ID A9HFM4_GLUDA Unreviewed; 437 AA. AC A9HFM4; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024, GN ECO:0000313|EMBL:CAP55383.1}; GN OrderedLocusNames=GDI1440 {ECO:0000313|EMBL:CAP55383.1}; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298 OS / CIP 103539 / LMG 7603 / PAl5). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP55383.1, ECO:0000313|Proteomes:UP000001176}; RN [1] {ECO:0000313|EMBL:CAP55383.1, ECO:0000313|Proteomes:UP000001176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / RC PAl5 {ECO:0000313|Proteomes:UP000001176}; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A., RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D., RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., RA Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B., RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., RA Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., RA Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.; RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte RT Gluconacetobacter diazotrophicus Pal5."; RL BMC Genomics 10:450-450(2009). 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}. 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:0000256|HAMAP- CC Rule:MF_01024}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01024, 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|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 --------------------------------------------------------------------------- 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; AM889285; CAP55383.1; -; Genomic_DNA. DR RefSeq; WP_012224737.1; NC_011365.1. DR STRING; 272568.GDI1440; -. DR KEGG; gdi:GDI1440; -. DR KEGG; gdj:Gdia_2140; -. DR eggNOG; COG0141; Bacteria. DR HOGENOM; CLU_006732_3_3_5; -. DR OrthoDB; 9805269at2; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000001176; 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 {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}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01024}; Reference proteome {ECO:0000313|Proteomes:UP000001176}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}. FT ACT_SITE 326 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT ACT_SITE 327 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-1" FT BINDING 129 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 213 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-2" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 258 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 258 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 261 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 261 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 360 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 360 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" FT BINDING 419 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 419 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024, FT ECO:0000256|PIRSR:PIRSR000099-3" SQ SEQUENCE 437 AA; 45822 MW; 64E29B040A3D94A7 CRC64; MKRLDTAQPD FRAAFARLLD DREGDTARVD APVAEILAAV RARGDEALCA YTARFDRMPV TPDRLRITEA EIEAACARVP PDLLAALDVA ATRIEAFHRA QMPADLRYTD ADGVDLGMRW TALDAVGLYV PGGTAAYPSS VLMNAMPARV AGAARLAMCV PTPDGVLNPL VLAAARRAGV TEIYRVGGAQ AVAAMAYGTA TIRPVDRVVG PGNAYVAEAK RQVFGRVGID SIAGPSEVVV VADSGTDPRI VALDLLAQAE HDALAQSILI TQDATLADRV AEAVEAELRT LPRAAIAGAS WGAHGAIITV RDLDEAASLI DAIAPEHLEL LLADPEPLFA RVRHAGAIFL GRQCAEAIGD YVGGPNHVLP TSRTARFASG LSVFDFLKRT TFIGAGPDAL RRIGPAAVAL ARAEGLDAHA LSVSARLDAV ARESDKA //