ID HISX_GLOVI Reviewed; 445 AA. AC Q7NL02; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 109. 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=gll1324; OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421). OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae; OC Gloeobacter. OX NCBI_TaxID=251221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29082 / PCC 7421; RX PubMed=14621292; DOI=10.1093/dnares/10.4.137; RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., RA Tabata S.; RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a RT cyanobacterium that lacks thylakoids."; RL DNA Res. 10:137-145(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; BA000045; BAC89265.1; -; Genomic_DNA. DR RefSeq; NP_924270.1; NC_005125.1. DR RefSeq; WP_011141324.1; NC_005125.1. DR AlphaFoldDB; Q7NL02; -. DR SMR; Q7NL02; -. DR STRING; 251221.gene:10758807; -. DR EnsemblBacteria; BAC89265; BAC89265; BAC89265. DR KEGG; gvi:gll1324; -. DR PATRIC; fig|251221.4.peg.1351; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_3; -. DR InParanoid; Q7NL02; -. DR OrthoDB; 9805269at2; -. DR PhylomeDB; Q7NL02; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000557; 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..445 FT /note="Histidinol dehydrogenase" FT /id="PRO_0000135775" FT ACT_SITE 328 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT ACT_SITE 329 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 130 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 215 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 329 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 362 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 362 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 416 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 421 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" FT BINDING 421 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024" SQ SEQUENCE 445 AA; 48032 MW; E74D1ABE35BBFDC7 CRC64; MLRLITQLSE AQTEIKRIAA RTHSEQVQHQ EATVREILQN VRRQGDEALL RYTLEFDQVR LAPGDLVVGA AELDAAYQRV STSLLKAIRL AKQRIEQFHR ERICKSWVQF QDRGIVLGRR YTPVDAAGLY IPGGRASYPS SVLMSAIPAV VAGVPRIVLV TPPNPEGKIN PAVLVAAQES GVHEIYRIGG AQAIGALTYG TRTIAPVSVI AGPGNIYVTL AKKLVYGEVG IDSLAGPSEV LIIADSTANP VFLAADMLAQ AEHDSLASAI LITPDGRLAE RTIEAVDRQL ENHPRRTLTE KSLANYGLVI VTADLAEAAA LSNLFAPEHL ELEVEDPWEL LEKVRHAGAI FLGHATPEAV GDYLAGPSHI LPTSGTARYA SGVGVETFQK CSSLVQYTPQ ALAEVGEAID ALTAAEGLPS HGDSVRLRLQ QYENPHSPTQ QQQEE //