TETX_BACT4
ID TETX_BACT4 Reviewed; 388 AA.
AC Q93L51;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Flavin-dependent monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000303|PubMed:15452119};
DE AltName: Full=TetX monooxygenase {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000303|PubMed:16128584};
DE Short=TetX {ECO:0000255|HAMAP-Rule:MF_00845};
DE EC=1.14.13.231 {ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000269|PubMed:15452119};
DE AltName: Full=TetX2 {ECO:0000303|PubMed:21590745};
GN Name=tetX2 {ECO:0000303|PubMed:11472924};
OS Bacteroides thetaiotaomicron.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=818;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BT5482A; TRANSPOSON=CTnDOT;
RX PubMed=11472924; DOI=10.1128/aem.67.8.3488-3495.2001;
RA Whittle G., Hund B.D., Shoemaker N.B., Salyers A.A.;
RT "Characterization of the 13-kilobase ermF region of the Bacteroides
RT conjugative transposon CTnDOT.";
RL Appl. Environ. Microbiol. 67:3488-3495(2001).
RN [2]
RP FUNCTION IN INACTIVATING OXYTETRACYCLINE, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=BT5482A; TRANSPOSON=CTnDOT;
RX PubMed=15452119; DOI=10.1074/jbc.m409573200;
RA Yang W., Moore I.F., Koteva K.P., Bareich D.C., Hughes D.W., Wright G.D.;
RT "TetX is a flavin-dependent monooxygenase conferring resistance to
RT tetracycline antibiotics.";
RL J. Biol. Chem. 279:52346-52352(2004).
RN [3]
RP FUNCTION IN INACTIVATING TIGECYCLINE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ANTIBIOTIC RESISTANCE.
RC STRAIN=BT5482A; TRANSPOSON=CTnDOT;
RX PubMed=16128584; DOI=10.1021/bi0506066;
RA Moore I.F., Hughes D.W., Wright G.D.;
RT "Tigecycline is modified by the flavin-dependent monooxygenase TetX.";
RL Biochemistry 44:11829-11835(2005).
RN [4]
RP FUNCTION IN INACTIVATING TETRACYCLINE AND ANALOGS, AND ANTIBIOTIC
RP RESISTANCE.
RX PubMed=26097034; DOI=10.1016/j.chembiol.2015.05.017;
RA Forsberg K.J., Patel S., Wencewicz T.A., Dantas G.;
RT "The Tetracycline Destructases: A Novel Family of Tetracycline-Inactivating
RT Enzymes.";
RL Chem. Biol. 22:888-897(2015).
RN [5]
RP FUNCTION IN INACTIVATING CHLORTETRACYCLINE, AND ACTIVITY REGULATION.
RX PubMed=28481346; DOI=10.1038/nchembio.2376;
RA Park J., Gasparrini A.J., Reck M.R., Symister C.T., Elliott J.L.,
RA Vogel J.P., Wencewicz T.A., Dantas G., Tolia N.H.;
RT "Plasticity, dynamics, and inhibition of emerging tetracycline resistance
RT enzymes.";
RL Nat. Chem. Biol. 13:730-736(2017).
RN [6] {ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD WITH
RP AND WITHOUT ANTIBIOTICS, COFACTOR, SUBUNIT, AND DOMAIN.
RC STRAIN=BT5482A; TRANSPOSON=CTnDOT;
RX PubMed=21402075; DOI=10.1016/j.febslet.2011.03.012;
RA Volkers G., Palm G.J., Weiss M.S., Wright G.D., Hinrichs W.;
RT "Structural basis for a new tetracycline resistance mechanism relying on
RT the TetX monooxygenase.";
RL FEBS Lett. 585:1061-1066(2011).
RN [7] {ECO:0007744|PDB:3P9U}
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD,
RP COFACTOR, SUBUNIT, AND DOMAIN.
RX PubMed=21590745; DOI=10.1002/prot.23052;
RA Walkiewicz K., Davlieva M., Wu G., Shamoo Y.;
RT "Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline
RT degrading monooxygenase at 2.8 A resolution.";
RL Proteins 79:2335-2340(2011).
