HISX_BRUSU
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 03-AUG-2022, entry version 112.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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 EnsemblBacteria; AEM17614; AEM17614; BS1330_I0253.
DR GeneID; 45051388; -.
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 OMA; MVTGPGN; -.
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 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 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
