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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_EMENI              Reviewed;        1583 AA.
P07547; C8VRD2; Q5BFH2;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
26-MAY-2009, sequence version 3.
25-OCT-2017, entry version 162.
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=aromA; Synonyms=aroA, aroM; ORFNames=AN0708;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=R153;
PubMed=3515316; DOI=10.1093/nar/14.5.2201;
Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R.;
"The isolation and nucleotide sequence of the complex AROM locus of
Aspergillus nidulans.";
Nucleic Acids Res. 14:2201-2213(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473.
STRAIN=R153;
PubMed=3906567; DOI=10.1093/nar/13.22.8119;
Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R.;
"Nucleotide sequence encoding the biosynthetic dehydroquinase function
of the penta-functional arom locus of Aspergillus nidulans.";
Nucleic Acids Res. 13:8119-8128(1985).
[5]
SEQUENCE REVISION TO C-TERMINUS.
Hawkins A.R.;
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION OF INTRON.
PubMed=8611179; DOI=10.1042/bj3130941;
Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H.,
Coggins J.R., Hawkins A.R.;
"Comparative analysis of the QUTR transcription repressor protein and
the three C-terminal domains of the pentafunctional AROM enzyme.";
Biochem. J. 313:941-950(1996).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD;
ZINC AND SUBSTRATE ANALOG, AND SUBUNIT.
PubMed=9685163; DOI=10.1038/28431;
Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A.;
"Structure of dehydroquinate synthase reveals an active site capable
of multistep catalysis.";
Nature 394:299-302(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP;
NAD; ZINC AND SUBSTRATE ANALOG.
PubMed=12614613; DOI=10.1016/S0022-2836(03)00086-X;
Nichols C.E., Ren J., Lamb H.K., Hawkins A.R., Stammers D.K.;
"Ligand-induced conformational changes and a mechanism for domain
closure in Aspergillus nidulans dehydroquinate synthase.";
J. Mol. Biol. 327:129-144(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.
PubMed=15103156; DOI=10.1107/S0907444904004743;
Nichols C.E., Hawkins A.R., Stammers D.K.;
"Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate
synthase at 1.7 A resolution from crystals grown following enzyme
turnover.";
Acta Crystallogr. D 60:971-973(2004).
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
-!- 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,
ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAA28836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA28836.1; Type=Frameshift; Positions=534, 545, 708, 733, 743; Evidence={ECO:0000305};
Sequence=EAA65484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X05204; CAA28836.1; ALT_SEQ; Genomic_DNA.
EMBL; AACD01000010; EAA65484.1; ALT_SEQ; Genomic_DNA.
EMBL; AACD01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BN001308; CBF88944.1; -; Genomic_DNA.
PIR; A24962; BVASA1.
RefSeq; XP_658312.1; XM_653220.1.
PDB; 1DQS; X-ray; 1.80 A; A/B=1-393.
PDB; 1NR5; X-ray; 2.10 A; A/B=1-393.
PDB; 1NRX; X-ray; 2.90 A; A/B=1-393.
PDB; 1NUA; X-ray; 2.85 A; A/B=1-393.
PDB; 1NVA; X-ray; 2.62 A; A/B=1-393.
PDB; 1NVB; X-ray; 2.70 A; A/B=1-393.
PDB; 1NVD; X-ray; 2.51 A; A/B=1-393.
PDB; 1NVE; X-ray; 2.58 A; A/B/C/D=1-393.
PDB; 1NVF; X-ray; 2.80 A; A/B/C=1-393.
PDB; 1SG6; X-ray; 1.70 A; A/B=1-393.
PDBsum; 1DQS; -.
PDBsum; 1NR5; -.
PDBsum; 1NRX; -.
PDBsum; 1NUA; -.
PDBsum; 1NVA; -.
PDBsum; 1NVB; -.
PDBsum; 1NVD; -.
PDBsum; 1NVE; -.
PDBsum; 1NVF; -.
PDBsum; 1SG6; -.
ProteinModelPortal; P07547; -.
SMR; P07547; -.
STRING; 162425.CADANIAP00001961; -.
EnsemblFungi; CADANIAT00001961; CADANIAP00001961; CADANIAG00001961.
EnsemblFungi; EAA65484; EAA65484; AN0708.2.
GeneID; 2876485; -.
