FAC13_MYCTU
ID FAC13_MYCTU Reviewed; 503 AA.
AC P9WQ37; F2GNX9; L0TEI7; O53306; Q7D654;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase FadD13;
DE EC=6.2.1.3 {ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20027301};
DE AltName: Full=Fatty acyl-CoA ligase;
DE Short=FACL;
DE Short=FACL13;
DE AltName: Full=Fatty acyl-CoA synthetase;
DE Short=ACS;
DE Short=FACS;
DE AltName: Full=Very-long-chain fatty-acyl-CoA synthetase;
DE Short=ACSVL;
GN Name=fadD13; OrderedLocusNames=Rv3089;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RX PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT in the cell envelope.";
RL FEMS Microbiol. Lett. 227:53-63(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Erdman;
RX PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA Ramanathan V.D., Tyagi A.K.;
RT "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT pigs.";
RL J. Bacteriol. 187:4173-4186(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16893682; DOI=10.1016/j.tube.2006.01.021;
RA Cheruvu M., Plikaytis B.B., Shinnick T.M.;
RT "The acid-induced operon Rv3083-Rv3089 is required for growth of
RT Mycobacterium tuberculosis in macrophages.";
RL Tuberculosis 87:12-20(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19182784; DOI=10.1038/nchembio.143;
RA Arora P., Goyal A., Natarajan V.T., Rajakumara E., Verma P., Gupta R.,
RA Yousuf M., Trivedi O.A., Mohanty D., Tyagi A., Sankaranarayanan R.,
RA Gokhale R.S.;
RT "Mechanistic and functional insights into fatty acid activation in
RT Mycobacterium tuberculosis.";
RL Nat. Chem. Biol. 5:166-173(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-172; VAL-209; ALA-211;
RP ALA-302; TRP-377; ASP-382; SER-404 AND LYS-487, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=20027301; DOI=10.1371/journal.pone.0008387;
RA Khare G., Gupta V., Gupta R.K., Gupta R., Bhat R., Tyagi A.K.;
RT "Dissecting the role of critical residues and substrate preference of a
RT fatty acyl-CoA synthetase (FadD13) of Mycobacterium tuberculosis.";
RL PLoS ONE 4:E8387-E8387(2009).
RN [7]
RP MUTAGENESIS OF ARG-397 AND LYS-487.
RX PubMed=20454815; DOI=10.1007/s00894-010-0727-3;
RA Jatana N., Jangid S., Khare G., Tyagi A.K., Latha N.;
RT "Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from
RT Mycobacterium tuberculosis--a potential target for the development of
RT antitubercular drugs.";
RL J. Mol. Model. 17:301-313(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 1-396, MUTAGENESIS OF THR-214;
RP ALA-302; GLY-406 AND LYS-487, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SELECTIVITY.
RX PubMed=22206988; DOI=10.1016/j.jmb.2011.12.031;
RA Goyal A., Verma P., Anandhakrishnan M., Gokhale R.S., Sankaranarayanan R.;
RT "Molecular basis of the functional divergence of fatty acyl-AMP ligase
RT biosynthetic enzymes of Mycobacterium tuberculosis.";
RL J. Mol. Biol. 416:221-238(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF ARG-9; ARG-17; ARG-195; ARG-197 AND ARG-244, AND LIPID
RP ACCOMMODATION.
RX PubMed=22560731; DOI=10.1016/j.str.2012.03.012;
RA Andersson C.S., Lundgren C.A., Magnusdottir A., Ge C., Wieslander A.,
RA Martinez Molina D., Hogbom M.;
RT "The Mycobacterium tuberculosis very-long-chain fatty acyl-CoA synthetase:
RT structural basis for housing lipid substrates longer than the enzyme.";
RL Structure 20:1062-1070(2012).
