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N-acetyltransferase Eis (EC 2.3.1.-) (Aminoglycoside N-acetyltransferase) (Enhanced intracellular survival protein) (Protein-lysine N-acetyltransferase)

 EIS_MYCTU               Reviewed;         402 AA.
P9WFK7; L0TCA0; P71727; Q9RG79;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
15-FEB-2017, sequence version 2.
25-OCT-2017, entry version 29.
RecName: Full=N-acetyltransferase Eis {ECO:0000305};
EC=2.3.1.- {ECO:0000269|PubMed:19906990, ECO:0000269|PubMed:21628583, ECO:0000269|PubMed:22547814};
AltName: Full=Aminoglycoside N-acetyltransferase {ECO:0000303|PubMed:19906990, ECO:0000303|PubMed:21628583};
AltName: Full=Enhanced intracellular survival protein {ECO:0000303|PubMed:10629183, ECO:0000303|PubMed:17449476};
AltName: Full=Protein-lysine N-acetyltransferase {ECO:0000305|PubMed:22547814};
Name=eis {ECO:0000303|PubMed:10629183}; OrderedLocusNames=Rv2416c;
ORFNames=MTCY253.04;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-402, AND FUNCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10629183; DOI=10.1128/JB.182.2.377-384.2000;
Wei J., Dahl J., Moulder J.W., Roberts E.A., O'Gaora P., Young D.B.,
Friedman R.L.;
"Identification of a Mycobacterium tuberculosis gene that enhances
mycobacterial survival in macrophages.";
J. Bacteriol. 182:377-384(2000).
[3]
PROTEIN SEQUENCE OF 2-7, AND SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=11401966; DOI=10.1128/IAI.69.7.4295-4302.2001;
Dahl J.L., Wei J., Moulder J.W., Laal S., Friedman R.L.;
"Subcellular localization of the intracellular survival-enhancing Eis
protein of Mycobacterium tuberculosis.";
Infect. Immun. 69:4295-4302(2001).
[4]
FUNCTION.
STRAIN=H37Rv;
PubMed=17449476; DOI=10.1074/jbc.C600280200;
Lella R.K., Sharma C.;
"Eis (enhanced intracellular survival) protein of Mycobacterium
tuberculosis disturbs the cross regulation of T-cells.";
J. Biol. Chem. 282:18671-18675(2007).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Ra, and H37Rv;
PubMed=17259625; DOI=10.1099/mic.0.2006/002642-0;
Samuel L.P., Song C.H., Wei J., Roberts E.A., Dahl J.L.,
Barry C.E. III, Jo E.K., Friedman R.L.;
"Expression, production and release of the Eis protein by
Mycobacterium tuberculosis during infection of macrophages and its
effect on cytokine secretion.";
Microbiology 153:529-540(2007).
[6]
FUNCTION, ANTIBIOTIC RESISTANCE, ACETYLTRANSFERASE ACTIVITY ON
AMINOGLYCOSIDES, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19906990; DOI=10.1073/pnas.0907925106;
Zaunbrecher M.A., Sikes R.D. Jr., Metchock B., Shinnick T.M.,
Posey J.E.;
"Overexpression of the chromosomally encoded aminoglycoside
acetyltransferase eis confers kanamycin resistance in Mycobacterium
tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 106:20004-20009(2009).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
STRAIN=H37Rv;
PubMed=21187903; DOI=10.1371/journal.ppat.1001230;
Shin D.M., Jeon B.Y., Lee H.M., Jin H.S., Yuk J.M., Song C.H.,
Lee S.H., Lee Z.W., Cho S.N., Kim J.M., Friedman R.L., Jo E.K.;
"Mycobacterium tuberculosis eis regulates autophagy, inflammation, and
cell death through redox-dependent signaling.";
PLoS Pathog. 6:E1001230-E1001230(2010).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[9]
FUNCTION, ACETYLTRANSFERASE ACTIVITY ON CAPREOMYCIN, SUBSTRATE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=23233486; DOI=10.1093/jac/dks497;
Houghton J.L., Green K.D., Pricer R.E., Mayhoub A.S.,
Garneau-Tsodikova S.;
"Unexpected N-acetylation of capreomycin by mycobacterial Eis
enzymes.";
J. Antimicrob. Chemother. 68:800-805(2013).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH COENZYME A AND
ACETAMIDE, FUNCTION, ACETYLTRANSFERASE ACTIVITY ON AMINOGLYCOSIDES,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN,
REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF HIS-119; TYR-126;
TRP-197; ASP-292; TYR-310 AND 400-PHE--PHE-402.
