HISX_LACLA
ID HISX_LACLA Reviewed; 431 AA.
AC Q02136;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=hisD; OrderedLocusNames=LL1209; ORFNames=L0067;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA Delorme C., Ehrlich S.D., Renault P.;
RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6571-6579(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=7687248; DOI=10.1128/jb.175.14.4391-4399.1993;
RA Delorme C., Godon J.-J., Ehrlich S.D., Renault P.;
RT "Gene inactivation in Lactococcus lactis: histidine biosynthesis.";
RL J. Bacteriol. 175:4391-4399(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: This protein is inactive in the dairy strain IL1403. The
CC histidine biosynthesis pathway is not functional in the dairy strain
CC IL1403. {ECO:0000305}.
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DR EMBL; U92974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE005176; AAK05307.1; -; Genomic_DNA.
DR PIR; A86776; A86776.
DR PIR; E45734; E45734.
DR RefSeq; NP_267365.1; NC_002662.1.
DR AlphaFoldDB; Q02136; -.
DR SMR; Q02136; -.
DR STRING; 272623.L0067; -.
DR PaxDb; Q02136; -.
DR EnsemblBacteria; AAK05307; AAK05307; L0067.
DR KEGG; lla:L0067; -.
DR PATRIC; fig|272623.7.peg.1304; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_0_9; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000002196; Chromosome.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..431
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135783"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VARIANT 38
FT /note="A -> E (in strain: IL1403)"
FT VARIANT 43
FT /note="N -> S (in strain: IL1403)"
FT VARIANT 69
FT /note="R -> P (in strain: IL1403)"
FT VARIANT 74
FT /note="A -> T (in strain: IL1403)"
FT VARIANT 164
FT /note="A -> T (in strain: IL1403)"
FT VARIANT 245
FT /note="K -> E (in strain: IL1403)"
FT VARIANT 248
FT /note="K -> N (in strain: IL1403)"
FT VARIANT 295
FT /note="R -> S (in strain: IL1403)"
FT VARIANT 301..303
FT /note="SIR -> YIS (in strain: IL1403)"
FT VARIANT 316
FT /note="D -> E (in strain: IL1403)"
FT VARIANT 403
FT /note="D -> A (in strain: IL1403)"
FT CONFLICT 25
FT /note="V -> L (in Ref. 3; AAK05307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 47411 MW; 3FFD2B5C75F9D1B0 CRC64;
MLKQIDYQGK LEEIAEKFQG RKTEVSKEVN KTVQQIVADI QKNGDTALFN YAKKFDGYDV
NTSNLLVTRM EREAGLEQID EDYFRILRRT KSQIEEFHKH QLGNSWNIFK ENGVIMGQIA
RPLERVALYV PGGTAAYPST VIMNAVPALL AGVKEIIMIT PVKADGKVNP NILAAAEVCG
IETIYKVGGA QGVAAVAYGT ESIPKVDKIV GPGNIFVATA KKICYGVVDI DMIAGPSEVL
VIADKTAKPK YIAADLMAQA EHDKLASAIL VTTSEKLVQQ VDEELNRQVQ NLERREIIES
SIRNYGGAIV VKNIDDAFDV SNQLAPEHLE VLTSEPLTQL PKIKNAGSIF IGEYTPEPLG
DYMSGSNHVL PTGGTAKFYS GLGVYNFIKY LTYSYYPKEV LADFKEDVET FAKSEGLTAH
ANSISVRFDE M
