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   25-NOV-2008, entry version 55.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=91239521; PubMed=2034659;
RA   Nagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A.,
RA   Ryals J.;
RT   "Structural and functional conservation of histidinol dehydrogenase
RT   between 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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2
CC       NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine 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
CC       by different genes.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; M60466; AAA32991.1; -; mRNA.
DR   PIR; A39358; A39358.
DR   HSSP; P06988; 1K75.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001692; Histidinol_DHase.
DR   InterPro; IPR012131; Hstdl_DHase_prok.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   ProDom; PD002680; Histidinol_dh; 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       Chloroplast.
FT   CHAIN        32    469       Histidinol dehydrogenase, chloroplastic.
FT                                /FTId=PRO_0000007216.
FT   ACT_SITE    357    357       Proton acceptor (By similarity).
FT   ACT_SITE    358    358       Proton acceptor (By similarity).
FT   METAL       289    289       Zinc (By similarity).
FT   METAL       292    292       Zinc (By similarity).
FT   METAL       391    391       Zinc (By similarity).
FT   METAL       450    450       Zinc (By similarity).
FT   BINDING     156    156       NAD (By similarity).
FT   BINDING     218    218       NAD (By similarity).
FT   BINDING     241    241       NAD (By similarity).
FT   BINDING     267    267       Substrate (By similarity).
FT   BINDING     289    289       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
FT   BINDING     358    358       Substrate (By similarity).
FT   BINDING     391    391       Substrate (By similarity).
FT   BINDING     445    445       Substrate (By similarity).
FT   BINDING     450    450       Substrate (By similarity).
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
//