STRAIN=H37Rv;
PubMed=21628583; DOI=10.1073/pnas.1105379108;
Chen W., Biswas T., Porter V.R., Tsodikov O.V., Garneau-Tsodikova S.;
"Unusual regioversatility of acetyltransferase Eis, a cause of drug
resistance in XDR-TB.";
Proc. Natl. Acad. Sci. U.S.A. 108:9804-9808(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
STRAIN=H37Rv;
PubMed=22547814; DOI=10.1073/pnas.1120251109;
Kim K.H., An D.R., Song J., Yoon J.Y., Kim H.S., Yoon H.J., Im H.N.,
Kim J., Kim do J., Lee S.J., Kim K.H., Lee H.M., Kim H.J., Jo E.K.,
Lee J.Y., Suh S.W.;
"Mycobacterium tuberculosis Eis protein initiates suppression of host
immune responses by acetylation of DUSP16/MKP-7.";
Proc. Natl. Acad. Sci. U.S.A. 109:7729-7734(2012).
[12]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF MUTANT ALA-204 IN COMPLEX
WITH COENZYME A AND TOBRAMYCIN, FUNCTION, ACETYLTRANSFERASE ACTIVITY
ON AMINOGLYCOSIDES, AND MUTAGENESIS OF CYS-204.
PubMed=24106131; DOI=10.1002/cbic.201300359;
Houghton J.L., Biswas T., Chen W., Tsodikov O.V.,
Garneau-Tsodikova S.;
"Chemical and structural insights into the regioversatility of the
aminoglycoside acetyltransferase Eis.";
ChemBioChem 14:2127-2135(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ALA-204 IN COMPLEXES
WITH COENZYME A AND ISOTHIAZOLE S,S-DIOXIDE HETEROCYCLIC INHIBITORS,
AND ENZYME REGULATION.
PubMed=27010218; DOI=10.1021/acschembio.6b00110;
Willby M.J., Green K.D., Gajadeera C.S., Hou C., Tsodikov O.V.,
Posey J.E., Garneau-Tsodikova S.;
"Potent inhibitors of acetyltransferase Eis overcome kanamycin
resistance in Mycobacterium tuberculosis.";
ACS Chem. Biol. 11:1639-1646(2016).
-!- FUNCTION: Effector that is released into the host cell and affects
host immune responses; it negatively modulates inflammation,
macrophage autophagy, and cell death through redox-dependent
signaling (PubMed:17259625, PubMed:21187903). Acts as an
acetyltransferase. Acetylates 'Lys-55' of dual-specificity protein
phosphatase 16 (DUSP16)/mitogen-activated protein kinase
phosphatase-7 (MKP-7), a JNK-specific phosphatase; this leads to
the inhibition of JNK-dependent autophagy, phagosome maturation,
and ROS (reactive oxygen species) generation for enhanced
intracellular survival of M.tuberculosis (PubMed:22547814).
Inhibits Con A-mediated T-cell proliferation in vitro
(PubMed:17449476). Treatment of T-cells with Eis inhibits ERK1/2,
JAK pathway, and subsequent production of tumor necrosis factor-
alpha (TNF-alpha) and interleukin-4 (IL-4); on the contrary, there
is increased production of interferon-gamma (IFN-gamma) and
interleukin-10 (IL-10), which indicates that immunity in response
to Eis treatment is skewed away from a protective T(H)1 response
and Eis disturbs the cross regulation of T-cells
(PubMed:17449476). When expressed in M.smegmatis, enhances
intracellular survival of the bacteria in host macrophages during
infection (PubMed:10629183). {ECO:0000269|PubMed:10629183,
ECO:0000269|PubMed:17259625, ECO:0000269|PubMed:17449476,
ECO:0000269|PubMed:21187903, ECO:0000269|PubMed:22547814}.
