ID   HISX_CLOAB              Reviewed;         431 AA.
AC   Q97KI2;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD; OrderedLocusNames=CA_C0937;
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21359325; PubMed=11466286;
RX   DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78913.1; -; Genomic_DNA.
DR   PIR; F97015; F97015.
DR   RefSeq; NP_347573.1; -.
DR   HSSP; P06988; 1K75.
DR   GeneID; 1117120; -.
DR   GenomeReviews; AE001437_GR; CA_C0937.
DR   KEGG; cac:CAC0937; -.
DR   NMPDR; fig|272562.1.peg.1102; -.
DR   HOGENOM; Q97KI2; -.
DR   OMA; Q97KI2; LDAHKNA.
DR   BioCyc; CACE272562:CAC0937-MON; -.
DR   BRENDA; 1.1.1.23; 2866.
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    431       Histidinol dehydrogenase.
FT                                /FTId=PRO_0000135756.
FT   ACT_SITE    329    329       Proton acceptor (By similarity).
FT   ACT_SITE    330    330       Proton acceptor (By similarity).
FT   METAL       261    261       Zinc (By similarity).
FT   METAL       264    264       Zinc (By similarity).
FT   METAL       363    363       Zinc (By similarity).
FT   METAL       422    422       Zinc (By similarity).
FT   BINDING     131    131       NAD (By similarity).
FT   BINDING     193    193       NAD (By similarity).
FT   BINDING     216    216       NAD (By similarity).
FT   BINDING     239    239       Substrate (By similarity).
FT   BINDING     261    261       Substrate (By similarity).
FT   BINDING     264    264       Substrate (By similarity).
FT   BINDING     330    330       Substrate (By similarity).
FT   BINDING     363    363       Substrate (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
FT   BINDING     422    422       Substrate (By similarity).
SQ   SEQUENCE   431 AA;  46930 MW;  70AFA3CB1946DF19 CRC64;
     MEDIIRIIQD GSLDGEKYFQ SLKERQGKEN AEIIKTVKFI IDNVKENGDK ALIEYTSKFD
     KVELQSIEVT KEEIKAAYSK VENDFICALK TAKENIEEYH SKQVQNSYVI TKENGIVMGR
     TVRGLDKVGI YVPGGTAAYP SSVIMNAVPA KVAGVNKIIM TTPPMKDGFV NPSILVAADL
     AGVDKIYKVG GAQAIAALAF GTETIDKVDK IVGPGNIFVA MAKKSVYGFV DIDMIAGPSE
     ILVISDETGN PKFIAADLMS QAEHDTLASS ILVTTSKELI GKVIEEIKLQ VEGLSRKEII
     LEALRNFGAI ILVDSISRAI EIGNVVAPEH LEIITPNPFE YLNDIKNAGS IFLGSYSPEP
     LGDYMAGPNH VLPTSGTARF SSPLSVDDFV KKSSYLYYSE KALRNVNDKV VKIAETEGLT
     AHANSIKVRF K
//