AZOR_ECOLI
ID AZOR_ECOLI Reviewed; 201 AA.
AC P41407; P77143; Q93V21;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305};
DE EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:19666717};
DE AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000303|PubMed:16684776};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:11583992};
GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000303|PubMed:11583992};
GN Synonyms=acpD; OrderedLocusNames=b1412, JW1409;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Kitakawa M., Kasai H., Baba T., Honjo A., Isono K.;
RT "Nucleotide sequence of the replication terminus region of Escherichia
RT coli.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
RC STRAIN=K12;
RX PubMed=7899078; DOI=10.1093/nar/23.4.595;
RA Moriya H., Kasai H., Isono K.;
RT "Cloning and characterization of the hrpA gene in the terC region of
RT Escherichia coli that is highly similar to the DEAH family RNA helicase
RT genes of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 23:595-598(1995).
RN [6]
RP PROTEIN SEQUENCE OF 2-16, AND PRELIMINARY FUNCTION.
RX PubMed=2168383; DOI=10.1128/jb.172.9.5445-5449.1990;
RA Fischl A.S., Kennedy E.P.;
RT "Isolation and properties of acyl carrier protein phosphodiesterase of
RT Escherichia coli.";
RL J. Bacteriol. 172:5445-5449(1990).
RN [7]
RP PROTEIN SEQUENCE OF 2-8, COFACTOR, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11583992; DOI=10.1074/jbc.m104483200;
RA Nakanishi M., Yatome C., Ishida N., Kitade Y.;
RT "Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase.";
RL J. Biol. Chem. 276:46394-46399(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=19666717; DOI=10.1128/jb.00552-09;
RA Liu G., Zhou J., Fu Q.S., Wang J.;
RT "The Escherichia coli azoreductase AzoR is involved in resistance to thiol-
RT specific stress caused by electrophilic quinones.";
RL J. Bacteriol. 191:6394-6400(2009).
RN [9]
RP FUNCTION.
RX PubMed=23795903; DOI=10.1111/jam.12294;
RA Mercier C., Chalansonnet V., Orenga S., Gilbert C.;
RT "Characteristics of major Escherichia coli reductases involved in aerobic
RT nitro and azo reduction.";
RL J. Appl. Microbiol. 115:1012-1022(2013).
RN [10]
RP CRYSTALLIZATION.
RX PubMed=16511052; DOI=10.1107/s1744309105007918;
RA Ito K., Nakanishi M., Lee W.-C., Sasaki H., Zenno S., Saigo K., Kitade Y.,
RA Tanokura M.;
RT "Crystallization and preliminary X-ray analysis of azoR (azoreductase) from
RT Escherichia coli.";
RL Acta Crystallogr. F 61:399-402(2005).
RN [11] {ECO:0007744|PDB:1TIK}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-201.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of acyl carrier protein phosphodiesterase.";
RL Submitted (JUN-2004) to the PDB data bank.
RN [12] {ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-201 IN COMPLEXES WITH FMN, AND
RP SUBUNIT.
RX PubMed=16684776; DOI=10.1074/jbc.m513345200;
RA Ito K., Nakanishi M., Lee W.C., Sasaki H., Zenno S., Saigo K., Kitade Y.,
RA Tanokura M.;
RT "Three-dimensional structure of AzoR from Escherichia coli. An
RT oxidereductase conserved in microorganisms.";
RL J. Biol. Chem. 281:20567-20576(2006).
RN [13] {ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B, ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-201 OF OXIDIZED AND REDUCED
RP FORMS IN COMPLEXES WITH FMN AND DICOUMAROL INHIBITOR, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS
RP OF ARG-60; TYR-121 AND PHE-163.
RX PubMed=18337254; DOI=10.1074/jbc.m710070200;
RA Ito K., Nakanishi M., Lee W.C., Zhi Y., Sasaki H., Zenno S., Saigo K.,
RA Kitade Y., Tanokura M.;
RT "Expansion of substrate specificity and catalytic mechanism of azoreductase
RT by X-ray crystallography and site-directed mutagenesis.";
RL J. Biol. Chem. 283:13889-13896(2008).
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones. Can reduce several benzo-,
CC naphtho-, and anthraquinone compounds. {ECO:0000269|PubMed:19666717}.
