ID HISX_ZYMMO Reviewed; 430 AA. AC Q9RH05; Q5NM85; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 3. DT 27-MAR-2024, entry version 125. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; Synonyms=hdh; OrderedLocusNames=ZMO1551; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Zymomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RA Kang H.L., Kang H.S.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., RA Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). RN [3] RP SEQUENCE REVISION. RX PubMed=19816441; DOI=10.1038/nbt1009-893; RA Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B., RA Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M., RA Chang Y.J., Samatova N.F., Brown S.D.; RT "Improved genome annotation for Zymomonas mobilis."; RL Nat. Biotechnol. 27:893-894(2009). 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 -!- SEQUENCE CAUTION: CC Sequence=AAF18281.1; Type=Frameshift; Evidence={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; AF088897; AAF18281.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE008692; AAV90175.2; -; Genomic_DNA. DR RefSeq; WP_011241316.1; NZ_CP035711.1. DR AlphaFoldDB; Q9RH05; -. DR SMR; Q9RH05; -. DR STRING; 264203.ZMO1551; -. DR GeneID; 79905112; -. DR KEGG; zmo:ZMO1551; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_5; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001173; 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..430 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135889" 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 130 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 214 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" 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 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" FT CONFLICT 406..430 FT /note="PAAVTLAKAEGLPAHAESVISRLNK -> LRL (in Ref. 1; FT AAF18281)" FT /evidence="ECO:0000305" SQ SEQUENCE 430 AA; 46339 MW; 213A0D3F7609A6C4 CRC64; MLLKLDSRKA DFQADFTRLV DERRESEGDV SRDVSAIIAD VKKRGDVAIA ELTQKFDRHD LNKGGWQLTQ EEIKKACDSL PSELMDALKL AATRIRYCHE NQLPESSEMT DAAGVRMGVR WQAVEAAGLY VPGGRAAYCS SVLMNAVPAK VAGVKRLVMV TPTPDGFVNP AVIAAAVISE VDEIWKIGGA QAVAALALGT EKIKPVDVVV GPGNAWVAEA KRQLYGQVGI DMVAGPSEIV VVADKDNDPE WLAADLLSQA EHDPTSQSIL ISDSEDLIEK TIEAVGRRLE KLETQKVARE SWDKHGATIL VQSLDEAPAL VDRLAPEHLE LAVADPDALF ANVHHSGSVF LGRYTPEAIG DYVGGPNHVL PTGRRARFSS GLSVIDFMKR TTYLNCSQEA LSKIGPAAVT LAKAEGLPAH AESVISRLNK //