ARNA_ECOLI
ID ARNA_ECOLI Reviewed; 660 AA.
AC P77398; Q56VX0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Bifunctional polymyxin resistance protein ArnA;
DE AltName: Full=Polymyxin resistance protein PmrI;
DE Includes:
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase;
DE EC=2.1.2.13 {ECO:0000269|PubMed:15807526};
DE AltName: Full=ArnAFT;
DE AltName: Full=UDP-L-Ara4N formyltransferase;
DE Includes:
DE RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating;
DE EC=1.1.1.305 {ECO:0000269|PubMed:15491143};
DE AltName: Full=ArnADH;
DE AltName: Full=UDP-GlcUA decarboxylase;
DE AltName: Full=UDP-glucuronic acid dehydrogenase;
GN Name=arnA; Synonyms=pmrI, yfbG; OrderedLocusNames=b2255, JW2249;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION OF C-TERMINAL DOMAIN, AND
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11706007; DOI=10.1074/jbc.m109377200;
RA Breazeale S.D., Ribeiro A.A., Raetz C.R.H.;
RT "Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-
RT resistant Escherichia coli. Origin of lipid A species modified with 4-
RT amino-4-deoxy-L-arabinose.";
RL J. Biol. Chem. 277:2886-2896(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP INDUCTION BY BASR.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15569938; DOI=10.1073/pnas.0406038101;
RA Winfield M.D., Groisman E.A.;
RT "Phenotypic differences between Salmonella and Escherichia coli resulting
RT from the disparate regulation of homologous genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17162-17167(2004).
RN [6]
RP FUNCTION OF N-TERMINAL DOMAIN, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15695810; DOI=10.1074/jbc.m414265200;
RA Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.;
RT "A formyltransferase required for polymyxin resistance in Escherichia coli
RT and the modification of lipid A with 4-amino-4-deoxy-L-arabinose:
RT identification and function of UDP-4-deoxy-4-formamido-L-arabinose.";
RL J. Biol. Chem. 280:14154-14167(2005).
RN [7]
RP PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17928292; DOI=10.1074/jbc.m706172200;
RA Yan A., Guan Z., Raetz C.R.H.;
RT "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin
RT resistance in Escherichia coli.";
RL J. Biol. Chem. 282:36077-36089(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 306-660, FUNCTION, CATALYTIC
RP ACTIVITY OF C-TERMINAL DOMAIN, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15491143; DOI=10.1021/bi048551f;
RA Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
RT "Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A
RT key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and
RT polymyxin resistance.";
RL Biochemistry 43:13370-13379(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-300, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF ASN-102; HIS-104 AND ASP-140, AND REACTION
RP MECHANISM.
RX PubMed=15807526; DOI=10.1021/bi047384g;
RA Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
RT "Crystal structure and mechanism of the Escherichia coli ArnA (PmrI)
RT transformylase domain. An enzyme for lipid A modification with 4-amino-4-
RT deoxy-L-arabinose and polymyxin resistance.";
RL Biochemistry 44:5328-5338(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH UMP AND N-5-FTHF, AND
RP MUTAGENESIS OF SER-433 AND GLU-434.
RX PubMed=15809294; DOI=10.1074/jbc.m501534200;
RA Williams G.J., Breazeale S.D., Raetz C.R.H., Naismith J.H.;
RT "Structure and function of both domains of ArnA, a dual function
RT decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-
RT arabinose biosynthesis.";
RL J. Biol. Chem. 280:23000-23008(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH UDP-GLCUA AND NAD
RP ANALOG AND OF 306-660 OF MUTANTS ALA-433; GLU-619; MET-619 AND TYR-619,
RP MUTAGENESIS OF SER-433 AND ARG-619, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=15939024; DOI=10.1016/j.str.2005.03.018;
RA Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
RT "Structure and mechanism of ArnA: conformational change implies ordered
RT dehydrogenase mechanism in key enzyme for polymyxin resistance.";
RL Structure 13:929-942(2005).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the oxidative
CC decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-
CC arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-
CC amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-
CC arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A
CC and is required for resistance to polymyxin and cationic antimicrobial
CC peptides. {ECO:0000269|PubMed:11706007, ECO:0000269|PubMed:15491143,
CC ECO:0000269|PubMed:15695810, ECO:0000269|PubMed:15807526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-
CC threo-pentopyranos-4-ulose; Xref=Rhea:RHEA:24702, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58710; EC=1.1.1.305;
CC Evidence={ECO:0000269|PubMed:15491143};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24703;
CC Evidence={ECO:0000305|PubMed:15491143};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-
CC arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-
CC formamido-beta-L-arabinose; Xref=Rhea:RHEA:24706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:58708,
CC ChEBI:CHEBI:58709; EC=2.1.2.13;
CC Evidence={ECO:0000269|PubMed:15807526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24707;
CC Evidence={ECO:0000305|PubMed:15807526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.76 mM for NAD(+) {ECO:0000269|PubMed:15491143};
CC KM=0.086 mM for UDP-GlcUA {ECO:0000269|PubMed:15491143};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
CC arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from
CC UDP-alpha-D-glucuronate: step 1/3. {ECO:0000269|PubMed:17928292}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
CC arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from
CC UDP-alpha-D-glucuronate: step 3/3. {ECO:0000269|PubMed:17928292}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:17928292}.
CC -!- SUBUNIT: Homohexamer, formed by a dimer of trimers.
CC {ECO:0000269|PubMed:15809294, ECO:0000269|PubMed:15939024}.
CC -!- INTERACTION:
CC P77398; P77398: arnA; NbExp=3; IntAct=EBI-545305, EBI-545305;
CC P77398; P76092: ynbC; NbExp=2; IntAct=EBI-545305, EBI-544837;
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:15569938}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP-
CC L-Ara4N formyltransferase subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. UDP-glucuronic acid decarboxylase
CC subfamily. {ECO:0000305}.
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DR EMBL; AY057445; AAL23678.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75315.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16078.1; -; Genomic_DNA.
DR PIR; E64996; E64996.
DR RefSeq; NP_416758.1; NC_000913.3.
DR RefSeq; WP_000860273.1; NZ_LN832404.1.
DR PDB; 1U9J; X-ray; 2.40 A; A=306-660.
DR PDB; 1YRW; X-ray; 1.70 A; A=1-300.
DR PDB; 1Z73; X-ray; 2.50 A; A=306-660.
DR PDB; 1Z74; X-ray; 2.70 A; A=306-660.
DR PDB; 1Z75; X-ray; 2.40 A; A=306-660.
DR PDB; 1Z7B; X-ray; 2.31 A; A=306-660.
DR PDB; 1Z7E; X-ray; 3.00 A; A/B/C/D/E/F=1-660.
DR PDB; 2BLL; X-ray; 2.30 A; A=317-660.
DR PDB; 2BLN; X-ray; 1.20 A; A/B=1-305.
DR PDB; 4WKG; X-ray; 2.70 A; A/B/C/D/E/F=1-660.
DR PDB; 6PIH; EM; 6.60 A; A/B/C/D/E/F=1-300, G/H/I/J/K/L=317-660.
DR PDB; 6PIK; EM; 7.80 A; A/B/C/D=1-300, E/F/G/H=317-660.
DR PDBsum; 1U9J; -.
DR PDBsum; 1YRW; -.
DR PDBsum; 1Z73; -.
DR PDBsum; 1Z74; -.
DR PDBsum; 1Z75; -.
DR PDBsum; 1Z7B; -.
DR PDBsum; 1Z7E; -.
DR PDBsum; 2BLL; -.
DR PDBsum; 2BLN; -.
DR PDBsum; 4WKG; -.
DR PDBsum; 6PIH; -.
DR PDBsum; 6PIK; -.
DR AlphaFoldDB; P77398; -.
DR SMR; P77398; -.
DR BioGRID; 4260497; 265.
DR BioGRID; 851996; 2.
DR DIP; DIP-11961N; -.
DR IntAct; P77398; 15.
DR STRING; 511145.b2255; -.
DR DrugBank; DB03256; (6R)-Folinic acid.
DR DrugBank; DB03685; Uridine monophosphate.
DR PaxDb; P77398; -.
DR PRIDE; P77398; -.
DR EnsemblBacteria; AAC75315; AAC75315; b2255.
DR EnsemblBacteria; BAA16078; BAA16078; BAA16078.
DR GeneID; 947683; -.
DR KEGG; ecj:JW2249; -.
DR KEGG; eco:b2255; -.
DR PATRIC; fig|1411691.4.peg.4482; -.
DR EchoBASE; EB3844; -.
DR eggNOG; COG0223; Bacteria.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_23_1_6; -.
DR InParanoid; P77398; -.
DR OMA; VRYCVKY; -.
DR PhylomeDB; P77398; -.
