ID   HISX_MYCSM              Reviewed;         445 AA.
AC   P28736;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   PubMed=1435262; DOI=10.1111/j.1365-2958.1992.tb01468.x;
RA   Hinshelwood S., Stoker N.G.;
RT   "Cloning of mycobacterial histidine synthesis genes by complementation of a
RT   Mycobacterium smegmatis auxotroph.";
RL   Mol. Microbiol. 6:2887-2895(1992).
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}.
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DR   EMBL; X65542; CAA46509.1; -; Genomic_DNA.
DR   PIR; S26209; S26209.
DR   AlphaFoldDB; P28736; -.
DR   SMR; P28736; -.
DR   OMA; YIAGPNH; -.
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..445
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135798"
FT   ACT_SITE        342
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         430
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  46703 MW;  19996D28D4591170 CRC64;
     MNMMAKFQMS RIDLRNRVLS AAQLRSALPR GGVDVDAVVP KVRPIVDAVA QRGAQAALEY
     GESFDGIRPE TVRVPRELLS QALENLDADV RAALQVSIDR ARAVHADQRR TDTTTTLAPG
     ATVTERWVPV ERVGLYVPGG NAVYPSSVVM NVVPAQTAGV DSMVIASPPQ GQFGGRPHPT
     ILAAAALLGV DEVWAVGGAQ AVALLAYGGT DTDGAELAPV DMITGPGNIY VTAAKRICRS
     QVGIDAEAGP TEIAILADHT ADPVHVAADL ISQAEHDEMA ASVLVTDSET LAEATDRELA
     NQLATTKHVE RVTAALSGKQ SAIVLVDDID AGVRTVNAYA AEHLEIQTVD APGVAGRIRS
     AGAIFVGAWS PVSLGDYCAG SNHVLPTAGC ARHSSGLSVQ TFLRGIHVVE YDEAALKDVS
     GHVITLSKAE DLPAHGEAVR RRFER
//