FENR_ECOLI
ID FENR_ECOLI Reviewed; 248 AA.
AC P28861; P11007; Q2M8M0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000305};
DE EC=1.18.1.2 {ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:21306142, ECO:0000269|PubMed:8449868};
DE EC=1.19.1.1 {ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:9839946};
DE AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000303|PubMed:12234497};
DE AltName: Full=Ferredoxin--NADP reductase {ECO:0000303|PubMed:8449868};
DE Short=FNR {ECO:0000303|PubMed:8449868};
DE AltName: Full=Flavodoxin--NADP reductase {ECO:0000305};
DE Short=FLDR {ECO:0000303|PubMed:9839946};
DE AltName: Full=Methyl viologen resistance protein A {ECO:0000303|PubMed:2834327};
DE AltName: Full=dA1 {ECO:0000303|PubMed:8449868};
GN Name=fpr {ECO:0000303|PubMed:8449868};
GN Synonyms=mvrA {ECO:0000303|PubMed:2834327};
GN OrderedLocusNames=b3924, JW3895;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=8449868; DOI=10.1128/jb.175.6.1590-1595.1993;
RA Bianchi V., Reichard P., Eliasson R., Pontis E., Krook M., Joernvall H.,
RA Haggaard-Ljungquist E.;
RT "Escherichia coli ferredoxin NADP+ reductase: activation of E. coli
RT anaerobic ribonucleotide reduction, cloning of the gene (fpr), and
RT overexpression of the protein.";
RL J. Bacteriol. 175:1590-1595(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1400248; DOI=10.1128/jb.174.21.6981-6991.1992;
RA Truniger V., Boos W., Sweet G.;
RT "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella
RT flexneri.";
RL J. Bacteriol. 174:6981-6991(1992).
RN [6]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2834327; DOI=10.1128/jb.170.5.2136-2142.1988;
RA Morimyo M.;
RT "Isolation and characterization of methyl viologen-sensitive mutants of
RT Escherichia coli K-12.";
RL J. Bacteriol. 170:2136-2142(1988).
RN [7]
RP PROTEIN SEQUENCE OF 2-14, AND SUBCELLULAR LOCATION.
RX PubMed=7961651; DOI=10.1016/s0021-9258(18)46999-2;
RA Jenkins C.M., Waterman M.R.;
RT "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support
RT bovine cytochrome P450c17 hydroxylase activities.";
RL J. Biol. Chem. 269:27401-27408(1994).
RN [8]
RP FUNCTION.
RX PubMed=7042345;
RA Blaschkowski H.P., Neuer G., Ludwig-Festl M., Knappe J.;
RT "Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-
RT acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases
RT participating in the activation of pyruvate formate-lyase.";
RL Eur. J. Biochem. 123:563-569(1982).
RN [9]
RP FUNCTION.
RX PubMed=8267617; DOI=10.1006/bbrc.1993.2548;
RA Bianchi V., Eliasson R., Fontecave M., Mulliez E., Hoover D.M.,
RA Matthews R.G., Reichard P.;
RT "Flavodoxin is required for the activation of the anaerobic ribonucleotide
RT reductase.";
RL Biochem. Biophys. Res. Commun. 197:792-797(1993).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9839946; DOI=10.1046/j.1432-1327.1998.2570577.x;
RA McIver L., Leadbeater C., Campopiano D.J., Baxter R.L., Daff S.N.,
RA Chapman S.K., Munro A.W.;
RT "Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key
RT components of electron transfer in Escherichia coli.";
RL Eur. J. Biochem. 257:577-585(1998).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-144; ARG-174 AND
RP ARG-184.
RX PubMed=11085917; DOI=10.1042/bj3520257;
RA Leadbeater C., McIver L., Campopiano D.J., Webster S.P., Baxter R.L.,
RA Kelly S.M., Price N.C., Lysek D.A., Noble M.A., Chapman S.K., Munro A.W.;
RT "Probing the NADPH-binding site of Escherichia coli flavodoxin
RT oxidoreductase.";
RL Biochem. J. 352:257-266(2000).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12234497; DOI=10.1016/s0003-9861(02)00421-6;
RA Wan J.T., Jarrett J.T.;
RT "Electron acceptor specificity of ferredoxin (flavodoxin):NADP+
RT oxidoreductase from Escherichia coli.";
RL Arch. Biochem. Biophys. 406:116-126(2002).
RN [13] {ECO:0007744|PDB:1FDR}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT, AND
RP MUTAGENESIS OF GLN-126.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=9149148; DOI=10.1006/jmbi.1997.0957;
RA Ingelman M., Blanchi V., Eklund H.;
RT "The three-dimensional structure of flavodoxin reductase from Escherichia
RT coli at 1.7-A resolution.";
RL J. Mol. Biol. 268:147-157(1997).
RN [14] {ECO:0007744|PDB:2XNJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-247 IN COMPLEX WITH FAD AND
RP NADP, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-126.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=21306142; DOI=10.1021/bi101772a;
RA Musumeci M.A., Botti H., Buschiazzo A., Ceccarelli E.A.;
RT "Swapping FAD binding motifs between plastidic and bacterial ferredoxin-
RT NADP(H) reductases.";
RL Biochemistry 50:2111-2122(2011).
