ID HISX_LISMF Reviewed; 427 AA. AC Q722Y3; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 102. 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=LMOf2365_0596; OS Listeria monocytogenes serotype 4b (strain F2365). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F2365; RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H., RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., RA Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne RT pathogen Listeria monocytogenes reveal new insights into the core genome RT components of this species."; RL Nucleic Acids Res. 32:2386-2395(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; AE017262; AAT03378.1; -; Genomic_DNA. DR RefSeq; WP_003725469.1; NC_002973.6. DR AlphaFoldDB; Q722Y3; -. DR SMR; Q722Y3; -. DR KEGG; lmf:LMOf2365_0596; -. DR HOGENOM; CLU_006732_3_3_9; -. DR UniPathway; UPA00031; UER00014. 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; Zinc. FT CHAIN 1..427 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135792" FT ACT_SITE 322 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 323 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 257 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 323 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 356 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 356 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 410 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 415 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 415 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 427 AA; 46147 MW; 015FC5F410CC90A3 CRC64; MKILTGTVNE LLNELKIETD TNTSIQVETE VKTIIEKVKT AGDQALFDFT SKFDGVGLTE LRVPAADIQA ASAKIEPAFL DALQQAKVNI ESFHSKQKQH AFLDSEKDGV IRGQLIRPLE TVGVYVPGGT AAYPSSVLMN VLPAKIAGVK RIVMITPPGE NGINPYVLAS AQLAGVDEIY QVGGAHGIAA LAHGTESIPK VDKIVGPGNI YVATAKREVF GLVDIDMIAG PSEIVVLADE NANPAFIAAD LLSQAEHDIL ARAILITTSK KIAEETQNEI DKQLENLPRK AIAQKSIETR GKIIIAATTQ EMFDIMNEIA PEHLEVQLEN PMNYLYQIKN AGSIFLGSYA SEPLGDYFAG PNHVLPTSGT AKFFSPLGVE DFTKRSAFIS YTKEALAKEK DAIVLLAKKE GLDAHAKAIQ IRFEEEN //