HISX_STRCO
ID HISX_STRCO Reviewed; 441 AA.
AC P16245; Q59834; Q9S2T5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=hisD; OrderedLocusNames=SCO2054; ORFNames=SC4G6.23c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=1488552; DOI=10.1016/0923-2508(92)90063-t;
RA Limauro D., Avitabile A., Puglia A.M., Bruni C.B.;
RT "Further characterization of the histidine gene cluster of Streptomyces
RT coelicolor A3(2): nucleotide sequence and transcriptional analysis of
RT hisD.";
RL Res. Microbiol. 143:683-693(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-441.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=2199329; DOI=10.1016/0378-1119(90)90436-u;
RA Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.;
RT "Cloning and characterization of the histidine biosynthetic gene cluster of
RT Streptomyces coelicolor A3(2).";
RL Gene 90:31-41(1990).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL939111; CAB51446.1; -; Genomic_DNA.
DR EMBL; X64420; CAA45767.1; -; Genomic_DNA.
DR EMBL; M31628; AAA26755.1; -; Genomic_DNA.
DR PIR; T35083; T35083.
DR RefSeq; NP_626314.1; NC_003888.3.
DR RefSeq; WP_011028117.1; NZ_VNID01000001.1.
DR AlphaFoldDB; P16245; -.
DR SMR; P16245; -.
DR STRING; 100226.SCO2054; -.
DR GeneID; 1097488; -.
DR KEGG; sco:SCO2054; -.
DR PATRIC; fig|100226.15.peg.2086; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_1_11; -.
DR InParanoid; P16245; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; P16245; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..441
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135860"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
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 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 262
FT /note="Q -> L (in Ref. 2; CAA45767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 46493 MW; 3B0B26BA17F91743 CRC64;
MISRIDLRGD ALPEGPALRD LLPRADFDVS VALEKVRPIC EAVHHRGDAA LIDFTEQFDG
VRLERVRVPA EELTRALEGL DPEVRAALEE SIRRARLVHR EQRRATHTTQ VVPGGSVTEK
WVPVERVGLY VPGGRSVYPS SVVMNVVPAQ EAGVGSIALA SPAQAEFGGI PHPTILAACA
LLGVDEVYAA GGATAVAMFA YGTESCPPAN MVTGPGNIWV AAAKRFFTGK IGIDAEAGPT
EIAVLADSTA DPVHVASDLI SQAEHDPLAA AVLVTDSAEL ADAVEKELQP QVEATKHIED
RIRPALAGRQ SAIVLVDGLD EGLRVVDAYG AEHLEIQTAD AAAVADRVKN AGAIFVGPWA
PVSLGDYAAG SNHVLPTGGC ACHSSGLSVQ SFLRGIHIVD YTRDALAEVA RHVVTLAEAE
DLPAHGAAIK ARFEWKVPES K
