FABH_ECOLI
ID FABH_ECOLI Reviewed; 317 AA.
AC P0A6R0; P24249;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=EcFabH;
GN Name=fabH; OrderedLocusNames=b1091, JW1077;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30.
RC STRAIN=K12;
RX PubMed=1551888; DOI=10.1016/s0021-9258(19)50498-7;
RA Tsay J.-T., Oh W., Larson T.J., Jackowski S., Rock C.O.;
RT "Isolation and characterization of the beta-ketoacyl-acyl carrier protein
RT synthase III gene (fabH) from Escherichia coli K-12.";
RL J. Biol. Chem. 267:6807-6814(1992).
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 1-76.
RC STRAIN=K12;
RX PubMed=1447160; DOI=10.1128/jb.174.23.7873-7874.1992;
RA Oh W., Larson T.J.;
RT "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the
RT Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 174:7873-7874(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-317.
RX PubMed=1314802; DOI=10.1128/jb.174.9.2851-2857.1992;
RA Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J.,
RA Stuitje A.R.;
RT "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD
RT gene, encoding malonyl coenzyme A-acyl carrier protein transacylase.";
RL J. Bacteriol. 174:2851-2857(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
RC STRAIN=K12;
RX PubMed=1339356; DOI=10.1016/0014-5793(92)80128-4;
RA Magnuson K., Oh W., Larson T.J., Cronan J.E. Jr.;
RT "Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme
RT A-acyl carrier protein transacylase of Escherichia coli.";
RL FEBS Lett. 299:262-266(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7592873; DOI=10.1074/jbc.270.44.26538;
RA Heath R.J., Rock C.O.;
RT "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in
RT completing cycles of fatty acid elongation in Escherichia coli.";
RL J. Biol. Chem. 270:26538-26542(1995).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=8631920; DOI=10.1074/jbc.271.18.10996;
RA Heath R.J., Rock C.O.;
RT "Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by
RT acyl-acyl carrier protein in Escherichia coli.";
RL J. Biol. Chem. 271:10996-11000(1996).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8910376; DOI=10.1074/jbc.271.44.27795;
RA Heath R.J., Rock C.O.;
RT "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein
RT dehydratases in Escherichia coli fatty acid biosynthesis.";
RL J. Biol. Chem. 271:27795-27801(1996).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10629181; DOI=10.1128/jb.182.2.365-370.2000;
RA Choi K.-H., Heath R.J., Rock C.O.;
RT "Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining
RT factor in branched-chain fatty acid biosynthesis.";
RL J. Bacteriol. 182:365-370(2000).
RN [12]
RP DOMAIN, AND MUTAGENESIS OF LYS-214; ARG-249; ALA-253 AND 256-LYS-LYS-257.
RX PubMed=11078736; DOI=10.1074/jbc.m008042200;
RA Zhang Y.-M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O.,
RA White S.W.;
RT "Identification and analysis of the acyl carrier protein (ACP) docking site
RT on beta-ketoacyl-ACP synthase III.";
RL J. Biol. Chem. 276:8231-8238(2001).
RN [13]
RP INHIBITION BY ANTIBIOTICS.
RX PubMed=11375394; DOI=10.1074/jbc.m101769200;
RA Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H.,
RA Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M.,
RA Daines R.A., Lonsdale J.T.;
RT "Identification, substrate specificity, and inhibition of the Streptococcus
RT pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH).";
RL J. Biol. Chem. 276:30024-30030(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=10593943; DOI=10.1074/jbc.274.51.36465;
RA Qiu X., Janson C.A., Konstantinidis A.K., Nwagwu S., Silverman C.,
RA Smith W.W., Khandekar S., Lonsdale J., Abdel-Meguid S.S.;
RT "Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A
RT key condensing enzyme in bacterial fatty acid biosynthesis.";
RL J. Biol. Chem. 274:36465-36471(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=10673437; DOI=10.1016/s0969-2126(00)00094-0;
RA Davies C., Heath R.J., White S.W., Rock C.O.;
RT "The 1.8-A crystal structure and active-site architecture of beta-ketoacyl-
RT acyl carrier protein synthase III (FabH) from Escherichia coli.";
RL Structure 8:185-195(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=11243824; DOI=10.1006/jmbi.2000.4457;
RA Qiu X., Janson C.A., Smith W.W., Head M., Lonsdale J., Konstantinidis A.K.;
RT "Refined structures of beta-ketoacyl-acyl carrier protein synthase III.";
RL J. Mol. Biol. 307:341-356(2001).
CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis
CC by the addition to an acyl acceptor of two carbons from malonyl-ACP.
CC Catalyzes the first condensation reaction which initiates fatty acid
CC synthesis and may therefore play a role in governing the total rate of
CC fatty acid production. Possesses both acetoacetyl-ACP synthase and
CC acetyl transacylase activities. Has some substrate specificity for
CC acetyl-CoA. Its substrate specificity determines the biosynthesis of
CC straight-chain of fatty acids instead of branched-chain
CC (PubMed:7592873, PubMed:8631920, PubMed:8910376, PubMed:10629181). Can
CC also use propionyl-CoA, with lower efficiency (PubMed:8631920,
CC PubMed:10629181). {ECO:0000269|PubMed:10629181,
CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920,
CC ECO:0000269|PubMed:8910376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2
CC + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815,
CC ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + propanoyl-CoA = 3-oxopentanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42244, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9939, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:78449, ChEBI:CHEBI:78818;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8631920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42245;
CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8631920};
CC -!- ACTIVITY REGULATION: Negatively regulated by acyl-ACP, possibly by
CC binding to either the free enzyme or the acyl-enzyme intermediate.
CC {ECO:0000269|PubMed:8631920}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for acetyl-CoA {ECO:0000269|PubMed:8631920};
CC KM=5 uM for malonyl-[ACP] {ECO:0000269|PubMed:8631920};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP-
CC Rule:MF_01815, ECO:0000269|PubMed:11078736}.
CC -!- MISCELLANEOUS: Inhibited by the SB418011 antibiotic. Not inhibited by
CC cerulenin and thiolactomycin.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000305}.
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DR EMBL; M77744; AAA23749.1; -; Genomic_DNA.
DR EMBL; M96793; AAB59065.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74175.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35899.2; -; Genomic_DNA.
DR EMBL; M87040; AAA23741.1; -; Genomic_DNA.
DR EMBL; Z11565; CAA77659.1; -; Genomic_DNA.
DR PIR; A42431; A42431.
DR RefSeq; NP_415609.1; NC_000913.3.
DR RefSeq; WP_000288132.1; NZ_STEB01000016.1.
DR PDB; 1EBL; X-ray; 1.80 A; A/B=1-317.
DR PDB; 1HN9; X-ray; 2.00 A; A/B=1-317.
DR PDB; 1HND; X-ray; 1.60 A; A=1-317.
DR PDB; 1HNH; X-ray; 1.90 A; A=1-317.
DR PDB; 1HNJ; X-ray; 1.46 A; A=1-317.
DR PDB; 1HNK; X-ray; 1.90 A; A=1-317.
DR PDB; 1MZS; X-ray; 2.10 A; A=1-317.
DR PDB; 2EFT; X-ray; 2.00 A; A/B=1-317.
DR PDB; 2GYO; X-ray; 2.00 A; A/B=1-317.
DR PDB; 3IL9; X-ray; 1.85 A; A/B=1-317.
DR PDB; 4Z8D; X-ray; 2.00 A; A/B=1-317.
DR PDB; 5BNM; X-ray; 1.70 A; A/B=1-317.
DR PDB; 5BNR; X-ray; 1.89 A; A=1-317.
DR PDB; 5BNS; X-ray; 2.20 A; A/B=1-317.
DR PDB; 6X7R; X-ray; 1.35 A; A=1-317.
DR PDB; 6X7S; X-ray; 1.35 A; A=1-317.
DR PDBsum; 1EBL; -.
DR PDBsum; 1HN9; -.
DR PDBsum; 1HND; -.
DR PDBsum; 1HNH; -.
DR PDBsum; 1HNJ; -.
DR PDBsum; 1HNK; -.
DR PDBsum; 1MZS; -.
DR PDBsum; 2EFT; -.
DR PDBsum; 2GYO; -.
DR PDBsum; 3IL9; -.
DR PDBsum; 4Z8D; -.
DR PDBsum; 5BNM; -.
DR PDBsum; 5BNR; -.
DR PDBsum; 5BNS; -.
