ID IMDH_ECOLI Reviewed; 488 AA. AC P0ADG7; P06981; P76574; P78202; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 24-JAN-2024, entry version 140. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964}; DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964}; GN Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; Synonyms=guaR; GN OrderedLocusNames=b2508, JW5401; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=2860637; DOI=10.1093/nar/13.4.1303; RA Tiedeman A.A., Smith J.M.; RT "Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of RT Escherichia coli K12."; RL Nucleic Acids Res. 13:1303-1316(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of RT its sequence features."; RL DNA Res. 4:91-113(1997). 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 1-96. RX PubMed=2998937; DOI=10.1016/0378-1119(85)90068-x; RA Thomas M.S., Drabble W.T.; RT "Nucleotide sequence and organisation of the gua promoter region of RT Escherichia coli."; RL Gene 36:45-53(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90. RX PubMed=1736096; DOI=10.1007/bf00279799; RA Tesfa-Selase F., Drabble W.T.; RT "Regulation of the gua operon of Escherichia coli by the DnaA protein."; RL Mol. Gen. Genet. 231:256-264(1992). RN [7] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP PARTIAL PROTEIN SEQUENCE OF 1-11. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.; RL Submitted (FEB-1996) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 1-5. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9629924; DOI=10.1002/elps.1150190539; RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.; RT "Extraction of membrane proteins by differential solubilization for RT separation using two-dimensional gel electrophoresis."; RL Electrophoresis 19:837-844(1998). RN [10] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726; RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., RA Hochstrasser D.F.; RT "Protein identification with N and C-terminal sequence tags in proteome RT projects."; RL J. Mol. Biol. 278:599-608(1998). RN [11] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVITY REGULATION, AND RP MUTAGENESIS OF ASP-13; ASP-50; GLU-54; ASP-138; ASP-200; ASP-243; ASP-248; RP ASP-338; GLU-369; GLU-373 AND GLU-469. RC STRAIN=K12; RX PubMed=9341229; DOI=10.1021/bi9714161; RA Kerr K.M., Hedstrom L.; RT "The roles of conserved carboxylate residues in IMP dehydrogenase and RT identification of a transition state analog."; RL Biochemistry 36:13365-13373(1997). RN [12] RP DOMAIN CBS. RC STRAIN=K12 / BW25113; RX PubMed=18312263; DOI=10.1111/j.1365-2958.2008.06153.x; RA Pimkin M., Markham G.D.; RT "The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates RT purine nucleotide turnover."; RL Mol. Microbiol. 68:342-359(2008). RN [13] RP DOMAIN CBS. RC STRAIN=K12 / BW25113; RX PubMed=19153081; DOI=10.1074/jbc.m808541200; RA Pimkin M., Pimkina J., Markham G.D.; RT "A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate RT nucleotide biosynthesis."; RL J. Biol. Chem. 284:7960-7969(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-428, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to CC xanthosine 5'-phosphate (XMP), the first committed and rate-limiting CC step in the de novo synthesis of guanine nucleotides, and therefore CC plays an important role in the regulation of cell growth. CC {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:9341229}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; CC EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01964}; CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme conformation by CC binding to the same site as the amobile flap. In contrast, mizoribine CC monophosphate (MZP) is a competitive inhibitor that induces the closed CC conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor CC inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of CC bacterial IMPDH. IMP dehydrogenase subunit of E.coli contains a CC cysteine at the IMP binding site and is inhibited in a simple CC competitive manner by GMP. It does not exhibit allosteric properties as CC does IMP dehydrogenase from B.subtilis or S.typhimurium. CC {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:9341229}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=61 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:9341229}; CC KM=2000 uM for NAD(+) {ECO:0000269|PubMed:9341229}; CC KM=2.8 mM for K(+) {ECO:0000269|PubMed:9341229}; CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964, CC ECO:0000269|PubMed:9341229}. CC -!- DOMAIN: The CBS domain of IMPDH is a negative trans-regulator of CC adenylate nucleotide synthesis, and this role is independent of the CC catalytic function of IMPDH in the de novo GMP biosynthesis. Deletion CC of the CBS domain derepresses the synthesis of AMP from IMP. CC {ECO:0000269|PubMed:18312263, ECO:0000269|PubMed:19153081}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP- CC Rule:MF_01964}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA26133.1; Type=Erroneous initiation; Evidence={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; X02209; CAA26133.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC75561.