ID HISX_LEGPH Reviewed; 431 AA. AC Q5ZW87; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; GN OrderedLocusNames=lpg1199; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC OS 33152 / DSM 7513). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A., RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., RA Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella pneumophila."; RL Science 305:1966-1968(2004). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000255|HAMAP-Rule:MF_01024}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01024}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01024}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01024}. 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; AE017354; AAU27284.1; -; Genomic_DNA. DR RefSeq; WP_010946932.1; NC_002942.5. DR RefSeq; YP_095231.1; NC_002942.5. DR AlphaFoldDB; Q5ZW87; -. DR SMR; Q5ZW87; -. DR STRING; 272624.lpg1199; -. DR PaxDb; 272624-lpg1199; -. DR KEGG; lpn:lpg1199; -. DR PATRIC; fig|272624.6.peg.1261; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_0_6; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000609; Chromosome. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule. 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; IEA:UniProtKB-UniRule. 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..431 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135786" FT ACT_SITE 325 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 326 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 124 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 210 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 261 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 326 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 359 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 413 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 418 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 418 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 431 AA; 46714 MW; A9B4D2B3857D6529 CRC64; MLTIKNWQLL SENDKKLCLS RPRQSSAIKE NVLEIINQVQ LSGDKALYDL TKQFDRVNLQ YLQVPQEKIE QANIPKNALN AITQAIGTIS SYHQSLLPEN TEISTASGIT IRNVYRPIQK VGLYVPGGNK TPLVSSLLMQ AIPAKVAGCP IKVLCTPPDA EGEINEHILV AARLCGIDTI YAIGGAQAIA AMAYGTESVI KVDKIFGPGN SYVTQAKTLV AIDADGAAID MPAGPSEVMI LADTEANPEF IAADLLAQAE HGPDSQVILI CDECELANQV NQQLEIQMSY LSRIEFIKRS LANSRIIICS NQSEQLDIIN SYAPEHLIIN RKNPEPWVEK IVAAGTVFLG SWAAETMGDY VTGSNHVLPT SGFARNHSGL STLDFMTRFT VQAINQEAIR NLGPAAMTLA ELEGLDAHAN AVQIRLNTLG D //