATGVWTD EIQALSKQRG RFQVRVSKGV HVVVPRDRIV SDVAMILRTK KSVMFIIPWG
NHWIIGTTDT DWNLDLAHPA ATKADIDYIL QTVNTVLATP LTHADIDGVY AGLRPLLAGE
SDDTSKLTRE HAVAVPVAGL VAIAGGKYTT YRVMAADAID AAVAFVPARV APSITEKVGL
LGADGYFALI NQVEHVAALQ GLHPYRVRHL LDRYGALIGD VLALAAEAPD LLSPIQEAPG
YLKVEARYAV TAEGALHLED ILARRMRVSI EYPHRGVACA REVADVVAPV LGWTAEDIDR
EVATYNARVE AEVLSQAQPD DVSADMLRAS APEARTKIIE PVSLT