ID Q5CPN1_CRYPI Unreviewed; 416 AA. AC Q5CPN1; DT 12-APR-2005, integrated into UniProtKB/TrEMBL. DT 12-APR-2005, sequence version 1. DT 24-JAN-2024, entry version 121. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=cgd2_210 {ECO:0000313|EMBL:EAK87381.1}; OS Cryptosporidium parvum (strain Iowa II). OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium. OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK87381.1, ECO:0000313|Proteomes:UP000006726}; RN [1] {ECO:0000313|EMBL:EAK87381.1, ECO:0000313|Proteomes:UP000006726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726}; RX PubMed=15044751; DOI=10.1126/science.1094786; RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G., RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P., RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L., RA Anantharaman V., Aravind L., Kapur V.; RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum."; RL Science 304:441-445(2004). 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAK87381.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAEE01000013; EAK87381.1; -; Genomic_DNA. DR RefSeq; XP_625390.1; XM_625390.1. DR AlphaFoldDB; Q5CPN1; -. DR STRING; 353152.Q5CPN1; -. DR EnsemblProtists; EAK87381; EAK87381; cgd2_210. DR GeneID; 3372365; -. DR KEGG; cpv:cgd2_210; -. DR VEuPathDB; CryptoDB:cgd2_210; -. DR InParanoid; Q5CPN1; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000006726; Chromosome 2. 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000006726}. FT DOMAIN 13..184 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 205..361 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 216 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 18..23 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 106 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 165 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 283..284 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 283 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 416 AA; 46077 MW; 9CFAD9998DB3A140 CRC64; MCLRQHLRCS SLKVTIFGAG SFGSAISCVV GYNTERTLIF NSEVKLWLYD ERLESGEYLA DVINRDHVNV KYLPDFKLPN NIRAVTDLKE ACEDCNLMIF VIPSQFIRSV ASQIRKLDID FSRAVRAVSL TKGFLVENGH PFLISKIIEE ELGIDCCVLS GANVASGLAA KEFGEATLAC SDYDDAYIWQ YLFDTPWFKI DCVPDVICTE LFGGLKNIIA LLVGMIQGLG CGTNTVAAVM RLGVLEMILY GSIFFNIRSS IMTRVFFESC GIADLVTTCL GGRNVRGGKA FTLSNGQKPW EEIEAEVTGG QHLAGLVTLK EINETLEVLL IEKSIDVDKH FPLFRSCFKI AYTGAPPRSL IDILGRNELR ELRFVPSGLL SLIDDSPNHG EVMQRSSSRQ VGSLILSKTQ SCMQYE //