ID SUFS_ECOLI Reviewed; 406 AA. AC P77444; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 199. DE RecName: Full=Cysteine desulfurase; DE EC=2.8.1.7 {ECO:0000305|PubMed:10329673}; DE AltName: Full=Cysteine sulfinate desulfinase; DE Short=CSD; DE EC=3.13.1.- {ECO:0000269|PubMed:10329673}; DE AltName: Full=Selenocysteine beta-lyase; DE Short=SCL; DE AltName: Full=Selenocysteine lyase; DE EC=4.4.1.16 {ECO:0000269|PubMed:10329673}; DE AltName: Full=Selenocysteine reductase; GN Name=sufS; Synonyms=csdB {ECO:0000303|PubMed:10329673}, ynhB; GN OrderedLocusNames=b1680, JW1670; 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], PROTEIN SEQUENCE OF 1-10, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.8 RP ANGSTROMS). RC STRAIN=K12; RX PubMed=10329673; DOI=10.1074/jbc.274.21.14768; RA Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N.; RT "A nifS-like gene, csdB, encodes an Escherichia coli counterpart of RT mammalian selenocysteine lyase. Gene cloning, purification, RT characterization and preliminary X-ray crystallographic studies."; RL J. Biol. Chem. 274:14768-14772(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(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 GENE NAME. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=10322040; DOI=10.1128/jb.181.10.3307-3309.1999; RA Patzer S.I., Hantke K.; RT "SufS is a NifS-like protein, and SufD is necessary for stability of the RT 2Fe-2S FhuF protein in Escherichia coli."; RL J. Bacteriol. 181:3307-3309(1999). RN [6] RP FUNCTION. RX PubMed=10829016; DOI=10.1074/jbc.m000926200; RA Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.; RT "Escherichia coli NifS-like proteins provide selenium in the pathway for RT the biosynthesis of selenophosphate."; RL J. Biol. Chem. 275:23769-23773(2000). RN [7] RP MUTAGENESIS OF CYS-364. RX PubMed=10739946; DOI=10.1093/oxfordjournals.jbchem.a022641; RA Mihara H., Kurihara T., Yoshimura T., Esaki N.; RT "Kinetic and mutational studies of three NifS homologs from Escherichia RT coli: mechanistic difference between L-cysteine desulfurase and L- RT selenocysteine lyase reactions."; RL J. Biochem. 127:559-567(2000). RN [8] RP FUNCTION IN FE-S CLUSTER SYSTEM. RX PubMed=12089140; DOI=10.1074/jbc.c200365200; RA Takahashi Y., Tokumoto U.; RT "A third bacterial system for the assembly of iron-sulfur clusters with RT homologs in archaea and plastids."; RL J. Biol. Chem. 277:28380-28383(2002). RN [9] RP FUNCTION. RX PubMed=11997471; DOI=10.1073/pnas.102176099; RA Mihara H., Kato S., Lacourciere G.M., Stadtman T.C., Kennedy R.A.J.D., RA Kurihara T., Tokumoto U., Takahashi Y., Esaki N.; RT "The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA RT and the selenocysteine-containing formate dehydrogenase H."; RL Proc. Natl. Acad. Sci. U.S.A. 99:6679-6683(2002). RN [10] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SUFE AND SUFBCD RP COMPLEX. RC STRAIN=K12 / TG1; RX PubMed=12876288; DOI=10.1074/jbc.m305953200; RA Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.; RT "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form RT a new type of cysteine desulfurase."; RL J. Biol. Chem. 278:38352-38359(2003). RN [11] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SUFE AND SUFBCD RP COMPLEX. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=12941942; DOI=10.1074/jbc.m308004200; RA Outten F.W., Wood M.J., Munoz F.M., Storz G.; RT "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase RT activity as part of a sulfur transfer pathway for Fe-S cluster assembly in RT Escherichia coli."; RL J. Biol. Chem. 278:45713-45719(2003). RN [12] RP ACTIVITY REGULATION, AND INTERACTION WITH SUFE. RX PubMed=14644425; DOI=10.1016/s0014-5793(03)01244-4; RA Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E., RA Fontecave M.; RT "Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for RT sulfur transfer from SufS to SufE."; RL FEBS Lett. 555:263-267(2003). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=10684605; DOI=10.1021/bi991732a; RA Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y.; RT "Structure of a NifS homologue: X-ray structure analysis of CsdB, an RT Escherichia coli counterpart of mammalian selenocysteine lyase."; RL Biochemistry 39:1263-1273(2000). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF HIS-55; HIS-123 RP AND ARG-379. RX PubMed=11983074; DOI=10.1093/oxfordjournals.jbchem.a003151; RA Mihara H., Fujii T., Kato S., Kurihara T., Hata Y., Esaki N.; RT "Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS RT homolog: implications for its specificity toward selenocysteine."; RL J. Biochem. 