ID HISX_RHOBA Reviewed; 460 AA. AC Q7UX39; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 112. 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=RB1584; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae; OC Rhodopirellula. OX NCBI_TaxID=243090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10527 / NCIMB 13988 / SH1; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., RA Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain RT 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). 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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; BX294135; CAD72173.1; -; Genomic_DNA. DR RefSeq; NP_864492.1; NC_005027.1. DR RefSeq; WP_011118440.1; NC_005027.1. DR AlphaFoldDB; Q7UX39; -. DR SMR; Q7UX39; -. DR STRING; 243090.RB1584; -. DR EnsemblBacteria; CAD72173; CAD72173; RB1584. DR KEGG; rba:RB1584; -. DR PATRIC; fig|243090.15.peg.740; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_0; -. DR InParanoid; Q7UX39; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001025; 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 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..460 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135834" FT ACT_SITE 358 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 359 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 291 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 294 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 392 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 392 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 446 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 451 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 451 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 460 AA; 48514 MW; 507E4E5DAE69E1BF CRC64; MFRIVAVPEF SIQTVDARDP SSSEAAETLA ALREKLSPRG DLVSPRGREL TLKVFGKALS PIEVVETICK DVQSQGTEAL LRYTKSLDGA ELTADTLRVP EEDLKAAHAV ADPKLIETIG RIRDNIATFQ SAILHRDVTI TPRPGVSLTQ RYVPIPRVGI CVPGGAAAYP STVMMTAIPA QVAGVDEIAV VAPPTPFGAY NTDMLATCHE LGIKEVYRCG GAQAVAAMAY GCDALPAVDK IVGPGNLFVA LAKKHVFGTV DIDSFAGPSE VIVIADESAN AAFVASDLLA QAEHSPGSAI LITWDESLLT SVQAELSRQL GELERGDLAR DALSDFGALV LARDADHACE LTDSFAPEHL QIETREPESL IAKIRHSGAA FLGHHTPVAL GDYAAGPSHV LPTGGTCRWA AGLSANSFLR SGSVTQFDQS ALSAIAQDVI TVAEKEGLTA HARSISIRTE //