CC -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC composition and permeability of the envelope on its exposure to acidic
CC pH (PubMed:15937179). Catalyzes the activation of long-chain fatty
CC acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the
CC multifunctional polyketide synthase (PKS) type III for further chain
CC extension (PubMed:19182784, PubMed:20027301, PubMed:22560731). It has
CC preference for the fatty acid with long chain length in the following
CC order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic
CC acid (C16) (PubMed:20027301). {ECO:0000269|PubMed:15937179,
CC ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20027301,
CC ECO:0000269|PubMed:22560731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20027301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexacosanoate = AMP + diphosphate + hexacosanoyl-
CC CoA; Xref=Rhea:RHEA:43748, ChEBI:CHEBI:30616, ChEBI:CHEBI:31013,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:20027301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43749;
CC Evidence={ECO:0000269|PubMed:20027301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:20027301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:20027301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784,
CC ECO:0000269|PubMed:20027301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20027301};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000269|PubMed:19182784};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for CoA (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC KM=0.11 mM for CoASH (at pH 8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC KM=19.79 uM for palmitic acid (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC KM=0.23 mM for ATP (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC KM=0.25 mM for ATP (at pH 8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC Vmax=14.62 pmol/min/ug enzyme (at pH 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20027301, ECO:0000269|PubMed:22206988};
CC Note=kcat is 0.03 sec(-1) for palmitic acid (at pH 8 and at 37
CC degrees Celsius).;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20027301}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22560731};
CC Peripheral membrane protein {ECO:0000269|PubMed:22560731}.
CC Note=Membrane-associated through distinctive regions rich in arginine
CC and aromatic residues. {ECO:0000269|PubMed:22560731}.
CC -!- INDUCTION: Expression is controlled by VirS. Induced at acidic pH and
CC in macrophages. {ECO:0000269|PubMed:14568148}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the mymA operon causes altered
CC cell wall structure, reduced contents and altered composition of
CC mycolic acids along with the accumulation of saturated C24 and C26
CC fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC acidic pH. Also impairs ability to survive in macrophages.
CC {ECO:0000269|PubMed:15937179, ECO:0000269|PubMed:16893682}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45898.1; -; Genomic_DNA.
DR PIR; E70853; E70853.
DR RefSeq; NP_217605.1; NC_000962.3.
DR RefSeq; WP_003416081.1; NZ_NVQJ01000011.1.
DR PDB; 3R44; X-ray; 1.80 A; A=1-503.
DR PDB; 3T5B; X-ray; 2.35 A; A=1-396.
DR PDB; 3T5C; X-ray; 2.09 A; A/B=1-396.
DR PDBsum; 3R44; -.
DR PDBsum; 3T5B; -.
DR PDBsum; 3T5C; -.
DR AlphaFoldDB; P9WQ37; -.
DR SMR; P9WQ37; -.
DR STRING; 83332.Rv3089; -.
DR SwissLipids; SLP:000000980; -.
DR PaxDb; P9WQ37; -.
DR GeneID; 888666; -.
DR KEGG; mtu:Rv3089; -.
DR TubercuList; Rv3089; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; TPSDWAW; -.
DR PhylomeDB; P9WQ37; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IDA:MTBBASE.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010447; P:response to acidic pH; IEP:MTBBASE.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome.
FT CHAIN 1..503
FT /note="Long-chain-fatty-acid--CoA ligase FadD13"
FT /id="PRO_0000420960"
FT SITE 9
FT /note="Membrane interaction"
FT /evidence="ECO:0000305|PubMed:22560731"
FT SITE 17
FT /note="Membrane interaction"
FT /evidence="ECO:0000305|PubMed:22560731"
FT SITE 195
FT /note="Membrane interaction"
FT /evidence="ECO:0000305|PubMed:22560731"
FT SITE 197
FT /note="Membrane interaction"
FT /evidence="ECO:0000305|PubMed:22560731"
FT SITE 214
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000305|PubMed:22206988"
FT SITE 244
FT /note="Membrane interaction"
FT /evidence="ECO:0000305|PubMed:22560731"
FT SITE 302
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000305|PubMed:22206988"
FT MUTAGEN 9
FT /note="R->A: Alteration of the strength of the membrane
FT binding; when associated with A-9; A-195; A-197 and A-244."
FT /evidence="ECO:0000269|PubMed:22560731"
FT MUTAGEN 17
FT /note="R->A: Alteration of the strength of the membrane
FT binding; when associated with A-9; A-17; A-197 and A-244."
FT /evidence="ECO:0000269|PubMed:22560731"
FT MUTAGEN 172
FT /note="K->A: Slight reduction of the fatty acyl-CoA ligase
FT activity. Slight increase of susceptibility to
FT proteolysis."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 195
FT /note="R->A: Alteration of the strength of the membrane
FT binding; when associated with A-9; A-17; A-197 and A-244."
FT /evidence="ECO:0000269|PubMed:22560731"
FT MUTAGEN 197
FT /note="R->A: Alteration of the strength of the membrane
FT binding; when associated with A-9; A-17; A-195 and A-244."
