CARB_ECOLI
ID CARB_ECOLI Reviewed; 1073 AA.
AC P00968;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN Name=carB {ECO:0000303|PubMed:6308632}; Synonyms=pyrA;
GN OrderedLocusNames=b0033, JW0031;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-2.
RC STRAIN=K12;
RX PubMed=6308632; DOI=10.1073/pnas.80.15.4629;
RA Nyunoya H., Lusty C.J.;
RT "The carB gene of Escherichia coli: a duplicated gene coding for the large
RT subunit of carbamoyl-phosphate synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6377309; DOI=10.1073/pnas.81.13.4139;
RA Bouvier J., Patte J.-C., Stragier P.;
RT "Multiple regulatory signals in the control region of the Escherichia coli
RT carAB operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=6330744; DOI=10.1073/pnas.81.13.4134;
RA Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M.,
RA Charlier D.R.M., Glansdorff N., Pierard A.;
RT "DNA sequence of the carA gene and the control region of carAB: tandem
RT promoters, respectively controlled by arginine and the pyrimidines,
RT regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia
RT coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=9174345; DOI=10.1021/bi970503q;
RA Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.;
RT "Structure of carbamoyl phosphate synthetase: a journey of 96 A from
RT substrate to product.";
RL Biochemistry 36:6305-6316(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE.
RX PubMed=9636022; DOI=10.1021/bi9807761;
RA Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M.,
RA Holden H.M.;
RT "Carbamoyl phosphate synthetase: caught in the act of glutamine
RT hydrolysis.";
RL Biochemistry 37:8825-8831(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE.
RX PubMed=10089390; DOI=10.1107/s0907444998006234;
RA Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.;
RT "The structure of carbamoyl phosphate synthetase determined to 2.1-A
RT resolution.";
RL Acta Crystallogr. D 55:8-24(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP MANGANESE.
RX PubMed=10029528; DOI=10.1021/bi982517h;
RA Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.;
RT "Carbamoyl phosphate synthetase: closure of the B-domain as a result of
RT nucleotide binding.";
RL Biochemistry 38:2347-2357(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE.
RX PubMed=10587438; DOI=10.1021/bi991741j;
RA Thoden J.B., Huang X., Raushel F.M., Holden H.M.;
RT "The small subunit of carbamoyl phosphate synthetase: snapshots along the
RT reaction pathway.";
RL Biochemistry 38:16158-16166(1999).
RN [13] {ECO:0007744|PDB:1CE8}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND MANGANESE.
RX PubMed=10428826; DOI=10.1074/jbc.274.32.22502;
RA Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.;
RT "The binding of inosine monophosphate to Escherichia coli carbamoyl
RT phosphate synthetase.";
RL J. Biol. Chem. 274:22502-22507(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01210};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01210};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01210};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of
CC heterodimers (alpha,beta)4. {ECO:0000255|HAMAP-Rule:MF_01210}.
CC -!- INTERACTION:
CC P00968; P0A6F1: carA; NbExp=14; IntAct=EBI-546118, EBI-546107;
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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DR EMBL; J01597; AAA23539.1; -; Genomic_DNA.
DR EMBL; V01500; CAA24744.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73144.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96602.1; -; Genomic_DNA.
DR PIR; A01198; SYECCP.
DR RefSeq; NP_414574.1; NC_000913.3.
DR RefSeq; WP_001126348.1; NZ_LN832404.1.
DR PDB; 1A9X; X-ray; 1.80 A; A/C/E/G=1-1073.
DR PDB; 1BXR; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDB; 1C30; X-ray; 2.00 A; A/C/E/G=1-1073.
DR PDB; 1C3O; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDB; 1CE8; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDB; 1CS0; X-ray; 2.00 A; A/C/E/G=1-1073.
DR PDB; 1JDB; X-ray; 2.10 A; B/E/H/K=1-1073.
DR PDB; 1KEE; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDB; 1M6V; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDB; 1T36; X-ray; 2.10 A; A/C/E/G=1-1073.
DR PDBsum; 1A9X; -.
DR PDBsum; 1BXR; -.
DR PDBsum; 1C30; -.
DR PDBsum; 1C3O; -.
DR PDBsum; 1CE8; -.
DR PDBsum; 1CS0; -.
