NAGA_ECOLI
ID NAGA_ECOLI Reviewed; 382 AA.
AC P0AF18; P15300;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:2190615};
DE Short=GlcNAc 6-P deacetylase {ECO:0000303|PubMed:9143339};
DE EC=3.5.1.25 {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048, ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
GN Name=nagA; OrderedLocusNames=b0677, JW0663;
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=2668691; DOI=10.1111/j.1365-2958.1989.tb00197.x;
RA Plumbridge J.;
RT "Sequence of the nagBACD operon in Escherichia coli K12 and pattern of
RT transcription within the nag regulon.";
RL Mol. Microbiol. 3:505-515(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2190615; DOI=10.1139/o90-017;
RA Peri K.G., Goldie H., Waygood E.B.;
RT "Cloning and characterization of the N-acetylglucosamine operon of
RT Escherichia coli.";
RL Biochem. Cell Biol. 68:123-137(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=K12;
RX PubMed=4861885; DOI=10.1042/bj1050121;
RA White R.J., Pasternak C.A.;
RT "The purification and properties of N-acetylglucosamine 6-phosphate
RT deacetylase from Escherichia coli.";
RL Biochem. J. 105:121-125(1967).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=8349539; DOI=10.1128/jb.175.16.4951-4956.1993;
RA Plumbridge J.A., Cochet O., Souza J.M., Altamirano M.M., Calcagno M.L.,
RA Badet B.;
RT "Coordinated regulation of amino sugar-synthesizing and -degrading enzymes
RT in Escherichia coli K-12.";
RL J. Bacteriol. 175:4951-4956(1993).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=9143339; DOI=10.1006/abbi.1997.9780;
RA Souza J.M., Plumbridge J.A., Calcagno M.L.;
RT "N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli:
RT purification and molecular and kinetic characterization.";
RL Arch. Biochem. Biophys. 340:338-346(1997).
RN [9]
RP CRYSTALLIZATION.
RC STRAIN=K12;
RX PubMed=10771446; DOI=10.1107/s0907444900003668;
RA Ferreira F.M., Mendoza-Hernandez G., Calcagno M.L., Minauro F.,
RA Delboni L.F., Oliva G.;
RT "Crystallization and preliminary crystallographic analysis of N-
RT acetylglucosamine 6-phosphate deacetylase from Escherichia coli.";
RL Acta Crystallogr. D 56:670-672(2000).
RN [10]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA Mori H., Ishihama A., Utsumi R.;
RT "Identification and molecular characterization of the Mg2+ stimulon of
RT Escherichia coli.";
RL J. Bacteriol. 185:3696-3702(2003).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59;
RP ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=17567047; DOI=10.1021/bi700543x;
RA Hall R.S., Xiang D.F., Xu C., Raushel F.M.;
RT "N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a
RT single divalent metal ion.";
RL Biochemistry 46:7942-7952(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=16630633; DOI=10.1016/j.jmb.2006.03.024;
RA Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R.,
RA Fischer H., Calcagno M.L., Oliva G.;
RT "Structural analysis of N-acetylglucosamine-6-phosphate deacetylase
RT apoenzyme from Escherichia coli.";
RL J. Mol. Biol. 359:308-321(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX
RP WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND
RP ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR,
RP SUBUNIT, AND ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=17567048; DOI=10.1021/bi700544c;
RA Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C.,
RA Almo S.C., Raushel F.M.;
RT "Structural diversity within the mononuclear and binuclear active sites of
RT N-acetyl-D-glucosamine-6-phosphate deacetylase.";
RL Biochemistry 46:7953-7962(2007).
CC -!- FUNCTION: Involved in the first step in the biosynthesis of amino-
CC sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-
CC phosphate and acetate. In vitro, can also hydrolyze substrate analogs
CC such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D-
CC glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D-
CC galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate.
CC {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048, ECO:0000269|PubMed:2190615,
CC ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC Note=Binds 1 divalent metal cation per subunit. The highest efficient
CC metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and
CC Ni(2+). {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:17567048};
CC -!- ACTIVITY REGULATION: Inhibited by high substrate concentration and by
CC products glucosamine 6-phosphate and acetate. Completely inactivated by
CC the treatment with 5,5'-dithio-bis(2-nitrobenzoate) or 2,2'-dithio-
CC pyridine (2-DPDS). Inhibited by 1,10-phenanthroline and EDTA.
CC {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for N-acetyl-glucosamine 6-phosphate (at 30 degrees Celsius
CC and pH 7.5) {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC KM=0.8 mM for N-acetyl-glucosamine 6-phosphate (at 37 degrees Celsius
CC and pH 8.0) {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC KM=20 mM for glucosamine 6-phosphate (at 30 degrees Celsius and pH
CC 7.5) {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC KM=20 mM for acetate (at 30 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC KM=0.08 mM for N-acetyl-D-glucosamine-6-phosphate (at 30 degrees
CC Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)
CC {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC KM=1.24 mM for N-acetyl-D-galactosamine-6-phosphate (at 30 degrees
CC Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)
CC {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC ECO:0000269|PubMed:9143339};
CC Note=kcat is 102 sec(-1) for the deacetylation of N-acetyl-D-
CC glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA catalyzes the
CC hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate substrate about
CC an order of magnitude better than does the Zn-substituted enzyme. The
CC N-trifluoroacetyl substituted substrate is hydrolyzed 26 times faster
CC than the natural substrate, but the N-formyl substrate is hydrolyzed
CC more slowly by a factor of 5. {ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17567047,
CC ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC {ECO:0000305|PubMed:2190615}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16630633,
CC ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048,
CC ECO:0000269|PubMed:9143339}.