DR PDBsum; 6X7R; -.
DR PDBsum; 6X7S; -.
DR AlphaFoldDB; P0A6R0; -.
DR SMR; P0A6R0; -.
DR BioGRID; 4261031; 467.
DR DIP; DIP-48255N; -.
DR IntAct; P0A6R0; 5.
DR STRING; 511145.b1091; -.
DR ChEMBL; CHEMBL4914; -.
DR DrugBank; DB02316; 1-(5-Carboxypentyl)-5-[(2,6-Dichlorobenzyl)Oxy]-1 H-Indole-2-Carboxylic Acid.
DR DrugBank; DB01034; Cerulenin.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03661; L-cysteic acid.
DR DrugBank; DB04524; Malonyl-CoA.
DR DrugBank; DB02039; S-Acetyl-Cysteine.
DR DrugCentral; P0A6R0; -.
DR SwissLipids; SLP:000000852; -.
DR CarbonylDB; P0A6R0; -.
DR jPOST; P0A6R0; -.
DR PaxDb; P0A6R0; -.
DR PRIDE; P0A6R0; -.
DR EnsemblBacteria; AAC74175; AAC74175; b1091.
DR EnsemblBacteria; BAA35899; BAA35899; BAA35899.
DR GeneID; 66670643; -.
DR GeneID; 946003; -.
DR KEGG; ecj:JW1077; -.
DR KEGG; eco:b1091; -.
DR PATRIC; fig|1411691.4.peg.1177; -.
DR EchoBASE; EB0273; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_1_6; -.
DR InParanoid; P0A6R0; -.
DR OMA; WGSEGDK; -.
DR PhylomeDB; P0A6R0; -.
DR BioCyc; EcoCyc:FABH-MON; -.
DR BioCyc; MetaCyc:FABH-MON; -.
DR BRENDA; 2.3.1.180; 2026.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P0A6R0; -.
DR PRO; PR:P0A6R0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:CACAO.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01815; FabH; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR004655; FabH_synth.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR00747; fabH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110424"
FT REGION 245..249
FT /note="ACP-binding"
FT ACT_SITE 112
FT /evidence="ECO:0000305|PubMed:10593943,
FT ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824"
FT ACT_SITE 244
FT /evidence="ECO:0000305|PubMed:10593943,
FT ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824"
FT ACT_SITE 274
FT /evidence="ECO:0000305|PubMed:10593943,
FT ECO:0000305|PubMed:10673437, ECO:0000305|PubMed:11243824"
FT MUTAGEN 112
FT /note="C->S: Loss of activity."
FT MUTAGEN 214
FT /note="K->E,A: Strongly reduces the binding to malonyl-ACP
FT but not that of the substrate."
FT /evidence="ECO:0000269|PubMed:11078736"
FT MUTAGEN 244
FT /note="H->A: Loss of activity."
FT MUTAGEN 249
FT /note="R->E,A: Abolishes the binding to malonyl-ACP but not
FT that of the substrate."
FT /evidence="ECO:0000269|PubMed:11078736"
FT MUTAGEN 253
FT /note="A->Y: Abolishes both binding to malonyl-ACP and
FT binding to substrate."
FT /evidence="ECO:0000269|PubMed:11078736"
FT MUTAGEN 256..257
FT /note="KK->AA: Strongly reduces both binding to malonyl-ACP
FT and binding to substrate."
FT /evidence="ECO:0000269|PubMed:11078736"
FT MUTAGEN 256..257
FT /note="KK->EE: Abolishes the binding to malonyl-ACP but not
FT that of the substrate."
FT /evidence="ECO:0000269|PubMed:11078736"
FT MUTAGEN 274
FT /note="N->A: Loss of activity."
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1EBL"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4Z8D"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6X7R"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:6X7R"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6X7R"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:6X7R"
SQ SEQUENCE 317 AA; 33515 MW; BF3192CFF36023D3 CRC64;
MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET VSTMGFEAAT
RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI KGCPAFDVAA ACAGFTYALS
VADQYVKSGA VKYALVVGSD VLARTCDPTD RGTIIIFGDG AGAAVLAASE EPGIISTHLH
ADGSYGELLT LPNADRVNPE NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW
LVPHQANLRI ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL
LEAFGGGFTW GSALVRF
