HISX_SALTY
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 03-AUG-2022, entry version 157.
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; Proteobacteria; 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; P10370; -.
DR EnsemblBacteria; AAL20976; AAL20976; STM2072.
DR GeneID; 1253593; -.
DR KEGG; stm:STM2072; -.
DR PATRIC; fig|99287.12.peg.2194; -.
DR HOGENOM; CLU_006732_3_0_6; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; P10370; -.
DR BioCyc; SENT99287:STM2072-MON; -.
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 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 PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 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
