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HISX_CAUVC
ID   HISX_CAUVC              Reviewed;         428 AA.
AC   Q9A5V1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; OrderedLocusNames=CC_2346;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24317.1; -; Genomic_DNA.
DR   PIR; A87540; A87540.
DR   RefSeq; NP_421149.1; NC_002696.2.
DR   RefSeq; WP_010920204.1; NC_002696.2.
DR   AlphaFoldDB; Q9A5V1; -.
DR   SMR; Q9A5V1; -.
DR   STRING; 190650.CC_2346; -.
DR   EnsemblBacteria; AAK24317; AAK24317; CC_2346.
DR   KEGG; ccr:CC_2346; -.
DR   PATRIC; fig|190650.5.peg.2367; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   OMA; MVTGPGN; -.
DR   BioCyc; CAULO:CC2346-MON; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001816; 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..428
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135753"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
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         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         411
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         416
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ   SEQUENCE   428 AA;  45154 MW;  89F4ECF58D67F2F2 CRC64;
     MRRFLFSDPD FQTAFKAFLD ERRGSPADVD AAVAGVLEAV RTQGIEALLD YSRRFDKVDL
     TAETIRVTAE EIEAGAAETP ADVREAIAFA AARIRAYHSR QRPADQAWTD EAGVELGWRW
     TPLEAVGVYV PGGRAAYPST VLMNAVPAQV AGVDRIAMVT PPGKLQPAVL AAAKEAGVTE
     IWRVGGAQAV AALAYGAGPI QPVDKIVGPG NAYVTAAKRR LYGVVGIDAL AGPSEIVVVA
     DNKNNPDWIA ADLLSQAEHD PAAQSILITD DEAFAAAVEQ AIAERLKTLA TGEDAAASWR
     DHGAVIIAPL DESPALVDAI APEHVEFALD NPERLSDRVR HAGAIFLGRV TPEAIGDYVA
     GSNHVLPTSR AARFQSGLSI YDFIKRTSIV KCDPASFAVL GPHTVALAKA EGLPAHALSA
     SVRLPSGD
 
 
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