HISX_BRAOC
ID HISX_BRAOC Reviewed; 469 AA.
AC P24226;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Histidinol dehydrogenase, chloroplastic;
DE Short=HDH;
DE EC=1.1.1.23;
DE Flags: Precursor;
GN Name=HDH;
OS Brassica oleracea var. capitata (Cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3716;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2034659; DOI=10.1073/pnas.88.10.4133;
RA Nagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A., Ryals J.;
RT "Structural and functional conservation of histidinol dehydrogenase between
RT plants and microbes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: Cabbage may contain multiple HDH isozymes encoded by
CC different genes.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M60466; AAA32991.1; -; mRNA.
DR PIR; A39358; A39358.
DR AlphaFoldDB; P24226; -.
DR SMR; P24226; -.
DR BindingDB; P24226; -.
DR ChEMBL; CHEMBL4350; -.
DR BRENDA; 1.1.1.23; 947.
DR UniPathway; UPA00031; UER00014.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
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-UniPathway.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Chloroplast; Direct protein sequencing;
KW Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Plastid;
KW Transit peptide; Zinc.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT CHAIN 32..469
FT /note="Histidinol dehydrogenase, chloroplastic"
FT /id="PRO_0000007216"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 50959 MW; EC63FA4B7B2E19CA CRC64;
MSFDLSRLSL TSSPRLSFLT RTATKKGFVR CSMKSYRLSE LSFSQVENLK ARPRIDFSSI
FTTVNPIIDA VRSKGDTAVK EYTERFDKVQ LNKVVEDVSE LDIPELDSAV KEAFDVAYDN
IYAFHFAQMS TEKSVENMKG VRCKRVSRSI GSVGLYVPGG TAVLPSTALM LAIPAQIAGC
KTVVLATPPT KEGSICKEVL YCAKRAGVTH ILKAGGAQAI AAMAWGTDSC PKVEKIFGPG
NQYVTAAKMI LQNSEAMVSI DMPAGPSEVL VIADEHASPV YIAADLLSQA EHGPDSQVVL
VVVGDGVNLK AIEEEIAKQC KSLPRGEFAS KALSHSFTVF ARDMIEAITF SNLYAPEHLI
INVKDAEKWE GLIENAGSVF IGPWTPESVG DYASGTNHVL PTYGYARMYS GVSLDSFLKF
MTVQSLTEEG LRNLGPYVAT MAEIEGLDAH KRAVTLRLKD IEAKQTQTK