KEGG; ani:AN0708.2; -.
HOGENOM; HOG000007970; -.
InParanoid; P07547; -.
KO; K13830; -.
OrthoDB; EOG092C02JU; -.
BRENDA; 4.2.3.4; 517.
SABIO-RK; P07547; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
EvolutionaryTrace; P07547; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
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; -; 2.
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.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 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.
1: Evidence at protein level;
3D-structure; 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 1583 Pentafunctional AROM polypeptide.
/FTId=PRO_0000140859.
NP_BIND 44 46 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
NP_BIND 81 84 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
NP_BIND 114 116 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
NP_BIND 139 140 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
NP_BIND 179 182 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
NP_BIND 870 877 ATP. {ECO:0000255|HAMAP-Rule:MF_03143}.
REGION 1 384 3-dehydroquinate synthase.
REGION 194 197 Substrate binding 2.
REGION 264 268 Substrate binding 2.
REGION 397 842 EPSP synthase.
REGION 863 1055 Shikimate kinase.
REGION 1056 1276 3-dehydroquinase.
REGION 1289 1583 Shikimate dehydrogenase.
ACT_SITE 260 260 Proton acceptor; for 3-dehydroquinate
synthase activity.
ACT_SITE 275 275 Proton acceptor; for 3-dehydroquinate
synthase activity.
ACT_SITE 824 824 For EPSP synthase activity.
{ECO:0000255|HAMAP-Rule:MF_03143}.
ACT_SITE 1179 1179 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
ACT_SITE 1207 1207 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000255|HAMAP-
Rule:MF_03143}.
METAL 194 194 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
METAL 271 271 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
METAL 287 287 Zinc; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
BINDING 119 119 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
BINDING 130 130 Substrate 1.
BINDING 146 146 Substrate 2.
BINDING 152 152 Substrate 2.
BINDING 161 161 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
BINDING 162 162 Substrate 2.
BINDING 190 190 NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
ECO:0000269|PubMed:12614613,
ECO:0000269|PubMed:9685163}.
BINDING 250 250 Substrate 2.
BINDING 271 271 Substrate 2.
BINDING 287 287 Substrate 2.
BINDING 356 356 Substrate 2.
CONFLICT 62 62 A -> R (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 77 77 A -> R (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 226 226 R -> T (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 235 235 I -> T (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 403 403 Q -> H (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 535 535 A -> P (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 646 646 S -> C (in Ref. 1; CAA28836).
{ECO:0000305}.
CONFLICT 862 862 A -> G (in Ref. 1; CAA28836 and 4; no
nucleotide entry). {ECO:0000305}.
CONFLICT 984 984 T -> S (in Ref. 1; CAA28836 and 4; no
nucleotide entry). {ECO:0000305}.
CONFLICT 1048 1048 K -> G (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1093 1093 D -> N (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1154 1154 E -> D (in Ref. 1; CAA28836 and 4; no
nucleotide entry). {ECO:0000305}.
CONFLICT 1345 1349 SVTIP -> FRNNS (in Ref. 1; CAA28836).
{ECO:0000305}.
STRAND 5 9 {ECO:0000244|PDB:1SG6}.
STRAND 12 18 {ECO:0000244|PDB:1SG6}.
HELIX 21 24 {ECO:0000244|PDB:1SG6}.
HELIX 26 33 {ECO:0000244|PDB:1SG6}.
STRAND 37 44 {ECO:0000244|PDB:1SG6}.
HELIX 45 65 {ECO:0000244|PDB:1SG6}.
STRAND 66 68 {ECO:0000244|PDB:1SG6}.
STRAND 71 77 {ECO:0000244|PDB:1SG6}.
HELIX 81 83 {ECO:0000244|PDB:1SG6}.
HELIX 86 97 {ECO:0000244|PDB:1SG6}.
STRAND 99 101 {ECO:0000244|PDB:1SG6}.
STRAND 108 114 {ECO:0000244|PDB:1SG6}.
HELIX 115 127 {ECO:0000244|PDB:1SG6}.
HELIX 128 130 {ECO:0000244|PDB:1SG6}.
STRAND 133 138 {ECO:0000244|PDB:1SG6}.
HELIX 141 145 {ECO:0000244|PDB:1SG6}.
