THIO_ECOLI
ID THIO_ECOLI Reviewed; 109 AA.
AC P0AA25; P00274; P76750; Q2M889; Q47674; Q8XAT2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Thioredoxin 1;
DE Short=Trx-1;
GN Name=trxA; Synonyms=fipA, tsnC; OrderedLocusNames=b3781, JW5856;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098320; DOI=10.1007/bf01116889;
RA Hoeoeg J.-O., von Bahr-Lindstroem H., Josephson S., Wallace B.J.,
RA Kushner S.R., Joernvall H., Holmgren A.;
RT "Nucleotide sequence of the thioredoxin gene from Escherichia coli.";
RL Biosci. Rep. 4:917-923(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6099324; DOI=10.1016/0378-1119(84)90015-5;
RA Wallace B.J., Kushner S.R.;
RT "Genetic and physical analysis of the thioredoxin (trxA) gene of
RT Escherichia coli K-12.";
RL Gene 32:399-408(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3891733; DOI=10.1128/jb.163.1.311-316.1985;
RA Lim C.-J., Geraghty D., Fuchs J.A.;
RT "Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-
RT 12.";
RL J. Bacteriol. 163:311-316(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wallace B.J., Zownir O., Kushner S.R.;
RT "Physical analysis of the thioredoxin gene from Escherichia coli K-12.";
RL (In) Holmgren A. (eds.);
RL Thioredoxin and glutaredoxin systems, structure and function, pp.11-19,
RL Raven Press, New York (1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-109.
RC STRAIN=B;
RX PubMed=4883076; DOI=10.1111/j.1432-1033.1968.tb00470.x;
RA Holmgren A.;
RT "Thioredoxin. 6. The amino acid sequence of the protein from Escherichia
RT coli B.";
RL Eur. J. Biochem. 6:475-484(1968).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=1094461; DOI=10.1073/pnas.72.6.2305;
RA Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I.;
RT "Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
RX PubMed=4616096; DOI=10.1016/0022-2836(74)90262-9;
RA Soederberg B.-O., Holmgren A., Braenden C.-I.;
RT "Structure of oxidized thioredoxin to 4 with 5-A resolution.";
RL J. Mol. Biol. 90:143-152(1974).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
RX PubMed=2181145; DOI=10.1016/0022-2836(90)90313-b;
RA Katti S.K., le Master D.M., Eklund H.;
RT "Crystal structure of thioredoxin from Escherichia coli at 1.68-A
RT resolution.";
RL J. Mol. Biol. 212:167-184(1990).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37.
RX PubMed=8098620; DOI=10.1021/bi00070a017;
RA Nikkola M., Gleason F.K., Fuchs J.A., Eklund H.;
RT "Crystal structure analysis of a mutant Escherichia coli thioredoxin in
RT which lysine 36 is replaced by glutamic acid.";
RL Biochemistry 32:5093-5098(1993).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=10489448; DOI=10.1107/s0907444999008756;
RA Schultz L.W., Chivers P.T., Raines R.T.;
RT "The CXXC motif: crystal structure of an active-site variant of Escherichia
RT coli thioredoxin.";
RL Acta Crystallogr. D 55:1533-1538(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB.
RX PubMed=10947986; DOI=10.1126/science.289.5482.1190;
RA Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
RT "Twists in catalysis: alternating conformations of Escherichia coli
RT thioredoxin reductase.";
RL Science 289:1190-1194(2000).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=2193685; DOI=10.1021/bi00469a016;
RA Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E.;
RT "Three-dimensional solution structure of the reduced form of Escherichia
RT coli thioredoxin determined by nuclear magnetic resonance spectroscopy.";
RL Biochemistry 29:4129-4136(1990).
RN [18]
RP STRUCTURE BY NMR.
RX PubMed=7812718; DOI=10.1016/s0969-2126(94)00086-7;
RA Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A., Wright P.E.,
RA Dyson H.J.;
RT "High-resolution solution structures of oxidized and reduced Escherichia
RT coli thioredoxin.";
RL Structure 2:853-868(1994).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions.
CC -!- SUBUNIT: Monomer. Interacts with bacteriophage T3 DNA polymerase.
CC {ECO:0000269|PubMed:10947986}.
