ID ARO1_PNECA Reviewed; 1581 AA. AC Q12659; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Pentafunctional AROM polypeptide; DE Includes: DE RecName: Full=3-dehydroquinate synthase; DE EC=4.2.3.4; DE Includes: DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase; DE EC=2.5.1.19; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase; DE Short=EPSP synthase; DE Short=EPSPS; DE Includes: DE RecName: Full=Shikimate kinase; DE EC=2.7.1.71; DE Includes: DE RecName: Full=3-dehydroquinate dehydratase; DE Short=3-dehydroquinase; DE EC=4.2.1.10; DE Includes: DE RecName: Full=Shikimate dehydrogenase; DE EC=1.1.1.25; GN Name=AROM; OS Pneumocystis carinii. OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis. OX NCBI_TaxID=4754; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94172285; PubMed=8126418; RA Banerji S., Wakefield A.E., Allen A.G., Maskell D.J., Peters S.E., RA Hopkin J.M.; RT "The cloning and characterization of the arom gene of Pneumocystis RT carinii."; RL J. Gen. Microbiol. 139:2901-2914(1993). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: CC step 2/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: CC step 3/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: CC step 4/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: CC step 5/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: CC step 6/7. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC dehydroquinate synthase family. CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase CC family. CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate 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; L18918; AAA17839.1; -; Unassigned_DNA. DR PIR; T30832; T30832. DR HSSP; P07547; 1NVE. DR BRENDA; 1.1.1.25; 3409. DR BRENDA; 2.5.1.19; 3409. DR BRENDA; 2.7.1.71; 3409. DR BRENDA; 4.2.1.10; 3409. DR BRENDA; 4.2.3.4; 3409. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:EC. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:EC. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferas...; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:EC. DR GO; GO:0004765; F:shikimate kinase activity; IEA:EC. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic pro...; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR018508; 3-dehydroquinate_DH_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002658; DHQ_synth_AroB. DR InterPro; IPR016037; DHQ_synth_AroB_sub. DR InterPro; IPR001381; DHquinase_I. DR InterPro; IPR001986; EPSP_synthase_core. DR InterPro; IPR006264; EPSP_synthase_subgroup. DR InterPro; IPR008289; Pentafunct_AroM. DR InterPro; IPR010110; Shik_DH_AROM. DR InterPro; IPR000623; Shik_kinase. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Gene3D; G3DSA:3.65.10.10; EPSP_synthase; 1. DR PANTHER; PTHR21090:SF1; DHQ_synth_AroB; 1. