ID PUR4_SALTY Reviewed; 1295 AA.
AC P74881;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=STM2565;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RA Zilles J.L., Downs D.M.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ATP ANALOG; ADP AND
RP MAGNESIUM.
RX PubMed=15301531; DOI=10.1021/bi0491301;
RA Anand R., Hoskins A.A., Stubbe J., Ealick S.E.;
RT "Domain organization of Salmonella typhimurium formylglycinamide
RT ribonucleotide amidotransferase revealed by X-ray crystallography.";
RL Biochemistry 43:10328-10342(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM.
RX PubMed=22683785; DOI=10.1107/s0907444912006543;
RA Tanwar A.S., Morar M., Panjikar S., Anand R.;
RT "Formylglycinamide ribonucleotide amidotransferase from Salmonella
RT typhimurium: role of ATP complexation and the glutaminase domain in
RT catalytic coupling.";
RL Acta Crystallogr. D 68:627-636(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF WILD-TYPE; MUTANTS TRP-209 AND
RP ALA-1263 IN COMPLEX WITH ADP AND MAGNESIUM, FUNCTION, AND MUTAGENESIS OF
RP PHE-209; THR-683; LEU-1181 AND ARG-1263.
RX PubMed=24223728; DOI=10.1371/journal.pone.0077781;
RA Tanwar A.S., Goyal V.D., Choudhary D., Panjikar S., Anand R.;
RT "Importance of hydrophobic cavities in allosteric regulation of
RT formylglycinamide synthetase: insight from xenon trapping and statistical
RT coupling analysis.";
RL PLoS ONE 8:E77781-E77781(2013).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC {ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:24223728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00419};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR EMBL; U68728; AAB08888.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21459.1; -; Genomic_DNA.
DR RefSeq; NP_461500.1; NC_003197.2.
DR RefSeq; WP_000970045.1; NC_003197.2.
DR PDB; 1T3T; X-ray; 1.90 A; A=1-1295.
DR PDB; 3UGJ; X-ray; 1.78 A; A=1-1295.
DR PDB; 3UJN; X-ray; 2.98 A; A=1-1295.
DR PDB; 3UMM; X-ray; 3.20 A; A=1-1295.
DR PDB; 4L78; X-ray; 2.18 A; A=1-1295.
DR PDB; 4LGY; X-ray; 1.48 A; A=1-1295.
DR PDB; 4MGH; X-ray; 2.65 A; A=1-1295.
DR PDB; 4R7G; X-ray; 2.90 A; A=1-1295.
DR PDB; 6JT7; X-ray; 1.86 A; A=1-1295.
DR PDB; 6JT8; X-ray; 1.90 A; A=1-1295.
DR PDB; 6JT9; X-ray; 2.10 A; A=1-1295.
DR PDB; 6JTA; X-ray; 1.75 A; A=1-1295.
DR PDB; 6LYK; X-ray; 1.70 A; A=1-1295.
DR PDB; 6LYL; X-ray; 2.10 A; A=1-1295.
DR PDB; 6LYM; X-ray; 2.46 A; A=1-1295.
DR PDB; 6LYO; X-ray; 1.87 A; A=1-1295.
DR PDB; 7DW7; X-ray; 1.80 A; A=1-1295.
DR PDBsum; 1T3T; -.
DR PDBsum; 3UGJ; -.
DR PDBsum; 3UJN; -.
DR PDBsum; 3UMM; -.
DR PDBsum; 4L78; -.
DR PDBsum; 4LGY; -.
DR PDBsum; 4MGH; -.
DR PDBsum; 4R7G; -.
DR PDBsum; 6JT7; -.
DR PDBsum; 6JT8; -.
DR PDBsum; 6JT9; -.
DR PDBsum; 6JTA; -.
DR PDBsum; 6LYK; -.
DR PDBsum; 6LYL; -.
DR PDBsum; 6LYM; -.
DR PDBsum; 6LYO; -.
DR PDBsum; 7DW7; -.
DR AlphaFoldDB; P74881; -.
DR SMR; P74881; -.
DR STRING; 99287.STM2565; -.
DR PaxDb; 99287-STM2565; -.
DR GeneID; 1254087; -.
DR KEGG; stm:STM2565; -.
DR PATRIC; fig|99287.12.peg.2706; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; P74881; -.
DR BioCyc; SENT99287:STM2565-MONOMER; -.
DR BRENDA; 6.3.5.3; 5542.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; P74881; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02193; PurL; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100418"
FT DOMAIN 1042..1295
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1135
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 386..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419,
FT ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785,
FT ECO:0000269|PubMed:24223728"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419,
FT ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785,
FT ECO:0000269|PubMed:24223728"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419,
FT ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785,
FT ECO:0000269|PubMed:24223728"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419,
FT ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785,
FT ECO:0000269|PubMed:24223728"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 209
FT /note="F->W: This mutant shows a perturbation of the local
FT environment, however has a secondary structure content and
FT a FGAM synthase activity very similar to the wild-type
FT protein."
FT /evidence="ECO:0000269|PubMed:24223728"
FT MUTAGEN 683
FT /note="T->W: This mutant shows a disturbance in the
FT secondary structure of the protein and causes a 30% loss in
FT FGAM synthase activity."
FT /evidence="ECO:0000269|PubMed:24223728"
FT MUTAGEN 1181
FT /note="L->F: This mutant has a lower overall folding of the
FT secondary structure and shows a 60% loss in FGAM synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:24223728"
FT MUTAGEN 1181
FT /note="L->W: This mutant has the same secondary structure
FT content and FGAM synthetase activity as the wild-type
FT protein and exhibits almost no destabilization."
