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Database: UniProt
Entry: P07547
LinkDB: P07547
Original site: P07547 
ID   ARO1_EMENI              Reviewed;        1583 AA.
AC   P07547; C8VRD2; Q5BFH2;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   01-OCT-2014, entry version 139.
DE   RecName: Full=Pentafunctional AROM polypeptide {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=DHQS {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_03143};
DE     AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=SK {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03143};
DE   Includes:
DE     RecName: Full=Shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03143};
DE              EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_03143};
GN   Name=aromA; Synonyms=aroA, aroM; ORFNames=AN0708;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R153;
RX   PubMed=3515316; DOI=10.1093/nar/14.5.2201;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473.
RC   STRAIN=R153;
RX   PubMed=3906567; DOI=10.1093/nar/13.22.8119;
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   [5]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Hawkins A.R.;
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION OF INTRON.
RX   PubMed=8611179;
RA   Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H.,
RA   Coggins J.R., Hawkins A.R.;
RT   "Comparative analysis of the QUTR transcription repressor protein and
RT   the three C-terminal domains of the pentafunctional AROM enzyme.";
RL   Biochem. J. 313:941-950(1996).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD;
RP   ZINC AND SUBSTRATE ANALOG, AND SUBUNIT.
RX   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).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP;
RP   NAD; ZINC AND SUBSTRATE ANALOG.
RX   PubMed=12614613; DOI=10.1016/S0022-2836(03)00086-X;
RA   Nichols C.E., Ren J., Lamb H.K., Hawkins A.R., Stammers D.K.;
RT   "Ligand-induced conformational changes and a mechanism for domain
RT   closure in Aspergillus nidulans dehydroquinate synthase.";
RL   J. Mol. Biol. 327:129-144(2003).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.
RX   PubMed=15103156; DOI=10.1107/S0907444904004743;
RA   Nichols C.E., Hawkins A.R., Stammers D.K.;
RT   "Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate
RT   synthase at 1.7 A resolution from crystals grown following enzyme
RT   turnover.";
RL   Acta Crystallogr. D 60:971-973(2004).
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. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143,
CC       ECO:0000269|PubMed:12614613, ECO:0000269|PubMed:9685163}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
CC       family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the 4th section; belongs to the type-I 3-
CC       dehydroquinase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA28836.1; Type=Frameshift; Positions=534, 545, 708, 733, 743; Evidence={ECO:0000305};
CC       Sequence=EAA65484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X05204; CAA28836.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000010; EAA65484.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN001308; CBF88944.1; -; Genomic_DNA.
DR   PIR; A24962; BVASA1.
DR   RefSeq; XP_658312.1; XM_653220.1.
DR   PDB; 1DQS; X-ray; 1.80 A; A/B=1-393.
DR   PDB; 1NR5; X-ray; 2.10 A; A/B=1-393.
DR   PDB; 1NRX; X-ray; 2.90 A; A/B=1-393.
DR   PDB; 1NUA; X-ray; 2.85 A; A/B=1-393.
DR   PDB; 1NVA; X-ray; 2.62 A; A/B=1-393.
DR   PDB; 1NVB; X-ray; 2.70 A; A/B=1-393.
DR   PDB; 1NVD; X-ray; 2.51 A; A/B=1-393.
DR   PDB; 1NVE; X-ray; 2.58 A; A/B/C/D=1-393.
DR   PDB; 1NVF; X-ray; 2.80 A; A/B/C=1-393.
DR   PDB; 1SG6; X-ray; 1.70 A; A/B=1-393.
DR   PDBsum; 1DQS; -.
DR   PDBsum; 1NR5; -.
DR   PDBsum; 1NRX; -.
DR   PDBsum; 1NUA; -.
DR   PDBsum; 1NVA; -.
DR   PDBsum; 1NVB; -.
DR   PDBsum; 1NVD; -.
DR   PDBsum; 1NVE; -.
DR   PDBsum; 1NVF; -.
DR   PDBsum; 1SG6; -.
DR   ProteinModelPortal; P07547; -.
DR   STRING; 162425.CADANIAP00001961; -.
DR   EnsemblFungi; CADANIAT00001961; CADANIAP00001961; CADANIAG00001961.
DR   GeneID; 2876485; -.
DR   KEGG; ani:AN0708.2; -.
DR   eggNOG; COG0337; -.
DR   HOGENOM; HOG000007970; -.
DR   OrthoDB; EOG7KQ28X; -.
DR   SABIO-RK; P07547; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00086.
DR   UniPathway; UPA00053; UER00087.
DR   UniPathway; UPA00053; UER00088.
DR   UniPathway; UPA00053; UER00089.
DR   EvolutionaryTrace; P07547; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:ASPGD.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IDA:ASPGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IPI:ASPGD.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:ASPGD.
DR   GO; GO:0004765; F:shikimate kinase activity; IDA:ASPGD.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IDA:ASPGD.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IDA:ASPGD.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   HAMAP; MF_00110; DHQ_synthase; 1.