-!- FUNCTION: Can also acetylate multiple amine groups of many
aminoglycoside (AG) antibiotics, leading to their inactivation,
and thus contributes to drug resistance (PubMed:19906990,
PubMed:21628583, PubMed:24106131). Is also able to acetylate and
deactivate the cyclic peptide antibiotic capreomycin, but not the
other anti-tuberculous drugs isoniazid and pyrazinamide
(PubMed:23233486). Acetylates kanamycin (KAN) more efficiently
than amikacin (AMK), even though Eis seems to bind AMK with higher
affinity (PubMed:19906990). Does not acetylate and inactivate
streptomycin, apramycin and spectinomycin (PubMed:19906990,
PubMed:21628583). {ECO:0000269|PubMed:19906990,
ECO:0000269|PubMed:21628583, ECO:0000269|PubMed:23233486,
ECO:0000269|PubMed:24106131}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = [protein]-
N(6)-acetyl-L-lysine + CoA. {ECO:0000269|PubMed:22547814}.
-!- ENZYME REGULATION: Is potently inhibited by several small-molecule
that share an isothiazole S,S-dioxide heterocyclic core. Some of
these inhibitors, when used in combination with KAN against
resistant M.tuberculosis, efficiently overcome Eis-mediated KAN
resistance by restoring the antibacterial activity of KAN.
{ECO:0000269|PubMed:27010218}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=112 uM for amikacin {ECO:0000269|PubMed:19906990};
KM=75 uM for amikacin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=73 uM for amikacin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:22547814};
KM=154 uM for kanamycin {ECO:0000269|PubMed:19906990};
KM=99 uM for kanamycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=81 uM for kanamycin A (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:22547814};
KM=178 uM for neamine (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=98 uM for neomycin B (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=48 uM for netilmicin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=82 uM for paromomycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=85 uM for paromomycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:22547814};
KM=58 uM for sisomicin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=63 uM for tobramycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:21628583};
KM=71 uM for tobramycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:22547814};
KM=654 uM for capreomycin (at 25 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:23233486};
Note=kcat is 0.020 sec(-1) with amikacin as substrate. kcat is
0.039 sec(-1) with kanamycin as substrate. kcat is 0.070 sec(-1)
with neamine as substrate. kcat is 0.130 sec(-1) with neomycin B
as substrate. kcat is 0.482 sec(-1) with netilmicin as
substrate. kcat is 0.058 sec(-1) with paromomycin as substrate.
kcat is 0.270 sec(-1) with sisomicin as substrate. kcat is 0.162
sec(-1) with tobramycin as substrate (at 25 degrees Celsius and
pH 8.0) (PubMed:21628583). kcat is 0.017 sec(-1) with amikacin
as substrate. kcat is 0.032 sec(-1) with kanamycin A as
substrate. kcat is 0.032 sec(-1) with paromomycin as substrate.
kcat is 0.179 sec(-1) with tobramycin as substrate (at 25
degrees Celsius and pH 8.0) (PubMed:22547814). kcat is 1.25
sec(-1) with capreomycin as substrate (at 25 degrees Celsius and
pH 8.0) (PubMed:23233486). Catalytic efficiency is 3-fold higher
for acetylation of kanamycin than for acetylation of amikacin
(PubMed:19906990). {ECO:0000269|PubMed:19906990,
ECO:0000269|PubMed:21628583, ECO:0000269|PubMed:22547814};
-!- SUBUNIT: Homohexamer; trimer of dimers.
{ECO:0000269|PubMed:21628583, ECO:0000269|PubMed:22547814}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15929122, EBI-15929122;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11401966}. Host
cytoplasmic vesicle, host phagosome {ECO:0000269|PubMed:17259625}.
Bacterial extracellular vesicle {ECO:0000269|PubMed:17259625}.
