ID   HISX_BRUSU              Reviewed;         430 AA.
AC   Q8G2R2; G0KBV1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=BR0252, BS1330_I0253;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014291; AAN29201.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM17614.1; -; Genomic_DNA.
DR   RefSeq; WP_004687945.1; NZ_KN046804.1.
DR   PDB; 4G07; X-ray; 1.95 A; A=1-430.
DR   PDB; 4G09; X-ray; 1.90 A; A=1-430.
DR   PDBsum; 4G07; -.
DR   PDBsum; 4G09; -.
DR   AlphaFoldDB; Q8G2R2; -.
DR   SMR; Q8G2R2; -.
DR   BindingDB; Q8G2R2; -.
DR   ChEMBL; CHEMBL5431; -.
DR   GeneID; 55590035; -.
DR   KEGG; bms:BR0252; -.
DR   KEGG; bsi:BS1330_I0253; -.
DR   PATRIC; fig|204722.21.peg.1041; -.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   PhylomeDB; Q8G2R2; -.
DR   BRENDA; 1.1.1.23; 8693.
DR   UniPathway; UPA00031; UER00014.
DR   PRO; PR:Q8G2R2; -.
DR   Proteomes; UP000007104; Chromosome I.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..430
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135741"
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"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           12..20
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           30..44
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           70..79
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           82..100
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           139..152
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           189..198
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           215..224
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          238..243
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           249..260
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          267..273
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           275..291
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           296..305
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           314..324
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          327..333
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   TURN            339..342
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          347..352
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           357..362
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           375..377
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           384..387
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   STRAND          388..395
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           398..414
FT                   /evidence="ECO:0007829|PDB:4G09"
FT   HELIX           418..430
FT                   /evidence="ECO:0007829|PDB:4G09"
SQ   SEQUENCE   430 AA;  46072 MW;  2752FA59731001E0 CRC64;
     MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL DYSRRFDRID
     LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA RQLPKDDRYT DALGVELGSR
     WTAIEAVGLY VPGGTASYPS SVLMNAMPAK VAGVDRIVMV VPAPDGNLNP LVLVAARLAG
     VSEIYRVGGA QAIAALAYGT ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL
     IVADKDNNPD WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA
     SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF IGGYTPEVIG
     DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ LRALGPAAIE IARAEGLDAH
     AQSVAIRLNL
//