GPDA_LEIMA
ID GPDA_LEIMA Reviewed; 367 AA.
AC Q4QHG4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal;
DE EC=1.1.1.8;
GN Name=GPD; ORFNames=LmjF10.0510, LmjF_10_0510;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; FR796406; CAJ02624.1; -; Genomic_DNA.
DR RefSeq; XP_001681384.1; XM_001681332.1.
DR AlphaFoldDB; Q4QHG4; -.
DR SMR; Q4QHG4; -.
DR STRING; 5664.LmjF.10.0510; -.
DR EnsemblProtists; CAJ02624; CAJ02624; LMJF_10_0510.
DR GeneID; 5649653; -.
DR KEGG; lma:LMJF_10_0510; -.
DR VEuPathDB; TriTrypDB:LmjF.10.0510; -.
DR VEuPathDB; TriTrypDB:LMJLV39_100011000; -.
DR VEuPathDB; TriTrypDB:LMJSD75_100011100; -.
DR eggNOG; KOG2711; Eukaryota.
DR InParanoid; Q4QHG4; -.
DR OMA; LATCNSP; -.
DR Proteomes; UP000000542; Chromosome 10.
DR GO; GO:0005829; C:cytosol; EXP:GeneDB.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0020015; C:glycosome; EXP:GeneDB.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IDA:GeneDB.
DR GO; GO:0051287; F:NAD binding; IDA:GeneDB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Glycosome; NAD; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..367
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT glycosomal"
FT /id="PRO_0000262291"
FT MOTIF 365..367
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 23..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 367 AA; 39299 MW; 49F47113F30B5657 CRC64;
MISTKRHINT NELLHLSKAV VFGSGAFGTA LAMVLSKKCR EVCVWHIKEE EARLVNEKRE
NDLYLRGVQL ASNIIFTSDV DEAYKGAELI LFVIPTQFLR GFFQKSGGNL IAYAKARQVP
VLVCTKGIER STLKFPAQIV GEFFPSNLLS VLAGPSFAIE VATGVFTCVS VASADINVAR
RLQRIMTTGD RSFVCWATTD TVGCEVASAV KNVLAIGSGV ANGLGMGLNA RAALITRGLL
EIRDLTAALG GDGSAIFGLA GFGDLQLTCS SELSRNFTVG KKLGKGLSLE EIQRTSKAVA
EGVATAEPLV RLAQQLKVTM PLCQQIYEVV YKKKNPRAAI ADLLSCGLQD EGLPPLFKKS
AATPSKL