FT /evidence="ECO:0000269|PubMed:22560731"
FT MUTAGEN 209
FT /note="V->D: Strong reduction of the fatty acyl-CoA ligase
FT activity. No significant change in the total expression
FT level, however the cytoplasmic expression is reduced.
FT Slight increase of susceptibility to proteolysis."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 211
FT /note="A->G: Slight increase of the fatty acyl-CoA ligase
FT activity. Reduced rate of proteolytic degradation."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 214
FT /note="T->W: Shows a marked decrease in the activity with
FT lauric and palmitic acid (C12 and C16 fatty acid) with a
FT simultaneous increase in the activity with caprylic acid
FT (C8 fatty acid)."
FT /evidence="ECO:0000269|PubMed:22206988"
FT MUTAGEN 244
FT /note="R->A: Alteration of the strength of the membrane
FT binding; when associated with A-17; A-195; A-195 and A-
FT 197."
FT /evidence="ECO:0000269|PubMed:22560731"
FT MUTAGEN 302
FT /note="A->G: Slight increase of the fatty acyl-CoA ligase
FT activity. Reduced rate of proteolytic degradation."
FT /evidence="ECO:0000269|PubMed:20027301,
FT ECO:0000269|PubMed:22206988"
FT MUTAGEN 302
FT /note="A->W: Does not show activity with small, medium or
FT long acyl chains."
FT /evidence="ECO:0000269|PubMed:20027301,
FT ECO:0000269|PubMed:22206988"
FT MUTAGEN 377
FT /note="W->A: Strong reduction of the fatty acyl-CoA ligase
FT activity. Enhanced affinity towards palmitic acid binding.
FT No significant change in the total expression level,
FT however the cytoplasmic expression is low. Slight increase
FT of susceptibility to proteolysis."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 382
FT /note="D->A: Strong reduction of the fatty acyl-CoA ligase
FT activity. No significant change in the total expression
FT level, however the cytoplasmic expression is reduced."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 397
FT /note="R->A: Reduction of binding affinity for fatty
FT acids."
FT /evidence="ECO:0000269|PubMed:20454815"
FT MUTAGEN 404
FT /note="S->A: Slight reduction of the fatty acyl-CoA ligase
FT activity. Enhanced affinity towards palmitic acid binding."
FT /evidence="ECO:0000269|PubMed:20027301"
FT MUTAGEN 406
FT /note="G->L: No effect on the formation of acyl-adenylate
FT intermediate. However, it shows very poor catalytic
FT efficiency to form acyl-CoA."
FT /evidence="ECO:0000269|PubMed:22206988"
FT MUTAGEN 487
FT /note="K->A: Strong reduction of the fatty acyl-CoA ligase
FT activity. Reduction of binding affinity for ATP."
FT /evidence="ECO:0000269|PubMed:20027301,
FT ECO:0000269|PubMed:20454815, ECO:0000269|PubMed:22206988"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3R44"
FT TURN 318..323
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 343..355
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 424..434
FT /evidence="ECO:0007829|PDB:3R44"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 438..447
FT /evidence="ECO:0007829|PDB:3R44"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 454..464
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3R44"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:3R44"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:3R44"
SQ SEQUENCE 503 AA; 54459 MW; B4CF011549E7B620 CRC64;
MKNIGWMLRQ RATVSPRLQA YVEPSTDVRM TYAQMNALAN RCADVLTALG IAKGDRVALL
MPNSVEFCCL FYGAAKLGAV AVPINTRLAA PEVSFILSDS GSKVVIYGAP SAPVIDAIRA
QADPPGTVTD WIGADSLAER LRSAAADEPA VECGGDDNLF IMYTSGTTGH PKGVVHTHES
VHSAASSWAS TIDVRYRDRL LLPLPMFHVA ALTTVIFSAM RGVTLISMPQ FDATKVWSLI
VEERVCIGGA VPAILNFMRQ VPEFAELDAP DFRYFITGGA PMPEALIKIY AAKNIEVVQG
YALTESCGGG TLLLSEDALR KAGSAGRATM FTDVAVRGDD GVIREHGEGE VVIKSDILLK
EYWNRPEATR DAFDNGWFRT GDIGEIDDEG YLYIKDRLKD MIISGGENVY PAEIESVIIG
VPGVSEVAVI GLPDEKWGEI AAAIVVADQN EVSEQQIVEY CGTRLARYKL PKKVIFAEAI
PRNPTGKILK TVLREQYSAT VPK