RN [8] {ECO:0007744|PDB:3V3N}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND
RP MINOCYCLINE, FUNCTION, REACTION MECHANISM, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF LYS-64; PHE-235; THR-280;
RP SER-326 AND ASN-371, AND EXPRESSION IN E.COLI.
RX PubMed=23236139; DOI=10.1073/pnas.1209335110;
RA Walkiewicz K., Benitez Cardenas A.S., Sun C., Bacorn C., Saxer G.,
RA Shamoo Y.;
RT "Small changes in enzyme function can lead to surprisingly large fitness
RT effects during adaptive evolution of antibiotic resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21408-21413(2012).
RN [9] {ECO:0007744|PDB:3V3O}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND
RP TIGECYCLINE, AND COFACTOR.
RA Walkiewicz K., Shamoo Y.;
RT "Crystal structure of TetX2 T280A: an adaptive mutant in complex with
RT tigecycline.";
RL Submitted (DEC-2011) to the PDB data bank.
RN [10] {ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 11-388 IN COMPLEX WITH FAD AND
RP WITH ANTIBIOTICS, COFACTOR, AND SUBUNIT.
RX PubMed=23999299; DOI=10.1107/s0907444913013802;
RA Volkers G., Damas J.M., Palm G.J., Panjikar S., Soares C.M., Hinrichs W.;
RT "Putative dioxygen-binding sites and recognition of tigecycline and
RT minocycline in the tetracycline-degrading monooxygenase TetX.";
RL Acta Crystallogr. D 69:1758-1767(2013).
CC -!- FUNCTION: An FAD-requiring monooxygenase active on tetracycline
CC antibiotic derivatives, which leads to their inactivation
CC (PubMed:15452119, PubMed:16128584). Hydroxylates carbon 11a of
CC oxytetracycline and tigecycline (PubMed:15452119, PubMed:26097034).
CC Acts on many tetracycline analogs (chlorotetracycline, demeclocycline,
CC doxycycline, minocycline, oxytetracyclinee), probably by
CC monooxygenization (PubMed:15452119, PubMed:16128584). Tigecycline, a
CC new generation tetracycline antibiotic, is rendered less effective
CC against E.coli by this monooxygenation, is much weaker at inhibiting
CC translation in vitro and binds Mg(2+) considerably less well
CC (PubMed:16128584, PubMed:26097034). Expression in E.coli BW25113
CC reduces its growth rate about 5%. The reaction probably proceeds by FAD
CC reduction by NADPH and, second, hydroxylation of antibiotic in a ping-
CC pong mechanism (PubMed:23236139). Degrades chlortetracycline, probably
CC by monooxygenation (PubMed:15452119, PubMed:28481346). Slowly oxidizes
CC anhydrotetracycline, the final substrate in tetracycline biosynthesis
CC (PubMed:26097034). {ECO:0000255|HAMAP-Rule:MF_00845,
CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:16128584,
CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:26097034,
CC ECO:0000269|PubMed:28481346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetracycline + H(+) + NADPH + O2 = an 11a-
CC hydroxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61444,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:144644,
CC ChEBI:CHEBI:144645; Evidence={ECO:0000255|HAMAP-Rule:MF_00845,
CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:16128584,
CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:26097034,
CC ECO:0000269|PubMed:28481346};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + tetracycline = 11a-hydroxytetracycline +
CC H2O + NADP(+); Xref=Rhea:RHEA:50004, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77932, ChEBI:CHEBI:132727;
CC EC=1.14.13.231; Evidence={ECO:0000305|PubMed:15452119,
CC ECO:0000305|PubMed:26097034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + tigecycline = 11a-hydroxytigecycline + H2O
CC + NADP(+); Xref=Rhea:RHEA:61448, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142708, ChEBI:CHEBI:142709;