DR   HAMAP; MF_00210; EPSP_synth; 1.
DR   HAMAP; MF_03143; Pentafunct_AroM; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR006264; EPSP_synthase.
DR   InterPro; IPR023193; EPSP_synthase_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008289; Pentafunct_AroM.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR010110; Shikimate_DH_AroM-type.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
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   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55205; SSF55205; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis;
KW   Aromatic amino acid biosynthesis; ATP-binding; Complete proteome;
KW   Cytoplasm; Kinase; Lyase; Metal-binding; Multifunctional enzyme; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1   1583       Pentafunctional AROM polypeptide.
FT                                /FTId=PRO_0000140859.
FT   NP_BIND      44     46       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   NP_BIND      81     84       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   NP_BIND     114    116       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   NP_BIND     139    140       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   NP_BIND     179    182       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   NP_BIND     870    877       ATP. {ECO:0000255|HAMAP-Rule:MF_03143}.
FT   REGION        1    384       3-dehydroquinate synthase.
FT   REGION      194    197       Substrate binding 2.
FT   REGION      264    268       Substrate binding 2.
FT   REGION      397    842       EPSP synthase.
FT   REGION      863   1055       Shikimate kinase.
FT   REGION     1056   1276       3-dehydroquinase.
FT   REGION     1289   1583       Shikimate dehydrogenase.
FT   ACT_SITE    260    260       Proton acceptor; for 3-dehydroquinate
FT                                synthase activity.
FT   ACT_SITE    275    275       Proton acceptor; for 3-dehydroquinate
FT                                synthase activity.
FT   ACT_SITE    824    824       For EPSP synthase activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03143}.
FT   ACT_SITE   1179   1179       Proton acceptor; for 3-dehydroquinate
FT                                dehydratase activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_03143}.
FT   ACT_SITE   1207   1207       Schiff-base intermediate with substrate;
FT                                for 3-dehydroquinate dehydratase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_03143}.
FT   METAL       194    194       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   METAL       271    271       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   METAL       287    287       Zinc; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   BINDING     119    119       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   BINDING     130    130       Substrate 1.
FT   BINDING     146    146       Substrate 2.
FT   BINDING     152    152       Substrate 2.
FT   BINDING     161    161       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   BINDING     162    162       Substrate 2.
FT   BINDING     190    190       NAD. {ECO:0000255|HAMAP-Rule:MF_03143,
FT                                ECO:0000269|PubMed:12614613,
FT                                ECO:0000269|PubMed:9685163}.
FT   BINDING     250    250       Substrate 2.
FT   BINDING     271    271       Substrate 2.
FT   BINDING     287    287       Substrate 2.
FT   BINDING     356    356       Substrate 2.
FT   CONFLICT     62     62       A -> R (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT     77     77       A -> R (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    226    226       R -> T (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    235    235       I -> T (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    403    403       Q -> H (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    535    535       A -> P (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    646    646       S -> C (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   CONFLICT    862    862       A -> G (in Ref. 1; CAA28836 and 4; no
FT                                nucleotide entry). {ECO:0000305}.
FT   CONFLICT    984    984       T -> S (in Ref. 1; CAA28836 and 4; no
FT                                nucleotide entry). {ECO:0000305}.
FT   CONFLICT   1048   1048       K -> G (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT   1093   1093       D -> N (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT   1154   1154       E -> D (in Ref. 1; CAA28836 and 4; no
FT                                nucleotide entry). {ECO:0000305}.
FT   CONFLICT   1345   1349       SVTIP -> FRNNS (in Ref. 1; CAA28836).
FT                                {ECO:0000305}.
FT   STRAND        5      9
FT   STRAND       12     18
FT   HELIX        21     24
FT   HELIX        26     33
FT   STRAND       37     44
FT   HELIX        45     65
FT   STRAND       66     68
FT   STRAND       71     77
FT   HELIX        81     83
FT   HELIX        86     97
FT   STRAND       99    101
FT   STRAND      108    114
FT   HELIX       115    127
FT   HELIX       128    130
FT   STRAND      133    138
FT   HELIX       141    145
FT   TURN        146    148
FT   STRAND      152    157
FT   STRAND      160    167
FT   STRAND      171    176
FT   HELIX       177    181
FT   HELIX       185    200
FT   HELIX       204    222
FT   STRAND      227    229
FT   HELIX       233    235
FT   HELIX       236    255
FT   TURN        257    259
FT   HELIX       263    268
FT   HELIX       271    281
FT   TURN        282    284
FT   HELIX       287    304
FT   HELIX       310    322
FT   HELIX       332    337
FT   TURN        338    340
FT   HELIX       345    353
FT   STRAND      362    365
FT   STRAND      368    370
FT   STRAND      373    378
FT   STRAND      380    383
FT   HELIX       384    390
SQ   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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