PUR9_CHICK
ID PUR9_CHICK Reviewed; 593 AA.
AC P31335;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Bifunctional purine biosynthesis protein ATIC;
DE AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase {ECO:0000303|PubMed:17324932};
DE Short=ATIC {ECO:0000303|PubMed:17324932};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE EC=2.1.2.3 {ECO:0000269|PubMed:12501179};
DE AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE Short=AICAR formyltransferase;
DE AltName: Full=AICAR transformylase;
DE Includes:
DE RecName: Full=IMP cyclohydrolase;
DE EC=3.5.4.10 {ECO:0000250|UniProtKB:P31939};
DE AltName: Full=IMP synthase;
DE AltName: Full=Inosinicase;
GN Name=ATIC; Synonyms=PURH;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1937050; DOI=10.1016/0378-1119(91)90199-l;
RA Ni L., Guan K., Zalkin H., Dixon J.E.;
RT "De novo purine nucleotide biosynthesis: cloning, sequencing and expression
RT of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-
RT ribonucleotide transformylase-IMP cyclohydrolase.";
RL Gene 106:197-205(1991).
RN [2] {ECO:0007744|PDB:1G8M}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GMP, AND SUBUNIT.
RX PubMed=11323713; DOI=10.1038/87555;
RA Greasley S.E., Horton P., Ramcharan J., Beardsley G.P., Benkovic S.J.,
RA Wilson I.A.;
RT "Crystal structure of a bifunctional transformylase and cyclohydrolase
RT enzyme in purine biosynthesis.";
RL Nat. Struct. Biol. 8:402-406(2001).
RN [3] {ECO:0007744|PDB:1M9N}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH AICAR AND XMP,
RP FUNCTION, SUBUNIT, AND PATHWAY.
RX PubMed=12501179; DOI=10.1021/bi020505x;
RA Wolan D.W., Greasley S.E., Beardsley G.P., Wilson I.A.;
RT "Structural insights into the avian AICAR transformylase mechanism.";
RL Biochemistry 41:15505-15513(2002).
RN [4] {ECO:0007744|PDB:1OZ0}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH BETA-DADF INHIBITOR.
RX PubMed=12974624; DOI=10.1021/bi030106h;
RA Wolan D.W., Greasley S.E., Wall M.J., Benkovic S.J., Wilson I.A.;
RT "Structure of avian AICAR transformylase with a multisubstrate adduct
RT inhibitor beta-DADF identifies the folate binding site.";
RL Biochemistry 42:10904-10914(2003).
RN [5] {ECO:0007744|PDB:1THZ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 326203-A INHIBITOR,
RP AND ACTIVITY REGULATION.
RX PubMed=15355974; DOI=10.1074/jbc.m406801200;
RA Xu L., Li C., Olson A.J., Wilson I.A.;
RT "Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide
RT transformylase in complex with a novel non-folate inhibitor identified by
RT virtual ligand screening.";
RL J. Biol. Chem. 279:50555-50565(2004).
RN [6] {ECO:0007744|PDB:2B1G, ECO:0007744|PDB:2B1I, ECO:0007744|PDB:2IU0, ECO:0007744|PDB:2IU3}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) IN COMPLEXES WITH TRANSITION STATE
RP ANALOG INHIBITORS, AND ACTIVITY REGULATION.
RX PubMed=17324932; DOI=10.1074/jbc.m607293200;
RA Xu L., Chong Y., Hwang I., D'Onofrio A., Amore K., Beardsley G.P., Li C.,
RA Olson A.J., Boger D.L., Wilson I.A.;
RT "Structure-based design, synthesis, evaluation, and crystal structures of
RT transition state analogue inhibitors of inosine monophosphate
RT cyclohydrolase.";
RL J. Biol. Chem. 282:13033-13046(2007).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of
CC purine biosynthesis (PubMed:12501179). Acts as a transformylase that
CC incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-
CC phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the
CC intermediate formyl-AICAR (FAICAR) (PubMed:12501179). Can use both 10-
CC formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor
CC in this reaction. Also catalyzes the cyclization of FAICAR to IMP.
CC Promotes insulin receptor/INSR autophosphorylation and is involved in
CC INSR internalization (By similarity). {ECO:0000250|UniProtKB:P31939,
CC ECO:0000269|PubMed:12501179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000269|PubMed:12501179};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193;
CC Evidence={ECO:0000305|PubMed:12501179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate;
CC Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447;
CC Evidence={ECO:0000250|UniProtKB:P31939};
CC -!- ACTIVITY REGULATION: AMP and XMP inhibit AICAR formyltransferase
CC activity (By similarity). AICAR formyltransferase activity is
CC competitively inhibited by 2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfo-
CC phenyl)-1H-pyrazol-4-ylazo]-4-sulfo-benzoic acid (326203-A)
CC (PubMed:15355974). FAICAR cyclization is competitively inhibited by
CC 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one-2,2-dioxide and
CC the corresponding nucleoside and nucleoside monophosphate
CC (PubMed:17324932). {ECO:0000250|UniProtKB:P31939,
CC ECO:0000269|PubMed:15355974, ECO:0000269|PubMed:17324932}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000269|PubMed:12501179}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000250|UniProtKB:P31939}.
CC -!- SUBUNIT: Homodimer (PubMed:11323713, PubMed:12501179). Associates with
CC internalized INSR complexes on Golgi/endosomal membranes. Interacts
CC with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is
CC proposed to be part of a signaling network regulating INSR
CC autophosphorylation and endocytosis (By similarity).
