LPXC_ECOLI
ID LPXC_ECOLI Reviewed; 305 AA.
AC P0A725; P07652;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000303|PubMed:8530464};
DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000303|PubMed:8530464, ECO:0000303|Ref.7};
DE EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:11148046, ECO:0000269|PubMed:15705580, ECO:0000269|PubMed:8530464, ECO:0000269|PubMed:8824222};
DE AltName: Full=Protein EnvA {ECO:0000305};
DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000303|PubMed:8824222};
GN Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000303|PubMed:8530464};
GN Synonyms=asmB {ECO:0000303|PubMed:8752330},
GN envA {ECO:0000303|PubMed:3000876}; OrderedLocusNames=b0096, JW0094;
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;
RX PubMed=2824434; DOI=10.1128/jb.169.12.5408-5415.1987;
RA Beall B., Lutkenhaus J.;
RT "Sequence analysis, transcriptional organization, and insertional
RT mutagenesis of the envA gene of Escherichia coli.";
RL J. Bacteriol. 169:5408-5415(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 1-82.
RC STRAIN=K12;
RX PubMed=3000876; DOI=10.1016/0378-1119(85)90179-9;
RA Yi Q.-M., Lutkenhaus J.;
RT "The nucleotide sequence of the essential cell-division gene ftsZ of
RT Escherichia coli.";
RL Gene 36:241-247(1985).
RN [6]
RP PROTEIN SEQUENCE OF 1-19, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8530464; DOI=10.1074/jbc.270.51.30384;
RA Young K., Silver L.L., Bramhill D., Cameron P., Eveland S.S., Raetz C.R.,
RA Hyland S.A., Anderson M.S.;
RT "The envA permeability/cell division gene of Escherichia coli encodes the
RT second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-
RT acetylglucosamine deacetylase.";
RL J. Biol. Chem. 270:30384-30391(1995).
RN [7]
RP FUNCTION.
RA Young K., Silver L.L., Bramhill D., Caceres C.A., Stachula S.A.,
RA Shelly S.E., Raetz C.R.H., Anderson M.S.;
RT "The second step of lipid A biosynthesis, UDP-3-O-acyl-GlcNAc deacetylase
RT is encoded by the pleotropic permeability/cell division gene envA of
RT E.coli.";
RL FASEB J. 7:1268-1268(1993).
RN [8]
RP VARIANTS.
RX PubMed=8752330; DOI=10.1128/jb.178.17.5138-5143.1996;
RA Kloser A.W., Laird M.W., Misra R.;
RT "asmB, a suppressor locus for assembly-defective OmpF mutants of
RT Escherichia coli, is allelic to envA (lpxC).";
RL J. Bacteriol. 178:5138-5143(1996).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=8824222; DOI=10.1074/jbc.271.42.25898;
RA Sorensen P.G., Lutkenhaus J., Young K., Eveland S.S., Anderson M.S.,
RA Raetz C.R.;
RT "Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine
RT deacetylase in Escherichia coli. The second enzymatic step of lipid a
RT biosynthesis.";
RL J. Biol. Chem. 271:25898-25905(1996).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10026271; DOI=10.1021/bi982339s;
RA Jackman J.E., Raetz C.R., Fierke C.A.;
RT "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of
RT Escherichia coli is a zinc metalloenzyme.";
RL Biochemistry 38:1902-1911(1999).
RN [11]
RP DEGRADATION BY FTSH PROTEASE, AND ACTIVITY REGULATION.
RC STRAIN=K12 / W3110, and W2252;
RX PubMed=10048027; DOI=10.1046/j.1365-2958.1999.01221.x;
RA Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H.,
RA Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T.,
RA Matsuzawa H.;
RT "Balanced biosynthesis of major membrane components through regulated
RT degradation of the committed enzyme of lipid A biosynthesis by the AAA
RT protease FtsH (HflB) in Escherichia coli.";
RL Mol. Microbiol. 31:833-844(1999).
RN [12]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-19; GLU-78; HIS-79; HIS-238;
RP ASP-242; ASP-246 AND HIS-265.
RX PubMed=11148046; DOI=10.1021/bi001872g;
RA Jackman J.E., Raetz C.R., Fierke C.A.;
RT "Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-
RT N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding
RT site.";
RL Biochemistry 40:514-523(2001).
