ID A7AQJ0_BABBO Unreviewed; 354 AA. AC A7AQJ0; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 24-JAN-2024, entry version 93. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=BBOV_IV004480 {ECO:0000313|EMBL:BAN65625.1, GN ECO:0000313|EMBL:EDO06809.1}; OS Babesia bovis. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Babesiidae; Babesia. OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO06809.1, ECO:0000313|Proteomes:UP000002173}; RN [1] {ECO:0000313|EMBL:EDO06809.1, ECO:0000313|Proteomes:UP000002173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO06809.1}; RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148; RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S., RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D., RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H., RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr., RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F., RA Nene V.M.; RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan RT hemoprotozoa."; RL PLoS Pathog. 3:1401-1413(2007). RN [2] {ECO:0000313|EMBL:EDO06809.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO06809.1}; RA Nene V.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAN65625.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Texas {ECO:0000313|EMBL:BAN65625.1}; RX PubMed=25124460; DOI=10.1186/1471-2164-15-678; RA Yamagishi J., Wakaguri H., Yokoyama N., Yamashita R., Suzuki Y., Xuan X., RA Igarashi I.; RT "The Babesia bovis gene and promoter model: an update from full-length EST RT analysis."; RL BMC Genomics 15:678-678(2014). RN [4] {ECO:0000313|Proteomes:UP000002173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533; RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R., RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.; RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and RT invertebrate hosts."; RL Data Brief 33:106533-106533(2020). RN [5] {ECO:0000313|Proteomes:UP000002173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=33069745; RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R., RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.; RT "Comparative analysis of gene expression between Babesia bovis blood stages RT and kinetes allowed by improved genome annotation."; RL Int. J. Parasitol. 51:123-136(2021). 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 --------------------------------------------------------------------------- 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; AK441831; BAN65625.1; -; mRNA. DR EMBL; AAXT01000002; EDO06809.1; -; Genomic_DNA. DR RefSeq; XP_001610377.1; XM_001610327.1. DR STRING; 5865.A7AQJ0; -. DR EnsemblProtists; EDO06809; EDO06809; BBOV_IV004480. DR GeneID; 5478611; -. DR KEGG; bbo:BBOV_IV004480; -. DR VEuPathDB; PiroplasmaDB:BBOV_IV004480; -. DR eggNOG; KOG2711; Eukaryota. DR Proteomes; UP000002173; Unassembled WGS sequence. 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; PS00957; NAD_G3PDH; 1. PE 2: Evidence at transcript level; 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:UP000002173}. FT DOMAIN 6..176 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 198..343 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 207 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 11..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 98 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 271..272 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 271 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 354 AA; 38854 MW; A61041E1CF19F8A8 CRC64; MATGKKVCVV GCGNWGSAVA KLVAENTPRY PEFDDTVIIY VLEEVFEGRN LSEIINTDHE NKKYLPGIKL PHNILAVPDL KQCIQDSDIF IIVIPHQFVN STVAKIKSFN VMKPGSLAIN LVKGIELTEK VVNCFTDTIE KELGIPCLAL SGANVAKNVA MEEFSEATIG YKNKEHAVLF QRLFDRPYFK INCVPGVSAV QVFGAIKNAV AIAAGFCDGL GLGSNTKAAI MRIGLNEIYR FACKFFKDIN TDVVFESAGV ADLITTCIGG RNVRCAAEFA KHGGKKSWHD IENEMLGGQK LQGTSTCEEV YKVLVAHNME NDFPLFVVTY NIAFQGAEPA ELIRKFSNET LNPF //