CC -!- FUNCTION: Also exhibits azoreductase activity (PubMed:11583992,
CC PubMed:18337254). Catalyzes the reductive cleavage of the azo bond in
CC aromatic azo compounds to the corresponding amines (PubMed:11583992,
CC PubMed:18337254). Can reduce ethyl red, methyl red and p-methyl red,
CC but is not able to convert sulfonated azo dyes (PubMed:11583992,
CC PubMed:18337254, PubMed:23795903). The stoichiometry implies that 2
CC cycles of the ping-pong mechanism are required for the cleavage of the
CC azo bond (PubMed:11583992). Can also act as a nitroreductase and is
CC able to reduce nitro compounds such as 7-nitrocoumarin-3-carboxylic
CC acid (7NCCA) (PubMed:23795903). {ECO:0000269|PubMed:11583992,
CC ECO:0000269|PubMed:18337254, ECO:0000269|PubMed:23795903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+);
CC Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:19666717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65953;
CC Evidence={ECO:0000269|PubMed:19666717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) =
CC 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH;
CC Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01216, ECO:0000269|PubMed:11583992,
CC ECO:0000269|PubMed:18337254};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC Evidence={ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254,
CC ECO:0000269|PubMed:19666717};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:18337254};
CC -!- ACTIVITY REGULATION: The azo reduction activity is inhibited by
CC dicoumarol. {ECO:0000269|PubMed:11583992}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 uM for anthaquinone-2-sulfonate {ECO:0000269|PubMed:19666717};
CC KM=14.6 uM for antraquinone-2,6-disulfonate
CC {ECO:0000269|PubMed:19666717};
CC KM=87.3 uM for 2-hydroxy-1,4-naphthoquinone
CC {ECO:0000269|PubMed:19666717};
CC KM=1704 uM for 2-methyl-1,4-benzoquinone
CC {ECO:0000269|PubMed:19666717};
CC KM=17.9 uM for methyl red {ECO:0000269|PubMed:11583992};
CC KM=41.9 uM for methyl red {ECO:0000269|PubMed:18337254};
CC KM=266 uM for p-methyl red {ECO:0000269|PubMed:18337254};
CC KM=31.6 uM for NADH {ECO:0000269|PubMed:11583992};
CC KM=70.6 uM for NADH {ECO:0000269|PubMed:18337254};
CC Note=kcat is 1.1 sec(-1) with anthaquinone-2-sulfonate as substrate.
CC kcat is 2.6 sec(-1) with antraquinone-2,6-disulfonate as substrate.
CC kcat is 5.8 sec(-1) with 2-hydroxy-1,4-naphthoquinone as substrate.
CC kcat is 72.0 sec(-1) with 2-methyl-1,4-benzoquinone as substrate.
CC {ECO:0000269|PubMed:19666717};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216,
CC ECO:0000269|PubMed:11583992, ECO:0000269|PubMed:16684776,
CC ECO:0000269|PubMed:18337254}.
CC -!- INDUCTION: Expression is induced by electrophiles, including 2-
CC methylhydroquinone, catechol, menadione, and diamide.
CC {ECO:0000269|PubMed:19666717}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant displays reduced viability when
CC exposed to electrophilic quinones. {ECO:0000269|PubMed:19666717}.
CC -!- MISCELLANEOUS: NADH cannot be replaced with NADPH for both reductase
CC activities (PubMed:11583992, PubMed:19666717). Quinone compounds are
CC better substrates than the model azo substrate methyl red
CC (PubMed:19666717). AzoR probably does not contribute to dye reduction
CC in vivo (PubMed:19666717). {ECO:0000269|PubMed:11583992,
CC ECO:0000269|PubMed:19666717}.
CC -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an ACP phosphodiesterase, but ACP
CC phosphodiesterase activity was not detected in vivo or in vitro in
CC further analysis. {ECO:0000269|PubMed:11583992,
CC ECO:0000305|PubMed:2168383}.
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DR EMBL; D85081; BAA25408.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74494.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15024.1; -; Genomic_DNA.
DR EMBL; D42105; BAA07684.1; -; Genomic_DNA.
DR PIR; G64892; G64892.
DR RefSeq; NP_415930.1; NC_000913.3.
DR RefSeq; WP_000048950.1; NZ_SSZK01000021.1.
DR PDB; 1TIK; X-ray; 2.30 A; A=2-201.
DR PDB; 1V4B; X-ray; 1.80 A; A=2-201.
DR PDB; 2D5I; X-ray; 2.20 A; A=2-201.
DR PDB; 2Z98; X-ray; 1.40 A; A=2-201.
DR PDB; 2Z9B; X-ray; 1.70 A; A=2-201.