RN [13]
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=15705580; DOI=10.1074/jbc.m413560200;
RA Hernick M., Gennadios H.A., Whittington D.A., Rusche K.M.,
RA Christianson D.W., Fierke C.A.;
RT "UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions
RT through a general acid-base catalyst pair mechanism.";
RL J. Biol. Chem. 280:16969-16978(2005).
RN [14]
RP DEGRADATION BY FTSH PROTEASE, ACTIVITY REGULATION, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=16420369; DOI=10.1111/j.1365-2958.2005.04994.x;
RA Fuehrer F., Langklotz S., Narberhaus F.;
RT "The C-terminal end of LpxC is required for degradation by the FtsH
RT protease.";
RL Mol. Microbiol. 59:1025-1036(2006).
RN [15]
RP DRUG TARGET.
RX PubMed=18289052; DOI=10.2174/138920108783497668;
RA Barb A.W., Zhou P.;
RT "Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase
RT of bacterial lipid A synthesis.";
RL Curr. Pharm. Biotechnol. 9:9-15(2008).
RN [16]
RP COFACTOR, AND MUTAGENESIS OF CYS-63.
RX PubMed=20136146; DOI=10.1021/bi902066t;
RA Hernick M., Gattis S.G., Penner-Hahn J.E., Fierke C.A.;
RT "Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-
RT acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with
RT altered ligand affinity.";
RL Biochemistry 49:2246-2255(2010).
RN [17]
RP COFACTOR.
RX PubMed=20709752; DOI=10.1074/jbc.m110.147173;
RA Gattis S.G., Hernick M., Fierke C.A.;
RT "Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-
RT acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II)
RT depending on cellular conditions.";
RL J. Biol. Chem. 285:33788-33796(2010).
RN [18]
RP DRUG TARGET.
RX PubMed=20019290; DOI=10.1177/1087057109355319;
RA Langsdorf E.F., Malikzay A., Lamarr W.A., Daubaras D., Kravec C., Zhang R.,
RA Hart R., Monsma F., Black T., Ozbal C.C., Miesel L., Lunn C.A.;
RT "Screening for antibacterial inhibitors of the UDP-3-O-(R-3-
RT hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) using a high-
RT throughput mass spectrometry assay.";
RL J. Biomol. Screen. 15:52-61(2010).
RN [19]
RP DEGRADATION BY FTSH PROTEASE, AND ACTIVITY REGULATION.
RX PubMed=21193611; DOI=10.1128/jb.01043-10;
RA Langklotz S., Schaekermann M., Narberhaus F.;
RT "Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of
RT LpxC is conserved in enterobacteria but not in all gram-negative
RT bacteria.";
RL J. Bacteriol. 193:1090-1097(2011).
RN [20]
RP DEGRADATION BY FTSH PROTEASE, AND ACTIVITY REGULATION.
RX PubMed=23417489; DOI=10.1128/jb.02134-12;
RA Schaekermann M., Langklotz S., Narberhaus F.;
RT "FtsH-mediated coordination of lipopolysaccharide biosynthesis in
RT Escherichia coli correlates with the growth rate and the alarmone
RT (p)ppGpp.";
RL J. Bacteriol. 195:1912-1919(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH
RP UDP-(3-O-(R-HYDROXYMYRISTOYL))-GLUCOSAMINE AND ZINC, AND ACTIVE SITE.
RX PubMed=24108127; DOI=10.1074/jbc.m113.513028;
RA Clayton G.M., Klein D.J., Rickert K.W., Patel S.B., Kornienko M.,
RA Zugay-Murphy J., Reid J.C., Tummala S., Sharma S., Singh S.B., Miesel L.,
RA Lumb K.J., Soisson S.M.;
RT "Structure of the bacterial deacetylase LpxC bound to the nucleotide
RT reaction product reveals mechanisms of oxyanion stabilization and proton
RT transfer.";
RL J. Biol. Chem. 288:34073-34080(2013).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITORS AND ZINC.