CC Evidence={ECO:0000269|PubMed:16128584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + oxytetracycline = 11a-hydroxy-
CC oxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61452,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133011,
CC ChEBI:CHEBI:144646; Evidence={ECO:0000269|PubMed:15452119};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00845,
CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:21402075,
CC ECO:0000269|PubMed:21590745, ECO:0000269|PubMed:23236139,
CC ECO:0000269|PubMed:23999299, ECO:0000269|Ref.9};
CC Note=Binds 1 FAD per subunit, which helps bind the antibiotic
CC substrate. {ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745,
CC ECO:0000269|PubMed:23236139, ECO:0000269|PubMed:23999299,
CC ECO:0000269|Ref.9};
CC -!- ACTIVITY REGULATION: Anhydrotetracycline, a poor substrate, prevents
CC tetracycline degradation in vitro. {ECO:0000269|PubMed:28481346}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.9 uM for demeclocycline {ECO:0000269|PubMed:15452119};
CC KM=28.4 uM for minocycline {ECO:0000269|PubMed:15452119};
CC KM=35.0 uM for minocycline {ECO:0000269|PubMed:23236139};
CC KM=44.0 uM for tigecycline {ECO:0000269|PubMed:16128584};
CC KM=54.0 uM for tetracycline {ECO:0000269|PubMed:15452119};
CC KM=76.3 uM for oxytetracycline {ECO:0000269|PubMed:15452119};
CC KM=83.7 uM for doxycycline {ECO:0000269|PubMed:15452119};
CC KM=110 uM for chlortetracycline {ECO:0000269|PubMed:15452119};
CC KM=133 uM for NADPH {ECO:0000269|PubMed:15452119};
CC KM=75.0 uM for NADPH {ECO:0000269|PubMed:23236139};
CC Note=kcat varies from 1.3 sec(-1) for oxytetracycline to 0.12 sec(-1)
CC for minocycline. {ECO:0000269|PubMed:15452119};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:15452119};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00845,
CC ECO:0000269|PubMed:15452119, ECO:0000269|PubMed:21402075,
CC ECO:0000269|PubMed:21590745, ECO:0000269|PubMed:23236139,
CC ECO:0000269|PubMed:23999299}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00845}.
CC -!- DOMAIN: Consists of an N-terminal FAD-binding domain with a Rossman
CC fold and a C-terminal substrate-binding domain. {ECO:0000255|HAMAP-
CC Rule:MF_00845, ECO:0000269|PubMed:21402075,
CC ECO:0000269|PubMed:21590745, ECO:0000269|PubMed:23236139,
CC ECO:0000269|PubMed:23999299}.
CC -!- MISCELLANEOUS: Encoded in a conjugative transposon. Immediately
CC upstream of this gene is an N-terminally truncated tetX1 gene that is
CC inactive. {ECO:0000269|PubMed:11472924}.
CC -!- MISCELLANEOUS: Tetracycline antibiotics bind to the ribosomal acceptor
CC site (A-site), preventing binding of the aminoacyl-tRNA to the A-site.
CC The hydrophilic side of tetracycline makes many hydrogen-bonding
CC interactions with oxygen atoms of the ribosome's phosphate backbone.
CC {ECO:0000305|PubMed:16128584}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00845}.
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DR EMBL; AJ311171; CAC47932.1; -; Genomic_DNA.
DR RefSeq; WP_008651082.1; NZ_RWHY01000040.1.
DR PDB; 2XDO; X-ray; 2.09 A; A/B/C/D=11-388.
DR PDB; 2XYO; X-ray; 3.00 A; A/B/C/D=11-388.
DR PDB; 2Y6Q; X-ray; 2.37 A; A/B/C/D=11-388.
DR PDB; 2Y6R; X-ray; 3.10 A; A/B/C/D=11-388.
DR PDB; 3P9U; X-ray; 2.81 A; A/B/C/D=11-388.
DR PDB; 3V3N; X-ray; 2.70 A; A/B/C/D=11-388.
DR PDB; 3V3O; X-ray; 2.90 A; A/B/C/D=11-388.
DR PDB; 4A6N; X-ray; 2.30 A; A/B/C/D=11-388.
DR PDB; 4A99; X-ray; 2.18 A; A/B/C/D=11-388.
DR PDB; 4GUV; X-ray; 2.73 A; A/B/C/D=11-388.
DR PDBsum; 2XDO; -.
DR PDBsum; 2XYO; -.
DR PDBsum; 2Y6Q; -.
DR PDBsum; 2Y6R; -.
DR PDBsum; 3P9U; -.
DR PDBsum; 3V3N; -.
DR PDBsum; 3V3O; -.
