ID HISX_BURM1 Reviewed; 438 AA. AC Q845V3; A9AE01; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 27-MAR-2024, entry version 124. 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}; GN OrderedLocusNames=Bmul_0328, BMULJ_02926; OS Burkholderia multivorans (strain ATCC 17616 / 249). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=395019; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12754231; DOI=10.1128/jb.185.11.3333-3343.2003; RA Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.; RT "Distribution and organization of auxotrophic genes on the multichromosomal RT genome of Burkholderia multivorans ATCC 17616."; RL J. Bacteriol. 185:3333-3343(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616 / 249; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC RT 17616."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17616 / 249; RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., RA Hattori M., Tsuda M.; RT "Complete genome sequence of Burkholderia multivorans ATCC 17616."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; AB091436; BAC65270.1; -; Genomic_DNA. DR EMBL; CP000868; ABX14023.1; -; Genomic_DNA. DR EMBL; AP009385; BAG44811.1; -; Genomic_DNA. DR RefSeq; WP_006400584.1; NC_010804.1. DR AlphaFoldDB; Q845V3; -. DR SMR; Q845V3; -. DR STRING; 395019.BMULJ_02926; -. DR KEGG; bmj:BMULJ_02926; -. DR KEGG; bmu:Bmul_0328; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_4; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000008815; Chromosome 1. 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..438 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135749" FT ACT_SITE 335 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 336 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 138 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 222 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 267 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 270 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 270 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 336 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 369 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 423 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 428 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 428 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT CONFLICT 90..101 FT /note="AALEAAAARVRG -> GRAGSGCRTRAR (in Ref. 1; BAC65270)" FT /evidence="ECO:0000305" SQ SEQUENCE 438 AA; 46515 MW; 8F702C8C7E014B1D CRC64; MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA AVLEYTNRFD RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR GYHEKQKIEC GTHSWQYTES DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGVKNDLV LAAALLGGVD RVFTIGGAQA VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM IAGPSEILVL CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ IRHAGAIFLG RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS LIEVSAEGAH TLGEIAAELA YGEGLQAHAK SAEFRMKG //