ID   HISXH_RUEPO             Reviewed;         433 AA.
AC   Q5LUS2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=SPO0981;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P06988};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06988};
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000031; AAV94285.1; -; Genomic_DNA.
DR   RefSeq; WP_011046729.1; NC_003911.12.
DR   AlphaFoldDB; Q5LUS2; -.
DR   SMR; Q5LUS2; -.
DR   STRING; 246200.SPO0981; -.
DR   PaxDb; 246200-SPO0981; -.
DR   KEGG; sil:SPO0981; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_0_5; -.
DR   OrthoDB; 9805269at2; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
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; IEA:InterPro.
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   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:SF14; HISTIDINOL DEHYDROGENASE; 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   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..433
FT                   /note="Histidinol dehydrogenase homolog"
FT                   /id="PRO_0000135847"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   433 AA;  45353 MW;  B67DC5531FADA3A3 CRC64;
     MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS GEIVVSPDQV
     ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL RPGLIAGQKQ IPLAAAGAYV
     PGGRYAHIAS ALMSIATARA AGVGQITAVS PPQVGRGVHP AILYAMSLAG ADRILALGGV
     QGVAALAFGL FGAPPADILV GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL
     TVAWDLVGQA EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV
     ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA FGDKASGPNH
     VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT ATISRAEGME GHARTADIRL
     EKLRPTLRQV GTG
//