ID HISX_MANSM Reviewed; 428 AA. AC Q65RB1; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, 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=MS1892; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E; RX PubMed=15378067; DOI=10.1038/nbt1010; RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., RA Jeong H., Hur C.G., Kim J.J.; RT "The genome sequence of the capnophilic rumen bacterium Mannheimia RT succiniciproducens."; RL Nat. Biotechnol. 22:1275-1281(2004). 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; AE016827; AAU38499.1; -; Genomic_DNA. DR RefSeq; WP_011201052.1; NC_006300.1. DR AlphaFoldDB; Q65RB1; -. DR SMR; Q65RB1; -. DR STRING; 221988.MS1892; -. DR KEGG; msu:MS1892; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_0_6; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000607; 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; Zinc. FT CHAIN 1..428 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135793" FT ACT_SITE 323 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 324 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 127 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 185 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 208 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 234 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 256 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 357 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 357 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 411 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 416 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 428 AA; 46088 MW; 7923F52A6F7C11AF CRC64; MQTLIWKDLT EQEKKQALTR PAISAAGNIK DAVDAIRENV VANGDKALFE LSEKFDRVKL NSLEVSEQQI EEAAQRLPEE LKQAIQNAKK NIEAFHLAQV PVEADVETQS GVRCQVLTRP INRVGLYIPG GSAPLFSTVL MLAIPAKIAG CKKIVLCSPP PIADAILYAA NLCGVETIYQ VGGAQAVVAM AFGTETVAKV DKIFGPGNAF VTEAKRQVSQ AVNGAAIDMQ AGPSEVLVLA DENADPDFVA SDLLSQAEHG ADSQVILVTP SERLALETEL AVERQLTTLP RSEIAQKALA HSRIFIAENL QQCVEISNEY APEHLVVQVQ NARDLLSNID NAGSIFLGAY SPESMGDYAS GTNHVLPTYG YTRTSSSLGL ADFSKRMTVQ ELSPQGFKDL AKTVEVMAAA ERLDAHKQAV SIRLAKIK //