ID   HISX_CHLTE              Reviewed;         428 AA.
AC   Q8KEY6;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=CT0546;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM71788.1; -; Genomic_DNA.
DR   RefSeq; NP_661446.1; -.
DR   HSSP; P06988; 1KAE.
DR   GeneID; 1006212; -.
DR   GenomeReviews; AE006470_GR; CT0546.
DR   KEGG; cte:CT0546; -.
DR   NMPDR; fig|194439.1.peg.540; -.
DR   TIGR; CT0546; -.
DR   HOGENOM; Q8KEY6; -.
DR   OMA; Q8KEY6; LGVETFM.
DR   BioCyc; CTEP194439:CT_0546-MON; -.
DR   BRENDA; 1.1.1.23; 189605.
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    428       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135754.
FT   ACT_SITE    324    324       Proton acceptor (By similarity).
FT   ACT_SITE    325    325       Proton acceptor (By similarity).
FT   METAL       256    256       Zinc (By similarity).
FT   METAL       259    259       Zinc (By similarity).
FT   METAL       358    358       Zinc (By similarity).
FT   METAL       417    417       Zinc (By similarity).
FT   BINDING     126    126       NAD (By similarity).
FT   BINDING     188    188       NAD (By similarity).
FT   BINDING     211    211       NAD (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     325    325       Substrate (By similarity).
FT   BINDING     358    358       Substrate (By similarity).
FT   BINDING     412    412       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
SQ   SEQUENCE   428 AA;  46264 MW;  513422F758545954 CRC64;
     MLTIYHFPQD EAALREQLNR TVSFDPDAQR TVDDILYRVR TEGDAAVLDY TERFQGIRLY
     DMRVPEAEIE AAYAAADPEF IAILEEAFAN ITAFHRNEAE KSFFYEQKGG VILGQRVTPM
     EKALLYVPGG KAAYPSSVLM NAAPAQVAGV DEISMTTPCD AEGKVNPHIL AAAKVAGITS
     VYRLGGAQAV AAFAYGTATI PKVDIVTGPG NKYVALAKKQ VFGHVAIDSI AGPSEVVVIA
     DAGAEPEFIV MDMFAQAEHD PDASAVLITP SAELADAVRE TAARLAGTML RGEVITRALT
     DNGAIVVTGS MQEACKVSDM IAPEHLELHV DNPWEILPDL RHAGAIFMGQ WSCETVGDYF
     AGPNHTLPTN GTARFFSPLS VRDFVKHTSI IAWSKSELAR TGEKIARFAD HEGLQAHAEA
     VRVRLKHL
//