ID A0A2D5G776_UNCDE Unreviewed; 439 AA. AC A0A2D5G776; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 29-MAY-2024, entry version 19. DE SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:MAC44545.1}; GN Name=hisD {ECO:0000313|EMBL:MAC44545.1}; GN ORFNames=CL913_11510 {ECO:0000313|EMBL:MAC44545.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Myxococcota; Myxococcia. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAC44545.1, ECO:0000313|Proteomes:UP000226839}; RN [1] {ECO:0000313|Proteomes:UP000226839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|PIRNR:PIRNR000099, CC ECO:0000256|RuleBase:RU004175}. 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:MAC44545.1}. 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; NYVT01000106; MAC44545.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2D5G776; -. DR Proteomes; UP000226839; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro. DR CDD; cd06572; Histidinol_dh; 1. DR Gene3D; 1.20.5.1300; -; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR NCBIfam; TIGR00069; hisD; 1. DR PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000099}; Zinc {ECO:0000256|ARBA:ARBA00022833}. FT ACT_SITE 334 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1" FT ACT_SITE 335 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1" SQ SEQUENCE 439 AA; 47270 MW; ABA9C7896385F247 CRC64; MSTVSFHETS KLKAKDYKAL LKRSEADLSS FLEKVQPIIE AVRAEGDEAL VRFGQQLDGS TPLSKEALKV SETEFAVAFE EVEEAVIEAI RYGITNIRIF HEEQKPETMW MKEIRPGAYA GDRLTPIRSV AIYVPRGKGA FPSVTMMTTV PGVVAEVPKL AVFTPPLPNG SVDAATLVAA SIAGVDTVYK CGGAQAVAAA AFGTETVERA LKIVGPGSPW VVAAKRLLSD IIDPGLPAGP SEAIIFADDS VHGGLAALDL LIEAEHGPDS SAYLVTHSRR VAEEAMAALP DHWAKMTAQR EEFSKIVLTG PYGGILLTSS VEESYQFIND YAPEHLELLS TEPFTHLGHI TEAAEILMGP HTPVCIGNFS LGPNAVLPTS QGAQTYGPLS VHDFMKRSSV GYVTPPAYPE LAKRARVLAR YEGFSSHENA VSPIRERYL //