ID HISX_PYRFU Reviewed; 375 AA. AC O59626; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2002, sequence version 2. DT 27-MAR-2024, entry version 133. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=PF1659; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RA Kanai A., Oida H., Hasegawa A., Doi H.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). 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; AB013080; BAA25804.1; -; Genomic_DNA. DR EMBL; AE009950; AAL81783.1; -; Genomic_DNA. DR RefSeq; WP_011012805.1; NZ_CP023154.1. DR AlphaFoldDB; O59626; -. DR SMR; O59626; -. DR STRING; 186497.PF1659; -. DR PaxDb; 186497-PF1659; -. DR GeneID; 41713487; -. DR KEGG; pfu:PF1659; -. DR PATRIC; fig|186497.12.peg.1725; -. DR eggNOG; arCOG04352; Archaea. DR HOGENOM; CLU_006732_3_3_2; -. DR OrthoDB; 36308at2157; -. DR PhylomeDB; O59626; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001013; 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 Gene3D; 1.20.5.1300; -; 2. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3. DR HAMAP; MF_01024; HisD; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR012131; Hstdl_DH. DR NCBIfam; TIGR00069; hisD; 1. DR PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1. DR Pfam; PF00815; Histidinol_dh; 2. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; ALDH-like; 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..375 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135903" FT ACT_SITE 274 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 99 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 226 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 362 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 367 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 367 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT CONFLICT 97 FT /note="G -> R (in Ref. 1; BAA25804)" FT /evidence="ECO:0000305" SQ SEQUENCE 375 AA; 42178 MW; F8874116A40B1A1B CRC64; MDIEEYVREI LKDIRERGLE AIREYSKKFD GYEGPFEVSK EEFKEAEERI PERDKEIIKR TLKRIEKYHR KQLKQDILYI ENGSLYGLIY KPLKRIGIYV PGGKPLPSTL MMVGVPARVA GVKEIVVTNP PKDGKVNPYI LYIAKLLKIE EVYKLGGIQA IAAMAYGIGM KKVQKIFGPG NKFVNEAKRQ VFGIVGIDSL AGPSEIAVIA DESADKDFVL YDLLSQLEHG KDSKAWLLTT SKELADYCNR EGITVIVCSS LEECCKKANE IAPEHLEIIT REPLKLVDLI ENAGAIYLGL YTPVPAADYF LGVNHVLPTG GAAKFMGVLT VWDFMKPISI AMVSREEFIS ERELGIRLAE IEGIELHKKS LEVRK //