ID HISX_AQUAE Reviewed; 426 AA. AC O66976; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=aq_782; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, CC ChEBI:CHEBI:57945; EC=1.1.1.23; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000305}. 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; AE000657; AAC06931.1; -; Genomic_DNA. DR PIR; E70368; E70368. DR RefSeq; NP_213537.1; NC_000918.1. DR RefSeq; WP_010880475.1; NC_000918.1. DR AlphaFoldDB; O66976; -. DR SMR; O66976; -. DR STRING; 224324.aq_782; -. DR EnsemblBacteria; AAC06931; AAC06931; aq_782. DR KEGG; aae:aq_782; -. DR PATRIC; fig|224324.8.peg.621; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_0; -. DR InParanoid; O66976; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. 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 HAMAP; MF_01024; HisD; 1. 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 Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..426 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135717" FT ACT_SITE 323 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 324 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 210 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 233 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 411 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 416 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 426 AA; 47447 MW; 3F54ED61A772C005 CRC64; MRIEDLRKED WKLNERLEYL AKRGEILEEE YEKSVKEILK RVREEGDRAV IEFTKKFDGV ELTPENMEVP FEELEKAYEE IEPEVREALE FAENRIRVFH EKQLENSFFK EEEGIILGQK VVPLEKVGVY VPGGKAAYPS TVLMNVVPAS VAGVEEIIMV SPKPNKYTLA AAYIAGVSRV FQVGGAQAIG ALAYGTEKIP KVDKIVGPGN IYVALAKKLV FGTVDIDMIA GPSEVLVIAD ERANPTWVAA DMLSQAEHDE LAASILLTPS EELANKVKEE VERLLSQLER KEIAQKSLEK FGTIFLVKDL YHACEVANYI APEHLEVMVR EPMALLPELK HAGAIFLGDY TTEPLGDYVL GPNHTLPTGG STRFFSPLGV YDFIKRSSVL YVSREGFKRV ANQAEAIAKA EGLTAHALAV KVRKND //