Host extracellular space {ECO:0000269|PubMed:17259625}. Note=Eis
is present in the macrophage cytoplasm from 4 h to 96 h post-
infection. {ECO:0000269|PubMed:17259625}.
-!- DOMAIN: The Eis monomer consists of three regions that are
assembled into a heart-shaped molecule (PubMed:21628583). This
shape is formed by an unusual fusion of two general control non-
derepressible 5 (GCN5)-related N-acetyltransferase (GNAT) regions
and a C-terminal region (PubMed:21628583). The N-acetyltransferase
domain of Eis is responsible for its modulation of ROS generation
and proinflammatory responses in macrophages (PubMed:21187903).
{ECO:0000269|PubMed:21187903, ECO:0000269|PubMed:21628583}.
-!- DISRUPTION PHENOTYPE: No significant difference in terms of
intracellular survival in U-397 macrophages and in an in vivo
mouse aerosol model of infection (PubMed:17259625). A strain
lacking this gene induces more TNF-alpha but less IL-10 production
in primary human monocytes than wild-type (PubMed:17259625).
Macrophages infected with a M.tuberculosis eis-deletion mutant
display markedly increased accumulation of massive autophagic
vacuoles and formation of autophagosomes in vitro and in vivo
(PubMed:21187903). Infection of macrophages with this mutant
increases the production of tumor necrosis factor-alpha and
interleukin-6 over the levels produced by infection with wild-type
or complemented strains (PubMed:21187903). Elevated ROS generation
in macrophages infected with this mutant (for which NADPH oxidase
and mitochondria are largely responsible) render the cells highly
sensitive to autophagy activation and cytokine production; despite
considerable activation of autophagy and proinflammatory
responses, these infected macrophages undergo caspase-independent
cell death (PubMed:21187903). {ECO:0000269|PubMed:17259625,
ECO:0000269|PubMed:21187903}.
-!- MISCELLANEOUS: Increased expression of eis due to point mutations
in the promoter region of eis is responsible for resistance to the
second-line injectable drug kanamycin in a number of
M.tuberculosis clinical isolates, through acetylation of its amino
groups, which leads to inactivation of the drug.
{ECO:0000269|PubMed:19906990}.
-!- SIMILARITY: Belongs to the acetyltransferase Eis family.
{ECO:0000255|HAMAP-Rule:MF_01812}.
-!- SEQUENCE CAUTION:
Sequence=AAF03768.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL123456; CCP45207.1; -; Genomic_DNA.
EMBL; AF144099; AAF03768.1; ALT_INIT; Genomic_DNA.
PIR; C70685; C70685.
RefSeq; NP_216932.2; NC_000962.3.
RefSeq; WP_003903886.1; NC_000962.3.
PDB; 3R1K; X-ray; 1.95 A; A=1-402.
PDB; 3RYO; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-402.
PDB; 3SXO; X-ray; 2.50 A; A/B=1-402.
PDB; 3UY5; X-ray; 2.50 A; A=1-402.
PDB; 4JD6; X-ray; 3.50 A; A/B/C/D/E/F=1-402.
PDB; 5EBV; X-ray; 2.20 A; A=2-402.
PDB; 5EC4; X-ray; 2.21 A; A=2-402.
PDB; 5IV0; X-ray; 2.10 A; A=1-402.
PDB; 5TVJ; X-ray; 2.30 A; A=2-402.
PDBsum; 3R1K; -.
PDBsum; 3RYO; -.
PDBsum; 3SXO; -.
PDBsum; 3UY5; -.
PDBsum; 4JD6; -.
PDBsum; 5EBV; -.
PDBsum; 5EC4; -.
PDBsum; 5IV0; -.
PDBsum; 5TVJ; -.
ProteinModelPortal; P9WFK7; -.
SMR; P9WFK7; -.
STRING; 83332.Rv2416c; -.
PaxDb; P9WFK7; -.
EnsemblBacteria; CCP45207; CCP45207; Rv2416c.
GeneID; 885903; -.
KEGG; mtu:Rv2416c; -.
KEGG; mtv:RVBD_2416c; -.