RX PubMed=24117400; DOI=10.1021/cb400067g;
RA Lee C.J., Liang X., Gopalaswamy R., Najeeb J., Ark E.D., Toone E.J.,
RA Zhou P.;
RT "Structural basis of the promiscuous inhibitor susceptibility of
RT Escherichia coli LpxC.";
RL ACS Chem. Biol. 9:237-246(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-
CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the
CC committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:8530464,
CC ECO:0000269|PubMed:8824222, ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine +
CC H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate;
CC Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388,
CC ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:11148046,
CC ECO:0000269|PubMed:15705580, ECO:0000269|PubMed:8530464,
CC ECO:0000269|PubMed:8824222};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388,
CC ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:20709752};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20136146, ECO:0000269|PubMed:20709752};
CC Note=Can use either Fe(2+) or Zn(2+). The metal cofactor can switch
CC between Fe(2+) and Zn(2+) in response to metal availability. Metal
CC switching may be important for regulating the LpxC activity upon
CC changes in environmental conditions. Has a significantly higher
CC affinity for Zn(2+), but exhibits higher activity with Fe(2+)
CC (PubMed:20136146, PubMed:20709752). Can also use Co(2+), Ni(2+) and, to
CC a lesser extent, Mn(2+) (PubMed:10026271).
CC {ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:20136146,
CC ECO:0000269|PubMed:20709752};
CC -!- ACTIVITY REGULATION: Regulation occurs at the protein level, via
CC degradation of LpxC by the FtsH protease (PubMed:10048027,
CC PubMed:16420369, PubMed:21193611, PubMed:23417489). Degradation is
CC growth rate-dependent. LpxC is degraded rapidly during slow growth,
CC probably to avoid toxic overproduction of lipopolysaccharides, but is
CC highly stable under optimal growth conditions (PubMed:23417489).
CC Increased amounts of LpxC are made under conditions that reduce the
CC lipid A content of cells (PubMed:8824222). Inhibited by metal chelators
CC such as EDTA and dipicolinic acid (DPA) and by high concentrations of
CC Zn(2+) (PubMed:10026271). {ECO:0000269|PubMed:10026271,
CC ECO:0000269|PubMed:10048027, ECO:0000269|PubMed:16420369,
CC ECO:0000269|PubMed:21193611, ECO:0000269|PubMed:23417489,
CC ECO:0000269|PubMed:8824222}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 30 degrees
CC Celsius) {ECO:0000269|PubMed:10026271};
CC KM=0.6 uM for UDP-3-O-myristoyl-N-acetylglucosamine (at 1 degree
CC Celsius) {ECO:0000269|PubMed:10026271};
CC Note=kcat is 3.3 sec(-1) at 30 degrees Celsius. kcat is 0.09 sec(-1)
CC at 1 degree Celsius. {ECO:0000269|PubMed:10026271};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00388,
CC ECO:0000269|PubMed:8530464}.
CC -!- DOMAIN: The N-terminus is required for deacetylase activity. The C-
CC terminus contains a signal sequence necessary for FtsH-dependent
CC degradation. {ECO:0000269|PubMed:16420369}.
CC -!- PTM: Degraded by FtsH. {ECO:0000269|PubMed:10048027,
CC ECO:0000269|PubMed:16420369, ECO:0000269|PubMed:21193611,
CC ECO:0000269|PubMed:23417489}.
CC -!- MISCELLANEOUS: Due to its important role in lipid A synthesis, LpxC is
CC an attractive target for the development of new antibacterial agents to
CC treat Gram-negative infections. Many potent LpxC inhibitors with a
CC variety of chemical scaffolds and distinct antibiotic profiles have
CC been discovered. {ECO:0000269|PubMed:18289052,
CC ECO:0000269|PubMed:20019290, ECO:0000269|PubMed:24117400}.
CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP-
CC Rule:MF_00388}.
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DR EMBL; M19211; AAA83849.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38873.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73207.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96664.1; -; Genomic_DNA.
DR PIR; A28381; BVECEA.
DR RefSeq; NP_414638.1; NC_000913.3.
DR RefSeq; WP_000595482.1; NZ_STEB01000010.1.
DR PDB; 4IS9; X-ray; 2.13 A; A/B=1-300.
DR PDB; 4ISA; X-ray; 1.80 A; A=1-300.
DR PDB; 4MDT; X-ray; 2.59 A; A/B/C/D=1-305.
DR PDB; 4MQY; X-ray; 2.00 A; A=1-305.
DR PDBsum; 4IS9; -.
DR PDBsum; 4ISA; -.
DR PDBsum; 4MDT; -.
DR PDBsum; 4MQY; -.
DR AlphaFoldDB; P0A725; -.
DR SMR; P0A725; -.
DR BioGRID; 4261858; 381.
DR BioGRID; 849217; 2.