131:679-685(2002). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH RP L-CYSTEINE AND L-SELENOCYSTEINE, AND PYRIDOXAL PHOSPHATE AT LYS-226. RX PubMed=11827487; DOI=10.1006/jmbi.2001.5308; RA Lima C.D.; RT "Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural RT basis for perselenide and persulfide intermediate formation."; RL J. Mol. Biol. 315:1199-1208(2002). CC -!- FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to CC yield L-alanine, an essential step in sulfur metabolism for CC biosynthesis of a variety of sulfur-containing biomolecules. Component CC of the suf operon, which is activated and required under specific CC conditions such as oxidative stress and iron limitation. Acts as a CC potent selenocysteine lyase in vitro, that mobilizes selenium from L- CC selenocysteine. Selenocysteine lyase activity is however unsure in CC vivo. Can also desulfinate L-cysteine sulfinate (3-sulfino-L-alanine). CC {ECO:0000269|PubMed:10329673, ECO:0000269|PubMed:10829016, CC ECO:0000269|PubMed:11997471, ECO:0000269|PubMed:12089140, CC ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L- CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA- CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, CC ChEBI:CHEBI:64428; EC=2.8.1.7; CC Evidence={ECO:0000305|PubMed:10329673}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-selenocysteine + AH2 = hydrogenselenide + L-alanine + A + CC H(+); Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843, CC ChEBI:CHEBI:57972; EC=4.4.1.16; CC Evidence={ECO:0000269|PubMed:10329673}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-sulfino-L-alanine + H2O = sulfite + L-alanine + H(+); CC Xref=Rhea:RHEA:28278, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17359, ChEBI:CHEBI:57972, ChEBI:CHEBI:61085; CC Evidence={ECO:0000269|PubMed:10329673}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:10329673}; CC -!- ACTIVITY REGULATION: Displays a strong preference for selenocysteine as CC a substrate in vitro and is only very slightly active using cysteine. CC The interactions with SufE and the SufBCD complex act synergistically CC to enhance, up to 50-fold, its cysteine desulfurase activity. CC {ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942, CC ECO:0000269|PubMed:14644425}. CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. CC -!- SUBUNIT: Homodimer (PubMed:10329673). Interacts with SufE and the CC SufBCD complex composed of SufB, SufC and SufD. The interaction with CC SufE is required to mediate the direct transfer of the sulfur atom from CC the S-sulfanylcysteine. {ECO:0000269|PubMed:10329673, CC ECO:0000269|PubMed:11827487, ECO:0000269|PubMed:12876288, CC ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:14644425}. CC -!- INTERACTION: CC P77444; P76194: sufE; NbExp=3; IntAct=EBI-1124981, EBI-1124973; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- INDUCTION: Suf operon is under both the Fe-dependent Fur repressor and CC the oxidative stress dependent OxyR activator. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. Csd subfamily. {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; AB055108; BAB21542.1; -; Genomic_DNA. DR EMBL; U00096; AAC74750.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15457.1; -; Genomic_DNA. DR PIR; H64925; H64925. DR RefSeq; NP_416195.1; NC_000913.3. DR RefSeq; WP_000577988.1; NZ_CP009789.1. DR PDB; 1C0N; X-ray; 2.80 A; A=1-406. DR PDB; 1I29; X-ray; 2.80 A; A=1-406. DR PDB; 1JF9; X-ray; 2.00 A; A=1-406. DR PDB; 1KMJ; X-ray; 2.00 A; A=1-406. DR PDB; 1KMK; X-ray; 2.20 A; A=1-406. DR PDB; 5DB5; X-ray; 2.75 A; A/B=1-406. DR PDB; 6MR2; X-ray; 2.40 A; A=1-406. DR PDB; 6MR6; X-ray; 2.02 A; A=1-406. DR PDB; 6MRE; X-ray; 2.50 A; A=1-406. DR PDB; 6MRH; X-ray; 2.02 A; A=1-406. DR PDB; 6MRI; X-ray; 2.62 A; A=1-406. DR PDB; 6O10; X-ray; 2.00 A; A=1-406. DR PDB; 6O11; X-ray; 1.84 A; A=1-406. DR PDB; 6O12; X-ray; 2.05 A; A=1-406. DR PDB; 6O13; X-ray; 2.20 A; A=1-406. DR PDB; 6UY5; X-ray; 1.50 A; A/B=1-406. DR PDB; 7RRN; X-ray; 2.30 A; A=1-406. DR PDB; 7RUJ; X-ray; 2.50 A; A=1-406. DR PDB; 7RW3; X-ray; 2.30 A; A=1-406. DR PDB; 8VBS; X-ray; 3.31 A; A/B=1-406. DR PDB; 9D2D; X-ray; 2.70 A; A=1-406. DR AlphaFoldDB; P77444; -. DR SMR; P77444; -. DR BioGRID; 4260281; 107. DR BioGRID; 850545; 4. DR ComplexPortal; CPX-2124; sufS cysteine desulfurase complex. DR DIP; DIP-9324N; -. DR FunCoup; P77444; 699. DR IntAct; P77444; 14. DR STRING; 511145.b1680; -. DR DrugBank; DB04217; L-2-amino-3-butynoic acid. DR DrugBank; DB02761; S-Mercaptocysteine. DR DrugBank; DB03049; S-Selanyl Cysteine. DR DrugBank; DB02345; Selenocysteine. DR jPOST; P77444; -. DR PaxDb; 511145-b1680; -. DR EnsemblBacteria; AAC74750; AAC74750; b1680. DR GeneID; 946185; -. DR KEGG; ecj:JW1670; -. DR KEGG; eco:b1680; -. DR KEGG; ecoc:C3026_09625; -. DR PATRIC; fig|1411691.4.peg.578; -. DR EchoBASE; EB3720; -. DR eggNOG; COG0520; Bacteria. DR HOGENOM; CLU_003433_2_5_6; -. DR InParanoid; P77444; -. DR OMA; LVTWQQI; -. DR OrthoDB; 9808002at2; -. DR PhylomeDB; P77444; -. DR BioCyc; EcoCyc:G6906-MONOMER; -. DR BioCyc; MetaCyc:G6906-MONOMER; -. DR BRENDA; 2.8.1.7; 2026. DR BRENDA; 4.4.1.16; 2026. DR UniPathway; UPA00266; -. DR EvolutionaryTrace; P77444; -. DR PRO; PR:P77444; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P77444; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:EcoCyc. DR GO; GO:0008826; F:cysteine sulfinate desulfinase activity; EXP:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. DR GO; GO:0009000; F:selenocysteine lyase activity; IDA:EcoCyc. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc. DR GO; GO:0001887; P:selenium compound metabolic process; IGI:EcoCyc. DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc. DR CDD; cd06453; SufS_like; 1. DR FunFam; 3.40.640.10:FF:000042; Cysteine desulfurase; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01831; SufS_aminotrans_5; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR010970; Cys_dSase_SufS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; NF006791; PRK09295.1; 1. DR NCBIfam; TIGR01979; sufS; 1. DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1. DR PANTHER; PTHR43586:SF25; CYSTEINE DESULFURASE; 1. DR Pfam; PF00266; Aminotran_5; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. DR PDBsum; 1C0N; -. DR PDBsum; 1I29; -. DR PDBsum; 1JF9; -. DR PDBsum; 1KMJ; -. DR PDBsum; 1KMK; -. DR PDBsum; 5DB5; -. DR PDBsum; 6MR2; -. DR PDBsum; 6MR6; -. DR PDBsum; 6MRE; -. DR PDBsum; 6MRH; -. DR PDBsum; 6MRI; -. DR PDBsum; 6O10; -. DR PDBsum; 6O11; -. DR PDBsum; 6O12; -. DR PDBsum; 6O13; -. DR PDBsum; 6UY5; -. DR PDBsum; 7RRN; -. DR PDBsum; 7RUJ; -. DR PDBsum; 7RW3; -. DR PDBsum; 8VBS; -. DR PDBsum; 9D2D; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Lyase; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..406 FT /note="Cysteine desulfurase" FT /id="PRO_0000150329" FT ACT_SITE 364 FT /note="Cysteine persulfide intermediate" FT MOD_RES 226 FT /note="N6-(pyridoxal phosphate)lysine" FT MUTAGEN 55 FT /note="H->A: No effect." FT /evidence="ECO:0000269|PubMed:11983074" FT MUTAGEN 123 FT /note="H->A: Loss of function; possibly due to FT destabilization of PLP in the active site." FT /evidence="ECO:0000269|PubMed:11983074" FT MUTAGEN 364 FT /note="C->A: Abolishes activity towards L-cysteine but not FT towards selenocysteine." FT /evidence="ECO:0000269|PubMed:10739946" FT MUTAGEN 379 FT /note="R->A: Loss of function." FT /evidence="ECO:0000269|PubMed:11983074" FT HELIX 5..9 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 13..16 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 33..36 FT /evidence="ECO:0007829|PDB:8VBS" FT HELIX 37..49 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:6O11" FT HELIX 60..79 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 165..173 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 183..192 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 202..207 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 218..224 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 225..228 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 250..252 FT /evidence="ECO:0007829|PDB:7RUJ" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:6MRH" FT STRAND 256..260 FT /evidence="ECO:0007829|PDB:6UY5" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 281..297 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 299..317 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 323..327 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 366..371 FT /evidence="ECO:0007829|PDB:6UY5" FT STRAND 377..381 FT /evidence="ECO:0007829|PDB:6UY5" FT HELIX 388..405 FT /evidence="ECO:0007829|PDB:6UY5" SQ SEQUENCE 406 AA; 44434 MW; 9374C43C3AD9D8E3 CRC64; MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG YAAVHRGIHT LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE NPLAEMITLA HQHGAKVLVD GAQAVMHHPV DVQALDCDFY VFSGHKLYGP TGIGILYVKE ALLQEMPPWE GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR IHRLLG //