PATRIC; fig|83332.12.peg.2706; -.
TubercuList; Rv2416c; -.
eggNOG; ENOG4105HHS; Bacteria.
eggNOG; COG4552; LUCA.
Proteomes; UP000001584; Chromosome.
GO; GO:0097691; C:bacterial extracellular vesicle; IEA:UniProtKB-SubCell.
GO; GO:0043655; C:extracellular space of host; IEA:UniProtKB-SubCell.
GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
GO; GO:0034069; F:aminoglycoside N-acetyltransferase activity; IDA:MTBBASE.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030649; P:aminoglycoside antibiotic catabolic process; IMP:MTBBASE.
GO; GO:0044119; P:growth of symbiont in host cell; IMP:MTBBASE.
GO; GO:0044121; P:growth of symbiont in host organelle; IMP:MTBBASE.
GO; GO:0052164; P:modulation by symbiont of defense-related host reactive oxygen species production; IDA:MTBBASE.
GO; GO:0052167; P:modulation by symbiont of host innate immune response; IDA:MTBBASE.
GO; GO:0052040; P:modulation by symbiont of host programmed cell death; IDA:MTBBASE.
GO; GO:0052035; P:positive regulation by symbiont of host inflammatory response; IDA:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 3.30.1050.10; -; 1.
HAMAP; MF_01812; Eis; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR025559; Eis_dom.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR022902; NAcTrfase_Eis.
InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
Pfam; PF13530; SCP2_2; 1.
SUPFAM; SSF55718; SSF55718; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Antibiotic resistance;
Complete proteome; Direct protein sequencing;
Host cytoplasmic vesicle; Reference proteome; Secreted; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11401966}.
CHAIN 2 402 N-acetyltransferase Eis.
/FTId=PRO_0000220262.
DOMAIN 3 154 N-acetyltransferase.
REGION 85 87 Acetyl-CoA binding.
{ECO:0000244|PDB:3RYO,
ECO:0000269|PubMed:22547814,
ECO:0000305|PubMed:21628583}.
REGION 93 98 Acetyl-CoA binding.
{ECO:0000244|PDB:3RYO,
ECO:0000269|PubMed:22547814,
ECO:0000305|PubMed:21628583,
ECO:0000305|PubMed:24106131,
ECO:0000305|PubMed:27010218}.
REGION 121 122 Acetyl-CoA binding.
{ECO:0000244|PDB:3RYO,
ECO:0000269|PubMed:22547814,
ECO:0000305|PubMed:21628583}.
ACT_SITE 126 126 Proton donor.
{ECO:0000305|PubMed:21628583}.
ACT_SITE 402 402 Proton acceptor; via carboxylate.
{ECO:0000305|PubMed:21628583}.
MUTAGEN 119 119 H->A: Decreases catalytic activity on AG
substrates, leads to a change in the
number of acetylated sites.
{ECO:0000269|PubMed:21628583}.
MUTAGEN 126 126 Y->A: Abolishes catalytic activity on AG
substrates.
{ECO:0000269|PubMed:21628583}.
MUTAGEN 197 197 W->A: Abolishes catalytic activity on AG
substrates.
{ECO:0000269|PubMed:21628583}.
MUTAGEN 204 204 C->A: No effect on catalytic activity on
AG substrates. Prevents artifactual CoA
adduct formation during crystallization.
{ECO:0000269|PubMed:24106131}.
MUTAGEN 292 292 D->A: Nearly abolishes catalytic activity
on AG substrates.
{ECO:0000269|PubMed:21628583}.
MUTAGEN 310 310 Y->A: Nearly abolishes catalytic activity
on AG substrates.
{ECO:0000269|PubMed:21628583}.
MUTAGEN 400 402 Missing: Nearly abolishes catalytic
activity on AG substrates.
{ECO:0000269|PubMed:21628583}.
STRAND 4 6 {ECO:0000244|PDB:3R1K}.
HELIX 10 12 {ECO:0000244|PDB:3R1K}.
HELIX 13 23 {ECO:0000244|PDB:3R1K}.
STRAND 24 26 {ECO:0000244|PDB:5EC4}.