DR PDB; 2Z9C; X-ray; 2.30 A; A=2-201.
DR PDB; 2Z9D; X-ray; 2.10 A; A/B=2-201.
DR PDBsum; 1TIK; -.
DR PDBsum; 1V4B; -.
DR PDBsum; 2D5I; -.
DR PDBsum; 2Z98; -.
DR PDBsum; 2Z9B; -.
DR PDBsum; 2Z9C; -.
DR PDBsum; 2Z9D; -.
DR AlphaFoldDB; P41407; -.
DR SMR; P41407; -.
DR BioGRID; 4261518; 20.
DR STRING; 511145.b1412; -.
DR DrugBank; DB04392; Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone].
DR DrugBank; DB03247; Flavin mononucleotide.
DR jPOST; P41407; -.
DR PaxDb; P41407; -.
DR PRIDE; P41407; -.
DR EnsemblBacteria; AAC74494; AAC74494; b1412.
DR EnsemblBacteria; BAA15024; BAA15024; BAA15024.
DR GeneID; 947569; -.
DR KEGG; ecj:JW1409; -.
DR KEGG; eco:b1412; -.
DR PATRIC; fig|1411691.4.peg.859; -.
DR EchoBASE; EB2558; -.
DR eggNOG; COG1182; Bacteria.
DR HOGENOM; CLU_088964_0_0_6; -.
DR InParanoid; P41407; -.
DR OMA; AGITFKY; -.
DR PhylomeDB; P41407; -.
DR BioCyc; EcoCyc:G6731-MON; -.
DR BioCyc; MetaCyc:G6731-MON; -.
DR BRENDA; 1.7.1.17; 2026.
DR BRENDA; 1.7.1.6; 2026.
DR SABIO-RK; P41407; -.
DR EvolutionaryTrace; P41407; -.
DR PRO; PR:P41407; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050446; F:azobenzene reductase activity; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_01216; Azoreductase_type1; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR023048; NADH:quinone_OxRdtase_FMN_depd.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NAD;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11583992,
FT ECO:0000269|PubMed:2168383"
FT CHAIN 2..201
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_0000166310"
FT BINDING 10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|PubMed:16684776, ECO:0000269|PubMed:18337254,
FT ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I,
FT ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B,
FT ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D"
FT BINDING 16..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|PubMed:16684776, ECO:0000269|PubMed:18337254,
FT ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I,
FT ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B,
FT ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D"
FT BINDING 96..99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|PubMed:16684776, ECO:0000269|PubMed:18337254,
FT ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I,
FT ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B,
FT ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D"
FT BINDING 140..145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16684776,
FT ECO:0000269|PubMed:18337254, ECO:0007744|PDB:1V4B,
FT ECO:0007744|PDB:2D5I, ECO:0007744|PDB:2Z98,
FT ECO:0007744|PDB:2Z9B, ECO:0007744|PDB:2Z9C,
FT ECO:0007744|PDB:2Z9D"
FT MUTAGEN 60
FT /note="R->A: 27-fold increase in the Vmax value for p-
FT methyl red reduction."
FT /evidence="ECO:0000269|PubMed:18337254"
FT MUTAGEN 121
FT /note="Y->A: 10-fold increase in Km for NADH. Does not
FT significantly affect Km for methyl red and p-methyl red."
FT /evidence="ECO:0000269|PubMed:18337254"
FT MUTAGEN 163
FT /note="F->A: 10-fold increase in Km for NADH. Does not
FT significantly affect Km for methyl red and p-methyl red."
FT /evidence="ECO:0000269|PubMed:18337254"
FT CONFLICT 23..35
FT /note="DYFVEQWREKHSA -> IILLNNGAKSTPR (in Ref. 1; BAA25408
FT and 5; BAA07684)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2Z98"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:2Z98"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2Z98"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2Z98"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2Z9D"
FT HELIX 181..199
FT /evidence="ECO:0007829|PDB:2Z98"
SQ SEQUENCE 201 AA; 21658 MW; E28D30DC4DA42297 CRC64;
MSKVLVLKSS ILAGYSQSNQ LSDYFVEQWR EKHSADEITV RDLAANPIPV LDGELVGALR
PSDAPLTPRQ QEALALSDEL IAELKAHDVI VIAAPMYNFN ISTQLKNYFD LVARAGVTFR
YTENGPEGLV TGKKAIVITS RGGIHKDGPT DLVTPYLSTF LGFIGITDVK FVFAEGIAYG
PEMAAKAQSD AKAAIDSIVS A
