ID   B9GH07_POPTR            Unreviewed;       441 AA.
AC   B9GH07;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Histidinol dehydrogenase, chloroplastic {ECO:0000256|PIRNR:PIRNR000099};
DE            Short=HDH {ECO:0000256|PIRNR:PIRNR000099};
GN   ORFNames=POPTR_001G465300 {ECO:0000313|EMBL:PNT60305.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT60305.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT60305.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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=L-histidinol + 2 NAD(+) + H2O = L-histidine + 2 NADH + 3 H(+);
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:ARBA00049489,
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   EMBL; CM009290; PNT60305.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9GH07; -.
DR   SMR; B9GH07; -.
DR   Gramene; Potri.001G465300.2.v4.1; Potri.001G465300.2.v4.1; Potri.001G465300.v4.1.
DR   KEGG; pop:7480422; -.
DR   eggNOG; KOG2697; Eukaryota.
DR   HOGENOM; CLU_006732_3_0_1; -.
DR   OrthoDB; 1703565at2759; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000006729; Chromosome 1.
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:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   FunFam; 1.20.5.1300:FF:000002; Histidinol dehydrogenase, chloroplastic; 1.
DR   FunFam; 3.40.50.1980:FF:000002; Histidinol dehydrogenase, chloroplastic; 1.
DR   FunFam; 3.40.50.1980:FF:000011; Histidinol dehydrogenase, chloroplastic; 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|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Chloroplast {ECO:0000256|PIRNR:PIRNR000099};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000099-4};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000099};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000099}; Plastid {ECO:0000256|PIRNR:PIRNR000099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        329
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         416
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         421
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   441 AA;  47768 MW;  E10AFE0C50A7EAF6 CRC64;
     MCAMKSYRLS ELNNSEVESL KARPRIDFSS IFGIVNPIVD DVRQRGDAAV KDYTSRFDKV
     KLDKIVENVS ELPDPELDAT VKEAFDVAYN NIYAFHLAQK SVEKSVETMK GVRCKRVARS
     ISSVGLYVPG GTAVLPSTAL MLAIPAQIAG CKTVVLATPP AQDGSICKEV LYCAKKAGVT
     HILKAGGAQA ISAMAWGTES CPKAEKIFGP GNQYVTAAKM ILQNSEAMIS IDMPAGPSEV
     LVIADRYASP VHIAADLLSQ AEHGPDSQVV LVVAGDGVDM KAIEEEISKQ CQSLPRGEYA
     SKALSHSFTV FARDMVEAVS FSNLYAPEHL IINVKEAEKW ESFIENAGSV FLGPWTPESV
     GDYASGTNHV LPTYGYARMY GGVSLDSFQK YMTVQSLTEE GLRKLGPYVA TMAEVEGLDA
     HKRAVTLRLQ DIEARQVSNT R
//