ID HISX_MYCBO Reviewed; 444 AA. AC P63951; A0A1R3XYS9; O08396; X2BIB0; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-MAY-2022, sequence version 2. DT 24-JAN-2024, entry version 116. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=BQ2027_MB1625; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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 -!- SEQUENCE CAUTION: CC Sequence=SIU00229.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WNW9}; 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; LT708304; SIU00229.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_855278.1; NC_002945.3. DR AlphaFoldDB; P63951; -. DR SMR; P63951; -. DR PATRIC; fig|233413.5.peg.1774; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001419; 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..444 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135795" FT ACT_SITE 341 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 342 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 250 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 272 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 342 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 375 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 375 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 429 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 434 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 434 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 444 AA; 45941 MW; 31A898623DF1B0DD CRC64; MTAPPPVLTR IDLRGAELTA AELRAALPRG GADVEAVLPT VRPIVAAVAE RGAEAALDFG ASFDGVRPHA IRVPDAALDA ALAGLDCDVC EALQVMVERT RAVHSGQRRT DVTTTLGPGA TVTERWVPVE RVGLYVPGGN AVYPSSVVMN VVPAQAAGVD SLVVASPPQA QWDGMPHPTI LAAARLLGVD EVWAVGGAQA VALLAYGGTD TDGAALTPVD MITGPGNIYV TAAKRLCRSR VGIDAEAGPT EIAILADHTA DPVHVAADLI SQAEHDELAA SVLVTPSEDL ADATDAELAG QLQTTVHRER VTAALTGRQS AIVLVDDVDA AVLVVNAYAA EHLEIQTADA PQVASRIRSA GAIFVGPWSP VSLGDYCAGS NHVLPTAGCA RHSSGLSVQT FLRGIHVVEY TEAALKDVSG HVITLATAED LPAHGEAVRR RFER //