DR PDBsum; 1JDB; -.
DR PDBsum; 1KEE; -.
DR PDBsum; 1M6V; -.
DR PDBsum; 1T36; -.
DR AlphaFoldDB; P00968; -.
DR SMR; P00968; -.
DR BioGRID; 4259726; 41.
DR BioGRID; 849177; 2.
DR ComplexPortal; CPX-1937; Carbamoyl phosphate synthetase complex.
DR DIP; DIP-1025N; -.
DR IntAct; P00968; 14.
DR STRING; 511145.b0033; -.
DR jPOST; P00968; -.
DR PaxDb; P00968; -.
DR PRIDE; P00968; -.
DR EnsemblBacteria; AAC73144; AAC73144; b0033.
DR EnsemblBacteria; BAB96602; BAB96602; BAB96602.
DR GeneID; 944775; -.
DR KEGG; ecj:JW0031; -.
DR KEGG; eco:b0033; -.
DR PATRIC; fig|1411691.4.peg.2251; -.
DR EchoBASE; EB0133; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_6; -.
DR InParanoid; P00968; -.
DR OMA; IEPAGIH; -.
DR PhylomeDB; P00968; -.
DR BioCyc; EcoCyc:CARBPSYN-LARGE; -.
DR BioCyc; MetaCyc:CARBPSYN-LARGE; -.
DR BRENDA; 6.3.5.5; 2026.
DR SABIO-RK; P00968; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR EvolutionaryTrace; P00968; -.
DR PRO; PR:P00968; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:EcoliWiki.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki.
DR GO; GO:0000166; F:nucleotide binding; IDA:EcoliWiki.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IC:ComplexPortal.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:EcoliWiki.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Direct protein sequencing; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6308632"
FT CHAIN 2..1073
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145004"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 679..870
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 937..1073
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 2..403
FT /note="Carboxyphosphate synthetic domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT REGION 404..553
FT /note="Oligomerization domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT REGION 554..936
FT /note="Carbamoyl phosphate synthetic domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT REGION 937..1073
FT /note="Allosteric domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10428826,
FT ECO:0007744|PDB:1CE8"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10428826,
FT ECO:0007744|PDB:1CE8"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10029528,
FT ECO:0000269|PubMed:10089390, ECO:0000269|PubMed:10428826,
FT ECO:0000269|PubMed:10587438, ECO:0000269|PubMed:9636022,
FT ECO:0007744|PDB:1CE8"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10029528,
FT ECO:0000269|PubMed:10089390, ECO:0000269|PubMed:10428826,
FT ECO:0000269|PubMed:10587438, ECO:0000269|PubMed:9636022,
FT ECO:0007744|PDB:1CE8"
FT BINDING 705..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 829
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10428826,
FT ECO:0000269|PubMed:9636022, ECO:0007744|PDB:1CE8"
FT BINDING 841
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10428826,
FT ECO:0000269|PubMed:9636022, ECO:0007744|PDB:1CE8"
FT BINDING 841
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10029528,
FT ECO:0000269|PubMed:10089390"
FT BINDING 843
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10029528,
FT ECO:0000269|PubMed:10089390"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 338..342
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 460..479
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 510..519
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 576..591
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:1CS0"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 623..633
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 651..656
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 661..664
FT /evidence="ECO:0007829|PDB:1CS0"
FT HELIX 666..673
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 675..685
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 698..708
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 721..724
FT /evidence="ECO:0007829|PDB:1BXR"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 731..740
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 760..768
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 773..783
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 794..797
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:1JDB"
FT HELIX 803..819
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 824..832
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 837..843
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 850..857
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 861..869
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 874..877
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 896..899
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 915..923
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 924..934
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 941..948
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 951..954
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 957..966
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 975..982
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 989..992
FT /evidence="ECO:0007829|PDB:1CS0"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 998..1000
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 1001..1007
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 1011..1015
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 1020..1025
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 1027..1035
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 1039..1043
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 1044..1054
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 1058..1060
FT /evidence="ECO:0007829|PDB:1BXR"
FT HELIX 1065..1070
FT /evidence="ECO:0007829|PDB:1A9X"
SQ SEQUENCE 1073 AA; 117842 MW; A09D019CBDFF8D2B CRC64;
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK
