SDHA_ECOLI
ID SDHA_ECOLI Reviewed; 588 AA.
AC P0AC41; P10444; P78282;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE EC=1.3.5.1 {ECO:0000305|PubMed:19710024};
GN Name=sdhA; OrderedLocusNames=b0723, JW0713;
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=6383359; DOI=10.1042/bj2220519;
RA Wood D., Darlison M.G., Wilde R.J., Guest J.R.;
RT "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of
RT the succinate dehydrogenase of Escherichia coli.";
RL Biochem. J. 222:519-534(1984).
RN [2]
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 [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 578-588.
RC STRAIN=K12;
RX PubMed=6388571; DOI=10.1042/bj2230507;
RA Darlison M.G., Guest J.R.;
RT "Nucleotide sequence encoding the iron-sulphur protein subunit of the
RT succinate dehydrogenase of Escherichia coli.";
RL Biochem. J. 223:507-517(1984).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=24374335; DOI=10.1016/j.febslet.2013.12.019;
RA McNeil M.B., Hampton H.G., Hards K.J., Watson B.N., Cook G.M.,
RA Fineran P.C.;
RT "The succinate dehydrogenase assembly factor, SdhE, is required for the
RT flavinylation and activation of fumarate reductase in bacteria.";
RL FEBS Lett. 588:414-421(2014).
RN [12]
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLU-186 AND THR-187.
RC STRAIN=K12 / RP437;
RX PubMed=26644464; DOI=10.1074/jbc.m115.690396;
RA Maklashina E., Rajagukguk S., Starbird C.A., McDonald W.H., Koganitsky A.,
RA Eisenbach M., Iverson T.M., Cecchini G.;
RT "Binding of the covalent flavin assembly factor to the flavoprotein subunit
RT of complex II.";
RL J. Biol. Chem. 291:2904-2916(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE,
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12560550; DOI=10.1126/science.1079605;
RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H.,
RA Leger C., Byrne B., Cecchini G., Iwata S.;
RT "Architecture of succinate dehydrogenase and reactive oxygen species
RT generation.";
RL Science 299:700-704(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE,
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=16407191; DOI=10.1074/jbc.m508173200;
RA Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K.,
RA Omura S., Byrne B., Cecchini G., Iwata S.;
RT "Structural and computational analysis of the quinone-binding site of
RT complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron
RT transfer and proton conduction during ubiquinone reduction.";
RL J. Biol. Chem. 281:7309-7316(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND MALATE-LIKE
RP INTERMEDIATE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND
RP ACTIVE SITE.
RX PubMed=19710024; DOI=10.1074/jbc.m109.010058;
RA Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.;
RT "Structure of Escherichia coli succinate:quinone oxidoreductase with an
RT occupied and empty quinone-binding site.";
RL J. Biol. Chem. 284:29836-29846(2009).
CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are
CC responsible for the catalysis of fumarate and succinate
CC interconversion; the fumarate reductase is used in anaerobic growth,
CC and the succinate dehydrogenase is used in aerobic growth.
CC {ECO:0000269|PubMed:24374335, ECO:0000305|PubMed:12560550,
CC ECO:0000305|PubMed:16407191, ECO:0000305|PubMed:19710024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC Evidence={ECO:0000305|PubMed:19710024};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191,
CC ECO:0000269|PubMed:19710024};
CC Note=Flavinylated by SdhE, about 5% flavinylation occurs in the absence
CC of SdhE. {ECO:0000269|PubMed:26644464};
CC -!- ACTIVITY REGULATION: Inhibited by oxaloacetate.
CC {ECO:0000269|PubMed:12560550}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (bacterial route): step 1/1.
CC {ECO:0000305|PubMed:19710024}.
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic
CC anchor protein. The complex forms trimers. Can be cross-linked to SdhE
CC (PubMed:26644464). {ECO:0000269|PubMed:12560550,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16407191,
CC ECO:0000269|PubMed:19710024, ECO:0000269|PubMed:26644464}.
CC -!- INTERACTION:
CC P0AC41; P07014: sdhB; NbExp=2; IntAct=EBI-371263, EBI-1035514;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12560550,
CC ECO:0000269|PubMed:16079137}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}; Cytoplasmic
CC side {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}.
CC -!- DISRUPTION PHENOTYPE: No effect on anaerobic growth on glycerol
CC fumarate medium. {ECO:0000269|PubMed:18723842}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; J01619; AAA23895.1; -; Genomic_DNA.
DR EMBL; X00980; CAA25487.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73817.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35390.1; -; Genomic_DNA.
DR EMBL; X01070; CAA25533.1; -; Genomic_DNA.
DR PIR; B64808; DEECSF.
DR RefSeq; NP_415251.1; NC_000913.3.
DR RefSeq; WP_000775540.1; NZ_STEB01000035.1.
DR PDB; 1NEK; X-ray; 2.60 A; A=1-588.
DR PDB; 1NEN; X-ray; 2.90 A; A=1-588.
DR PDB; 2ACZ; X-ray; 3.10 A; A=1-588.
DR PDB; 2WDQ; X-ray; 2.40 A; A/E/I=1-588.
DR PDB; 2WDR; X-ray; 3.20 A; A/E/I=1-588.
DR PDB; 2WDV; X-ray; 3.20 A; A/E/I=1-588.
DR PDB; 2WP9; X-ray; 2.70 A; A/E/I=1-588.
DR PDB; 2WS3; X-ray; 3.20 A; A/E/I=1-588.
DR PDB; 2WU2; X-ray; 2.50 A; A/E/I=1-588.
DR PDB; 2WU5; X-ray; 2.80 A; A/E/I=1-588.
DR PDB; 7JZ2; EM; 2.50 A; A/E/I=1-588.
DR PDBsum; 1NEK; -.
DR PDBsum; 1NEN; -.
DR PDBsum; 2ACZ; -.
DR PDBsum; 2WDQ; -.
DR PDBsum; 2WDR; -.
DR PDBsum; 2WDV; -.
DR PDBsum; 2WP9; -.
DR PDBsum; 2WS3; -.
DR PDBsum; 2WU2; -.
DR PDBsum; 2WU5; -.
DR PDBsum; 7JZ2; -.
DR AlphaFoldDB; P0AC41; -.
DR SMR; P0AC41; -.
DR BioGRID; 4262907; 31.
DR BioGRID; 849776; 2.
DR ComplexPortal; CPX-1931; Respiratory chain complex II.
DR DIP; DIP-31877N; -.
DR IntAct; P0AC41; 91.
DR MINT; P0AC41; -.
DR STRING; 511145.b0723; -.
DR DrugBank; DB07671; 2-[1-METHYLHEXYL]-4,6-DINITROPHENOL.
DR DrugBank; DB04631; Atpenin A5.
DR DrugBank; DB08690; Ubiquinone Q2.
DR iPTMnet; P0AC41; -.
DR SWISS-2DPAGE; P0AC41; -.
DR jPOST; P0AC41; -.
DR PaxDb; P0AC41; -.
DR PRIDE; P0AC41; -.
DR EnsemblBacteria; AAC73817; AAC73817; b0723.
DR EnsemblBacteria; BAA35390; BAA35390; BAA35390.
DR GeneID; 66671007; -.
DR GeneID; 945402; -.
DR KEGG; ecj:JW0713; -.
DR KEGG; eco:b0723; -.
DR PATRIC; fig|1411691.4.peg.1549; -.
DR EchoBASE; EB0924; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_1_6; -.
DR InParanoid; P0AC41; -.
DR OMA; DPIPIQP; -.
DR PhylomeDB; P0AC41; -.
DR BioCyc; EcoCyc:SDH-FLAVO; -.
DR BioCyc; MetaCyc:SDH-FLAVO; -.
DR BRENDA; 1.3.5.1; 2026.
DR UniPathway; UPA00223; UER01005.
DR EvolutionaryTrace; P0AC41; -.
DR PHI-base; PHI:7964; -.
DR PRO; PR:P0AC41; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoliWiki.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IMP:EcoliWiki.
DR GO; GO:0009060; P:aerobic respiration; IGI:EcoliWiki.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IGI:EcoliWiki.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..588
FT /note="Succinate dehydrogenase flavoprotein subunit"
FT /id="PRO_0000158652"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:19710024"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT BINDING 37..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT BINDING 221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19710024"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19710024"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19710024"
FT BINDING 388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19710024"
FT BINDING 404..405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT MOD_RES 45
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:12560550,
FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 186
FT /note="E->M: Allows recovery of protein cross-linked to
FT SdhE, SdhA is flavinylated."
FT /evidence="ECO:0000269|PubMed:26644464"
FT MUTAGEN 187
FT /note="T->M: No recovery of protein cross-linked to SdhE,
FT SdhA is flavinylated."
FT /evidence="ECO:0000269|PubMed:26644464"
FT CONFLICT 20..22
FT /note="MRA -> IAR (in Ref. 1; AAA23895/CAA25487)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 82..101
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1NEK"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1NEK"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7JZ2"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1NEK"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 347..356
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1NEK"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 456..470
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 477..494
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:2WU2"
FT HELIX 508..532
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:7JZ2"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 554..560
FT /evidence="ECO:0007829|PDB:2WDQ"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:2WDQ"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:2WDQ"
SQ SEQUENCE 588 AA; 64422 MW; 837F9A63991B6CE8 CRC64;
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT
HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG
GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC
TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ
FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI
PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ
ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM
AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH
SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY
