ID   HISX_BUCMH              Reviewed;         201 AA.
AC   Q9RQ82;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-MAY-2023, entry version 79.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
DE   Flags: Fragment;
GN   Name=hisD;
OS   Buchnera aphidicola subsp. Melaphis rhois.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10555290; DOI=10.1093/oxfordjournals.molbev.a026071;
RA   Clark M.A., Moran N.A., Baumann P.;
RT   "Sequence evolution in bacterial endosymbionts having extreme base
RT   compositions.";
RL   Mol. Biol. Evol. 16:1586-1598(1999).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF129283; AAF13776.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RQ82; -.
DR   SMR; Q9RQ82; -.
DR   UniPathway; UPA00031; UER00014.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR012131; Hstdl_DH.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Zinc.
FT   CHAIN           1..>201
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135745"
FT   NON_TER         201
SQ   SEQUENCE   201 AA;  22028 MW;  E0FA5769CF7DB395 CRC64;
     MKNCLKIIHW DRCSIEEREK ILSRPILDDL SAIKKQVKTI ISDVNSLGDQ ALYNYTNIFD
     KIKLNNIKIS HQDLVKAELC IDVKAKNAIQ VAIDNIRTFH ISQNISTLNI EINKGIYCQQ
     IVRPIGSVGL YIPGGSAPLL STVLMLAIPA RIAGCKKIVL CSPPPITNEV LYASKICGVQ
     EIFQVGGAQA IAALGFGTET I
//