ID   A0A2D5G776_9DELT        Unreviewed;       439 AA.
AC   A0A2D5G776;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   05-DEC-2018, entry version 6.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024,
GN   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};
RN   [1] {ECO:0000313|EMBL:MAC44545.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CPC295 {ECO:0000313|EMBL:MAC44545.1};
RX   PubMed=29337314; DOI=.1038/sdata.2017.203;
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The reconstruction of 2,631 draft metagenome-assembled genomes from
RT   the global oceans.";
RL   Sci. Data 5:170203-170203(2018).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00728939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2
CC         NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC         ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729200};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00781837};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00729141}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|RuleBase:RU004175, ECO:0000256|SAAS:SAAS00827949}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01024}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:MAC44545.1}.
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DR   EMBL; NYVT01000106; MAC44545.1; -; Genomic_DNA.
DR   UniPathway; UPA00031; UER00014.
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:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729217};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728911};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00781816};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
KW   ECO:0000256|SAAS:SAAS00751613};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00751612};
KW   Zinc {ECO:0000256|SAAS:SAAS00781803}.
FT   ACT_SITE    334    334       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    335    335       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                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
//