ID   A0A2D5G776_UNCDE        Unreviewed;       439 AA.
AC   A0A2D5G776;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:MAC44545.1};
GN   Name=hisD {ECO:0000313|EMBL:MAC44545.1};
GN   ORFNames=CL913_11510 {ECO:0000313|EMBL:MAC44545.1};
OS   Deltaproteobacteria bacterium.
OC   Bacteria; Proteobacteria; Deltaproteobacteria.
OX   NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAC44545.1, ECO:0000313|Proteomes:UP000226839};
RN   [1] {ECO:0000313|Proteomes:UP000226839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MAC44545.1}.
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DR   EMBL; NYVT01000106; MAC44545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D5G776; -.
DR   Proteomes; UP000226839; Unassembled WGS sequence.
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   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   TIGRFAMs; TIGR00069; hisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000099}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
SQ   SEQUENCE   439 AA;  47270 MW;  ABA9C7896385F247 CRC64;
     MSTVSFHETS KLKAKDYKAL LKRSEADLSS FLEKVQPIIE AVRAEGDEAL VRFGQQLDGS
     TPLSKEALKV SETEFAVAFE EVEEAVIEAI RYGITNIRIF HEEQKPETMW MKEIRPGAYA
     GDRLTPIRSV AIYVPRGKGA FPSVTMMTTV PGVVAEVPKL AVFTPPLPNG SVDAATLVAA
     SIAGVDTVYK CGGAQAVAAA AFGTETVERA LKIVGPGSPW VVAAKRLLSD IIDPGLPAGP
     SEAIIFADDS VHGGLAALDL LIEAEHGPDS SAYLVTHSRR VAEEAMAALP DHWAKMTAQR
     EEFSKIVLTG PYGGILLTSS VEESYQFIND YAPEHLELLS TEPFTHLGHI TEAAEILMGP
     HTPVCIGNFS LGPNAVLPTS QGAQTYGPLS VHDFMKRSSV GYVTPPAYPE LAKRARVLAR
     YEGFSSHENA VSPIRERYL
//