ID A0A7W2CVX7_9ACTN Unreviewed; 450 AA. AC A0A7W2CVX7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-MAY-2023, entry version 7. DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|ARBA:ARBA00016531, ECO:0000256|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000256|ARBA:ARBA00012965, ECO:0000256|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024, GN ECO:0000313|EMBL:MBA4860090.1}; GN ORFNames=H1V43_01600 {ECO:0000313|EMBL:MBA4860090.1}; OS Streptomyces himalayensis subsp. aureolus. OC Bacteria; Actinomycetota; Streptomycetales; Streptomycetaceae; OC Streptomyces; Streptomyces himalayensis. OX NCBI_TaxID=2758039 {ECO:0000313|EMBL:MBA4860090.1, ECO:0000313|Proteomes:UP000586976}; RN [1] {ECO:0000313|EMBL:MBA4860090.1, ECO:0000313|Proteomes:UP000586976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSKA54 {ECO:0000313|EMBL:MBA4860090.1, RC ECO:0000313|Proteomes:UP000586976}; RA Mandal S., Maiti P.K.; RT "Streptomyces isolated from Indian soil."; RL Submitted (JUL-2020) 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:0000256|ARBA:ARBA00003850, ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001654, ECO:0000256|HAMAP- CC Rule:MF_01024}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRSR:PIRSR000099-4}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRSR:PIRSR000099-4}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000256|ARBA:ARBA00004940, ECO:0000256|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01024}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBA4860090.1}. 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; JACEQY010000001; MBA4860090.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W2CVX7; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000586976; Unassembled WGS sequence. 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 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 TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01024}; NAD {ECO:0000256|HAMAP-Rule:MF_01024}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01024}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}. FT ACT_SITE 332 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT ACT_SITE 333 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 262 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 333 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 366 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 420 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 425 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-4" FT BINDING 425 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" SQ SEQUENCE 450 AA; 47220 MW; 0A67AB97210CB97D CRC64; MISRIDLRGD ALPEGPALRD LLPRADFDVA AALEKVRPIC EAVHHRGDAA LIDYAEKFDG VRLDQVRVPA AALTRALEEL NPAVRAGLEE SIRRARIVHR EQRRTTHTTQ VVPGGTVTEK WVPVERVGLY APGGRAVYPS SVIMNVVPAQ EAGVPSMALA SPAQKDFGGL PHPTILAACA LLGIDEVYAA GGATAVAMFA YGTESCAPAN MVTGPGNIWV AAAKRYFTGR IGIDAEAGPT EIAILADDTA DPAHVASDLI SQAEHDPLAA AVLVTDSPDL ADAVEKELEP QVAATKHIED RIVPALSGKQ SAIVLVDGLE EGLRVVDAYG AEHLEIQTAD AAAVADRVKN AGAIFVGPWA PVSLGDYCAG SNHVLPTGGC ACHSSGLSVQ SFLRGIHIVD YTRDALAEVA HHVVTLAEAE DLPAHGAAVK ARFAGGEQDR RSGWKVPESK //