ID   HISX_SYNY3              Reviewed;         434 AA.
AC   P73058;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=slr1848;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
CC   -!- CAUTION: The conserved zinc-binding site Asp residue in position 364 is
CC       replaced by a Thr. {ECO:0000305}.
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DR   EMBL; BA000022; BAA17080.1; -; Genomic_DNA.
DR   PIR; S75166; S75166.
DR   AlphaFoldDB; P73058; -.
DR   SMR; P73058; -.
DR   IntAct; P73058; 3.
DR   STRING; 1148.1652156; -.
DR   PaxDb; P73058; -.
DR   EnsemblBacteria; BAA17080; BAA17080; BAA17080.
DR   KEGG; syn:slr1848; -.
DR   eggNOG; COG0141; Bacteria.
DR   InParanoid; P73058; -.
DR   OMA; VCTPPDK; -.
DR   PhylomeDB; P73058; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001425; 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: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; IBA:GO_Central.
DR   CDD; cd06572; Histidinol_dh; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..434
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135865"
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  46534 MW;  76F07AC33439B1E1 CRC64;
     MTRILKLSHL TPQQLNQLKR RSEQNIDQAL AIAKEVIEQV KMEGDAGVLH YSRQFDFAGA
     TAENLRVSEA EFAEAEKLVD PELRRAVEHA FRNIEKVHAG QMPPPMHLAE IEPGVFAGEK
     ITPLPTVGLY VPRGKGAFPS MMLMLAVPAR VAGVKKIVVC TPPDKEGKVE PVSLVTARMA
     GVDEVYKLGG VQALAAIAYG TKTVSKVDKL IGPCSIYGAA AKRLLSGIVD VGLPAGPSES
     IVLADETTDP KLAALDLLIE AEHGSDSAAL LVTHSASLAE KALGYLGEYL EKLPPWRKKF
     CEDGLGSYGG ILLTDSLQAS LDFINDYAPE HLQVLTADPL KLVGKIDNAG EILLGNYTPS
     SAATYAIGVN AVLPTGGFAR SYSAVSVFDF LKRSTLAYLT EEGFAGVKET VTTLADYEDF
     PAHALAIRER ENLL