GLPD2_MYCTU
ID GLPD2_MYCTU Reviewed; 585 AA.
AC P9WN79; L0TDR3; O07168; P64184;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase 2;
DE EC=1.1.5.3;
GN Name=glpD2; OrderedLocusNames=Rv3302c; ORFNames=MTCI418A.04c, MTV016.01c;
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}.
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DR EMBL; AL123456; CCP46121.1; -; Genomic_DNA.
DR PIR; H70533; H70533.
DR RefSeq; NP_217819.1; NC_000962.3.
DR RefSeq; WP_003417217.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WN79; -.
DR SMR; P9WN79; -.
DR STRING; 83332.Rv3302c; -.
DR PaxDb; P9WN79; -.
DR DNASU; 887211; -.
DR GeneID; 887211; -.
DR KEGG; mtu:Rv3302c; -.
DR TubercuList; Rv3302c; -.
DR eggNOG; COG0578; Bacteria.
DR OMA; CIVNAAG; -.
DR PhylomeDB; P9WN79; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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..585
FT /note="Glycerol-3-phosphate dehydrogenase 2"
FT /id="PRO_0000126102"
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