ID HIS2_KLULA Reviewed; 795 AA. AC O13471; Q6CUX9; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 2. DT 16-JUN-2009, entry version 68. 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; OrderedLocusNames=KLLA0C01452g; OS Kluyveromyces lactis (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37; RX MEDLINE=98301187; PubMed=9639316; RX DOI=10.1002/(SICI)1097-0061(199805)14:7<687::AID-YEA261>3.0.CO;2-4; RA Freire-Picos M.A., Hampsey M., Cerdan M.E.; RT "The HIS4 gene from the yeast Kluyveromyces lactis."; RL Yeast 14:687-691(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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; Y09503; CAA70698.1; -; Genomic_DNA. DR EMBL; CR382123; CAH01111.1; -; Genomic_DNA. DR RefSeq; XP_452260.1; -. DR HSSP; P06988; 1K75. DR GeneID; 2892606; -. DR KEGG; kla:KLLA0C01452g; -. DR HOGENOM; O13471; -. DR OMA; O13471; PESCGDY. DR BRENDA; 1.1.1.23; 74088. DR BRENDA; 3.5.4.19; 74088. DR BRENDA; 3.6.1.31; 74088. 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; Complete proteome; KW Histidine biosynthesis; Hydrolase; Metal-binding; KW Multifunctional enzyme; NAD; Nucleotide-binding; Oxidoreductase; Zinc. FT CHAIN 1 795 Histidine biosynthesis trifunctional FT protein. FT /FTId=PRO_0000135910. FT REGION 1 225 Phosphoribosyl-AMP cyclohydrolase. FT REGION 226 308 Phosphoribosyl-ATP pyrophosphohydrolase. FT REGION 309 795 Histidinol dehydrogenase. FT ACT_SITE 683 683 By similarity. FT ACT_SITE 684 684 By similarity. FT METAL 614 614 Zinc (By similarity). FT METAL 617 617 Zinc (By similarity). FT METAL 717 717 Zinc (By similarity). FT METAL 776 776 Zinc (By similarity). FT CONFLICT 162 163 VY -> DI (in Ref. 1; CAA70698). FT CONFLICT 580 582 QAL -> LAI (in Ref. 1; CAA70698). SQ SEQUENCE 795 AA; 86795 MW; 6D35F1632280D3B3 CRC64; MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI SVLLKDAKFE DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK DGAYQFSFGQ IQEIQQSQLV KASEISLETF TNSVLSGMKT DRPDGLYTTL VVDENERSLG LVYSNKESVS LAIETQTGIY FSRSRNEIWR KGATSGNVQK LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG LYGLQKLLQE RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED GKIVLNVVSA SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV ELTAKFDGVQ LETPVLEAPY PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ MQSETLDVET QPGVVCSRFP RPIEKVGLYI PGGTAILPST ALMLGVPAQV AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG AQAIAAMAYG TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP RVDIVRKCIA HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD HAGSIFVGAY TPESCGDYSS GTNHTLPTYG YARQYSGVNT ATFQKFITSQ VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV KIRMSKLGLL PSGFE //