ID A0A5B6UQD5_9ROSI Unreviewed; 436 AA. AC A0A5B6UQD5; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 26-FEB-2020, entry version 3. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185}; GN ORFNames=EPI10_026981 {ECO:0000313|EMBL:KAA3460300.1}; OS Gossypium australe. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium. OX NCBI_TaxID=47621 {ECO:0000313|EMBL:KAA3460300.1, ECO:0000313|Proteomes:UP000325315}; RN [1] {ECO:0000313|EMBL:KAA3460300.1, ECO:0000313|Proteomes:UP000325315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1801 {ECO:0000313|EMBL:KAA3460300.1}; RC TISSUE=Leaf {ECO:0000313|EMBL:KAA3460300.1}; RA Liu F.; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000256|PIRNR:PIRNR000185, ECO:0000256|RuleBase:RU004417}. 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:KAA3460300.1}. 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; SMMG02000009; KAA3460300.1; -; Genomic_DNA. DR Proteomes; UP000325315; Chromosome 12. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR CDD; cd01076; NAD_bind_1_Glu_DH; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR033922; NAD_bind_Glu_DH. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 2. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|PIRSR:PIRSR000185-2}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185, KW ECO:0000256|RuleBase:RU004417}. FT DOMAIN 178..433 FT /note="ELFV_dehydrog" FT /evidence="ECO:0000259|SMART:SM00839" FT ACT_SITE 102 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1" FT BINDING 66 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 90 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 185 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 216 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT BINDING 369 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2" FT SITE 142 FT /note="Important for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3" SQ SEQUENCE 436 AA; 48028 MW; F445F69291765F4E CRC64; MNALAATNRN FQLAARILGL DSKLHKSLLI PFREIKVECT VPRDDGSFVS YIGFRIQHDN ARGPMKGGIR YHPEVDPDEV NALAQLMTWK TAVANLPYGG AKGGIGCNPR ELTVSELERV TRVFTQKIHD LIGIHRDVPA PDMGTNSQTM AWILDEYSKF HGYSPAVVTG KPIELGGSLG REAATGLGVV FATEFLLDEY GMSIANMKFA IQGFGNVGSW AASFIHQKGG KVVAVSDITG AVKNPNGIDI PALLKHKEKA YSLKDFEGGD AMDLNDVLVH ECDVLIPCAL GGVLNKYILC TSYKQSLPFI NSFLFPFKNQ KENAADVKAK FIIEAANHPT DPEADEILSR KGVIILPDIY ANSGGVTVSY FEWVQNIQGF MWEEEKVNYE LKRYMKRAFN DIKAMCHTHN CNLRMGAFAL GVNKVARATV LRGWEA //