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Database: UniProt
Entry: R9LPY7_9FIRM
LinkDB: R9LPY7_9FIRM
Original site: R9LPY7_9FIRM 
ID   R9LPY7_9FIRM            Unreviewed;       430 AA.
AC   R9LPY7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024};
GN   ORFNames=C815_01391 {ECO:0000313|EMBL:EOS60401.1};
OS   Firmicutes bacterium M10-2.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS60401.1, ECO:0000313|Proteomes:UP000014154};
RN   [1] {ECO:0000313|EMBL:EOS60401.1, ECO:0000313|Proteomes:UP000014154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M10-2 {ECO:0000313|EMBL:EOS60401.1,
RC   ECO:0000313|Proteomes:UP000014154};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Firmicutes bacterium M10-2.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:0000256|HAMAP-
CC         Rule:MF_01024};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC         ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024,
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:EOS60401.1}.
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DR   EMBL; ASTB01000028; EOS60401.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9LPY7; -.
DR   STRING; 1235796.C815_01391; -.
DR   PATRIC; fig|1235796.3.peg.1399; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_0_9; -.
DR   OrthoDB; 9805269at2; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000014154; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01024};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01024}; Reference proteome {ECO:0000313|Proteomes:UP000014154};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   430 AA;  47135 MW;  3490CAA0C85EA0F2 CRC64;
     MLQALNKNDS QTLMKYVSER TQEISSDILI KVTEIIDQVR EQGDDALYEF TKKFDQIDLP
     SLKVSEEEME QAIRQCDPDF MEAMKQAKEN IEFYHQAQKQ NSFLLQKELN IYLGQRVIPL
     DSVGIYVPGG RAQYPSSVLM NAIPAHVAGV KRIVMVTPPN KQGTIHPNIA FAAKLAGITE
     IYKVGGAQAI AALAYGTGTI RAVDKIVGPG NIFVAAAKKL VFGKVDIDMI AGPSEILVIA
     DKNAKPEYVA ADLLSQAEHD PMACSILIST SQNLVDAVNK ELRKQAEELP KKEIVETSLA
     DHGHSIVCDT IEEAIAISNL IAPEHLELMI EDPMSYLGLV KHAGSVFLGY HTCESVGDYF
     GGTNHVLPTS GTARFSSALG VDSFIKKSSF LHYSKEALDM YGEMIVKMAQ EEQLDAHANA
     ILVRLKDGKQ
//
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