FT /evidence="ECO:0000269|PubMed:24223728"
FT MUTAGEN 1181
FT /note="L->Y: This mutant is extremely deleterious to the
FT structural integrity of the protein."
FT /evidence="ECO:0000269|PubMed:24223728"
FT MUTAGEN 1263
FT /note="R->A: This mutant is structurally identical to the
FT wild-type protein."
FT /evidence="ECO:0000269|PubMed:24223728"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:3UGJ"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 256..273
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 279..295
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 327..338
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:3UJN"
FT HELIX 362..380
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 411..420
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6LYK"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:6JTA"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 475..489
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 508..518
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 560..570
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 574..590
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 595..601
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 633..641
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 644..646
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:3UMM"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 671..674
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 679..686
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 692..699
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 701..705
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 708..723
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 735..741
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 749..761
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 764..768
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 771..778
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 782..795
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 799..809
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 822..830
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 831..834
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:3UMM"
FT HELIX 842..846
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:3UMM"
FT HELIX 860..875
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 880..884
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 889..901
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 903..908
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 910..912
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 916..921
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 925..932
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 936..945
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 949..951
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 952..968
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 971..977
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 978..996
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 999..1009
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1031..1034
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 1035..1037
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1041..1046
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1050..1052
FT /evidence="ECO:0007829|PDB:3UJN"
FT HELIX 1053..1062
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1066..1071
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1072..1076
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1082..1084
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1086..1090
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1095..1098
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1104..1111
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1114..1125
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1126..1128
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1130..1134
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1136..1143
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1145..1147
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1156..1158
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1166..1174
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1180..1182
FT /evidence="ECO:0007829|PDB:4LGY"
FT TURN 1183..1187
FT /evidence="ECO:0007829|PDB:3UJN"
FT STRAND 1189..1198
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1200..1202
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1206..1215
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1218..1223
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1227..1229
FT /evidence="ECO:0007829|PDB:3UJN"
FT TURN 1233..1235
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1236..1238
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1241..1243
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1244..1248
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1252..1260
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1261..1263
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1264..1266
FT /evidence="ECO:0007829|PDB:4LGY"
FT HELIX 1267..1269
FT /evidence="ECO:0007829|PDB:4LGY"
FT STRAND 1270..1272
FT /evidence="ECO:0007829|PDB:6JT7"
FT HELIX 1284..1294
FT /evidence="ECO:0007829|PDB:4LGY"
SQ SEQUENCE 1295 AA; 141472 MW; 55072EAD8712040D CRC64;
MMEILRGSPA LSAFRINKLL ARFQAANLQV HNIYAEYVHF ADLNAPLNDS EQAQLTRLLQ
YGPALSSHTP AGKLLLVTPR PGTISPWSSK ATDIAHNCGL QQVDRLERGV AYYIEASTLT
AEQWRQVAAE LHDRMMETVF SSLTDAEKLF IHHQPAPVSS VDLLGEGRQA LIDANLRLGL
ALAEDEIDYL QEAFTKLGRN PNDIELYMFA QANSEHCRHK IFNADWIIDG KPQPKSLFKM
IKNTFETTPD YVLSAYKDNA AVMEGSAVGR YFADHNTGRY DFHQEPAHIL MKVETHNHPT
AISPWPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL RIPGFEQPWE EDFGKPERIV
TALDIMTEGP LGGAAFNNEF GRPALTGYFR TYEEKVNSHN GEELRGYHKP IMLAGGIGNI
RADHVQKGEI VVGAKLIVLG GPAMNIGLGG GAASSMASGQ SDADLDFASV QRDNPEMERR
CQEVIDRCWQ LGDANPILFI HDVGAGGLSN AMPELVSDGG RGGKFELRDI LSDEPGMSPL
EIWCNESQER YVLAVAADQL PLFDELCKRE RAPYAVIGDA TEEQHLSLHD NHFDNQPIDL
PLDVLLGKTP KMTRDVQTLK AKGDALNRAD ITIADAVKRV LHLPTVAEKT FLVTIGDRTV
TGMVARDQMV GPWQVPVADC AVTTASLDSY YGEAMSIGER APVALLDFAA SARLAVGEAL
TNIAATQIGD IKRIKLSANW MAAAGHPGED AGLYDAVKAV GEELCPQLGL TIPVGKDSMS
MKTRWQEGNE QREMTSPLSL VISAFARVED VRHTLTPQLS TEDNALLLID LGKGHNALGA
TALAQVYRQL GDKPADVRDV AQLKGFYDAM QALVAARKLL AWHDRSDGGL LVTLAEMAFA
GHCGVQVDIA ALGDDHLAAL FNEELGGVIQ VRAEDRDAVE ALLAQYGLAD CVHYLGQALA
GDRFVITAND QTVFSESRTT LRVWWAETTW QMQRLRDNPQ CADQEHEAKA NDTDPGLNVK
LSFDINEDIA APYIATGARP KVAVLREQGV NSHVEMAAAF HRAGFDAIDV HMSDLLGGRI
GLGNFHALVA CGGFSYGDVL GAGEGWAKSI LFNHRVRDEF ETFFHRPQTL ALGVCNGCQM
MSNLRELIPG SELWPRFVRN HSDRFEARFS LVEVTQSPSL LLQGMVGSQM PIAVSHGEGR
VEVRDDAHLA ALESKGLVAL RYVDNFGKVT ETYPANPNGS PNGITAVTTE NGRVTIMMPH
PERVFRTVAN SWHPENWGED SPWMRIFRNA RKQLG
//
