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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]

 ARO1_NEUCR              Reviewed;        1563 AA.
Q8X071;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
23-MAY-2018, entry version 119.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
Name=aro-1 {ECO:0000255|HAMAP-Rule:MF_03143};
Synonyms=aro-2, aro-4, aro-5, aro-9; ORFNames=B14H13.20, NCU016321;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_03143}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03143}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000255|HAMAP-Rule:MF_03143}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000255|HAMAP-Rule:MF_03143}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
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EMBL; AL670001; CAD21207.1; -; Genomic_DNA.
EMBL; CM002237; EAA26764.1; -; Genomic_DNA.
PIR; S14749; S14749.
RefSeq; XP_956000.1; XM_950907.3.
ProteinModelPortal; Q8X071; -.
SMR; Q8X071; -.
PRIDE; Q8X071; -.
EnsemblFungi; EAA26764; EAA26764; NCU01632.
GeneID; 3872147; -.
KEGG; ncr:NCU01632; -.
EuPathDB; FungiDB:NCU01632; -.
HOGENOM; HOG000205493; -.
InParanoid; Q8X071; -.
KO; K13830; -.
OrthoDB; EOG092C02JU; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000001805; Chromosome 6, Linkage Group II.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-EC.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
CDD; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 3.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR018508; 3-dehydroquinate_DH_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Lyase;
Metal-binding; Multifunctional enzyme; NADP; Nucleotide-binding;
Oxidoreductase; Reference proteome; Transferase; Zinc.
CHAIN 1 1563 Pentafunctional AROM polypeptide.
/FTId=PRO_0000406727.
NP_BIND 48 50 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
NP_BIND 82 85 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
NP_BIND 113 115 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
NP_BIND 138 139 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
NP_BIND 178 181 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
NP_BIND 864 871 ATP. {ECO:0000255|HAMAP-Rule:MF_03143}.
REGION 1 382 3-dehydroquinate synthase.
REGION 193 196 Substrate binding 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
REGION 262 266 Substrate binding 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
REGION 395 834 EPSP synthase.
REGION 857 1051 Shikimate kinase.
REGION 1052 1265 3-dehydroquinase.
REGION 1278 1563 Shikimate dehydrogenase.
ACT_SITE 258 258 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
ACT_SITE 273 273 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
ACT_SITE 816 816 For EPSP synthase activity.
{ECO:0000255|HAMAP-Rule:MF_03143}.
ACT_SITE 1168 1168 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
ACT_SITE 1196 1196 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
METAL 193 193 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143}.
METAL 269 269 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143}.
METAL 285 285 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 118 118 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
BINDING 129 129 Substrate 1. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 145 145 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 151 151 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 160 160 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
BINDING 161 161 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 189 189 NAD. {ECO:0000255|HAMAP-Rule:MF_03143}.
BINDING 248 248 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 269 269 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 285 285 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
BINDING 354 354 Substrate 2. {ECO:0000255|HAMAP-
Rule:MF_03143}.
SEQUENCE 1563 AA; 170232 MW; 41EA4E40747C16C3 CRC64;
MAEPISNPTR INILGKDNII IDHGIWLNFV AQDLLQNIKS STYILITDTN LYKTYVPPFQ
SVFEKAAPQD VRLLTYAIPP GEYSKGRDTK AEIEDWMLSH QCTRDTVIIA LGGGVIGDMI
GYVAATFMRG VRFVQCPTTL LAMVDSSIGG KTAIDVPMGK NLIGAFWQPE RIYIDLTFLN
TLPVREFING MAEVIKTAAI WDENEFTALE ENAKAILEAV RSKNKSADRL APIRDILKRI
VLGSARVKAE VVSSDEREGG LRNLLNFGHS IGHAYEAILT PQVLHGEAVA IGMVKEAELA
RFLGVLRPSA VARLSKCIAS YDLPTSLQDK RIVKLTAGKE CPVDVLLQKM AVDKKNEGRK
KKIVLLSAIG KTYEPKASVV EDRAIRIVLS PCIRVFAGVP KDLNVSVTPP GSKSISNRAL
ILAALGEGTT RIHNLLHSDD TQVMLNAVAQ LQGASFSWEE GDVLVVKGNG GKLQATSTPL
YLGNAGTASR FLTSVAALCN PSDVNSTVLT GNARMKQRPI GALVDALRAN GVGVKYLEKE
HSLPVQVDAA GGLAGGVMEL AATISSQYVS SLLMAAPYAR EPVTLRLVGG KPISQPYIDM
TIAMMASFGV QVQRSAEDPN TYYIPQGTYK NPETYVVESD ASSATYPLAI AAITGTTCTV
PNIGSKSLQG DARFAIEVLR PMGCTVEQTD VSTTVTGPPI GTLKAIPHVD MEPMTDAFLT
ASVLAAVASG TTQITGIANQ RVKECNRILA MKDQLAKFGV HCNELEDGIE VIGIPYTELK
NPTEGIYCYD DHRVAMSFSV LSTISPHPVL ILERECTGKT WPGWWDTMSN YFKVHLEGEE
EPHSSHVSHE KPRKGNPKSI FIIGMRGAGK STAGKWMSEV LNRPLIDLDH ELERREGQTI
PEIIRSERGW EGFRKAELEL LEDVIKNNPT GHIFSCGGGI VETEAARKML LSYSQNGGIV
LLVHRDTDQV VEYLMRDKSR PAYSENIREV YYRRKPFFEE CSNFRYYSPH PDGSKALTEP
PFDFSQFLSV ICGHSNHLEE VKKKPHSFFV SLTVPNVSKA LDIIPKVVVG SDAVELRVDL
LEDYDPEFVA KQVALLRSAA RIPIVYTVRT VSQGGKFPDD DYELALKLYR TGLQAGVEYL
DLEMTMPDEV IEAVTNEKGY THIIASHHDP KATLSWKNGG WIQYYNKALQ HGDVVKLVGV
ARELADNFAL ARFKASLAAA HDKPLIALNM GAAGKLSRVL NGFLTPVSHP ALPSKAAPGQ
LSAAEIRQAL ALIGELEPRS FHLFGNPISA SRSPALHNAL FRDNGLPHQY SLFETDNAAD
VKDLIRAPGF GGASVTIPLK LDIMPLLDEV SDAAKVIGAV NTIIPVRNGD KVTLRGDNTD
WMGMVYALRN AGVVKCTKES PTAGMVVGAG GTTRAAVHAL HDLGFAPIYV VARNADRVKA
LAESFPAEYD IRSLSTPEEV AAESTAQPSV VISTIPADKP IDQSMREVIV ASLRHPSVAD
GKHVLLEMAY TPRHTPLMQL AEDAHWQTIP GLEVLAAQGW YQFQLWTGIT PIYTDAQAAV
MGN


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Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
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IBAN lautet DE8839050000107569353
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Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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