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16395.2; -; Genomic_DNA. DR EMBL; M10101; AAB18618.1; -; Genomic_DNA. DR PIR; C65027; DEECIP. DR RefSeq; NP_417003.1; NC_000913.3. DR RefSeq; WP_001299507.1; NZ_STEB01000011.1. DR PDB; 7QBJ; X-ray; 2.27 A; A/B/C/D=5-91, A/B/C/D=205-488. DR PDB; 7QDX; X-ray; 2.90 A; A/B=5-91, A/B=205-488. DR PDB; 7QEM; X-ray; 3.09 A; A/B/C/D=1-91, A/B/C/D=205-488. DR PDBsum; 7QBJ; -. DR PDBsum; 7QDX; -. DR PDBsum; 7QEM; -. DR AlphaFoldDB; P0ADG7; -. DR SMR; P0ADG7; -. DR BioGRID; 4263221; 88. DR BioGRID; 851324; 1. DR DIP; DIP-36207N; -. DR IntAct; P0ADG7; 1. DR STRING; 511145.b2508; -. DR BindingDB; P0ADG7; -. DR ChEMBL; CHEMBL3630; -. DR iPTMnet; P0ADG7; -. DR jPOST; P0ADG7; -. DR PaxDb; 511145-b2508; -. DR EnsemblBacteria; AAC75561; AAC75561; b2508. DR GeneID; 83579945; -. DR GeneID; 946985; -. DR KEGG; ecj:JW5401; -. DR KEGG; eco:b2508; -. DR PATRIC; fig|1411691.4.peg.4229; -. DR EchoBASE; EB0416; -. DR eggNOG; COG0516; Bacteria. DR eggNOG; COG0517; Bacteria. DR HOGENOM; CLU_022552_2_2_6; -. DR InParanoid; P0ADG7; -. DR OMA; MGYCGAK; -. DR OrthoDB; 9805398at2; -. DR PhylomeDB; P0ADG7; -. DR BioCyc; EcoCyc:IMP-DEHYDROG-MONOMER; -. DR BioCyc; MetaCyc:IMP-DEHYDROG-MONOMER; -. DR SABIO-RK; P0ADG7; -. DR UniPathway; UPA00601; UER00295. DR PRO; PR:P0ADG7; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc. DR GO; GO:1990829; F:C-rich single-stranded DNA binding; IDA:EcoCyc. DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0003938; F:IMP dehydrogenase activity; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc. DR GO; GO:0006177; P:GMP biosynthetic process; IMP:EcoCyc. DR GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central. DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc. DR GO; GO:0009411; P:response to UV; IMP:EcoCyc. DR CDD; cd04601; CBS_pair_IMPDH; 1. DR CDD; cd00381; IMPDH; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR046342; CBS_dom_sf. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR NCBIfam; TIGR01302; IMP_dehydrog; 1. DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01240; IMPDH; 1. DR SUPFAM; SSF54631; CBS-domain pair; 1. DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. DR SWISS-2DPAGE; P0ADG7; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; CBS domain; Direct protein sequencing; KW GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; Potassium; KW Purine biosynthesis; Reference proteome; Repeat. FT CHAIN 1..488 FT /note="Inosine-5'-monophosphate dehydrogenase" FT /id="PRO_0000093695" FT DOMAIN 93..149 FT /note="CBS 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT DOMAIN 153..214 FT /note="CBS 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT ACT_SITE 305 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT ACT_SITE 401 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 248..250 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 248 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 298..300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 300 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 302 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 303 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 305 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 338..340 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 361..362 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 385..389 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 415 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 469 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 470 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 471 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT MOD_RES 267 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 428 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MUTAGEN 13 FT /note="D->A: Causes a 38-fold increase in the value of Km FT for K(+). No change is observed in the value of Km for FT IMP." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 50 FT /note="D->A: Causes a 17-fold increase in the value of Km FT for K(+)." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 54 FT /note="E->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 138 FT /note="D->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 200 FT /note="D->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 243 FT /note="D->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 248 FT /note="D->A: Causes a 130-fold decrease in the value of FT kcat." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 338 FT /note="D->A: Decreases the value of kcat by 600-fold. FT Increases the value of Km for IMP by 12-fold." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 369 FT /note="E->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 373 FT /note="E->A: No effect." FT /evidence="ECO:0000269|PubMed:9341229" FT MUTAGEN 469 FT /note="E->A: Increases the value of Km for K(+) by FT 17-fold." FT /evidence="ECO:0000269|PubMed:9341229" FT CONFLICT 206 FT /note="R -> A (in Ref. 1; CAA26133/AAB18618)" FT /evidence="ECO:0000305" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 39..46 FT /evidence="ECO:0007829|PDB:7QBJ" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 55..62 FT /evidence="ECO:0007829|PDB:7QBJ" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 76..87 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 221..227 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 231..239 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 255..267 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 281..290 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 306..311 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7QBJ" FT TURN 328..332 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 335..339 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 344..352 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:7QBJ" FT TURN 362..366 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:7QDX" FT STRAND 370..377 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 427..445 FT /evidence="ECO:0007829|PDB:7QBJ" FT HELIX 450..456 FT /evidence="ECO:0007829|PDB:7QBJ" FT STRAND 459..461 FT /evidence="ECO:0007829|PDB:7QBJ" SQ SEQUENCE 488 AA; 52022 MW; B0FD0A786779C98E CRC64; MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD TVTEARLAIA LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV LPTTTLREVK ELTERNGFAG YPVVTEENEL VGIITGRDVR FVTDLNQPVS VYMTPKERLV TVREGEAREV VLAKMHEKRV EKALVVDDEF HLIGMITVKD FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA GVDVLLIDSS HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA IAAGASAVMV GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD RYFQSDNAAD KLVPEGIEGR VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI DELRTKAEFV RISGAGIQES HVHDVTITKE SPNYRLGS //