ARO1_CANAL
ID ARO1_CANAL Reviewed; 1551 AA.
AC Q5AME2; A0A1D8PL64; Q5AMU6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 130.
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};
GN OrderedLocusNames=CAALFM_C400890WA; ORFNames=CaO19.12175, CaO19.4704;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 Note=Binds 2 Zn(2+) ions per subunit.;
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; CP017626; AOW28880.1; -; Genomic_DNA.
DR RefSeq; XP_722769.2; XM_717676.2.
DR PDB; 6C5C; X-ray; 1.85 A; A/B=1-387.
DR PDBsum; 6C5C; -.
DR AlphaFoldDB; Q5AME2; -.
DR SMR; Q5AME2; -.
DR BioGRID; 1218632; 1.
DR STRING; 237561.Q5AME2; -.
DR PRIDE; Q5AME2; -.
DR GeneID; 3635680; -.
DR KEGG; cal:CAALFM_C400890WA; -.
DR CGD; CAL0000177892; ARO1.
DR VEuPathDB; FungiDB:C4_00890W_A; -.
DR HOGENOM; CLU_001201_1_2_1; -.
DR InParanoid; Q5AME2; -.
DR OrthoDB; 39786at2759; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR UniPathway; UPA00053; UER00088.
DR UniPathway; UPA00053; UER00089.
DR PRO; PR:Q5AME2; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004765; F:shikimate kinase activity; IBA:GO_Central.
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 InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
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; PF01488; Shikimate_DH; 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..1551
FT /note="Pentafunctional AROM polypeptide"
FT /id="PRO_0000406709"
FT REGION 1..379
FT /note="3-dehydroquinate synthase"
FT REGION 392..838
FT /note="EPSP synthase"
FT REGION 858..1048
FT /note="Shikimate kinase"
FT REGION 1049..1258
FT /note="3-dehydroquinase"
FT REGION 1271..1551
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 253
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 268
FT /note="Proton acceptor; for 3-dehydroquinate synthase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT ACT_SITE 1194
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 42..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 80..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 111..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 127
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 136..137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 143
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 149
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 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 159
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 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 191..194
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 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 243
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 257..261
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
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
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 280
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 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT BINDING 351
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 865..872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03143"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:6C5C"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:6C5C"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:6C5C"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:6C5C"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6C5C"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:6C5C"
SQ SEQUENCE 1551 AA; 169396 MW; 310DB8A3B63A81C8 CRC64;
MSIEKVPILG KETIHVGYGI ADHIVREVIA NLASSTYVIV TDTNMARTPQ YSKLTDDFKT
NLSEKRPESR LLTYCVSPGE NNKNRATKAA VEDFLLQQGC TRDTVILAVG GGVIGDMIGF
VAATFMRGVR VVQVPTTLLA MVDSSVGGKT AIDTPLGKNF IGAFHQPEYV FCDVSFLETL
PARQFINGMA EVVKTAAIWN EEEFTRLENF SKKFLSVVTS KKPDLQSIKA ELVKTVLESV
RVKAGVVSSD EKEAGLRNLL NFGHTIGHAI EAVLTPEALH GECVSIGMIK EAELSRYLGI
LPPVAVARLS KCLVAYGLPV SIDDKEFLKK VGPKRHYVEI DILLKKMAID KKNDGSKIRC
VLLEKIGKCY QLKAHQVSKQ DLSFVLTDEV LVHPFTNPPK ENIIVPPGSK SISNRALILA
ALGNGTVRVK NLLHSDDTKH MLDAVASLKG AEISTEDNGE TIVVKGNGGN LVTSGEELYL
GNAGTASRFL TTVASLVGKS QASDDVILTG NARMQERPIG PLVDALGSNG SEIEYLNKQG
SLPLKISAGN GLKGGRIELA ATISSQYVSS ILMCAPYAKE PVTLALVGGK PISQLYIDMT
CAMMKSFGIE VTKSTTEEYT YHIPKGTYKN PSEYVIESDA SSATYPLAFA AMTGTSCTIP
NIGSSSLQGD AKFAVDVLKP MGCKVEQTTT STTVTGPPRG HLKPLPHVDM EPMTDAFLTA
SVVAAVAKGG SSTSITGIAN QRVKECNRIE AMVTELAKFG VPANELPDGI EIHGIDIEDL
KTPEISKRGV SSYDDHRVAM SFSLLAGLCK EPVLILERST TGKTWPGWWD ILHSKFKIEL
DGYEPPFNTD KHVDKSSDKS IIVIGMRGTG KSTLSEWLAS FLGFKMLDMD KYLEEKLGTG
IKSLIKAKGW EYFRQEEAIV AKECFTKFSK GYVLSTGGGI VEGEDARQQL KSYADNGGIV
LHLHRDLDET VTFLAADTTR PAYSSEVQEV WLRREKWYHE CSNYHFYSSH CSTEDEFNHL
RRSFVNYIKL ITGAERPVVP AGRSAAVVLT SPDLNEVVGD LESITIGADA VELRVDLFKD
TSAEFVAAQI AVIRKHADLP IIYTVRTVSQ GGKFPDENVD ELKSLLLLGI RLGVAYVDLQ
LTAPNELIEE ISSKKGFTRV IGTYQDINGE LKWNNVEWKN KYNQGVSMNA DIVRLVGKAN
SIQDNLDLEN FKKQNTLKPL IAFNLGSQGK LSQVLNGTFT PISHKLLPND EEFLTIGELN
QTYFDIGGFT AKKFWVIGSP IEHSRSPNLH NAGYKALNLP YQFGRFEATD VDVVYDNLIN
KPDFGGLAIT MPLKLDIMKF ATKLSDAAET IGAVNTLIPI EGGYFGDNTD WVGISNSFIR
AGVPPKSSSN GLVVGAGGTS RAAIYALHQM GCAKIYLVNR TAAKLEELVK SFPKDYNLEI
VETEQQADKA SKVSLAVSCI PADKPLDGEV LKKIERILSN GSEQSAGFKP TLLEASYKPR
VTPIMKLTEE QYKWKVIPGV EMLVNQGDRQ FKLHTGFTAP YEIIHRAVVE E
