ID   HISX_CHLCH              Reviewed;         428 AA.
AC   Q3AR25;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   04-NOV-2008, entry version 22.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=Cag_1289;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB28550.1; -; Genomic_DNA.
DR   RefSeq; YP_379593.1; -.
DR   GeneID; 3747438; -.
DR   GenomeReviews; CP000108_GR; Cag_1289.
DR   KEGG; cch:Cag_1289; -.
DR   HOGENOM; Q3AR25; -.
DR   BioCyc; CCHL340177:CAG_1289-MON; -.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
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_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   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_0000229855.
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;  46058 MW;  9C84F276D42A901E CRC64;
     MLPLYRFPQE ASALQERLVR HVSFDEAAHK AVDEILAKVR QQGDRAVLNY TEQFQGVRLT
     SMQVDEEAIE MAYRHADPSL IATLHEAYAN IVRFHEHEVE RSFFYEAEGG VLLGQRVRPM
     ERAMLYVPGG KAAYPSSLLM NAAPAKVAGV CEIAVTTPCD ATGVVNPTIL AAAKVAGISS
     IYKIGGAQAV AAFAYGTESI PKVDIITGPG NKYVALAKKQ VFGHVAIDSI AGPSEVVIIA
     DESAHAEFVA LDMFAQAEHD PDASAVLITT SESFAQAVQQ AVASLLPTML RHETIASSLL
     HNGAMVLVPS LDDACAVSDM LAPEHLELHV VQPWDILPKL KHAGAIFMGS YSCETIGDYF
     AGPNHTLPTS GTARFFSPLS VRDFVKHTSI ISYSPEQLRS KGAQIAAFAD AEGLQAHAEA
     VRVRLKTL
//