HELIX 30 36 {ECO:0000244|PDB:3R1K}.
HELIX 37 39 {ECO:0000244|PDB:3R1K}.
STRAND 45 49 {ECO:0000244|PDB:3R1K}.
STRAND 58 71 {ECO:0000244|PDB:3R1K}.
TURN 72 74 {ECO:0000244|PDB:3R1K}.
STRAND 75 87 {ECO:0000244|PDB:3R1K}.
HELIX 89 91 {ECO:0000244|PDB:5EC4}.
STRAND 93 95 {ECO:0000244|PDB:3R1K}.
HELIX 96 110 {ECO:0000244|PDB:3R1K}.
STRAND 114 119 {ECO:0000244|PDB:3R1K}.
HELIX 127 129 {ECO:0000244|PDB:3R1K}.
STRAND 136 143 {ECO:0000244|PDB:3R1K}.
TURN 144 146 {ECO:0000244|PDB:3R1K}.
STRAND 153 155 {ECO:0000244|PDB:3R1K}.
STRAND 157 159 {ECO:0000244|PDB:3R1K}.
STRAND 164 166 {ECO:0000244|PDB:3R1K}.
HELIX 168 170 {ECO:0000244|PDB:3R1K}.
HELIX 172 185 {ECO:0000244|PDB:3R1K}.
HELIX 194 202 {ECO:0000244|PDB:3R1K}.
STRAND 215 219 {ECO:0000244|PDB:3R1K}.
STRAND 222 228 {ECO:0000244|PDB:3R1K}.
STRAND 235 245 {ECO:0000244|PDB:3R1K}.
HELIX 246 257 {ECO:0000244|PDB:3R1K}.
STRAND 263 269 {ECO:0000244|PDB:3R1K}.
HELIX 275 278 {ECO:0000244|PDB:3R1K}.
STRAND 279 281 {ECO:0000244|PDB:5EC4}.
HELIX 282 284 {ECO:0000244|PDB:3R1K}.
STRAND 285 292 {ECO:0000244|PDB:3R1K}.
STRAND 294 300 {ECO:0000244|PDB:3R1K}.
HELIX 301 307 {ECO:0000244|PDB:3R1K}.
STRAND 312 314 {ECO:0000244|PDB:3R1K}.
STRAND 317 323 {ECO:0000244|PDB:3R1K}.
TURN 324 326 {ECO:0000244|PDB:3R1K}.
STRAND 327 334 {ECO:0000244|PDB:3R1K}.
STRAND 337 342 {ECO:0000244|PDB:3R1K}.
STRAND 348 351 {ECO:0000244|PDB:3R1K}.
HELIX 353 360 {ECO:0000244|PDB:3R1K}.
STRAND 362 364 {ECO:0000244|PDB:3R1K}.
HELIX 366 371 {ECO:0000244|PDB:3R1K}.
STRAND 374 378 {ECO:0000244|PDB:3R1K}.
HELIX 380 390 {ECO:0000244|PDB:3R1K}.
SEQUENCE 402 AA; 43804 MW; EF06F75C00F05333 CRC64;
MTVTLCSPTE DDWPGMFLLA AASFTDFIGP ESATAWRTLV PTDGAVVVRD GAGPGSEVVG
MALYMDLRLT VPGEVVLPTA GLSFVAVAPT HRRRGLLRAM CAELHRRIAD SGYPVAALHA
SEGGIYGRFG YGPATTLHEL TVDRRFARFH ADAPGGGLGG SSVRLVRPTE HRGEFEAIYE
RWRQQVPGGL LRPQVLWDEL LAECKAAPGG DRESFALLHP DGYALYRVDR TDLKLARVSE
LRAVTADAHC ALWRALIGLD SMERISIITH PQDPLPHLLT DTRLARTTWR QDGLWLRIMN
VPAALEARGY AHEVGEFSTV LEVSDGGRFA LKIGDGRARC TPTDAAAEIE MDRDVLGSLY
LGAHRASTLA AANRLRTKDS QLLRRLDAAF ASDVPVQTAF EF


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