CYSJ_ECOLI
ID CYSJ_ECOLI Reviewed; 599 AA.
AC P38038; P14782; Q2MA65;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541};
DE Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541};
DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541, ECO:0000269|PubMed:10860732};
GN Name=cysJ {ECO:0000255|HAMAP-Rule:MF_01541};
GN OrderedLocusNames=b2764, JW2734;
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=B;
RX PubMed=2550423; DOI=10.1016/s0021-9258(18)71547-0;
RA Ostrowski J., Barber M.J., Rueger D.C., Miller B.E., Siegel L.M.,
RA Kredich N.M.;
RT "Characterization of the flavoprotein moieties of NADPH-sulfite reductase
RT from Salmonella typhimurium and Escherichia coli. Physicochemical and
RT catalytic properties, amino acid sequence deduced from DNA sequence of
RT cysJ, and comparison with NADPH-cytochrome P-450 reductase.";
RL J. Biol. Chem. 264:15796-15808(1989).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 594-599.
RC STRAIN=B;
RX PubMed=2670946; DOI=10.1016/s0021-9258(19)84893-7;
RA Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M.,
RA Kredich N.M.;
RT "Characterization of the cysJIH regions of Salmonella typhimurium and
RT Escherichia coli B. DNA sequences of cysI and cysH and a model for the
RT siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on
RT amino acid homology with spinach nitrite reductase.";
RL J. Biol. Chem. 264:15726-15737(1989).
RN [5]
RP CHARACTERIZATION OF FAD AND FMN DOMAINS.
RX PubMed=7589518; DOI=10.1016/0014-5793(95)01081-o;
RA Eschenbrenner M., Coves J., Fontecave M.;
RT "NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution
RT to the flavin content and subunit interaction.";
RL FEBS Lett. 374:82-84(1995).
RN [6]
RP CHARACTERIZATION AS A NADPH:FLAVIN OXIDOREDUCTASE.
RX PubMed=7657631; DOI=10.1074/jbc.270.35.20550;
RA Eschenbrenner M., Coves J., Fontecave M.;
RT "The flavin reductase activity of the flavoprotein component of sulfite
RT reductase from Escherichia coli. A new model for the protein structure.";
RL J. Biol. Chem. 270:20550-20555(1995).
RN [7]
RP CHARACTERIZATION OF FMN DOMAIN 1-220.
RX PubMed=9153434; DOI=10.1021/bi9623744;
RA Coves J., Zeghouf M., Macherel D., Guigliarelli B., Asso M., Fontecave M.;
RT "Flavin mononucleotide-binding domain of the flavoprotein component of the
RT sulfite reductase from Escherichia coli.";
RL Biochemistry 36:5921-5928(1997).
RN [8]
RP CHARACTERIZATION AS A NADPH-CYTOCHROME P450 REDUCTASE.
RX PubMed=9618257; DOI=10.1006/bbrc.1998.8671;
RA Zeghouf M., Defaye G., Fontecave M., Coves J.;
RT "The flavoprotein component of the Escherichia coli sulfite reductase can
RT act as a cytochrome P450c17 reductase.";
RL Biochem. Biophys. Res. Commun. 246:602-605(1998).
RN [9]
RP CHARACTERIZATION.
RX PubMed=9558350; DOI=10.1021/bi9728699;
RA Zeghouf M., Fontecave M., Macherel D., Coves J.;
RT "The flavoprotein component of the Escherichia coli sulfite reductase:
RT expression, purification, and spectral and catalytic properties of a
RT monomeric form containing both the flavin adenine dinucleotide and the
RT flavin mononucleotide cofactors.";
RL Biochemistry 37:6114-6123(1998).
RN [10]
RP CHARACTERIZATION OF FAD DOMAIN.
RX PubMed=10455035; DOI=10.1042/bj3420465;
RA Coves J., Lebrun C., Gervasi G., Dalbon P., Fontecave M.;
RT "Overexpression of the FAD-binding domain of the sulphite reductase
RT flavoprotein component from Escherichia coli and its inhibition by iodonium
RT diphenyl chloride.";
RL Biochem. J. 342:465-472(1999).
RN [11]
RP CHARACTERIZATION, AND STRUCTURE BY NMR OF 53-220.
RX PubMed=11888295; DOI=10.1021/bi016008i;
RA Champier L., Sibille N., Bersch B., Brutscher B., Blackledge M., Coves J.;
RT "Reactivity, secondary structure, and molecular topology of the Escherichia
RT coli sulfite reductase flavodoxin-like domain.";
RL Biochemistry 41:3770-3780(2002).
RN [12]
RP QUATERNARY STRUCTURE.
RX PubMed=10984484; DOI=10.1074/jbc.m005619200;
RA Zeghouf M., Fontecave M., Coves J.;
RT "A simplified functional version of the Escherichia coli sulfite
RT reductase.";
RL J. Biol. Chem. 275:37651-37656(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 226-599 IN COMPLEXES WITH FAD AND
RP NADP, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN
RP SEQUENCE, AND CATALYTIC ACTIVITY.
RX PubMed=10860732; DOI=10.1006/jmbi.2000.3748;
RA Gruez A., Pignol D., Zeghouf M., Coves J., Fontecave M., Ferrer J.-L.,
RA Fontecilla-Camps J.-C.;
RT "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite
RT reductase indicate a disordered flavodoxin-like module.";
RL J. Mol. Biol. 299:199-212(2000).
RN [14]
RP STRUCTURE BY NMR OF 53-218 IN COMPLEX WITH FMN.