CC -!- INTERACTION:
CC P0AA25; P0A9P4: trxB; NbExp=2; IntAct=EBI-368542, EBI-1029826;
CC P0AA25; P00581: 5; Xeno; NbExp=2; IntAct=EBI-368542, EBI-8664634;
CC P0AA25; O22160: At2g44920; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895776;
CC P0AA25; Q9SCY2: FKBP13; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895757;
CC P0AA25; Q9LXX5: PPD6; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895738;
CC P0AA25; Q9LU86: PRXQ; Xeno; NbExp=2; IntAct=EBI-368542, EBI-540311;
CC P0AA25; P23321: PSBO1; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449414;
CC P0AA25; Q9S841: PSBO2; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449424;
CC P0AA25; P81760: TL17; Xeno; NbExp=2; IntAct=EBI-368542, EBI-449573;
CC P0AA25; P82281: TL29; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895799;
CC P0AA25; Q39249: VDE1; Xeno; NbExp=2; IntAct=EBI-368542, EBI-2895666;
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA67582.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M26133; AAA24693.1; -; Genomic_DNA.
DR EMBL; K02845; AAA24534.1; ALT_INIT; Genomic_DNA.
DR EMBL; M10424; AAA24533.1; -; Genomic_DNA.
DR EMBL; M54881; AAA24696.1; -; Genomic_DNA.
DR EMBL; M12779; AAA24694.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67582.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76786.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77517.1; -; Genomic_DNA.
DR PIR; A91519; TXEC.
DR RefSeq; NP_418228.2; NC_000913.3.
DR RefSeq; WP_001280776.1; NZ_STEB01000021.1.
DR PDB; 1F6M; X-ray; 2.95 A; C/D/G/H=2-109.
DR PDB; 1KEB; X-ray; 1.80 A; A/B=2-109.
DR PDB; 1M7T; NMR; -; A=32-108.
DR PDB; 1OAZ; X-ray; 2.78 A; A/B=2-109.
DR PDB; 1SKR; X-ray; 2.40 A; B=2-109.
DR PDB; 1SKS; X-ray; 2.30 A; B=2-109.
DR PDB; 1SKW; X-ray; 2.30 A; B=2-109.
DR PDB; 1SL0; X-ray; 3.20 A; B/D=2-109.
DR PDB; 1SL1; X-ray; 2.20 A; B=2-109.
DR PDB; 1SL2; X-ray; 2.30 A; B=2-109.
DR PDB; 1SRX; X-ray; 2.80 A; A=2-109.
DR PDB; 1T7P; X-ray; 2.20 A; B=2-109.
DR PDB; 1T8E; X-ray; 2.54 A; B=2-109.
DR PDB; 1THO; X-ray; 2.30 A; A=2-109.
DR PDB; 1TK0; X-ray; 2.30 A; B=2-109.
DR PDB; 1TK5; X-ray; 2.20 A; B=2-109.
DR PDB; 1TK8; X-ray; 2.50 A; B=2-109.
DR PDB; 1TKD; X-ray; 2.49 A; B=2-109.
DR PDB; 1TXX; X-ray; 2.20 A; A=2-109.
DR PDB; 1X9M; X-ray; 2.10 A; B=2-109.
DR PDB; 1X9S; X-ray; 2.70 A; B=2-109.
DR PDB; 1X9W; X-ray; 2.30 A; B=2-109.
DR PDB; 1XOA; NMR; -; A=2-109.
DR PDB; 1XOB; NMR; -; A=2-109.
DR PDB; 1ZCP; X-ray; 2.30 A; A/B/C/D=2-109.
DR PDB; 1ZYQ; X-ray; 2.70 A; B=2-109.
DR PDB; 1ZZY; X-ray; 2.50 A; A/B=2-109.
DR PDB; 2AJQ; X-ray; 2.60 A; B/I=2-109.
DR PDB; 2BTO; X-ray; 2.50 A; T=2-109.
DR PDB; 2EIO; X-ray; 2.60 A; A/B/C/D=2-109.
DR PDB; 2EIQ; X-ray; 1.90 A; A/B=2-109.
DR PDB; 2EIR; X-ray; 2.50 A; A/B/C/D=2-109.
DR PDB; 2FCH; X-ray; 2.60 A; A/B/C/D/E/F/G=2-109.
DR PDB; 2FD3; X-ray; 2.45 A; A/B=2-109.
DR PDB; 2H6X; X-ray; 2.60 A; A/B=2-109.
DR PDB; 2H6Y; X-ray; 2.40 A; A/B=2-109.
DR PDB; 2H6Z; X-ray; 2.25 A; A/B=2-109.
DR PDB; 2H70; X-ray; 2.70 A; A/B=2-109.
DR PDB; 2H71; X-ray; 2.20 A; A/B=2-109.
DR PDB; 2H72; X-ray; 2.25 A; A/B=2-109.
DR PDB; 2H73; X-ray; 2.45 A; A/B=2-109.
DR PDB; 2H74; X-ray; 2.40 A; A/B=4-109.
DR PDB; 2H75; X-ray; 2.20 A; A/B=2-109.
DR PDB; 2H76; X-ray; 2.25 A; A/B=2-109.
DR PDB; 2O8V; X-ray; 3.00 A; B=2-109.
DR PDB; 2TIR; X-ray; 2.00 A; A=2-109.
DR PDB; 2TRX; X-ray; 1.68 A; A/B=2-109.
DR PDB; 3DYR; X-ray; 2.00 A; A/B=2-109.
DR PDB; 4HU7; X-ray; 1.40 A; A/B=2-109.
DR PDB; 4HU9; X-ray; 1.55 A; A=2-109.
DR PDB; 4HUA; X-ray; 1.10 A; A=2-109.
DR PDB; 4X43; X-ray; 1.65 A; A/B/C=2-109.
DR PDB; 5HR0; X-ray; 1.31 A; A/B=1-109.
DR PDB; 5HR1; X-ray; 2.14 A; A/B/C/D/E/F/G=1-107.
DR PDB; 5HR2; X-ray; 1.20 A; A=1-109.
DR PDB; 5HR3; X-ray; 1.10 A; A/B=1-109.
DR PDB; 5XOC; X-ray; 2.40 A; B=2-109.
DR PDB; 6GD1; X-ray; 2.01 A; A/B=1-109.
DR PDB; 6GDG; EM; 4.11 A; A=2-109.
DR PDB; 6H7J; X-ray; 2.80 A; E/F=2-109.
DR PDB; 6H7L; X-ray; 2.70 A; E/F=2-109.
DR PDB; 6H7M; X-ray; 2.76 A; E/F=2-109.
DR PDB; 6H7N; X-ray; 2.50 A; E/F=2-109.
DR PDB; 6H7O; X-ray; 2.80 A; E/F=2-109.
DR PDB; 6IBL; X-ray; 2.70 A; A/B=2-109.
DR PDB; 6LUR; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-109.
DR PDB; 6N7W; EM; 4.50 A; I=1-109.
DR PDB; 6P7E; X-ray; 3.00 A; E/F/G/H=1-109.
DR PDB; 6Y4Y; X-ray; 1.75 A; A/B/C/D=1-109.
DR PDB; 6Y4Z; X-ray; 1.90 A; A/B/C/D=1-109.
DR PDB; 6YEV; X-ray; 2.94 A; E/F/G=1-109.
DR PDB; 7SCD; X-ray; 2.90 A; A=1-108.
DR PDB; 7SCE; X-ray; 2.75 A; A=1-108.
DR PDBsum; 1F6M; -.
DR PDBsum; 1KEB; -.
DR PDBsum; 1M7T; -.
DR PDBsum; 1OAZ; -.
DR PDBsum; 1SKR; -.
DR PDBsum; 1SKS; -.
DR PDBsum; 1SKW; -.
DR PDBsum; 1SL0; -.
DR PDBsum; 1SL1; -.
DR PDBsum; 1SL2; -.
DR PDBsum; 1SRX; -.
DR PDBsum; 1T7P; -.
DR PDBsum; 1T8E; -.
DR PDBsum; 1THO; -.
DR PDBsum; 1TK0; -.
DR PDBsum; 1TK5; -.
DR PDBsum; 1TK8; -.
DR PDBsum; 1TKD; -.
DR PDBsum; 1TXX; -.
DR PDBsum; 1X9M; -.
DR PDBsum; 1X9S; -.
DR PDBsum; 1X9W; -.
DR PDBsum; 1XOA; -.
DR PDBsum; 1XOB; -.
DR PDBsum; 1ZCP; -.
DR PDBsum; 1ZYQ; -.
DR PDBsum; 1ZZY; -.
DR PDBsum; 2AJQ; -.
DR PDBsum; 2BTO; -.
DR PDBsum; 2EIO; -.
DR PDBsum; 2EIQ; -.
DR PDBsum; 2EIR; -.
DR PDBsum; 2FCH; -.
DR PDBsum; 2FD3; -.
DR PDBsum; 2H6X; -.
DR PDBsum; 2H6Y; -.
DR PDBsum; 2H6Z; -.
DR PDBsum; 2H70; -.
DR PDBsum; 2H71; -.
DR PDBsum; 2H72; -.
DR PDBsum; 2H73; -.
DR PDBsum; 2H74; -.
DR PDBsum; 2H75; -.
DR PDBsum; 2H76; -.
DR PDBsum; 2O8V; -.
DR PDBsum; 2TIR; -.
DR PDBsum; 2TRX; -.
DR PDBsum; 3DYR; -.
DR PDBsum; 4HU7; -.
DR PDBsum; 4HU9; -.
DR PDBsum; 4HUA; -.
DR PDBsum; 4X43; -.
DR PDBsum; 5HR0; -.
DR PDBsum; 5HR1; -.
DR PDBsum; 5HR2; -.
DR PDBsum; 5HR3; -.
DR PDBsum; 5XOC; -.
DR PDBsum; 6GD1; -.
DR PDBsum; 6GDG; -.
DR PDBsum; 6H7J; -.
DR PDBsum; 6H7L; -.
DR PDBsum; 6H7M; -.
DR PDBsum; 6H7N; -.
DR PDBsum; 6H7O; -.
DR PDBsum; 6IBL; -.
DR PDBsum; 6LUR; -.
DR PDBsum; 6N7W; -.
DR PDBsum; 6P7E; -.
DR PDBsum; 6Y4Y; -.
DR PDBsum; 6Y4Z; -.
DR PDBsum; 6YEV; -.
DR PDBsum; 7SCD; -.
DR PDBsum; 7SCE; -.
DR AlphaFoldDB; P0AA25; -.
DR BMRB; P0AA25; -.
DR SASBDB; P0AA25; -.
DR SMR; P0AA25; -.
DR BioGRID; 4263316; 300.
DR BioGRID; 852588; 8.
DR DIP; DIP-31856N; -.
DR IntAct; P0AA25; 99.
DR MINT; P0AA25; -.
DR STRING; 511145.b3781; -.
DR CarbonylDB; P0AA25; -.
DR iPTMnet; P0AA25; -.
DR SWISS-2DPAGE; P0AA25; -.
DR jPOST; P0AA25; -.
DR PaxDb; P0AA25; -.
DR PRIDE; P0AA25; -.
DR EnsemblBacteria; AAC76786; AAC76786; b3781.
DR EnsemblBacteria; BAE77517; BAE77517; BAE77517.
DR GeneID; 64173577; -.
DR GeneID; 67514182; -.
DR GeneID; 948289; -.
DR KEGG; ecj:JW5856; -.
DR KEGG; eco:b3781; -.
DR PATRIC; fig|511145.12.peg.3896; -.
DR EchoBASE; EB1024; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_6; -.
DR InParanoid; P0AA25; -.
DR OMA; QVGVAPK; -.
DR PhylomeDB; P0AA25; -.
DR BioCyc; EcoCyc:RED-THIOREDOXIN-MON; -.
DR BioCyc; MetaCyc:RED-THIOREDOXIN-MON; -.
DR EvolutionaryTrace; P0AA25; -.
DR PRO; PR:P0AA25; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:FlyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:EcoCyc.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:FlyBase.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Electron transport; Host-virus interaction; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4883076"
FT CHAIN 2..109
FT /note="Thioredoxin 1"
FT /id="PRO_0000120096"
FT DOMAIN 2..109
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 33
FT /note="Nucleophile"
FT ACT_SITE 36
FT /note="Nucleophile"
FT SITE 27
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 34
FT /note="Contributes to redox potential value"
FT SITE 35
FT /note="Contributes to redox potential value"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT DISULFID 33..36
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:10489448"
FT CONFLICT 72..73
FT /note="GI -> IG (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> AS (in Ref. 5; AAA24696)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4HUA"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:4HUA"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:4HUA"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:4HUA"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:4HUA"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:4HUA"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:4HUA"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:4HUA"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4HUA"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:4HUA"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:4HUA"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:4HUA"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:4HUA"
SQ SEQUENCE 109 AA; 11807 MW; EF5933EA29668EE9 CRC64;
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN
IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA
