ID ARO1_EMENI STANDARD; PRT; 1586 AA. AC P07547; DT 01-APR-1988 (Rel. 07, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase DE (EC 4.2.3.4); 3-dehydroquinate dehydratase (EC 4.2.1.10) (3- DE dehydroquinase); Shikimate dehydrogenase (EC 1.1.1.25); Shikimate DE kinase (EC 2.7.1.71); 3-phosphoshikimate 1-carboxyvinyltransferase DE (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP DE synthase) (EPSPS)]. GN Name=aroMA; Synonyms=aroM; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R153; RX MEDLINE=86176723; PubMed=3515316; RA Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R.; RT "The isolation and nucleotide sequence of the complex AROM locus of RT Aspergillus nidulans."; RL Nucleic Acids Res. 14:2201-2213(1986). RN [2] RP NUCLEOTIDE SEQUENCE OF 844-1474. RC STRAIN=R153; RX MEDLINE=86067221; PubMed=3906567; RA Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R.; RT "Nucleotide sequence encoding the biosynthetic dehydroquinase function RT of the penta-functional arom locus of Aspergillus nidulans."; RL Nucleic Acids Res. 13:8119-8128(1985). RN [3] RP SEQUENCE REVISION TO C-TERMINUS. RA Hawkins A.R.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393. RX MEDLINE=98348324; PubMed=9685163; DOI=10.1038/28431; RA Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A.; RT "Structure of dehydroquinate synthase reveals an active site capable RT of multistep catalysis."; RL Nature 394:299-302(1998). CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic CC reactions in prechorismate polyaromatic amino acid biosynthesis. CC -!- CATALYTIC ACTIVITY: 3-deoxy-arabino-heptulonate 7-phosphate = 3- CC 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: Aromatic amino acids biosynthesis; shikimate pathway; CC second step. CC -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway; CC third step. CC -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway; CC fourth step. CC -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway; CC fifth step. CC -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway; CC sixth step. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05204; CAA28836.1; -. DR PIR; A24962; BVASA1. DR PDB; 1DQS; X-ray; A/B=1-393. DR PDB; 1NR5; X-ray; A/B=1-393. DR PDB; 1NRX; X-ray; A/B=1-393. DR PDB; 1NUA; X-ray; A/B=1-393. DR PDB; 1NVA; X-ray; A/B=1-393. DR PDB; 1NVB; X-ray; A/B=1-393. DR PDB; 1NVD; X-ray; A/B=1-393. DR PDB; 1NVE; X-ray; A/B/C/D=1-393. DR PDB; 1NVF; X-ray; A/B/C=1-393. DR InterPro; IPR006264; AroA. DR InterPro; IPR002658; DHQ_synthase. DR InterPro; IPR001381; DHquinase_I. DR InterPro; IPR001986; EPSP_synth. DR InterPro; IPR008289; Pentafunct_AroM. DR InterPro; IPR000623; Shik_kinase. DR InterPro; IPR006151; Shikimate_DH. 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; PF01202; SKI; 1. DR PIRSF; PIRSF000514; Pentafunct_AroM; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR ProDom; PD005337; DHquinase_I; 1. DR ProDom; PD001867; EPSP_synth; 1. 