DR DIP; DIP-48045N; -.
DR IntAct; P0A725; 5.
DR STRING; 511145.b0096; -.
DR BindingDB; P0A725; -.
DR ChEMBL; CHEMBL5244; -.
DR SwissLipids; SLP:000001888; -.
DR jPOST; P0A725; -.
DR PaxDb; P0A725; -.
DR PRIDE; P0A725; -.
DR EnsemblBacteria; AAC73207; AAC73207; b0096.
DR EnsemblBacteria; BAB96664; BAB96664; BAB96664.
DR GeneID; 67416169; -.
DR GeneID; 944816; -.
DR KEGG; ecj:JW0094; -.
DR KEGG; eco:b0096; -.
DR PATRIC; fig|1411691.4.peg.2184; -.
DR EchoBASE; EB0261; -.
DR eggNOG; COG0774; Bacteria.
DR HOGENOM; CLU_046528_1_0_6; -.
DR InParanoid; P0A725; -.
DR OMA; IVFYRSD; -.
DR PhylomeDB; P0A725; -.
DR BioCyc; EcoCyc:UDPACYLGLCNACDEACETYL-MON; -.
DR BioCyc; MetaCyc:UDPACYLGLCNACDEACETYL-MON; -.
DR BRENDA; 3.5.1.108; 2026.
DR SABIO-RK; P0A725; -.
DR UniPathway; UPA00359; UER00478.
DR PRO; PR:P0A725; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0019213; F:deacetylase activity; IDA:EcoliWiki.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IDA:EcoCyc.
DR GO; GO:0103117; F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoliWiki.
DR Gene3D; 3.30.1700.10; -; 1.
DR Gene3D; 3.30.230.20; -; 1.
DR HAMAP; MF_00388; LpxC; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR004463; UDP-acyl_GlcNac_deAcase.
DR InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C.
DR InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N.
DR PANTHER; PTHR33694; PTHR33694; 1.
DR Pfam; PF03331; LpxC; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR TIGRFAMs; TIGR00325; lpxC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Iron;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..305
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT /id="PRO_0000191929"
FT ACT_SITE 265
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388,
FT ECO:0000305|PubMed:15705580, ECO:0000305|PubMed:24108127"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388,
FT ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388,
FT ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388,
FT ECO:0000269|PubMed:24108127, ECO:0000269|PubMed:24117400"
FT VARIANT 50
FT /note="F -> S (in ASMB2/3; reduced activity)"
FT /evidence="ECO:0000305|PubMed:8752330"
FT VARIANT 210
FT /note="G -> S (in ASMB1; reduced activity)"
FT /evidence="ECO:0000305|PubMed:8752330"
FT MUTAGEN 19
FT /note="H->A: 1400-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 19
FT /note="H->Q: 90-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 19
FT /note="H->Y: 200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 63
FT /note="C->A: Reduces level of inhibition by metal ions."
FT /evidence="ECO:0000269|PubMed:20136146"
FT MUTAGEN 78
FT /note="E->A: 700-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 78
FT /note="E->Q: 3000-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 79
FT /note="H->A: 2300-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 79
FT /note="H->Q: 1200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 238
FT /note="H->A: 1100-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 242
FT /note="D->A: 10-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 242
FT /note="D->Q: 2300-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 246
FT /note="D->A: 1800-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 265
FT /note="H->A: 3800-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT MUTAGEN 265
FT /note="H->Q: 5600-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:11148046"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4MQY"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:4MQY"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:4MQY"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4MQY"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4MQY"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4MQY"
SQ SEQUENCE 305 AA; 33956 MW; CA439A00813463AB CRC64;
MIKQRTLKRI VQATGVGLHT GKKVTLTLRP APANTGVIYR RTDLNPPVDF PADAKSVRDT
MLCTCLVNEH DVRISTVEHL NAALAGLGID NIVIEVNAPE IPIMDGSAAP FVYLLLDAGI
DELNCAKKFV RIKETVRVED GDKWAEFKPY NGFSLDFTID FNHPAIDSSN QRYAMNFSAD
AFMRQISRAR TFGFMRDIEY LQSRGLCLGG SFDCAIVVDD YRVLNEDGLR FEDEFVRHKM
LDAIGDLFMC GHNIIGAFTA YKSGHALNNK LLQAVLAKQE AWEYVTFQDD AELPLAFKAP
SAVLA
