ID HISX_BUCAI Reviewed; 435 AA. AC P57201; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=BU100; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. 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; BA000003; BAB12819.1; -; Genomic_DNA. DR RefSeq; NP_239933.1; NC_002528.1. DR RefSeq; WP_009874055.1; NC_002528.1. DR AlphaFoldDB; P57201; -. DR SMR; P57201; -. DR STRING; 563178.BUAP5A_098; -. DR EnsemblBacteria; BAB12819; BAB12819; BAB12819. DR KEGG; buc:BU100; -. DR PATRIC; fig|107806.10.peg.108; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_0_6; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001806; 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; -; 1. DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2. 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 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; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. 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..435 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135742" FT ACT_SITE 327 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 328 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 189 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 328 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 361 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 361 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 415 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 435 AA; 47844 MW; 83DD3DDC4E43430E CRC64; MKYFKNIIFW NKLHPDEQKK ILSRPILKEN NFIKKTVKEI IENVRLFGNS ALKKYTFLFD KQDINTFQVS KEKISSSSFY LSKVLKDSIS VAQKNITCFH KAQIPSKIDV ETEVGVRCEQ IYLPLNSIGI YIPGGTAPLF STVLMLAIPA KISGCKKIIL CSPPPISNEV LYAAHICGIH DIYQVGGAQA IAALALGTET VPKVDKIFGP GNAYVTEAKL QVSSIFNGTE IDMLAGPSEL LIIADNTANP DFIAADLLSQ AEHGVSSQVI LLTPCFELAE KVVLSINKQL NNLSRLSEIL KTLKNSSVII VKNLSECIEI SNMYAPEHLI IQTQSPREVL NYISNASSIF LGLWSPESAG DYASGTNHVL PTYGKSITNS SLGLCDFQKR VLVQELTAKG LMKLSNTIEI LSSAEKLQAH KNAVKIRVDF LKGKI //