ID   HIS2_CANAL              Reviewed;         838 AA.
AC   O74712;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Histidine biosynthesis trifunctional protein;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE              EC=3.5.4.19;
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE              EC=3.6.1.31;
DE   Includes:
DE     RecName: Full=Histidinol dehydrogenase;
DE              Short=HDH;
DE              EC=1.1.1.23;
GN   Name=HIS4;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 64385 / 1001;
RX   MEDLINE=98451822; PubMed=9778800;
RX   DOI=10.1002/(SICI)1097-0061(19980915)14:12<1147::AID-YEA297>3.3.CO;2-Z;
RA   Navarro-Garcia F., Perez-Diaz R., Negredo A., Pla J., Nombela C.;
RT   "Cloning and sequence of a 3.835 kbp DNA fragment containing the HIS4
RT   gene and a fragment of a PEX5-like gene from Candida albicans.";
RL   Yeast 14:1147-1157(1998).
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-
CC       phosphoribosyl)-5-((5-
CC       phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-ATP + H(2)O = 1-(5-
CC       phosphoribosyl)-AMP + diphosphate.
CC   -!- CATALYTIC ACTIVITY: L-histidinol + 2 NAD(+) = L-histidine + 2
CC       NADH.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC       dehydrogenase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ003115; CAA05871.1; -; Genomic_DNA.
DR   HSSP; P06988; 1K75.
DR   BRENDA; 1.1.1.23; 1124.
DR   BRENDA; 3.5.4.19; 1124.
DR   BRENDA; 3.6.1.31; 1124.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:EC.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016298; Histidine_synth_trifunct.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH_prok-type.
DR   InterPro; IPR002496; PRA_CycHdrlase.
DR   InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   PIRSF; PIRSF001257; His_trifunctional; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   ProDom; PD002680; Histidinol_dh; 1.
DR   ProDom; PD002610; PRA_cyclohydro; 1.
DR   ProDom; PD002611; Pra_PH/CH; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis;
KW   Hydrolase; Metal-binding; Multifunctional enzyme; NAD;
KW   Nucleotide-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    838       Histidine biosynthesis trifunctional
FT                                protein.
FT                                /FTId=PRO_0000135909.
FT   REGION        1    271       Phosphoribosyl-AMP cyclohydrolase.
FT   REGION      272    360       Phosphoribosyl-ATP pyrophosphohydrolase.
FT   REGION      361    838       Histidinol dehydrogenase.
FT   ACT_SITE    729    729       By similarity.
FT   ACT_SITE    730    730       By similarity.
FT   METAL       660    660       Zinc (By similarity).
FT   METAL       663    663       Zinc (By similarity).
FT   METAL       764    764       Zinc (By similarity).
FT   METAL       823    823       Zinc (By similarity).
SQ   SEQUENCE   838 AA;  91836 MW;  BFA0E97E9CA62C03 CRC64;
     MIFPILPVIS SPEDKQSIDE FSLVGQVLFP IESVSPKKHF IHQFPHDLDI FVNAIDNATT
     DQIVELLNVG IKQVFVNEKQ YHDAIEAGSP SSRFVVAVDV PSTELLTSEA SFVTSKPFSE
     SDLKKYNANE NRVIYIESNF TQDGAIELAK NYVPVIPSTK LTVKREEENK ISISAVFVST
     LTTDRPDGLY TTLITTPSPS YTALGIVYSS KDSIIAAIEE KVGVYQSRKR RDELWYKGKT
     SGATQKLVKL SKDCDSDVIQ FMVEPRTGYG FCHRETKFTC FGDDIADSPA RGLPKLDSTL
     QDRLENAPEG SYTKRLFDDE KLLIAKLKEE LDELIEAKSK EEIAWECADL VYFAMVWCIK
     HGVRLADIEK NLDVKSLKVS RRKGDAKPQY QEAPVNSSYK LEIVSVDDAA AVERAMTRPV
     QKTADIMKLV LPIIEKVKSD GDKALIELTS KFDGVKLDAP VLQAPFPADL MDISEEMKAA
     IDLSMQNIEK FHAAQLPKEK VMTVETSPGV YCSRFAKPIE NVGLYVPGGT AVLPSTAMML
     GVPAKVAGCK NIIVASPPSR ATGKLTPEVV YVAHKLGAKC IVMAGGAQAV TAMAYGTESV
     LKCDKILGPG NQFVTAAKMY VQNDTQALCS IDMPAGPSEV LVIADSNADA DFVASDLLSQ
     AEHGVDSQVI LIGVGLSDEK LNEFQAAVER QAKVLPRKDI VAKCLAHSYI LLAKTYKEAF
     DLSNQYAPEH LILQIDDAPS YVPDSIENAG SVFVGALSPE SCGDYSSGTN HTLPTYGYAR
     QYSGVNTATF QKFITSQEVT EKGLQNIGKA VMELARVEGL EAHRRAVEIR MERMAETK
//