ID   HISX_SALTY              Reviewed;         434 AA.
AC   P10370;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=STM2072;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA   Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT   "Structure and function of the Salmonella typhimurium and Escherichia coli
RT   K-12 histidine operons.";
RL   J. Mol. Biol. 203:585-606(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Barnes W.M., Husson R.N., Whittier R.;
RL   Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-15, AND MUTAGENESIS OF CYS-117 AND CYS-154.
RX   PubMed=8314784; DOI=10.1016/s0021-9258(19)85225-0;
RA   Teng H., Segura E., Grubmeyer C.;
RT   "Conserved cysteine residues of histidinol dehydrogenase are not involved
RT   in catalysis. Novel chemistry required for enzymatic aldehyde oxidation.";
RL   J. Biol. Chem. 268:14182-14188(1993).
RN   [5]
RP   SUBUNIT.
RC   STRAIN=LT2;
RX   PubMed=391222; DOI=10.1042/bj1810771;
RA   Buerger E., Goerisch H., Lingens F.;
RT   "The catalytically active form of histidinol dehydrogenase from Salmonella
RT   typhimurium.";
RL   Biochem. J. 181:771-774(1979).
RN   [6]
RP   PRELIMINARY ACTIVE SITE.
RX   PubMed=3533140; DOI=10.1021/bi00365a009;
RA   Grubmeyer C.T., Gray W.R.;
RT   "A cysteine residue (cysteine-116) in the histidinol binding site of
RT   histidinol dehydrogenase.";
RL   Biochemistry 25:4778-4784(1986).
RN   [7]
RP   COFACTOR.
RX   PubMed=2665648; DOI=10.1016/0003-9861(89)90224-5;
RA   Grubmeyer C., Skiadopoulos M., Senior A.E.;
RT   "L-histidinol dehydrogenase, a Zn2+-metalloenzyme.";
RL   Arch. Biochem. Biophys. 272:311-317(1989).
RN   [8]
RP   MUTAGENESIS OF HIS-99; HIS-262; HIS-327; HIS-367 AND HIS-419.
RX   PubMed=10353848; DOI=10.1021/bi982758p;
RA   Teng H., Grubmeyer C.;
RT   "Mutagenesis of histidinol dehydrogenase reveals roles for conserved
RT   histidine residues.";
RL   Biochemistry 38:7363-7371(1999).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
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;
CC         Evidence={ECO:0000269|PubMed:2665648};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:2665648};
CC       Note=Binds 1 zinc ion per subunit. At high pH manganese can replace
CC       zinc. {ECO:0000269|PubMed:2665648};
CC   -!- ACTIVITY REGULATION: Activity is lost when the metal is removed through
CC       urea denaturation or chelation, and can be regained by addition of
CC       metal.
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:0000269|PubMed:391222}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: PubMed:3533140 originally reported Cys-117 to be the active
CC       site. PubMed:8314784 has shown this to be wrong. {ECO:0000305}.
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DR   EMBL; X13464; CAA31823.1; -; Genomic_DNA.
DR   EMBL; J01804; AAA88615.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20976.1; -; Genomic_DNA.
DR   PIR; JS0157; DEEBHT.
DR   RefSeq; NP_461017.1; NC_003197.2.
DR   RefSeq; WP_000009626.1; NC_003197.2.
DR   AlphaFoldDB; P10370; -.
DR   SMR; P10370; -.
DR   STRING; 99287.STM2072; -.
DR   PaxDb; 99287-STM2072; -.
DR   GeneID; 1253593; -.
DR   KEGG; stm:STM2072; -.
DR   PATRIC; fig|99287.12.peg.2194; -.
DR   HOGENOM; CLU_006732_3_0_6; -.
DR   OMA; YIAGPNH; -.
DR   PhylomeDB; P10370; -.
DR   BioCyc; SENT99287:STM2072-MONOMER; -.
DR   BRENDA; 1.1.1.23; 5542.
DR   SABIO-RK; P10370; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Direct protein sequencing; Histidine biosynthesis;
KW   Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8314784"
FT   CHAIN           2..434
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135840"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         99
FT                   /note="H->N: Slight decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10353848"
FT   MUTAGEN         117
FT                   /note="C->A,S: Almost no change in activity."
FT                   /evidence="ECO:0000269|PubMed:8314784"
FT   MUTAGEN         154
FT                   /note="C->A,S: Almost no change in activity."
FT                   /evidence="ECO:0000269|PubMed:8314784"
FT   MUTAGEN         262
FT                   /note="H->N: 7000-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10353848"
FT   MUTAGEN         327
FT                   /note="H->N: 500-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10353848"
FT   MUTAGEN         367
FT                   /note="H->N: Slight decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10353848"
FT   MUTAGEN         419
FT                   /note="H->Q: 20-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:10353848"
SQ   SEQUENCE   434 AA;  45889 MW;  744EDDCDAB5DF6CE CRC64;
     MSFNTLIDWN SCSPEQQRAL LTRPAISASD SITRTVSDIL DNVKTRGDDA LREYSAKFDK
     TEVTALRVTP EEIAAAGARL SDELKQAMTA AVKNIETFHS AQTLPPVDVE TQPGVRCQQV
     TRPVSSVGLY IPGGSAPLFS TVLMLATPAR IAGCQKVVLC SPPPIADEIL YAAQLCGVQE
     IFNVGGAQAI AALAFGSESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL
     VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPDADIARK VAEAVERQLA ELPRADTARQ
     ALSASRLIVT KDLAQCVAIS NQYGPEHLII QTRNARDLVD AITSAGSVFL GDWSPESAGD
     YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKAGF SALASTIETL AAAERLTAHK
     NAVTLRVNAL KEQA
//