(data stored in ACNUC7421 zone)

SWISSPROT: HISX1_RUEPO

ID   HISX1_RUEPO             Reviewed;         435 AA.
AC   Q5LVV1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Histidinol dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01024};
DE            Short=HDH 1 {ECO:0000255|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN   Name=hisD1 {ECO:0000255|HAMAP-Rule:MF_01024};
GN   OrderedLocusNames=SPO0594;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93909.1; -; Genomic_DNA.
DR   RefSeq; WP_011046350.1; NC_003911.12.
DR   SMR; Q5LVV1; -.
DR   STRING; 246200.SPO0594; -.
DR   EnsemblBacteria; AAV93909; AAV93909; SPO0594.
DR   KEGG; sil:SPO0594; -.
DR   eggNOG; ENOG4105CEK; Bacteria.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K15509; -.
DR   OMA; CYGSLFL; -.
DR   OrthoDB; 935289at2; -.
DR   BioCyc; RPOM246200:G1G48-602-MONOMER; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001023; 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;
DR   PRODOM; Q5LVV1.
DR   SWISS-2DPAGE; Q5LVV1.
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    435       Histidinol dehydrogenase 1.
FT                                /FTId=PRO_0000135846.
FT   ACT_SITE    319    319       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   ACT_SITE    320    320       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   METAL       249    249       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       252    252       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       353    353       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   METAL       412    412       Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   BINDING     119    119       NAD. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   BINDING     181    181       NAD. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   BINDING     204    204       NAD. {ECO:0000255|HAMAP-Rule:MF_01024}.
FT   BINDING     227    227       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     249    249       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     252    252       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     320    320       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     353    353       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     407    407       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
FT   BINDING     412    412       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01024}.
SQ   SEQUENCE   435 AA;  46644 MW;  093DF7F337198357 CRC64;
     MTIEYLKKAS LTSKSDASDV QETVRAILAD IEAGGDQVAL DYAAKFDRYE GSIILSPEEI
     EAACAKVPEK LKADIRFAHD NVRRFAETQK ATLTDVELEV VPGVITGQKA IPVDAAGCYV
     PGGRYSHIAS AIMTVTTAKV AGCKHIMACS PPRPGVGVAP AIVYAAHICG ADTIMAIGGV
     QGVASMAFGL FGLPKAKILV GPGNQFVAEA KRMLFGRVGI DMIAGPTDSL ILADRTADPH
     IVTTDLVSQA EHGYNSPVWL VTDDRALAEK VIEMIPSYIA DLPEVNRDNA AAAWRDYAEV
     ILCADREEMA ATSDRYAPEH LTVMAEDLDW WLDRLSCYGS LFLGEESTVS YGDKAAGTNH
     VLPTSGAASY TGGLSVHKYM KIVTWQRGTR EGYKPVAEAT ARIARLEGME GHARAADVRL
     AKYFPDETFD LTANG
//

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