RX PubMed=15966732; DOI=10.1021/bi050437p;
RA Sibille N., Blackledge M., Brutscher B., Coves J., Bersch B.;
RT "Solution structure of the sulfite reductase flavodoxin-like domain from
RT Escherichia coli.";
RL Biochemistry 44:9086-9095(2005).
CC -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC 6-electron reduction of sulfite to sulfide. This is one of several
CC activities required for the biosynthesis of L-cysteine from sulfate.
CC The flavoprotein component catalyzes the electron flow from NADPH ->
CC FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01541, ECO:0000269|PubMed:10860732};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541,
CC ECO:0000269|PubMed:10860732};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541,
CC ECO:0000269|PubMed:10860732};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541,
CC ECO:0000269|PubMed:10860732};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541,
CC ECO:0000269|PubMed:10860732};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01541,
CC ECO:0000269|PubMed:10984484, ECO:0000269|PubMed:15966732}.
CC -!- INTERACTION:
CC P38038; P75863: ycbX; NbExp=5; IntAct=EBI-544440, EBI-544422;
CC -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC flavoprotein subunit CysJ family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
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DR EMBL; M23008; AAA23650.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69274.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75806.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76841.1; -; Genomic_DNA.
DR PIR; H65057; H65057.
DR RefSeq; NP_417244.1; NC_000913.3.
DR RefSeq; WP_000211913.1; NZ_LN832404.1.
DR PDB; 1DDG; X-ray; 2.01 A; A/B=226-599.
DR PDB; 1DDI; X-ray; 2.51 A; A=226-599.
DR PDB; 1YKG; NMR; -; A=53-219.
DR PDBsum; 1DDG; -.
DR PDBsum; 1DDI; -.
DR PDBsum; 1YKG; -.
DR AlphaFoldDB; P38038; -.
DR BMRB; P38038; -.
DR SASBDB; P38038; -.
DR SMR; P38038; -.
DR BioGRID; 4262283; 220.
DR BioGRID; 851569; 2.
DR ComplexPortal; CPX-5629; Sulfite reductase [NADPH] complex.
DR DIP; DIP-9381N; -.
DR IntAct; P38038; 4.
DR STRING; 511145.b2764; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR jPOST; P38038; -.
DR PaxDb; P38038; -.
DR PRIDE; P38038; -.
DR EnsemblBacteria; AAC75806; AAC75806; b2764.
DR EnsemblBacteria; BAE76841; BAE76841; BAE76841.
DR GeneID; 947239; -.
DR KEGG; ecj:JW2734; -.
DR KEGG; eco:b2764; -.
DR PATRIC; fig|1411691.4.peg.3973; -.
DR EchoBASE; EB0188; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_001570_17_7_6; -.
DR InParanoid; P38038; -.
DR OMA; QKRYQRD; -.
DR PhylomeDB; P38038; -.
DR BioCyc; EcoCyc:ALPHACOMP-MON; -.
DR BioCyc; MetaCyc:ALPHACOMP-MON; -.
DR BRENDA; 1.8.1.2; 2026.
DR UniPathway; UPA00140; UER00207.
DR EvolutionaryTrace; P38038; -.
DR PRO; PR:P38038; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0070401; F:NADP+ binding; IMP:CAFA.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:EcoCyc.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IC:ComplexPortal.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IDA:ComplexPortal.
DR DisProt; DP00190; -.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01541; CysJ; 1.
DR InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR029758; CysJ_Proteobact.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR01931; cysJ; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; FMN;
KW NADP; Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..599
FT /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT component"
FT /id="PRO_0000199923"
FT DOMAIN 64..202
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT DOMAIN 234..448
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 70..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:15966732"
FT BINDING 117..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:15966732"
FT BINDING 153..162
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:15966732"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 386..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 404..406
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 419..422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 519..520
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 525..529
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 561
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT BINDING 599
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541,
FT ECO:0000269|PubMed:10860732"
FT CONFLICT 156
FT /note="S -> T (in Ref. 1; AAA23650)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="M -> L (in Ref. 1; AAA23650)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="D -> E (in Ref. 1; AAA23650)"
FT /evidence="ECO:0000305"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1YKG"
FT HELIX 191..206
FT /evidence="ECO:0007829|PDB:1YKG"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1DDI"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:1DDG"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1DDG"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 399..407
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 483..490
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 528..534
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:1DDG"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 558..572
FT /evidence="ECO:0007829|PDB:1DDG"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:1DDG"
FT HELIX 578..590
FT /evidence="ECO:0007829|PDB:1DDG"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:1DDG"
SQ SEQUENCE 599 AA; 66270 MW; 6B39EF5C25265113 CRC64;
MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE
MPGITIISAS QTGNARRVAE ALRDDLLAAK LNVKLVNAGD YKFKQIASEK LLIVVTSTQG
EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDSSYEF FCQSGKDFDS KLAELGGERL
LDRVDADVEY QAAASEWRAR VVDALKSRAP VAAPSQSVAT GAVNEIHTSP YSKDAPLVAS
LSVNQKITGR NSEKDVRHIE IDLGDSGMRY QPGDALGVWY QNDPALVKEL VELLWLKGDE
PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK LQHYAATTPI
VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQAEVENE VHVTVGVVRY DVEGRARAGG
ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRAF MQQRAADEAP
GKNWLFFGNP HFTEDFLYQV EWQRYVKDGV LTRIDLAWSR DQKEKVYVQD KLREQGAELW
RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY
