ID   HISX_RUEPO              Reviewed;         433 AA.
AC   Q5LL27;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024};
GN   OrderedLocusNames=SPOA0202;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OG   Plasmid megaplasmid Spo.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000255|HAMAP-Rule:MF_01024}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01024};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01024};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01024}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR   EMBL; CP000032; AAV97336.1; -; Genomic_DNA.
DR   RefSeq; WP_011241981.1; NC_006569.1.
DR   AlphaFoldDB; Q5LL27; -.
DR   SMR; Q5LL27; -.
DR   PaxDb; 246200-SPOA0202; -.
DR   KEGG; sil:SPOA0202; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   OrthoDB; 9805269at2; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001023; Plasmid megaplasmid Spo.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Plasmid; Reference proteome; Zinc.
FT   CHAIN           1..433
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135848"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ   SEQUENCE   433 AA;  45887 MW;  C15B11CCF2ACC563 CRC64;
     MPQFLDSRQP DFETAFTALL GAKREDSPDV DAVVAGIIAD VRARGDAAVI ELTERFDRVA
     LTPQSLRFST EEIAQAVDEV PAPERAALEL AAARIRAYHE RQMPQDADWT DDTGARLGWR
     WSAVSAAGLY VPGGLASYPS SVLMNAIPAK VAGVGRLAIA VPTPDGQVNP LVLLAAQISG
     VDEVYRIGGA QAIAALAYGT DTIAPVDKIT GPGNAFVAAA KRRVFGKVGI DMIAGPSEIL
     VIADRDNDPD WIALDLLSQA EHDESAQSIL ITDDAAFGRA VAEAVDKRLE TLERRAIAGV
     SWRDFGAVIT VSDLDEAAAL SNRIAPEHLE LCVSDPEALA ARTIHAGAIF LGQYTPEAIG
     DYVGGPNHVL PTARSARFSS GLSVMDFLKR TTMSRMTPEA LRAIGPAAAQ LARSESLEAH
     GLSVQARLDR LNG
//