TURN 146 148 {ECO:0000244|PDB:1SG6}.
STRAND 152 157 {ECO:0000244|PDB:1SG6}.
STRAND 160 167 {ECO:0000244|PDB:1SG6}.
STRAND 171 176 {ECO:0000244|PDB:1SG6}.
HELIX 177 181 {ECO:0000244|PDB:1SG6}.
HELIX 185 200 {ECO:0000244|PDB:1SG6}.
HELIX 204 222 {ECO:0000244|PDB:1SG6}.
STRAND 227 229 {ECO:0000244|PDB:1NVA}.
HELIX 233 235 {ECO:0000244|PDB:1SG6}.
HELIX 236 255 {ECO:0000244|PDB:1SG6}.
TURN 257 259 {ECO:0000244|PDB:1NVF}.
HELIX 263 268 {ECO:0000244|PDB:1SG6}.
HELIX 271 281 {ECO:0000244|PDB:1SG6}.
TURN 282 284 {ECO:0000244|PDB:1SG6}.
HELIX 287 304 {ECO:0000244|PDB:1SG6}.
HELIX 310 322 {ECO:0000244|PDB:1SG6}.
HELIX 332 337 {ECO:0000244|PDB:1SG6}.
TURN 338 340 {ECO:0000244|PDB:1SG6}.
HELIX 345 353 {ECO:0000244|PDB:1SG6}.
STRAND 362 365 {ECO:0000244|PDB:1NVA}.
STRAND 368 370 {ECO:0000244|PDB:1SG6}.
STRAND 373 378 {ECO:0000244|PDB:1SG6}.
STRAND 380 383 {ECO:0000244|PDB:1NVA}.
HELIX 384 390 {ECO:0000244|PDB:1SG6}.
SEQUENCE 1583 AA; 172664 MW; FBC8610B961840D8 CRC64;
MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR
KAAAEITPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQN PPCGRDTVVI ALGGGVIGDL
TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL
ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EENAETILKA VRREVRPGEH RFEGIEEILK
ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF NMALDKKNDG
PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG VAQSSNVICA PPGSKSISNR
ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS
SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANGASIEYV
ERTGSLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP LAVAAVTGTT
CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRPLP NVDMEPMTDA
FLGASVLAAI ARGKESNHTT RIYGIANQRV KECNRIKAMK DELAKFGVIC REHDDGLEID
GIDRSNLRQP VGGVFCYDDH RVAFSFSVLS LVTPQPTLIL EKECVGKTWP GWWDTLRQLF
KVKLEGKELE EEPVAASGPD RANASIYIIG MRGAGKSTAG NWVSKALNRP FVDLDTELET
VEGMTIPDII KTRGWQGFRN AELEILKRTL KERSRGYVFA CGGGVVEMPE ARKLLTDYHK
TKGNVLLLMR DIKKIMDFLS IDKTRPAYVE DMMGVWLRRK PWFQECSNIQ YYSRDASPSG
LARASEDFNR FLQVATGQID SLSIIKEKEH SFFASLTLPD LREAGDILEE VCVGSDAVEL
RVDLLKDPAS NNDIPSVDYV VEQLSFLRSR VTLPIIFTIR TQSQGGRFPD NAHDAALELY
RLAFRSGCEF VDLEIAFPED MLRAVTEMKG FSKIIASHHD PKGELSWANM SWIKFYNKAL
EYGDIIKLVG VARNIDDNTA LRKFKNWAAE AHDVPLIAIN MGDQGQLSRI LNGFMTPVSH
PSLPFKAAPG QLSATEIRKG LSLMGEIKPK KFAIFGSPIS QSRSPALHNT LFAQVGLPHN
YTRLETTNAQ DVQEFIRSPD FGGASVTIPL KLDIMPLLDE VAAEAEIIGA VNTIIPVSTG
KNTPSRLVGR NTDWQGMILS LRKAGVYGPK RKDQEQSALV VGGGGTARAA IYALHNMGYS
PIYIVGRTPS KLENMVSTFP SSYNIRIVES PSSFESVPHV AIGTIPADQP IDPTMRETLC
HMFERAQEAD AEAVKAIEHA PRILLEMAYK PQVTALMRLA SDSGWKTIPG LEVLVGQGWY
QFKYWTGISP LYESARACSS PLI


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