ID   HISX_ARCFU              Reviewed;         404 AA.
AC   O30027;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=AF_0212;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
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DR   EMBL; AE000782; AAB91021.1; -; Genomic_DNA.
DR   PIR; D69276; D69276.
DR   RefSeq; NP_069050.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1483423; -.
DR   GenomeReviews; AE000782_GR; AF_0212.
DR   KEGG; afu:AF0212; -.
DR   NMPDR; fig|224325.1.peg.209; -.
DR   TIGR; AF_0212; -.
DR   HOGENOM; O30027; -.
DR   OMA; O30027; LGVETFM.
DR   BioCyc; AFUL224325:AF_0212-MON; -.
DR   BRENDA; 1.1.1.23; 7576.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01024; -; 1.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH_prok-type.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    404       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135890.
FT   ACT_SITE    300    300       Proton acceptor (By similarity).
FT   ACT_SITE    301    301       Proton acceptor (By similarity).
FT   METAL       244    244       Zinc (By similarity).
FT   METAL       247    247       Zinc (By similarity).
FT   METAL       334    334       Zinc (By similarity).
FT   METAL       393    393       Zinc (By similarity).
FT   BINDING     114    114       NAD (By similarity).
FT   BINDING     176    176       NAD (By similarity).
FT   BINDING     199    199       NAD (By similarity).
FT   BINDING     222    222       Substrate (By similarity).
FT   BINDING     244    244       Substrate (By similarity).
FT   BINDING     247    247       Substrate (By similarity).
FT   BINDING     301    301       Substrate (By similarity).
FT   BINDING     334    334       Substrate (By similarity).
FT   BINDING     388    388       Substrate (By similarity).
FT   BINDING     393    393       Substrate (By similarity).
SQ   SEQUENCE   404 AA;  44152 MW;  344264D010F20966 CRC64;
     MEEILRLRRS VSIDDYIEKV KPIVEAVKRE GDKAVIRFTR DLDGVELDSL RVTEDEFEKA
     YDAVDDGLID ALEVAKENIY RFHYVTSVER DMKVEFEDCV MGKIYTPIEK VGAYIPGGRA
     SYPSTALMIG VPAKIAGVEK LVACTPPNKD GKVNPLTLVA LDIAEFDEVY KAGGAQAIAA
     MAYGTETVEK VYKIVGPGNI YVTAAKLLVA KDVAIDMPAG PSEILVIADE TANADFIACD
     CLAQLEHDPM AVAVVLTTSR KVADEVEKKV KSEGDFSNFA VFVVEDLAEA FEISNEFAPE
     HLTVAVKNPE EWLGKVRNAG SVFLGNFSPV AAGDYASGTN HVLPTAGYAK IYGGLSVESF
     LKHFTFQMLS EESMRRIGGD VVKIAEAEGL RWHAESVRKR LEKI
//