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. KW 3D-structure; Aromatic amino acid biosynthesis; ATP-binding; Kinase; KW Lyase; Multifunctional enzyme; NADP; Oxidoreductase; Transferase. FT DOMAIN 1 384 3-dehydroquinate synthase. FT DOMAIN 397 843 EPSP synthase. FT DOMAIN 863 1056 Shikimate kinase. FT DOMAIN 1057 1277 3-dehydroquinase. FT DOMAIN 1290 1586 Shikimate 5-dehydrogenase. FT ACT_SITE 825 825 Potential. FT NP_BIND 871 878 ATP (By similarity). FT ACT_SITE 1180 1180 By similarity. FT ACT_SITE 1208 1208 Schiff-base intermediate (By similarity). FT STRAND 5 9 FT TURN 10 11 FT STRAND 12 17 FT TURN 19 20 FT HELIX 21 24 FT TURN 25 25 FT HELIX 26 33 FT STRAND 38 44 FT TURN 45 47 FT HELIX 48 62 FT TURN 63 65 FT STRAND 71 77 FT HELIX 81 83 FT HELIX 86 97 FT TURN 98 98 FT TURN 105 106 FT STRAND 108 113 FT HELIX 115 127 FT STRAND 128 128 FT TURN 129 130 FT STRAND 133 138 FT HELIX 141 145 FT TURN 146 148 FT STRAND 152 157 FT TURN 158 159 FT STRAND 160 167 FT STRAND 172 175 FT HELIX 177 182 FT HELIX 185 200 FT TURN 201 202 FT HELIX 204 222 FT HELIX 236 256 FT TURN 258 259 FT HELIX 263 268 FT TURN 269 270 FT HELIX 271 281 FT TURN 282 284 FT HELIX 287 304 FT TURN 305 306 FT HELIX 310 322 FT TURN 323 324 FT TURN 329 330 FT HELIX 332 337 FT TURN 338 340 FT HELIX 345 352 FT TURN 353 354 FT TURN 356 357 FT STRAND 359 359 FT TURN 360 361 FT STRAND 362 362 FT STRAND 364 365 FT STRAND 368 370 FT TURN 371 372 FT STRAND 373 374 FT STRAND 380 381 FT HELIX 384 387 FT HELIX 388 390 SQ SEQUENCE 1586 AA; 173187 MW; B4AD51605585043C CRC64; MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR KRAAEITPSP RLLIYNRPPG EVSKSRQTKA DIEDWMLSQN PPCGRDTVVI ALGGGVIGDL TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EENAETILKA VRREVTPGEH RFEGTEEILK ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF NMALDKKNDG PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG VAHSSNVICA PPGSKSISNR ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANVLPLNTS KGRASLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASCATYP LAVAAVTGTT CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRATS KRGYGTNDRC VPRCFRTGSH RPMEKSQTTP PVSSGIANQR VKECNRIKAM KDELAKFGVI CREHDDGLEI DGIDRSNLRQ PVGGVFCYDD HRVAFSFSVL SLVTPQPTLI LEKECVGKTW PGWWDTLRQL FKVKLEGKEL EEEPVAASGP DRGNASIYII GMRGAGKSTA GNWVSKALNR PFVDLDTELE TVEGMTIPDI IKTRGWQGFR NAELEILKRT LKERSRGYVF ACGGGVVEMP EARKLLTDYH KTKGNVLLLM RDIKKIMDFL SIDKSRPAYV EDMMGVWLRR KPWFQECSNI QYYSRDASPS GLARASEDFN RFLQVATGQI DSLSIIKEKE HSFFASLTLP DLREAGDILE EVCVGSDAVE LRVDLLKDPA SNNDIPSVDY VVEQLSFLRS RVTLPIIFTI RTQSQGGRFP DNAHDAALEL YRLAFRSGCE FVDLDIAFPE DMLRAVTEMK GFSKIIASHH DPKGELSWAN MSWIKFYNKA LEYGDIIKLV GVARNIDDNT ALRKFKNWAA EAHDVPLIAI NMGDQGQLSR ILNGFMTPVS HPSLPFKAAP GQLSATEIRK GLSLMGEIKP KKFAIFGSPI SQSRSPALHN TLFAQVGLPH NYTRLETTNA QDVQEFIRSP DFGGAFRNNS LKLDIMPLLD EVAAEAEIIG AVNTIIPVST GKNTPSRLVG RNTDWQGMIL SLRKAGVYGP KRKDQEQSAL VVGGGGTARA AIYALHNMGY SPIYIVGRTP SKLENMVSTF PSSYNIRIVE SPSSFESVPH VAIGTIPADQ PIDPTMRETL CHMFERAQEA DAEAVKAIEH APRILLEMAY KPQVTALMRL ASDSGWKTIP GLEVLVGQGW YHSLNTGLGS RRYMRVPGHV APPSFN //