CC -!- FUNCTION: Transports electrons between flavodoxin or ferredoxin and
CC NADPH (PubMed:8449868, PubMed:9839946, PubMed:12234497,
CC PubMed:21306142). Reduces flavodoxin 1, flavodoxin 2 and ferredoxin,
CC ferredoxin being the kinetically and thermodynamically preferred
CC partner (PubMed:12234497). Required for the activation of several
CC enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide
CC reductase and cobalamin-dependent methionine synthase (PubMed:7042345,
CC PubMed:8267617). {ECO:0000269|PubMed:12234497,
CC ECO:0000269|PubMed:21306142, ECO:0000269|PubMed:7042345,
CC ECO:0000269|PubMed:8267617, ECO:0000269|PubMed:8449868,
CC ECO:0000269|PubMed:9839946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2;
CC Evidence={ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:21306142,
CC ECO:0000269|PubMed:8449868};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC Evidence={ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:9839946};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:8449868};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.85 uM for NADPH {ECO:0000269|PubMed:9839946};
CC KM=3.9 uM for NADPH {ECO:0000269|PubMed:11085917};
CC KM=2.04 mM for NADH {ECO:0000269|PubMed:11085917};
CC KM=12.0 uM for ferredoxin {ECO:0000269|PubMed:12234497};
CC KM=7.6 uM for flavodoxin 1 {ECO:0000269|PubMed:12234497};
CC KM=4.0 uM for flavodoxin 2 {ECO:0000269|PubMed:12234497};
CC KM=6.84 uM for flavodoxin {ECO:0000269|PubMed:9839946};
CC KM=17.6 uM for cytochrome c {ECO:0000269|PubMed:9839946};
CC KM=23.6 uM for potassium ferricyanide {ECO:0000269|PubMed:9839946};
CC Note=kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-
CC 1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1)
CC with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin
CC 1 as substrate. kcat is 0.0039 sec(-1) with flavodoxin 2 as substrate
CC (PubMed:12234497). {ECO:0000269|PubMed:11085917,
CC ECO:0000269|PubMed:12234497};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9149148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7961651}.
CC -!- DISRUPTION PHENOTYPE: The deletion mutant is highly sensitive to methyl
CC viologen. {ECO:0000269|PubMed:2834327}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:2834327 authors incorrectly assigned the protein to be
CC part of FPR, the C-terminal of GlpX. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Z11767; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L04757; AAA23805.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03056.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76906.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77386.1; -; Genomic_DNA.
DR EMBL; Z11767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M19644; AAA24189.1; ALT_SEQ; Genomic_DNA.
DR PIR; S40867; S40867.
DR RefSeq; NP_418359.1; NC_000913.3.
DR RefSeq; WP_000796332.1; NZ_SSZK01000014.1.
DR PDB; 1FDR; X-ray; 1.70 A; A=1-248.
DR PDB; 2XNJ; X-ray; 1.90 A; A/B=2-247.
DR PDBsum; 1FDR; -.
DR PDBsum; 2XNJ; -.
DR AlphaFoldDB; P28861; -.
DR SMR; P28861; -.
DR BioGRID; 4261115; 4.
DR IntAct; P28861; 6.
DR STRING; 511145.b3924; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR jPOST; P28861; -.
DR PaxDb; P28861; -.
DR PRIDE; P28861; -.
DR EnsemblBacteria; AAC76906; AAC76906; b3924.
DR EnsemblBacteria; BAE77386; BAE77386; BAE77386.
DR GeneID; 948414; -.
DR KEGG; ecj:JW3895; -.
DR KEGG; eco:b3924; -.
DR PATRIC; fig|1411691.4.peg.2781; -.
DR EchoBASE; EB1480; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_6; -.
DR InParanoid; P28861; -.
DR OMA; MTSEHYW; -.
DR PhylomeDB; P28861; -.
DR BioCyc; EcoCyc:FLAVONADPREDUCT-MON; -.
DR BioCyc; MetaCyc:FLAVONADPREDUCT-MON; -.
DR BRENDA; 1.18.1.2; 2026.
DR BRENDA; 1.19.1.1; 2026.
DR EvolutionaryTrace; P28861; -.
DR PRO; PR:P28861; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IDA:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0000303; P:response to superoxide; IMP:EcoCyc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoliWiki.
DR CDD; cd06195; FNR1; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7961651,
FT ECO:0000269|PubMed:8449868"
FT CHAIN 2..248
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167643"
FT DOMAIN 2..101
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 50..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0000269|PubMed:9149148, ECO:0007744|PDB:1FDR,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0000269|PubMed:9149148, ECO:0007744|PDB:1FDR,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 74..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0000269|PubMed:9149148, ECO:0007744|PDB:1FDR,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9149148,
FT ECO:0007744|PDB:1FDR"
FT BINDING 143..144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 173..174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 214..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0007744|PDB:2XNJ"
FT BINDING 247..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9149148,
FT ECO:0007744|PDB:1FDR"
FT MUTAGEN 126
FT /note="Q->R: No change in enzyme activity. Crystallized in
FT 1FDR and 2XNJ."
FT /evidence="ECO:0000269|PubMed:21306142,
FT ECO:0000269|PubMed:9149148"
FT MUTAGEN 144
FT /note="R->A: Increases Km for NADPH. 2-fold decrease in
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:11085917"
FT MUTAGEN 174
FT /note="R->A: Increases Km for NADPH. 13-fold decrease in
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:11085917"
FT MUTAGEN 184
FT /note="R->A: Increases Km for NADPH. 15-fold decrease in
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:11085917"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1FDR"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1FDR"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1FDR"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:1FDR"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2XNJ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1FDR"
SQ SEQUENCE 248 AA; 27751 MW; CBF46435A95709E4 CRC64;
MADWVTGKVT KVQNWTDALF SLTVHAPVLP FTAGQFTKLG LEIDGERVQR AYSYVNSPDN
PDLEFYLVTV PDGKLSPRLA ALKPGDEVQV VSEAAGFFVL DEVPHCETLW MLATGTAIGP
YLSILQLGKD LDRFKNLVLV HAARYAADLS YLPLMQELEK RYEGKLRIQT VVSRETAAGS
LTGRIPALIE SGELESTIGL PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG
HMTAEHYW
