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 02-SEP-2026, entry version 139. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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=N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6- CC phosphate + acetate; 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 CC N-acetyl-D-glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA CC catalyzes the hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate CC substrate about an order of magnitude better than does the CC Zn-substituted enzyme. The N-trifluoroacetyl substituted substrate is CC hydrolyzed 26 times faster than the natural substrate, but the CC N-formyl substrate is hydrolyzed more slowly by a factor of 5. CC {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_CP009789.1. 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 AlphaFoldDB; P0AF18; -. DR MDposit; P0AF18; -. DR MDRepo; P0AF18; -. DR SMR; P0AF18; -. DR BioGRID; 4261208; 31. DR DIP; DIP-10297N; -. DR FunCoup; P0AF18; 297. DR IntAct; P0AF18; 5. DR STRING; 511145.b0677; -. DR jPOST; P0AF18; -. DR PaxDb; 511145-b0677; -. DR EnsemblBacteria; AAC73771; AAC73771; b0677. DR GeneID; 75170675; -. DR GeneID; 75204968; -. DR GeneID; 945289; -. DR KEGG; ecj:JW0663; -. DR KEGG; eco:b0677; -. DR KEGG; ecoc:C3026_03365; -. 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; PCRKGAH; -. DR OrthoDB; 9776488at2; -. DR PhylomeDB; P0AF18; -. DR BioCyc; EcoCyc:NAG6PDEACET-MONOMER; -. DR BioCyc; MetaCyc:NAG6PDEACET-MONOMER; -. DR BRENDA; 3.5.1.25; 2026. DR SABIO-RK; P0AF18; -. DR UniPathway; UPA00629; UER00683. DR EvolutionaryTrace; P0AF18; -. DR PRO; PR:P0AF18; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AF18; -. DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. 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: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 FunFam; 3.20.20.140:FF:000004; N-acetylglucosamine-6-phosphate deacetylase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR00221; nagA; 1. DR NCBIfam; NF008371; PRK11170.1; 1. DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PDBsum; 1YMY; -. DR PDBsum; 1YRR; -. DR PDBsum; 2P50; -. DR PDBsum; 2P53; -. 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 FT H-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 FT H-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 FT 6000-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 //