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Database: UniProt
Entry: P00968
LinkDB: P00968
Original site: P00968 
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   13-FEB-2019, entry version 197.
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
RT   large 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
RT   coli 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.,
RA   Isono K., Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   0-2.4 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.,
RA   Mau B., 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
RT   MG1655 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
RT   Escherichia 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.,
RA   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
RP   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
RP   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
RT   of nucleotide binding.";
RL   Biochemistry 38:2347-2357(1999).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND
RP   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
RT   the reaction pathway.";
RL   Biochemistry 38:16158-16166(1999).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADP AND
RP   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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01210};
CC       Note=Binds 4 Mn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01210};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-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
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       Tetramer of heterodimers (alpha,beta)4. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- INTERACTION:
CC       P0A6F1:carA; NbExp=14; IntAct=EBI-546118, EBI-546107;
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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   ProteinModelPortal; P00968; -.
DR   SMR; P00968; -.
DR   BioGrid; 4259726; 41.
DR   ComplexPortal; CPX-1937; Carbamoyl phosphate synthetase complex.
DR   DIP; DIP-1025N; -.
DR   IntAct; P00968; 14.
DR   STRING; 316385.ECDH10B_0034; -.
DR   EPD; P00968; -.
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   EcoGene; EG10135; carB.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   InParanoid; P00968; -.
DR   KO; K01955; -.
DR   PhylomeDB; P00968; -.
DR   BioCyc; EcoCyc:CARBPSYN-LARGE; -.
DR   BioCyc; ECOL316407:JW0031-MONOMER; -.
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; IEA:UniProtKB-UniRule.
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;
KW   ATP-binding; Complete proteome; Direct protein sequencing; Ligase;
KW   Manganese; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis;
KW   Reference proteome; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:6308632}.
FT   CHAIN         2   1073       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145004.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      679    870       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      937   1073       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     705    762       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        2    403       Carboxyphosphate synthetic domain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION      404    553       Oligomerization domain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION      554    936       Carbamoyl phosphate synthetic domain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION      937   1073       Allosteric domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   METAL       285    285       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   METAL       299    299       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   METAL       299    299       Manganese 2.
FT                                {ECO:0000269|PubMed:10029528,
FT                                ECO:0000269|PubMed:10089390,
FT                                ECO:0000269|PubMed:10428826,
FT                                ECO:0000269|PubMed:10587438,
FT                                ECO:0000269|PubMed:9636022}.
FT   METAL       301    301       Manganese 2.
FT                                {ECO:0000269|PubMed:10029528,
FT                                ECO:0000269|PubMed:10089390,
FT                                ECO:0000269|PubMed:10428826,
FT                                ECO:0000269|PubMed:10587438,
FT                                ECO:0000269|PubMed:9636022}.
FT   METAL       829    829       Manganese 3.
FT                                {ECO:0000269|PubMed:9636022}.
FT   METAL       841    841       Manganese 3.
FT                                {ECO:0000269|PubMed:9636022}.
FT   METAL       841    841       Manganese 4.
FT                                {ECO:0000269|PubMed:10029528,
FT                                ECO:0000269|PubMed:10089390}.
FT   METAL       843    843       Manganese 4.
FT                                {ECO:0000269|PubMed:10029528,
FT                                ECO:0000269|PubMed:10089390}.
FT   STRAND        9     13       {ECO:0000244|PDB:1A9X}.
FT   HELIX        25     40       {ECO:0000244|PDB:1A9X}.
FT   STRAND       43     47       {ECO:0000244|PDB:1A9X}.
FT   HELIX        54     56       {ECO:0000244|PDB:1A9X}.
FT   HELIX        58     60       {ECO:0000244|PDB:1A9X}.
FT   STRAND       61     65       {ECO:0000244|PDB:1A9X}.
FT   HELIX        71     81       {ECO:0000244|PDB:1A9X}.
FT   STRAND       84     87       {ECO:0000244|PDB:1A9X}.
FT   STRAND       89     91       {ECO:0000244|PDB:1A9X}.
FT   HELIX        92    104       {ECO:0000244|PDB:1A9X}.
FT   HELIX       107    111       {ECO:0000244|PDB:1A9X}.
FT   HELIX       120    127       {ECO:0000244|PDB:1A9X}.
FT   HELIX       129    138       {ECO:0000244|PDB:1A9X}.
FT   STRAND      145    151       {ECO:0000244|PDB:1A9X}.
FT   HELIX       152    162       {ECO:0000244|PDB:1A9X}.
FT   STRAND      164    170       {ECO:0000244|PDB:1A9X}.
FT   TURN        175    178       {ECO:0000244|PDB:1A9X}.
FT   STRAND      180    184       {ECO:0000244|PDB:1A9X}.
FT   HELIX       185    198       {ECO:0000244|PDB:1A9X}.
FT   STRAND      204    208       {ECO:0000244|PDB:1A9X}.
FT   STRAND      213    222       {ECO:0000244|PDB:1A9X}.
FT   STRAND      228    238       {ECO:0000244|PDB:1A9X}.
FT   HELIX       244    246       {ECO:0000244|PDB:1A9X}.
FT   STRAND      249    252       {ECO:0000244|PDB:1A9X}.
FT   HELIX       258    275       {ECO:0000244|PDB:1A9X}.
FT   STRAND      279    288       {ECO:0000244|PDB:1A9X}.
FT   TURN        290    292       {ECO:0000244|PDB:1A9X}.
FT   STRAND      295    303       {ECO:0000244|PDB:1A9X}.
FT   HELIX       306    315       {ECO:0000244|PDB:1A9X}.
FT   HELIX       319    327       {ECO:0000244|PDB:1A9X}.
FT   HELIX       332    334       {ECO:0000244|PDB:1A9X}.
FT   TURN        338    342       {ECO:0000244|PDB:1A9X}.
FT   STRAND      344    346       {ECO:0000244|PDB:1A9X}.
FT   STRAND      353    361       {ECO:0000244|PDB:1A9X}.
FT   HELIX       364    366       {ECO:0000244|PDB:1A9X}.
FT   STRAND      382    390       {ECO:0000244|PDB:1A9X}.
FT   HELIX       391    401       {ECO:0000244|PDB:1A9X}.
FT   STRAND      402    405       {ECO:0000244|PDB:1A9X}.
FT   STRAND      407    409       {ECO:0000244|PDB:1A9X}.
FT   HELIX       420    429       {ECO:0000244|PDB:1A9X}.
FT   HELIX       435    444       {ECO:0000244|PDB:1A9X}.
FT   HELIX       449    456       {ECO:0000244|PDB:1A9X}.
FT   HELIX       460    479       {ECO:0000244|PDB:1A9X}.
FT   HELIX       481    483       {ECO:0000244|PDB:1A9X}.
FT   HELIX       486    494       {ECO:0000244|PDB:1A9X}.
FT   HELIX       499    505       {ECO:0000244|PDB:1A9X}.
FT   HELIX       510    519       {ECO:0000244|PDB:1A9X}.
FT   STRAND      525    528       {ECO:0000244|PDB:1A9X}.
FT   STRAND      541    547       {ECO:0000244|PDB:1A9X}.
FT   STRAND      557    559       {ECO:0000244|PDB:1A9X}.
FT   STRAND      561    565       {ECO:0000244|PDB:1A9X}.
FT   HELIX       576    591       {ECO:0000244|PDB:1A9X}.
FT   STRAND      595    599       {ECO:0000244|PDB:1A9X}.
FT   HELIX       606    608       {ECO:0000244|PDB:1CS0}.
FT   STRAND      612    617       {ECO:0000244|PDB:1A9X}.
FT   HELIX       623    633       {ECO:0000244|PDB:1A9X}.
FT   STRAND      636    639       {ECO:0000244|PDB:1A9X}.
FT   STRAND      641    643       {ECO:0000244|PDB:1A9X}.
FT   HELIX       645    648       {ECO:0000244|PDB:1A9X}.
FT   HELIX       651    656       {ECO:0000244|PDB:1A9X}.
FT   STRAND      661    664       {ECO:0000244|PDB:1CS0}.
FT   HELIX       666    673       {ECO:0000244|PDB:1A9X}.
FT   HELIX       675    685       {ECO:0000244|PDB:1A9X}.
FT   STRAND      692    694       {ECO:0000244|PDB:1A9X}.
FT   HELIX       698    708       {ECO:0000244|PDB:1A9X}.
FT   STRAND      710    715       {ECO:0000244|PDB:1A9X}.
FT   TURN        721    724       {ECO:0000244|PDB:1BXR}.
FT   STRAND      725    728       {ECO:0000244|PDB:1A9X}.
FT   HELIX       731    740       {ECO:0000244|PDB:1A9X}.
FT   STRAND      751    754       {ECO:0000244|PDB:1A9X}.
FT   STRAND      760    768       {ECO:0000244|PDB:1A9X}.
FT   STRAND      773    783       {ECO:0000244|PDB:1A9X}.
FT   HELIX       789    791       {ECO:0000244|PDB:1A9X}.
FT   STRAND      794    797       {ECO:0000244|PDB:1A9X}.
FT   STRAND      799    801       {ECO:0000244|PDB:1JDB}.
FT   HELIX       803    819       {ECO:0000244|PDB:1A9X}.
FT   STRAND      824    832       {ECO:0000244|PDB:1A9X}.
FT   STRAND      837    843       {ECO:0000244|PDB:1A9X}.
FT   HELIX       850    857       {ECO:0000244|PDB:1A9X}.
FT   HELIX       861    869       {ECO:0000244|PDB:1A9X}.
FT   HELIX       874    877       {ECO:0000244|PDB:1A9X}.
FT   STRAND      886    894       {ECO:0000244|PDB:1A9X}.
FT   HELIX       896    899       {ECO:0000244|PDB:1A9X}.
FT   STRAND      915    923       {ECO:0000244|PDB:1A9X}.
FT   HELIX       924    934       {ECO:0000244|PDB:1A9X}.
FT   STRAND      941    948       {ECO:0000244|PDB:1A9X}.
FT   HELIX       951    954       {ECO:0000244|PDB:1A9X}.
FT   HELIX       957    966       {ECO:0000244|PDB:1A9X}.
FT   STRAND      970    973       {ECO:0000244|PDB:1A9X}.
FT   HELIX       975    982       {ECO:0000244|PDB:1A9X}.
FT   TURN        983    985       {ECO:0000244|PDB:1A9X}.
FT   STRAND      989    992       {ECO:0000244|PDB:1CS0}.
FT   TURN        994    996       {ECO:0000244|PDB:1A9X}.
FT   STRAND      998   1000       {ECO:0000244|PDB:1A9X}.
FT   HELIX      1001   1007       {ECO:0000244|PDB:1A9X}.
FT   STRAND     1011   1015       {ECO:0000244|PDB:1A9X}.
FT   HELIX      1020   1025       {ECO:0000244|PDB:1A9X}.
FT   HELIX      1027   1035       {ECO:0000244|PDB:1A9X}.
FT   STRAND     1039   1043       {ECO:0000244|PDB:1A9X}.
FT   HELIX      1044   1054       {ECO:0000244|PDB:1A9X}.
FT   TURN       1058   1060       {ECO:0000244|PDB:1BXR}.
FT   HELIX      1065   1070       {ECO:0000244|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
//
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