ID A0A0D9Y5P0_9ORYZ Unreviewed; 473 AA.
AC A0A0D9Y5P0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Histidinol dehydrogenase, chloroplastic {ECO:0000256|PIRNR:PIRNR000099};
DE Short=HDH {ECO:0000256|PIRNR:PIRNR000099};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G09580.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM01G09580.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM01G09580.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000256|PIRNR:PIRNR000099}.
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,
CC ECO:0000256|PIRNR:PIRNR000099};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000099-4};
CC Note=Binds 1 zinc ion per subunit. {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|PIRNR:PIRNR000099}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|PIRNR:PIRNR000099}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|PIRNR:PIRNR000099,
CC ECO:0000256|RuleBase:RU004175}.
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DR AlphaFoldDB; A0A0D9Y5P0; -.
DR SMR; A0A0D9Y5P0; -.
DR STRING; 40148.A0A0D9Y5P0; -.
DR EnsemblPlants; OGLUM01G09580.1; OGLUM01G09580.1; OGLUM01G09580.
DR EnsemblPlants; OGLUM01G09580.2; OGLUM01G09580.2; OGLUM01G09580.
DR Gramene; OGLUM01G09580.1; OGLUM01G09580.1; OGLUM01G09580.
DR Gramene; OGLUM01G09580.2; OGLUM01G09580.2; OGLUM01G09580.
DR eggNOG; KOG2697; Eukaryota.
DR HOGENOM; CLU_006732_3_0_1; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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|PIRNR:PIRNR000099};
KW Chloroplast {ECO:0000256|PIRNR:PIRNR000099};
KW Histidine biosynthesis {ECO:0000256|PIRNR:PIRNR000099};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000099-4};
KW NAD {ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000099}; Plastid {ECO:0000256|PIRNR:PIRNR000099};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 473 AA; 50566 MW; E46A7D59CEC1B412 CRC64;
MSLRPGRAHP LAASPLHTPL PARPRPQLRL STSTSCAAMK SYRLSELSDA EVGGLKARPR
IDFSSIFGTV NPIVEDVRMR GDAAVKDYTV KFDKVALDDV VVRVSDLPDV ELDPAVKEAF
DVAYDNIYAF HVSQKLPEKT VENMKGVRCK RITRCIGSVG LYVPGGTAVL PSTALMLAVP
AQIAGCKTVV LATPPSRDGS ICKEVLYCAK KAGVTHVLKA GGAQAISAMA WGTVSCPKVE
KIFGPGNQYV TAAKMILQNS EAMVSIDMPA GPSEVLVIAD KYANPVHVAA DLLSQAEHGP
DSQVVLVVAG DGVDLGAIEA EVSKQCSALP RGEFASKALG HSFTVFAKDM VEAISFSNMY
APEHLIINVK DAEQWEDLVE NAGSVFLGQW TPESVGDYAS GTNHVLPTYG YARMYSGVSL
NSFLKYITVQ SLSEEGLRSL GPHVAKMAEV EGLEAHRRAV TLRLQDIEAT VTV
//