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01487; DHquinase_I; 1. DR Pfam; PF00275; EPSP_synthase; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR Pfam; PF01202; SKI; 1. DR PIRSF; PIRSF000514; Pentafunct_AroM; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR ProDom; PD005337; DHquinase_I; 1. DR ProDom; PD001867; EPSP_synth; 2. DR TIGRFAMs; TIGR01356; aroA; 1. DR TIGRFAMs; TIGR01357; aroB; 1. DR TIGRFAMs; TIGR01093; aroD; 1. DR TIGRFAMs; TIGR01809; Shik-DH-AROM; 1. DR PROSITE; PS01028; DEHYDROQUINASE_I; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Cytoplasm; Kinase; Lyase; Multifunctional enzyme; NADP; KW Nucleotide-binding; Oxidoreductase; Transferase. FT CHAIN 1 1581 Pentafunctional AROM polypeptide. FT /FTId=PRO_0000140860. FT NP_BIND 875 882 ATP (Potential). FT REGION 1 383 3-dehydroquinate synthase. FT REGION 395 840 EPSP synthase. FT REGION 867 1042 Shikimate kinase. FT REGION 1043 1284 3-dehydroquinase. FT REGION 1297 1581 Shikimate dehydrogenase. FT ACT_SITE 827 827 Potential. FT ACT_SITE 1189 1189 Proton acceptor (By similarity). FT ACT_SITE 1217 1217 Schiff-base intermediate with substrate FT (By similarity). SQ SEQUENCE 1581 AA; 178045 MW; 417A84356061170F CRC64; MKEIIKLSIL GKDSIHIGLH LWPHITNELF TCIFSPTYVI ITDSNIETLY IPSFKTYFIS MAKQRSINSR LLFFTIPPGE KSKSRKTKAL IEDWLLSEKC TRDTVIIAIG GGVIGDLVGY VSATFMRGVR FIQIPTTLLA MVDSSIGGKN SINTSYGKNA IGTIWQPERI FIDFTFLETL TEKEFINGIA ELIKTIIIWD ESEFASLENI SEKIAKTVRS MSLTSNKHSK FNEIIKDLKR YIISSIKIKA HIVSIDEKEK DLRTLLNFGH SIGHAIETVL APYILHGESI SIGMVKEAEL SRHLGILNPN VVSRLIKCLN TWGLPTSFKD RRFKEVILGK KHLIEDILEI MSIDKKNDSN NKKIVLLSAI GKTYEKKASS VSDDDIRTIL SQNILLYGIP LNAFQKHTTI TLPGSKSISN RALILASLSN GICYLKNFLH SDDTYYMLSA LEKLNAAEFK WEQDGDVLVV KGKSGYLENP QMELYLGNSG TTARFLTSIC TLVQPNSREN HLILTGSNRM KQRPIGPLVD ALKNNGCCIE YLELENCLPL LIKPKEIGLY GGNINLSATV SSQYVSSILM CSPYAKTQVT LSLIGGKPIS QPYIDMTISM MSSFGIKVTR SHSKENTYYI PKGCYTCPSE YIIEGDATSA TYPLAIAAIT GGSCTISNVG SASLQGDSKF SEYILKPMGC EVVQSPTTTY IKGPPKGKLK SLGSINMESM TDTFLTAAVL ASVAYEESKP YVTKITGISN QRIKECNRIN AMVCELKKFG IEAGELPDGI YVKALNTSNL PYSVEGINCY NDHRIAMSFS VLACISSKPT TILDKACVNK TWPYWWDILN STFKVQMKGI EFDLNPTINS SILHHPSECT IFLIGMRGAG KTTLGQLAAN FLGREFIDLD SIIEEDIKTT ILEFIQKYSW DVFRRKELHF LKTLLTEKKE NYIISCGGGI IETEEARDLL ISYIEANGIV IHIHRNIQDI IKYLNTDKTR APYQDNIMHV WERRKRWYNL CSSHQFHMTS TDPTEFKKNI PLNLKSSFNN FLRTITGKNN IFSLILKKKR SYFLSLAFSD LENIFSLLDI ITAGCDAIEI RIDLFQKPEE IDKYPSLEYI AEKIFLLRQK TSLPLIYTLR TTNHGGSFLS SEKKLAKEYI LHGAKWGFEF LDIELDIASE LFKTINNSWP YTKIIASYHN IEKPISCDDF EWIQKYKEAQ HYGHIIKLVG TSSSIEDNFF LEEFKSKFIN KKVPSIIINT GIKGQLSRIM NTFMTPVTHP SLPSKIAPGQ LSIKEINTAL HIMGLLPEKK YFLFGKPIKH SQSPNIHNLG FEILGLPYKY QLFETDSISE LKEILHLEEF GGASVTIPLK TNISILLDEI SDHAALIGSV NTITRTYNNG QYILKGENTD WQGIIKAIKN FNKFEKSFEN FSGFIIGAGG ASRAAIYALL SLGISPIYLI NRSKDKLNKL YHFFNTNHII PITEYHELNN INFDIRIGIS TIPTDNPIDP SVLEIAKIFF NLKRKSSEGI FLDMAYGSNT TDLTIIAKAC NWKIIHGLEI LLEQGSEQFL LWTETYIPYN QVKYAILGPN K //