DR BioCyc; EcoCyc:G7168-MON; -.
DR BioCyc; MetaCyc:G7168-MON; -.
DR BRENDA; 1.1.1.305; 2026.
DR BRENDA; 2.1.2.13; 2026.
DR SABIO-RK; P77398; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00492.
DR UniPathway; UPA00032; UER00494.
DR EvolutionaryTrace; P77398; -.
DR PRO; PR:P77398; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0099619; F:UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity; IDA:EcoCyc.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0099618; F:UDP-glucuronic acid dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:2001315; P:UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process; IMP:EcoCyc.
DR GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IDA:UniProtKB.
DR CDD; cd05257; Arna_like_SDR_e; 1.
DR HAMAP; MF_01166; ArnA; 1.
DR InterPro; IPR045869; Arna-like_SDR_e.
DR InterPro; IPR021168; Bifun_polymyxin_resist_ArnA.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR PIRSF; PIRSF036506; Bifun_polymyxin_resist_ArnA; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW Transferase.
FT CHAIN 1..660
FT /note="Bifunctional polymyxin resistance protein ArnA"
FT /id="PRO_0000083098"
FT REGION 1..304
FT /note="Formyltransferase ArnAFT"
FT REGION 314..660
FT /note="Dehydrogenase ArnADH"
FT ACT_SITE 104
FT /note="Proton donor; for formyltransferase activity"
FT ACT_SITE 434
FT /note="Proton acceptor; for decarboxylase activity"
FT ACT_SITE 619
FT /note="Proton donor; for decarboxylase activity"
FT BINDING 86..88
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT BINDING 114
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT BINDING 136..140
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT BINDING 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 368..369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 393
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 398
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 432..433
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 460
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 492
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 526..535
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 613
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT SITE 102
FT /note="Transition state stabilizer"
FT SITE 140
FT /note="Raises pKa of active site His"
FT MUTAGEN 102
FT /note="N->A: No formyltransferase activity."
FT /evidence="ECO:0000269|PubMed:15807526"
FT MUTAGEN 104
FT /note="H->A: 25-fold lower formyltransferase activity."
FT /evidence="ECO:0000269|PubMed:15807526"
FT MUTAGEN 104
FT /note="H->K: Less than 1% residual formyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:15807526"
FT MUTAGEN 140
FT /note="D->A,N: Less than 1% residual formyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:15807526"
FT MUTAGEN 433
FT /note="S->A: 40-fold lower specific activity."
FT /evidence="ECO:0000269|PubMed:15809294,
FT ECO:0000269|PubMed:15939024"
FT MUTAGEN 433
FT /note="S->T: No activity."
FT /evidence="ECO:0000269|PubMed:15809294,
FT ECO:0000269|PubMed:15939024"
FT MUTAGEN 434
FT /note="E->A: 100-fold lower specific activity."
FT /evidence="ECO:0000269|PubMed:15809294"
FT MUTAGEN 434
FT /note="E->Q: No activity."
FT /evidence="ECO:0000269|PubMed:15809294"
FT MUTAGEN 619
FT /note="R->E,Y: No activity."
FT /evidence="ECO:0000269|PubMed:15939024"
FT MUTAGEN 619
FT /note="R->M: 400-fold lower activity."
FT /evidence="ECO:0000269|PubMed:15939024"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2BLN"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:2BLN"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1Z7E"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 158..181
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2BLN"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 270..281
FT /evidence="ECO:0007829|PDB:2BLN"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:2BLN"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1Z7E"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:2BLL"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 402..409
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2BLL"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4WKG"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 462..481
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 510..521
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:2BLL"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 570..573
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 574..586
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:2BLL"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:1Z7E"
FT HELIX 624..630
FT /evidence="ECO:0007829|PDB:2BLL"
FT HELIX 638..652
FT /evidence="ECO:0007829|PDB:2BLL"
SQ SEQUENCE 660 AA; 74289 MW; A430928AB4041FA3 CRC64;
MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA ERGIPVYAPD
NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA FNLHGSLLPK YRGRAPLNWV
LVNGETETGV TLHRMVKRAD AGAIVAQLRI AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI
KHGNILEIAQ RENEATCFGR RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF
TVWSSRVHPH ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ
GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS DAISRFLNHP
HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC
VKYRKRIIFP STSEVYGMCS DKYFDEDHSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK
EGLQFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI
RDGIEALYRI IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF
RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL RTVDLTDKPS
