ID   E5G8L5_SALMU            Unreviewed;       185 AA.
AC   E5G8L5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=histidinol dehydrogenase {ECO:0000256|ARBA:ARBA00012965};
DE            EC=1.1.1.23 {ECO:0000256|ARBA:ARBA00012965};
DE   Flags: Fragment;
GN   Name=hisD {ECO:0000313|EMBL:ADQ92208.1};
OS   Salmonella muenchen.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=596 {ECO:0000313|EMBL:ADQ92208.1};
RN   [1] {ECO:0000313|EMBL:ADQ92208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SARA72 {ECO:0000313|EMBL:ADQ92208.1};
RX   PubMed=20970525; DOI=10.1016/j.meegid.2010.10.005;
RA   Bell R.L., Gonzalez-Escalona N., Stones R., Brown E.W.;
RT   "Phylogenetic evaluation of the 'Typhimurium' complex of Salmonella strains
RT   using a seven-gene multi-locus sequence analysis.";
RL   Infect. Genet. Evol. 11:83-91(2011).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000256|ARBA:ARBA00003850}.
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         Evidence={ECO:0000256|ARBA:ARBA00001654};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|ARBA:ARBA00004940}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU004175}.
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DR   EMBL; HM798121; ADQ92208.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5G8L5; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001692; Histidinol_DH_CS.
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   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADQ92208.1"
FT   NON_TER         185
FT                   /evidence="ECO:0000313|EMBL:ADQ92208.1"
SQ   SEQUENCE   185 AA;  19137 MW;  F84CC9C1D2D68ABA CRC64;
     TVLMLATPAR IAGCQNVVLC SPPPIADEIL YAAQLCGVQE IFNVGGAQAI AALAFGSESV
     PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD FVASDLLSQA
     EHGPDSQVIL LTPDADIACK VAEAVERQLA ELPRADTARQ ALSASRLIVT KDLAQCVAIS
     NQYGP
//