ID A0A2D5G776_9DELT Unreviewed; 439 AA. AC A0A2D5G776; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 10-APR-2019, entry version 8. DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213}; DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099}; DE EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213}; GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024, GN ECO:0000313|EMBL:MAC44545.1}; GN ORFNames=CL913_11510 {ECO:0000313|EMBL:MAC44545.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:MAC44545.1}; RN [1] {ECO:0000313|EMBL:MAC44545.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPC295 {ECO:0000313|EMBL:MAC44545.1}; RX PubMed=29337314; DOI=10.1038/sdata.2017.203; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The reconstruction of 2,631 draft metagenome-assembled genomes from RT the global oceans."; RL Sci. Data 5:170203-170203(2018). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, CC ECO:0000256|SAAS:SAAS00728939}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 CC NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, CC ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01024, CC ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00781837}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, CC ECO:0000256|SAAS:SAAS00729141}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, CC ECO:0000256|RuleBase:RU004175, ECO:0000256|SAAS:SAAS00827949}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01024}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:MAC44545.1}. 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; NYVT01000106; MAC44545.1; -; Genomic_DNA. DR UniPathway; UPA00031; UER00014. 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:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06572; Histidinol_dh; 1. 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; PTHR21256; 1. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 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 ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729217}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024, KW ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728911}; KW Metal-binding {ECO:0000256|SAAS:SAAS00781816}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, KW ECO:0000256|SAAS:SAAS00751613}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01024, KW ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00751612}; KW Zinc {ECO:0000256|SAAS:SAAS00781803}. FT ACT_SITE 334 334 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01024, ECO:0000256|PIRSR:PIRSR000099- FT 1}. FT ACT_SITE 335 335 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01024, ECO:0000256|PIRSR:PIRSR000099- FT 1}. SQ SEQUENCE 439 AA; 47270 MW; ABA9C7896385F247 CRC64; MSTVSFHETS KLKAKDYKAL LKRSEADLSS FLEKVQPIIE AVRAEGDEAL VRFGQQLDGS TPLSKEALKV SETEFAVAFE EVEEAVIEAI RYGITNIRIF HEEQKPETMW MKEIRPGAYA GDRLTPIRSV AIYVPRGKGA FPSVTMMTTV PGVVAEVPKL AVFTPPLPNG SVDAATLVAA SIAGVDTVYK CGGAQAVAAA AFGTETVERA LKIVGPGSPW VVAAKRLLSD IIDPGLPAGP SEAIIFADDS VHGGLAALDL LIEAEHGPDS SAYLVTHSRR VAEEAMAALP DHWAKMTAQR EEFSKIVLTG PYGGILLTSS VEESYQFIND YAPEHLELLS TEPFTHLGHI TEAAEILMGP HTPVCIGNFS LGPNAVLPTS QGAQTYGPLS VHDFMKRSSV GYVTPPAYPE LAKRARVLAR YEGFSSHENA VSPIRERYL //