ARO1_SCHPO
ID ARO1_SCHPO Reviewed; 1573 AA.
AC Q9P7R0;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
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=aro1 {ECO:0000255|HAMAP-Rule:MF_03143}; ORFNames=SPAC1834.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
CC reactions in prechorismate polyaromatic amino acid biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03143};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03143}.
CC -!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
CC 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}.
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DR EMBL; CU329670; CAB75770.1; -; Genomic_DNA.
DR PIR; T50113; T50113.
DR RefSeq; NP_594681.1; NM_001020110.2.
DR PDB; 5SWV; X-ray; 2.65 A; C=1043-1573.
DR PDBsum; 5SWV; -.
DR AlphaFoldDB; Q9P7R0; -.
DR SMR; Q9P7R0; -.
DR BioGRID; 278591; 6.
DR STRING; 4896.SPAC1834.02.1; -.
DR iPTMnet; Q9P7R0; -.
DR MaxQB; Q9P7R0; -.
DR PaxDb; Q9P7R0; -.
DR PRIDE; Q9P7R0; -.
DR EnsemblFungi; SPAC1834.02.1; SPAC1834.02.1:pep; SPAC1834.02.
DR GeneID; 2542115; -.
DR KEGG; spo:SPAC1834.02; -.
DR PomBase; SPAC1834.02; aro1.
DR VEuPathDB; FungiDB:SPAC1834.02; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_1_2_1; -.
DR InParanoid; Q9P7R0; -.
DR OMA; YCYDDHR; -.
DR PhylomeDB; Q9P7R0; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR PRO; PR:Q9P7R0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00502; DHQase_I; 1.
DR CDD; cd01556; EPSP_synthase; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR HAMAP; MF_03143; Pentafunct_AroM; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008289; Pentafunct_AroM.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PIRSF; PIRSF000514; Pentafunct_AroM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53223; SSF53223; 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; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW ATP-binding; Cytoplasm; Kinase; Lyase; Metal-binding;
KW Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..1573
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000140861"
FT REGION 1..384
FT /note="3-dehydroquinate synthase"
FT REGION 397..843
FT /note="EPSP synthase"
FT REGION 863..1058
FT /note="Shikimate kinase"
FT REGION 1059..1280
FT /note="3-dehydroquinase"
FT REGION 1293..1573
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 260
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 275
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 825
FT /note="For EPSP synthase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1182
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1211
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 46..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 83..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 114..116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 130
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 146
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 152
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 162
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 179..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194..197
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 250
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 264..268
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 356
FT /ligand="7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate"
FT /ligand_id="ChEBI:CHEBI:58394"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 870..877
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT HELIX 1045..1050
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1055..1059
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1064..1067
FT /evidence="ECO:0007829|PDB:5SWV"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1071..1074
FT /evidence="ECO:0007829|PDB:5SWV"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1079..1084
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1085..1087
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1094..1097
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1100..1111
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1118..1121
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1125..1127
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1129..1131
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1136..1148
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1152..1157
