ID A0A094PKU3_9ACTN Unreviewed; 444 AA.
AC A0A094PKU3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=GM44_1485 {ECO:0000313|EMBL:KGA11687.1};
OS actinobacterium acAMD-2.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504318 {ECO:0000313|EMBL:KGA11687.1, ECO:0000313|Proteomes:UP000029252};
RN [1] {ECO:0000313|EMBL:KGA11687.1, ECO:0000313|Proteomes:UP000029252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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; Evidence={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: 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:KGA11687.1}.
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; JNSE01000013; KGA11687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PKU3; -.
DR STRING; 1504318.GM44_1485; -.
DR PATRIC; fig|1504318.4.peg.299; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000029252; 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 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 132
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 201
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 224
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 247
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 269
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 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 272
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 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 371
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 371
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 430
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 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 444 AA; 46277 MW; 4A8D9DAB79145AAA CRC64;
MPVISRIDLR SYGANSRSQY AQVLPRAAVD ISSAVSIVTP LLNDIRERGL GAVIEATARF
DGVDLATTRV PQAALDAALA AMDPQVRLAV EEAARRARLV HEAQRRTDAV IRVSAGAEVI
EKWVPVQRVG LYVPGGLVAY PSSVVMNVIP ALVAGVESLA IASPPQREAA DPAFVGLPHP
AVLAACALLG VTEVYAVGGA QAIGMFAYGT SECAPVDLVT GPGNVYVAAA KRVVRGTIGI
DSEAGPTEIG ILADSSADPA FVAADLIAQA EHDENASCLL VTDSTELMDA VDREVAQQLT
TTVHRARVET ALTNQSAYAL VNDLDQGLDV VDAWAAEHLE VITVDAVERA ARVRNAGAIF
VGPWAPVSLG DYLAGSNHVL PTGGSARHTG GLSVQSFLRS MHVVNYTREA LAEVAPLIDA
LGGAEDLHSH VAAVRVRIPS GTDD
//