DR PDBsum; 4A6N; -.
DR PDBsum; 4A99; -.
DR PDBsum; 4GUV; -.
DR AlphaFoldDB; Q93L51; -.
DR SMR; Q93L51; -.
DR DrugBank; DB13092; Meclocycline.
DR GeneID; 66973561; -.
DR BRENDA; 1.14.13.231; 709.
DR EvolutionaryTrace; Q93L51; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00845; TetX_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR043683; TetX_monooxygenase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; FAD; Flavoprotein;
KW Monooxygenase; NADP; Nucleotide-binding; Oxidoreductase;
KW Transposable element.
FT CHAIN 1..388
FT /note="Flavin-dependent monooxygenase"
FT /id="PRO_0000448378"
FT BINDING 26..27
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO,
FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U,
FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O,
FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99,
FT ECO:0007744|PDB:4GUV"
FT BINDING 45..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO,
FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U,
FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O,
FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99,
FT ECO:0007744|PDB:4GUV"
FT BINDING 54
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845,
FT ECO:0000305|PubMed:21402075"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845,
FT ECO:0007744|PDB:3V3O"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845,
FT ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745,
FT ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO,
FT ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R,
FT ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N,
FT ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N,
FT ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO,
FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U,
FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O,
FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99,
FT ECO:0007744|PDB:4GUV"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3N,
FT ECO:0007744|PDB:4A99"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3O,
FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00845,
FT ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745,
FT ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO,
FT ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R,
FT ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N,
FT ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N,
FT ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV"
FT BINDING 321..324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21402075,
FT ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO,
FT ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q,
FT ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U,
FT ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O,
FT ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99,
FT ECO:0007744|PDB:4GUV"
FT MUTAGEN 64
FT /note="K->R: E.coli is more resistant to minocycline (MCN),
FT no change in affinity for MCN, decreased affinity for
FT NADPH, decreased growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 235
FT /note="F->Y: E.coli is more resistant to MCN, decreased
FT affinity for MCN, slightly decrased affinity for NADPH,
FT increased growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 280
FT /note="T->A: E.coli is more resistant to MCN, 2-fold
FT increased affinity for MCN, 4-fold increase for NADPH,
FT increased growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 280
FT /note="T->S: E.coli is more resistant to MCN, slightly
FT increased affinity for MCN, decreased affinity for NADPH,
FT decreased growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 326
FT /note="S->I: E.coli is more resistant to MCN, no change in
FT affinity for MCN or NADPH, increased growth rate in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 371
FT /note="N->I: E.coli is more resistant to MCN, 2-fold
FT increased affinity for MCN, slightly increased affinity for
FT NADPH, increased growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT MUTAGEN 371
FT /note="N->T: E.coli is more resistant to MCN, increased
FT affinity for MCN, decreased affinity for NADPH, increased
FT growth rate in E.coli."
FT /evidence="ECO:0000269|PubMed:23236139"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:4A99"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:2XDO"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3V3N"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3V3N"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3V3N"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2XDO"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3P9U"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2XDO"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4A99"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2XDO"
FT HELIX 346..376
FT /evidence="ECO:0007829|PDB:2XDO"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4A99"
SQ SEQUENCE 388 AA; 43708 MW; C0F8976A7A82F394 CRC64;
MTMRIDTDKQ MNLLSDKNVA IIGGGPVGLT MAKLLQQNGI DVSVYERDND REARIFGGTL
DLHKGSGQEA MKKAGLLQTY YDLALPMGVN IADEKGNILS TKNVKPENRF DNPEINRNDL
RAILLNSLEN DTVIWDRKLV MLEPGKKKWT LTFENKPSET ADLVILANGG MSKVRKFVTD
TEVEETGTFN IQADIHQPEI NCPGFFQLCN GNRLMASHQG NLLFANPNNN GALHFGISFK
TPDEWKNQTQ VDFQNRNSVV DFLLKEFSDW DERYKELIHT TLSFVGLATR IFPLEKPWKS
KRPLPITMIG DAAHLMPPFA GQGVNSGLVD ALILSDNLAD GKFNSIEEAV KNYEQQMFIY
GKEAQEESTQ NEIEMFKPDF TFQQLLNV