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1162..1170
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1176..1182
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1194..1204
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1208..1215
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1219..1235
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1240..1246
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1247..1249
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1250..1255
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1258..1263
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1267..1269
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1278..1287
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1295..1299
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1308..1319
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1324..1327
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1331..1333
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1334..1336
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1337..1340
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1345..1350
FT /evidence="ECO:0007829|PDB:5SWV"
FT TURN 1355..1358
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1359..1361
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1363..1365
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1367..1372
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1376..1385
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1387..1392
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1395..1406
FT /evidence="ECO:0007829|PDB:5SWV"
FT TURN 1407..1409
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1416..1420
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1424..1435
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1439..1446
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1448..1455
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1464..1471
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1474..1478
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1482..1487
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1491..1493
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1497..1508
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1509..1518
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1522..1525
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1527..1534
FT /evidence="ECO:0007829|PDB:5SWV"
FT STRAND 1538..1540
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1542..1558
FT /evidence="ECO:0007829|PDB:5SWV"
FT HELIX 1564..1572
FT /evidence="ECO:0007829|PDB:5SWV"
SQ SEQUENCE 1573 AA; 173782 MW; 418968DA6330280D CRC64;
MSNESNIITV PILGKDTVRV GFGIHQYICT EILENFKSST YVVITDSNIA PLYLEKIEST
FNKSIKDAKA EARLLTYVIP PGESSKCRAM KAEIEDWLLT QSCTRDTILI AMGGGVIGDL
VGYVAASFMR GIRFIQMPTT LLAMVDSSIG GKTGIDTPLG KNLVGAFWQP LRVYVDMVFL
HTLPPRQVIN GLSEIIKTAA MWNENDFQLL ENNSAVLLDA LNKPSVPGEY KFDSIKPLLQ
KIILSSIRTK CEVVTLDEHE GGLRNLLNFG HSIGHAYEAI LYPQILHGEC VAIGMVKEAE
LARYLGILKP NAVGRLTKCL VSYNLPISVN DPKVKKYASF KHCPVEKLIE YMAVDKKNQG
SKKRIVILKA IGETYEKHAT VVSDDDIRFI LSRDVKVDEF TKSSWDVVVT PPGSKSISNR
ALVLAAMGNG TCRLTNMLHS DDTQFMMSAL ESLGAATFSW EDGGETLVVK GNGGKLAVPK
EELYLGNAGT AARFLTGIAA LVSSKDGAKV VLTGNHRMKV RPIGPLVDAL RANGCEINYL
EKQGSLPLDL SSKNGLKGGI IELAATVSSQ YVSSILMCAP YASQPVTLKL VGGKPISQLY
IDMTIAMMAS FGVNVTKSTT EENTYNIPCG KYQNPPHYEI ESDASSATYP LAIAAITGTK
CTVPNIGSAS LQGDARFACD VLRPMGCTVE QTATSTTVQG PPKGTLKPLE SIDMETMTDA
FLTASVVAAV ACNVSEGDPV TRITGIANQR VKECNRIAAM VHELAKFGVR TGELEDGIYI
FGKNYKELKK PEEGIYTYDD HRIAMSFSVL SLICPSRTLI IDKACVEKTW PYWWDVLHQS
FGVKLTGATS VASDPLKGSI SKNASIILIG MRGAGKTTIG KIIAKQLNFK FLDLDELLED
YLEMPIAEVI FRMGWDAFRL EEHKVLRKFI TEHPEGYVAA SGGGVIEMDE SRNLLSNFVK
EGGIVLHVHR NLEHIKSYLS EDQTRPTYKD QESIDDVYKR RHVWYRECRS HYFISPVLSN
QVIDEKIQYS MSRFLDVVTG SSQVLQKFKT KKRSTFLTLN YPRIEDALPT LRDVTVGCDA
IEVRVDYLKD PKSSNGISSL DFVAEQISLL RCSTTLPIIF TIRTISQGGL FPNDKEEEAK
ELMLSAMRYG CDFVDVELGW SSETINILYQ HKGYTKLIMS WHDLSGTWSW ARPHEWMQKV
ELASSYADVI KLVGMANNLN DNLELEEFRT RITNSMDIPL ILFNMGRFGQ LSRILNKFMT
PVTHPLLPSK AAPGQLTVKQ LNEARVLIGE ILPEKFFLFG KPIKHSRSPI LHSTAYELLG
LPHTYEAFET DTVDEVQKVL NLPDFGGANV TIPYKLSVMK FMDELSDEAR FFGAVNTIIP
IRIGDKLVLR GDNTDWRGIY DTFANALDGV SLRDTNGLVI GAGGTSRAAI YSLHRLGVSR
IYLLNRTLAN SYRVQDVFPP DYNIHIIDSD NIPSEELSSV TLSAVVSTIP ADIELPEKVA
SVIKALLANK ADGGVFLDMA YKPLHTPLMA VASDLEWKCC NGLEALVRQG LASFHLWTGM
TAPFDAVYQK VIE
