ID A0A384LJQ7_PLAKH Unreviewed; 393 AA.
AC A0A384LJQ7; A0A1A7VFD9; B3L4U8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN ORFNames=PKNH_0912300 {ECO:0000313|EMBL:CAA9988170.1};
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9988170.1, ECO:0000313|Proteomes:UP000031513};
RN [1] {ECO:0000313|EMBL:CAA9988170.1, ECO:0000313|Proteomes:UP000031513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H {ECO:0000313|EMBL:CAA9988170.1,
RC ECO:0000313|Proteomes:UP000031513};
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA Newbold C.I., Barrell B.G., Berriman M.;
RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT with host range from monkey to man.";
RL Nature 455:799-803(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00001662,
CC ECO:0000256|RuleBase:RU361243};
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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DR EMBL; AM910991; CAA9988170.1; -; Genomic_DNA.
DR RefSeq; XP_002259146.1; XM_002259110.1.
DR AlphaFoldDB; A0A384LJQ7; -.
DR STRING; 5851.A0A384LJQ7; -.
DR GeneID; 7320708; -.
DR KEGG; pkn:PKNH_0912300; -.
DR VEuPathDB; PlasmoDB:PKNH_0912300; -.
DR InParanoid; A0A384LJQ7; -.
DR OMA; NRMFGNM; -.
DR OrthoDB; 3675564at2759; -.
DR Proteomes; UP000031513; Chromosome 9.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1.
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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Reference proteome {ECO:0000313|Proteomes:UP000031513};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..393
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030070941"
FT DOMAIN 41..211
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 231..378
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 46..51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 306..307
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 393 AA; 43800 MW; 3928D020A02C006C CRC64;
MKSYLSYFLL VPQLATCFSG SKPNVSRNTL VSNTTNNLPL KVSVIGSGSW GTVVSKIVAE
NTHKSKIFHP LVKMYVKEEI VDNDKLSNII NKKKENVKYM KGMKVPDNVL ATSNLKDAVE
GADLLIFVVP HQYLESVLNE IVKNENLKKD AKAISLMKGI KIDNCKPMLL SSVIEEKLNI
GCAALSGSNI ANELSTENFS ESTIGFEDAQ EAGIWQELFD RTYFKINCVE DKPGVETCGA
LKNVVALGVG FLDASSHSYN TKSAIIRIGL DEMKRFTRFF FPDVLDETFL DSCGLADLIT
TCLGGRNLKC AREFATRNGA DTWDQIEMEL LNGQKLQGIH TAKEVYSVLE HHKLKNEFPL
FTTIYEIAFL HKNPSSIIDV LSTKKLRHIK YKG
//
