(data stored in ACNUC10821 zone)

SWISSPROT: HISX_LISMF

ID   HISX_LISMF              Reviewed;         427 AA.
AC   Q722Y3;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 90.
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=LMOf2365_0596;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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
CC         NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23;
CC         Evidence={ECO:0000255|HAMAP-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-
CC       Rule:MF_01024};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine 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}.
DR   EMBL; AE017262; AAT03378.1; -; Genomic_DNA.
DR   RefSeq; WP_003725469.1; NC_002973.6.
DR   SMR; Q722Y3; -.
DR   EnsemblBacteria; AAT03378; AAT03378; LMOf2365_0596.
DR   KEGG; lmf:LMOf2365_0596; -.
DR   HOGENOM; HOG000243914; -.
DR   KO; K00013; -.
DR   OMA; QAEHDPM; -.
DR   BioCyc; LMON265669:G1G0V-611-MONOMER; -.
DR   UniPathway; UPA00031; UER00014.
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;
DR   PRODOM; Q722Y3.
DR   SWISS-2DPAGE; Q722Y3.
KW   Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Zinc.
FT   CHAIN         1    427       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135792.
FT   ACT_SITE    322    322       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   ACT_SITE    323    323       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   METAL       254    254       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       257    257       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       356    356       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       415    415       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   BINDING     232    232       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     254    254       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     257    257       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     323    323       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     356    356       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     410    410       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     415    415       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
SQ   SEQUENCE   427 AA;  46147 MW;  015FC5F410CC90A3 CRC64;
     MKILTGTVNE LLNELKIETD TNTSIQVETE VKTIIEKVKT AGDQALFDFT SKFDGVGLTE
     LRVPAADIQA ASAKIEPAFL DALQQAKVNI ESFHSKQKQH AFLDSEKDGV IRGQLIRPLE
     TVGVYVPGGT AAYPSSVLMN VLPAKIAGVK RIVMITPPGE NGINPYVLAS AQLAGVDEIY
     QVGGAHGIAA LAHGTESIPK VDKIVGPGNI YVATAKREVF GLVDIDMIAG PSEIVVLADE
     NANPAFIAAD LLSQAEHDIL ARAILITTSK KIAEETQNEI DKQLENLPRK AIAQKSIETR
     GKIIIAATTQ EMFDIMNEIA PEHLEVQLEN PMNYLYQIKN AGSIFLGSYA SEPLGDYFAG
     PNHVLPTSGT AKFFSPLGVE DFTKRSAFIS YTKEALAKEK DAIVLLAKKE GLDAHAKAIQ
     IRFEEEN
//

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