CC -!- INDUCTION: By N-acetylglucosamine. Induced by low extracellular levels
CC of magnesium via the PhoQ/PhoP two-component regulatory system.
CC {ECO:0000269|PubMed:12813061}.
CC -!- DISRUPTION PHENOTYPE: Synthesizes high levels of glucosamine-6-
CC phosphate deaminase and over half of the amount of glucosamine-6-
CC phosphate synthase compared to wild-type. {ECO:0000269|PubMed:8349539}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
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DR EMBL; X14135; CAA32353.1; -; Genomic_DNA.
DR EMBL; AF052007; AAC09325.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73771.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35320.1; -; Genomic_DNA.
DR PIR; A37018; A37018.
DR RefSeq; NP_415203.1; NC_000913.3.
DR RefSeq; WP_000271153.1; NZ_STEB01000044.1.
DR PDB; 1YMY; X-ray; 2.60 A; A/B=1-382.
DR PDB; 1YRR; X-ray; 2.00 A; A/B=1-382.
DR PDB; 2P50; X-ray; 2.20 A; A/B/C/D=1-382.
DR PDB; 2P53; X-ray; 2.10 A; A/B=1-382.
DR PDBsum; 1YMY; -.
DR PDBsum; 1YRR; -.
DR PDBsum; 2P50; -.
DR PDBsum; 2P53; -.
DR AlphaFoldDB; P0AF18; -.
DR SMR; P0AF18; -.
DR BioGRID; 4261208; 26.
DR DIP; DIP-10297N; -.
DR IntAct; P0AF18; 5.
DR STRING; 511145.b0677; -.
DR jPOST; P0AF18; -.
DR PaxDb; P0AF18; -.
DR PRIDE; P0AF18; -.
DR EnsemblBacteria; AAC73771; AAC73771; b0677.
DR EnsemblBacteria; BAA35320; BAA35320; BAA35320.
DR GeneID; 66671053; -.
DR GeneID; 945289; -.
DR KEGG; ecj:JW0663; -.
DR KEGG; eco:b0677; -.
DR PATRIC; fig|1411691.4.peg.1601; -.
DR EchoBASE; EB0626; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_2_6; -.
DR InParanoid; P0AF18; -.
DR OMA; HAFNAMP; -.
DR PhylomeDB; P0AF18; -.
DR BioCyc; EcoCyc:NAG6PDEACET-MON; -.
DR BioCyc; MetaCyc:NAG6PDEACET-MON; -.
DR BRENDA; 3.5.1.25; 2026.
DR SABIO-RK; P0AF18; -.
DR UniPathway; UPA00629; UER00683.
DR EvolutionaryTrace; P0AF18; -.
DR PRO; PR:P0AF18; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IDA:UniProtKB.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..382
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000170915"
FT ACT_SITE 273
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 142..143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 248..251
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17567048"
FT BINDING 306..308
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17567048"
FT MUTAGEN 59
FT /note="Q->H: Large decrease in catalytic activity and
FT substrate affinity, and increase in the average amount of
FT Zn bound to the protein, suggesting that an additional
FT metal ion can bind to this mutant; when associated with H-
FT 61."
FT /evidence="ECO:0000269|PubMed:17567047,
FT ECO:0000269|PubMed:17567048"
FT MUTAGEN 61
FT /note="N->H: Large decrease in catalytic activity and
FT substrate affinity, and increase in the average amount of
FT Zn bound to the protein, suggesting that an additional
FT metal ion can bind to this mutant; when associated with H-
FT 59."
FT /evidence="ECO:0000269|PubMed:17567047"
FT MUTAGEN 131
FT /note="E->Q,A: Large reduction in the amount of the metal
FT cofactor bound to the enzyme."
FT /evidence="ECO:0000269|PubMed:17567047"
FT MUTAGEN 143
FT /note="H->N: Dramatic decrease in catalytic activity and
FT moderate decrease in substrate affinity, producing a 6000-
FT fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17567047"
FT MUTAGEN 143
FT /note="H->Q: 180-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17567047"
FT MUTAGEN 251
FT /note="H->N: 500-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17567047"
FT MUTAGEN 273
FT /note="D->N,A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17567047"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1YRR"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2P50"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2P53"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2P53"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:1YRR"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1YRR"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1YRR"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2P53"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:1YRR"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:1YRR"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1YRR"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:1YRR"
SQ SEQUENCE 382 AA; 40949 MW; A10B015ADFC98FCA CRC64;
MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI LSPGFIDVQL
NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI TTSDELMKQG VRVMREYLAK
HPNQALGLHL EGPWLNLVKK GTHNPNFVRK PDAALVDFLC ENADVITKVT LAPEMVPAEV
ISKLANAGIV VSAGHSNATL KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD
IYCGIIADGL HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV
DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG TLAAGKVANL
TAFTPDFKIT KTIVNGNEVV TQ
