HISX_ECOLI
ID HISX_ECOLI Reviewed; 434 AA.
AC P06988; O08506; P78076; Q47254;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 189.
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, ECO:0000303|PubMed:3018428};
GN OrderedLocusNames=b2020, JW2002;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3018428; DOI=10.1007/bf00422061;
RA Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.;
RT "Nucleotide sequence of the Escherichia coli hisD gene and of the
RT Escherichia coli and Salmonella typhimurium hisIE region.";
RL Mol. Gen. Genet. 203:382-388(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3100 / ATCC 14948 / DSM 6302;
RX PubMed=2194167; DOI=10.1093/nar/18.12.3634;
RA Savic D.J., Jovanovic G., Kostic T.;
RT "Nucleotide and amino acid polymorphism in the gene for L-histidinol
RT dehydrogenase of Escherichia coli K12.";
RL Nucleic Acids Res. 18:3634-3634(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-319.
RX PubMed=6246067; DOI=10.1128/jb.142.1.32-42.1980;
RA Bruni C.B., Musti A.M., Frunzio R., Blasi F.;
RT "Structural and physiological studies of the Escherichia coli histidine
RT operon inserted into plasmid vectors.";
RL J. Bacteriol. 142:32-42(1980).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9] {ECO:0007744|PDB:1K75, ECO:0007744|PDB:1KAE, ECO:0007744|PDB:1KAH, ECO:0007744|PDB:1KAR}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH L-HISTIDINE; NAD AND
RP ZINC, ACTIVE SITE, AND COFACTOR.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=11842181; DOI=10.1073/pnas.022476199;
RA Barbosa J.A.R.G., Sivaraman J., Li Y., Larocque R., Matte A., Schrag J.D.,
RA Cygler M.;
RT "Mechanism of action and NAD+-binding mode revealed by the crystal
RT structure of L-histidinol dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1859-1864(2002).
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:0000269|PubMed:11842181};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11842181};
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01024, ECO:0000305}.
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DR EMBL; X13462; CAA31812.1; -; Genomic_DNA.
DR EMBL; X03972; CAA27610.1; -; Genomic_DNA.
DR EMBL; X52656; CAA36882.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75081.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15851.1; -; Genomic_DNA.
DR EMBL; M10483; AAA23962.1; -; Genomic_DNA.
DR PIR; C64967; DEECHT.
DR RefSeq; NP_416524.1; NC_000913.3.
DR RefSeq; WP_000009594.1; NZ_LN832404.1.
DR PDB; 1K75; X-ray; 1.75 A; A/B=1-434.
DR PDB; 1KAE; X-ray; 1.70 A; A/B=1-434.
DR PDB; 1KAH; X-ray; 2.10 A; A/B=1-434.
DR PDB; 1KAR; X-ray; 2.10 A; A/B=1-434.
DR PDBsum; 1K75; -.
DR PDBsum; 1KAE; -.
DR PDBsum; 1KAH; -.
DR PDBsum; 1KAR; -.
DR AlphaFoldDB; P06988; -.
DR SMR; P06988; -.
DR BioGRID; 4260403; 27.
DR BioGRID; 850878; 1.
DR IntAct; P06988; 7.
DR STRING; 511145.b2020; -.
DR ChEMBL; CHEMBL2366464; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB03811; Histidinol.
DR DrugBank; DB03366; Imidazole.
DR SWISS-2DPAGE; P06988; -.
DR jPOST; P06988; -.
DR PaxDb; P06988; -.
DR PRIDE; P06988; -.
DR EnsemblBacteria; AAC75081; AAC75081; b2020.
DR EnsemblBacteria; BAA15851; BAA15851; BAA15851.
DR GeneID; 66674082; -.
DR GeneID; 946531; -.
DR KEGG; ecj:JW2002; -.
DR KEGG; eco:b2020; -.
DR PATRIC; fig|1411691.4.peg.232; -.
DR EchoBASE; EB0442; -.
DR eggNOG; COG0141; Bacteria.
DR InParanoid; P06988; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; P06988; -.
DR BioCyc; EcoCyc:HISTDEHYD-MON; -.
DR BioCyc; MetaCyc:HISTDEHYD-MON; -.
DR BRENDA; 1.1.1.23; 2026.
DR UniPathway; UPA00031; UER00014.
DR EvolutionaryTrace; P06988; -.
DR PRO; PR:P06988; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
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; IDA:EcoCyc.
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; Direct protein sequencing;
KW Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..434
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135770"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:11842181"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11842181"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11842181"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11842181"
FT CONFLICT 15
FT /note="E -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="M -> T (in Ref. 2; CAA27610)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="S -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="V -> A (in Ref. 3; CAA36882)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 30..54
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1K75"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1KAR"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 82..100
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1KAH"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 275..289
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1KAE"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:1KAE"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:1KAE"
SQ SEQUENCE 434 AA; 46110 MW; 4B4F2EA00C9BEA4E CRC64;
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA LREYSAKFDK
TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT AQKLPPVDVE TQPGVRCQQV
TRPVASVGLY IPGGSAPLFS TVLMLATPAS IAGCKKVVLC SPPPIADEIL YAAQLCGVQD
VFNVGGAQAI AALAFGTESV PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL
VIADSGATPD FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL GDWSPESAGD
YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF SALASTIETL AAAERLTAHK
NAVTLRVNAL KEQA