CC {ECO:0000250|UniProtKB:P31939, ECO:0000269|PubMed:11323713,
CC ECO:0000269|PubMed:12501179}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000305|PubMed:17324932}.
CC -!- MISCELLANEOUS: The de novo purine synthesis pathway includes 10
CC sequential steps, beginning with phosphoribosyl pyrophosphate and
CC ending with inositol monophosphate (IMP), the first purin compound of
CC the pathway. {ECO:0000250|UniProtKB:P31939}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR EMBL; S64492; AAB20309.1; -; mRNA.
DR PIR; JQ1281; DTCHPH.
DR RefSeq; NP_990509.1; NM_205178.1.
DR PDB; 1G8M; X-ray; 1.75 A; A/B=1-593.
DR PDB; 1M9N; X-ray; 1.93 A; A/B=1-593.
DR PDB; 1OZ0; X-ray; 2.50 A; A/B=1-593.
DR PDB; 1THZ; X-ray; 1.80 A; A/B=1-593.
DR PDB; 2B1G; X-ray; 2.10 A; A/B/C/D=1-593.
DR PDB; 2B1I; X-ray; 2.02 A; A/B=1-593.
DR PDB; 2IU0; X-ray; 2.53 A; A/B=1-593.
DR PDB; 2IU3; X-ray; 2.90 A; A/B=1-593.
DR PDBsum; 1G8M; -.
DR PDBsum; 1M9N; -.
DR PDBsum; 1OZ0; -.
DR PDBsum; 1THZ; -.
DR PDBsum; 2B1G; -.
DR PDBsum; 2B1I; -.
DR PDBsum; 2IU0; -.
DR PDBsum; 2IU3; -.
DR AlphaFoldDB; P31335; -.
DR SMR; P31335; -.
DR STRING; 9031.ENSGALP00000005643; -.
DR PaxDb; P31335; -.
DR GeneID; 396091; -.
DR KEGG; gga:396091; -.
DR CTD; 471; -.
DR VEuPathDB; HostDB:geneid_396091; -.
DR eggNOG; KOG2555; Eukaryota.
DR InParanoid; P31335; -.
DR OrthoDB; 324473at2759; -.
DR PhylomeDB; P31335; -.
DR BRENDA; 2.1.2.3; 1306.
DR BRENDA; 3.5.4.10; 1306.
DR Reactome; R-GGA-419140; De novo synthesis of IMP.
DR SABIO-RK; P31335; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR EvolutionaryTrace; P31335; -.
DR PRO; PR:P31335; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.287.440; -; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; Multifunctional enzyme;
KW Purine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..593
FT /note="Bifunctional purine biosynthesis protein ATIC"
FT /id="PRO_0000192155"
FT DOMAIN 1..147
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..199
FT /note="IMP cyclohydrolase"
FT /evidence="ECO:0000305|PubMed:17324932"
FT REGION 200..593
FT /note="AICAR formyltransferase"
FT /evidence="ECO:0000305|PubMed:17324932"
FT ACT_SITE 138
FT /note="Proton donor/acceptor; for FAICAR cyclization
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT ACT_SITE 268
FT /note="Proton acceptor; for AICAR formyltransferase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 13..15
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000305|PubMed:11323713,
FT ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT ECO:0007744|PDB:1M9N"
FT BINDING 35..38
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000305|PubMed:11323713,
FT ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT ECO:0007744|PDB:1M9N"
FT BINDING 65..68
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000305|PubMed:11323713,
FT ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT ECO:0007744|PDB:1M9N"
FT BINDING 102..103
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000305|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 126..127
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000305|PubMed:11323713,
FT ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M,
FT ECO:0007744|PDB:1M9N"
FT BINDING 208..209
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 268
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 317
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 340
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 432
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 452
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT BINDING 453
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000305|PubMed:12974624,
FT ECO:0007744|PDB:1OZ0"
FT BINDING 542
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT BINDING 547
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000305|PubMed:12974624,
FT ECO:0007744|PDB:1OZ0"
FT BINDING 566..567
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000305|PubMed:12974624,
FT ECO:0007744|PDB:1OZ0"
FT BINDING 589
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:12501179,
FT ECO:0007744|PDB:1M9N"
FT SITE 267
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31939"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1M9N"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2IU0"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:1G8M"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 169..198
FT /evidence="ECO:0007829|PDB:1G8M"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 238..258
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:1G8M"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:1G8M"
FT TURN 312..317
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1OZ0"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 452..468
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 485..497
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 504..510
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:1G8M"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:1G8M"
FT HELIX 569..579
FT /evidence="ECO:0007829|PDB:1G8M"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:1G8M"
SQ SEQUENCE 593 AA; 64415 MW; BD1A34F03D96A136 CRC64;
MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR DVSDLTGFPE
MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV VCNLYPFVKT VSSPGVTVPE
AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA DYSSVAKEMA ASKDKDTSVE TRRHLALKAF
THTAQYDAAI SDYFRKEYSK GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN
LCDALNAWQL VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL
ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE ALKILSKKKN
GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL FKNIVTKNKT LPESAVRDLI
VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ SRIHCTRLAG DKANSWWLRH HPRVLSMKFK
AGVKRAEVSN AIDQYVTGTI GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD
AFFPFRDNVD RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH
