ALKB_ECOLI
ID ALKB_ECOLI Reviewed; 216 AA.
AC P05050;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase AlkB;
DE EC=1.14.11.33;
DE AltName: Full=Alkylated DNA repair protein AlkB;
DE AltName: Full=DNA oxidative demethylase AlkB;
GN Name=alkB; Synonyms=aidD; OrderedLocusNames=b2212, JW2200;
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 1-30.
RX PubMed=3536913; DOI=10.1016/s0021-9258(18)66785-7;
RA Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S., Sekiguchi M.;
RT "Structure and expression of the alkB gene of Escherichia coli related to
RT the repair of alkylated DNA.";
RL J. Biol. Chem. 261:15772-15777(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 1-53.
RC STRAIN=B;
RX PubMed=3887409; DOI=10.1073/pnas.82.9.2688;
RA Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D., Lindahl T.;
RT "Active site and complete sequence of the suicidal methyltransferase that
RT counters alkylation mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985).
RN [7]
RP CHARACTERIZATION.
RX PubMed=7928996; DOI=10.1128/jb.176.20.6255-6261.1994;
RA Chen B.J., Carroll P., Samson L.;
RT "The Escherichia coli AlkB protein protects human cells against alkylation-
RT induced toxicity.";
RL J. Bacteriol. 176:6255-6261(1994).
RN [8]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=12226668; DOI=10.1038/nature01048;
RA Falnes P.O., Johansen R.F., Seeberg E.;
RT "AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia
RT coli.";
RL Nature 419:178-182(2002).
RN [9]
RP FUNCTION.
RX PubMed=12594517; DOI=10.1038/nature01363;
RA Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F., Akbari M.,
RA Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E., Krokan H.E.;
RT "Human and bacterial oxidative demethylases repair alkylation damage in
RT both RNA and DNA.";
RL Nature 421:859-863(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-216 IN COMPLEX WITH SUBSTRATE;
RP ALPHA-KETOGLUTARATE AND IRON, FUNCTION, AND COFACTOR.
RX PubMed=16482161; DOI=10.1038/nature04561;
RA Yu B., Edstrom W.C., Benach J., Hamuro Y., Weber P.C., Gibney B.R.,
RA Hunt J.F.;
RT "Crystal structures of catalytic complexes of the oxidative DNA/RNA repair
RT enzyme AlkB.";
RL Nature 439:879-884(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 14-214 IN COMPLEX WITH DS-DNA;
RP ALPHA-KETOGLUTARATE AND METAL IONS.
RX PubMed=18432238; DOI=10.1038/nature06889;
RA Yang C.G., Yi C., Duguid E.M., Sullivan C.T., Jian X., Rice P.A., He C.;
RT "Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to
RT dsDNA.";
RL Nature 452:961-965(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 12-216 IN COMPLEXES WITH
RP TRINUCLEOTIDE SUBSTRATES; ALPHA-KETOGLUTARATE AND METAL IONS, COFACTOR, AND
RP FUNCTION.
RX PubMed=19706517; DOI=10.1073/pnas.0812938106;
RA Yu B., Hunt J.F.;
RT "Enzymological and structural studies of the mechanism of promiscuous
RT substrate recognition by the oxidative DNA repair enzyme AlkB.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14315-14320(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 12-216 IN COMPLEXES WITH REACTION
RP INTERMEDIATES; 2-OXOGLUTARIC ACID AND IRON, CATALYTIC ACTIVITY, FUNCTION,
RP AND COFACTOR.
RX PubMed=21068844; DOI=10.1038/nature09497;
RA Yi C., Jia G., Hou G., Dai Q., Zhang W., Zheng G., Jian X., Yang C.G.,
RA Cui Q., He C.;
RT "Iron-catalysed oxidation intermediates captured in a DNA repair
RT dioxygenase.";
RL Nature 468:330-333(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ALA-135 IN COMPLEX WITH
RP 2-OXOGLUTARIC ACID AND SUBSTRATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP AND MUTAGENESIS OF THR-51; TRP-69; TYR-76; ASP-135 AND ARG-161.
RX PubMed=20084272; DOI=10.1371/journal.pone.0008680;
RA Holland P.J., Hollis T.;
RT "Structural and mutational analysis of Escherichia coli AlkB provides
RT insight into substrate specificity and DNA damage searching.";
RL PLoS ONE 5:E8680-E8680(2010).
CC -!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA containing 3-
CC methylcytosine or 1-methyladenine by oxidative demethylation. Has
CC highest activity towards 3-methylcytosine. Has lower activity towards
CC alkylated DNA containing ethenoadenine, and no detectable activity
CC towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and
CC single-stranded substrates. Requires molecular oxygen, alpha-
CC ketoglutarate and iron. Provides extensive resistance to alkylating
CC agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1
CC agents). {ECO:0000269|PubMed:12226668, ECO:0000269|PubMed:12594517,
CC ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:19706517,
CC ECO:0000269|PubMed:20084272, ECO:0000269|PubMed:21068844}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a methylated nucleobase within DNA + O2 = a
CC nucleobase within DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:30299, Rhea:RHEA-COMP:12192, Rhea:RHEA-COMP:12193,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:32875,
CC ChEBI:CHEBI:64428; EC=1.14.11.33;
CC Evidence={ECO:0000269|PubMed:12226668, ECO:0000269|PubMed:20084272,
CC ECO:0000269|PubMed:21068844};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:19706517,
CC ECO:0000269|PubMed:20084272, ECO:0000269|PubMed:21068844};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805, ECO:0000269|PubMed:16482161,
CC ECO:0000269|PubMed:19706517, ECO:0000269|PubMed:20084272,
CC ECO:0000269|PubMed:21068844};
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02607; AAA23416.1; -; Genomic_DNA.
DR EMBL; U00008; AAA16409.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75272.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15995.1; -; Genomic_DNA.
DR EMBL; M10315; AAA23414.1; -; Genomic_DNA.
DR PIR; A24605; BVECKB.
DR RefSeq; NP_416716.1; NC_000913.3.
DR RefSeq; WP_000884971.1; NZ_SSZK01000030.1.
DR PDB; 2FD8; X-ray; 2.30 A; A=12-216.
DR PDB; 2FDF; X-ray; 2.10 A; A=12-216.
DR PDB; 2FDG; X-ray; 2.20 A; A=12-216.
DR PDB; 2FDH; X-ray; 2.10 A; A=12-216.
DR PDB; 2FDI; X-ray; 1.80 A; A=12-216.
DR PDB; 2FDJ; X-ray; 2.10 A; A=12-216.
DR PDB; 2FDK; X-ray; 2.30 A; A=12-216.
DR PDB; 3BI3; X-ray; 1.90 A; A=13-213.
DR PDB; 3BIE; X-ray; 1.68 A; A=13-214.
DR PDB; 3BKZ; X-ray; 1.65 A; A=14-214.
DR PDB; 3I2O; X-ray; 1.70 A; A=12-216.
DR PDB; 3I3M; X-ray; 1.50 A; A=12-216.
DR PDB; 3I3Q; X-ray; 1.40 A; A/B=12-216.
DR PDB; 3I49; X-ray; 1.60 A; A=12-216.
DR PDB; 3KHB; X-ray; 2.90 A; A/B=1-216.
DR PDB; 3KHC; X-ray; 2.20 A; A/B=1-216.
DR PDB; 3O1M; X-ray; 1.75 A; A=12-216.
DR PDB; 3O1O; X-ray; 1.92 A; A=12-216.
DR PDB; 3O1P; X-ray; 1.51 A; A=12-216.
DR PDB; 3O1R; X-ray; 1.77 A; A=12-216.
DR PDB; 3O1S; X-ray; 1.58 A; A=12-216.
DR PDB; 3O1T; X-ray; 1.48 A; A=12-216.
DR PDB; 3O1U; X-ray; 1.54 A; A=12-216.
DR PDB; 3O1V; X-ray; 1.90 A; A=12-216.
DR PDB; 3T3Y; X-ray; 2.00 A; A=12-216.
DR PDB; 3T4H; X-ray; 1.65 A; B=12-216.
DR PDB; 3T4V; X-ray; 1.73 A; A=12-216.
DR PDB; 4JHT; X-ray; 1.18 A; A=12-216.
DR PDB; 4NID; X-ray; 1.58 A; A=12-216.
DR PDB; 4NIG; X-ray; 1.52 A; A=12-216.
DR PDB; 4NIH; X-ray; 1.37 A; A=12-216.
DR PDB; 4NII; X-ray; 1.62 A; A=12-216.
DR PDB; 4RFR; X-ray; 1.50 A; B=14-216.
DR PDB; 4ZHN; X-ray; 1.33 A; A=12-216.
DR PDB; 6Y0Q; X-ray; 1.75 A; A=1-216.
DR PDB; 6YPV; X-ray; 2.10 A; A=1-216.
DR PDB; 7NRO; X-ray; 1.25 A; A=1-216.
DR PDBsum; 2FD8; -.
DR PDBsum; 2FDF; -.
DR PDBsum; 2FDG; -.
DR PDBsum; 2FDH; -.
DR PDBsum; 2FDI; -.
DR PDBsum; 2FDJ; -.
DR PDBsum; 2FDK; -.
DR PDBsum; 3BI3; -.
DR PDBsum; 3BIE; -.
DR PDBsum; 3BKZ; -.
DR PDBsum; 3I2O; -.
DR PDBsum; 3I3M; -.
DR PDBsum; 3I3Q; -.
DR PDBsum; 3I49; -.
DR PDBsum; 3KHB; -.
DR PDBsum; 3KHC; -.
DR PDBsum; 3O1M; -.
DR PDBsum; 3O1O; -.
DR PDBsum; 3O1P; -.
DR PDBsum; 3O1R; -.
DR PDBsum; 3O1S; -.
DR PDBsum; 3O1T; -.
DR PDBsum; 3O1U; -.
DR PDBsum; 3O1V; -.
DR PDBsum; 3T3Y; -.
DR PDBsum; 3T4H; -.
DR PDBsum; 3T4V; -.
DR PDBsum; 4JHT; -.
DR PDBsum; 4NID; -.
DR PDBsum; 4NIG; -.
DR PDBsum; 4NIH; -.
DR PDBsum; 4NII; -.
DR PDBsum; 4RFR; -.
DR PDBsum; 4ZHN; -.
DR PDBsum; 6Y0Q; -.
DR PDBsum; 6YPV; -.
DR PDBsum; 7NRO; -.
DR AlphaFoldDB; P05050; -.
DR SMR; P05050; -.
DR BioGRID; 4261918; 29.
DR BioGRID; 851049; 1.
DR DIP; DIP-9085N; -.
DR IntAct; P05050; 12.
DR STRING; 511145.b2212; -.
DR PaxDb; P05050; -.
DR PRIDE; P05050; -.
DR EnsemblBacteria; AAC75272; AAC75272; b2212.
DR EnsemblBacteria; BAA15995; BAA15995; BAA15995.
DR GeneID; 946708; -.
DR KEGG; ecj:JW2200; -.
DR KEGG; eco:b2212; -.
DR PATRIC; fig|1411691.4.peg.23; -.
DR EchoBASE; EB0036; -.
DR eggNOG; COG3145; Bacteria.
DR HOGENOM; CLU_039677_1_1_6; -.
DR InParanoid; P05050; -.
DR OMA; NCGPLGW; -.
DR PhylomeDB; P05050; -.
DR BioCyc; EcoCyc:EG10037-MON; -.
DR BioCyc; MetaCyc:EG10037-MON; -.
DR BRENDA; 1.14.11.33; 2026.
DR BRENDA; 1.14.11.54; 2026.
DR EvolutionaryTrace; P05050; -.
DR PRO; PR:P05050; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051213; F:dioxygenase activity; IDA:EcoliWiki.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IBA:GO_Central.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; IDA:UniProtKB.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc.
DR GO; GO:0070989; P:oxidative demethylation; IDA:UniProtKB.
DR GO; GO:0035513; P:oxidative RNA demethylation; IBA:GO_Central.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IDA:UniProtKB.
DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IDA:UniProtKB.
DR GO; GO:0072702; P:response to methyl methanesulfonate; IMP:EcoCyc.
DR GO; GO:0042245; P:RNA repair; IDA:UniProtKB.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR004574; Alkb.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR16557; PTHR16557; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR TIGRFAMs; TIGR00568; alkb; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Direct protein sequencing; DNA damage;
KW DNA repair; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..216
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB"
FT /id="PRO_0000066665"
FT DOMAIN 113..213
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482161,
FT ECO:0000269|PubMed:20084272"
FT BINDING 76..78
FT /ligand="substrate"
FT BINDING 120..122
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:16482161"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:16482161"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482161,
FT ECO:0000269|PubMed:20084272"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16482161,
FT ECO:0000269|PubMed:20084272"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:16482161"
FT BINDING 204..210
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT MUTAGEN 51
FT /note="T->A: Slightly reduced activity towards single-
FT stranded DNA containing 1-methyladenine. Reduces affinity
FT for undamaged DNA."
FT /evidence="ECO:0000269|PubMed:20084272"
FT MUTAGEN 69
FT /note="W->A: Abolishes activity towards single-stranded DNA
FT containing 1-methyladenine."
FT /evidence="ECO:0000269|PubMed:20084272"
FT MUTAGEN 76
FT /note="Y->A: Reduces affinity for damaged DNA and activity
FT towards single-stranded DNA containing 1-methyladenine."
FT /evidence="ECO:0000269|PubMed:20084272"
FT MUTAGEN 135
FT /note="D->A: Abolishes activity towards single-stranded DNA
FT containing 1-methyladenine. Alters substrate specificity,
FT so that the enzyme gains activity towards single-stranded
FT DNA containing 1-methylguanine."
FT /evidence="ECO:0000269|PubMed:20084272"
FT MUTAGEN 161
FT /note="R->A: No effect on enzyme activity. Decreases
FT affinity for damaged DNA."
FT /evidence="ECO:0000269|PubMed:20084272"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:4NID"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4JHT"
FT TURN 23..29
FT /evidence="ECO:0007829|PDB:4JHT"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 58..72
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4JHT"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4JHT"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:2FDK"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4JHT"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4JHT"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4JHT"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:4JHT"
SQ SEQUENCE 216 AA; 24076 MW; 494FE1E70EABD278 CRC64;
MLDLFADAEP WQEPLAAGAV ILRRFAFNAA EQLIRDINDV ASQSPFRQMV TPGGYTMSVA
MTNCGHLGWT THRQGYLYSP IDPQTNKPWP AMPQSFHNLC QRAATAAGYP DFQPDACLIN
RYAPGAKLSL HQDKDEPDLR APIVSVSLGL PAIFQFGGLK RNDPLKRLLL EHGDVVVWGG
ESRLFYHGIQ PLKAGFHPLT IDCRYNLTFR QAGKKE
