GLPD2_MYCBO
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 03-AUG-2022, entry version 102.
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; Actinobacteria; Corynebacteriales; 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 EnsemblBacteria; SIU01959; SIU01959; BQ2027_MB3330C.
DR PATRIC; fig|233413.5.peg.3660; -.
DR OMA; CIVNAAG; -.
DR Proteomes; UP000001419; 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_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