PANC_MYCTU
ID PANC_MYCTU Reviewed; 309 AA.
AC P9WIL5; L0TG74; O06280; P0A5R0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Pantothenate synthetase;
DE Short=PS;
DE EC=6.3.2.1;
DE AltName: Full=Pantoate--beta-alanine ligase;
DE AltName: Full=Pantoate-activating enzyme;
GN Name=panC; OrderedLocusNames=Rv3602c; ORFNames=MTCY07H7B.20;
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 PROTEIN SEQUENCE OF 2-11, FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=11669627; DOI=10.1021/bi011522+;
RA Zheng R., Blanchard J.S.;
RT "Steady-state and pre-steady-state kinetic analysis of Mycobacterium
RT tuberculosis pantothenate synthetase.";
RL Biochemistry 40:12904-12912(2001).
RN [3]
RP DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=H37Rv;
RX PubMed=12219086; DOI=10.1038/nm765;
RA Sambandamurthy V.K., Wang X., Chen B., Russell R.G., Derrick S.,
RA Collins F.M., Morris S.L., Jacobs W.R. Jr.;
RT "A pantothenate auxotroph of Mycobacterium tuberculosis is highly
RT attenuated and protects mice against tuberculosis.";
RL Nat. Med. 8:1171-1174(2002).
RN [4]
RP MUTAGENESIS OF HIS-44; HIS-47; ASN-69; GLN-72; LYS-160 AND GLN-164, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15170354; DOI=10.1021/bi049676n;
RA Zheng R., Dam T.K., Brewer C.F., Blanchard J.S.;
RT "Active site residues in Mycobacterium tuberculosis pantothenate synthetase
RT required in the formation and stabilization of the adenylate
RT intermediate.";
RL Biochemistry 43:7171-7178(2004).
RN [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=25246400; DOI=10.1128/aac.04028-14;
RA Dillon N.A., Peterson N.D., Rosen B.C., Baughn A.D.;
RT "Pantothenate and pantetheine antagonize the antitubercular activity of
RT pyrazinamide.";
RL Antimicrob. Agents Chemother. 58:7258-7263(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-300 OF MUTANT GLY-77 IN COMPLEX
RP WITH SUBSTRATES; ATP ANALOG AND MAGNESIUM ION, MUTAGENESIS OF GLU-77,
RP CATALYTIC ACTIVITY, CATALYTIC MECHANISM, AND SUBUNIT.
RX PubMed=12717031; DOI=10.1110/ps.0241803;
RA Wang S., Eisenberg D.;
RT "Crystal structures of a pantothenate synthetase from M. tuberculosis and
RT its complexes with substrates and a reaction intermediate.";
RL Protein Sci. 12:1097-1108(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; MAGNESIUM
RP ION AND ATP, CATALYTIC MECHANISM, AND SUBUNIT.
RX PubMed=16460002; DOI=10.1021/bi051873e;
RA Wang S., Eisenberg D.;
RT "Crystal structure of the pantothenate synthetase from Mycobacterium
RT tuberculosis, snapshots of the enzyme in action.";
RL Biochemistry 45:1554-1561(2006).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000269|PubMed:11669627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC Evidence={ECO:0000269|PubMed:12717031};
CC -!- ACTIVITY REGULATION: Pantothenate exhibits uncompetitive inhibition
CC toward both D-pantoate and ATP, and non-competitive inhibition toward
CC beta-alanine. AMPCPP exhibits competitive inhibition toward ATP,
CC uncompetitive inhibition toward beta-alanine, and non-competitive
CC inhibition toward D-pantoate. The enzyme is most active in the presence
CC of magnesium or manganese. Other divalent cations (cobalt, nickel,
CC zinc) are less effective. {ECO:0000269|PubMed:11669627}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for D-pantoate {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=800 uM for beta-alanine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=2600 uM for ATP {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=25.4 mM for 2-mercaptoethylamine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=36 mM for carbamate {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=72 mM for 5-aminovalerate {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=79 mM for methylamine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=84 mM for glycine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=93 mM for ethylamine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=103 mM for taurine {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=108 mM for glycolate {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=335 mM for gamma-aminobutyrate {ECO:0000269|PubMed:11669627,
CC ECO:0000269|PubMed:15170354};
CC KM=580 mM for gamma-amino-beta-hydroxybutyrate
CC {ECO:0000269|PubMed:11669627, ECO:0000269|PubMed:15170354};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=32545; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11669627};
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of panD and panC gives a
CC mutant unable to grow in the absence of panothenate. The double mutant
CC has a highly attenuated disease response in BALB/c and SCID mice;
CC immunocompromised BALB/c SCID mice survive on average 36 weeks as
CC opposed to 5 weeks for mice infected with wild-type bacteria, while
CC immunocompetent BALB/c mice survive indefinitely. In wild-type mice
CC bacteria grow for 3 weeks then undergo a steady decline, bacteria
CC persist over 8 months in SCID mice (PubMed:12219086). The double mutant
CC is sensitive to PZA but not POA in liquid culture, beta-alanine but not
CC pantothenate antagonize the effect of PZA at pH 5.8 (PubMed:25246400).
CC {ECO:0000269|PubMed:12219086, ECO:0000269|PubMed:25246400}.
CC -!- BIOTECHNOLOGY: Subcutaneous immunization with the double panD and panC
CC bacterial disruption mutant protects mice for over a year against
CC subsequent virulent M.tuberculosis (strain Erdman) infections; mice
CC show mild lung inflammation and fibrosis despite a chronic bacterila
CC infection. This is a promising attenuated vaccine strain.
CC {ECO:0000269|PubMed:12219086}.
CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC mechanism.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46425.1; -; Genomic_DNA.
DR PIR; C70955; C70955.
DR RefSeq; NP_218119.1; NC_000962.3.
DR RefSeq; WP_003419526.1; NZ_NVQJ01000056.1.
DR PDB; 1MOP; X-ray; 1.60 A; A/B=3-300.
DR PDB; 1N2B; X-ray; 1.70 A; A/B=3-300.
DR PDB; 1N2E; X-ray; 1.60 A; A/B=3-300.
DR PDB; 1N2G; X-ray; 1.80 A; A/B=3-300.
DR PDB; 1N2H; X-ray; 2.00 A; A/B=3-300.
DR PDB; 1N2I; X-ray; 1.70 A; A/B=3-300.
DR PDB; 1N2J; X-ray; 1.80 A; A/B=3-300.
DR PDB; 1N2O; X-ray; 2.10 A; A/B=3-300.
DR PDB; 2A7X; X-ray; 1.70 A; A=3-300.
DR PDB; 2A84; X-ray; 1.55 A; A=3-300.
DR PDB; 2A86; X-ray; 1.85 A; A/B=3-300.
DR PDB; 2A88; X-ray; 1.70 A; A=3-300.
DR PDB; 3COV; X-ray; 1.50 A; A/B=3-300.
DR PDB; 3COW; X-ray; 1.80 A; A/B=3-300.
DR PDB; 3COY; X-ray; 2.03 A; A/B=3-300.
DR PDB; 3COZ; X-ray; 2.00 A; A/B=3-300.
DR PDB; 3IMC; X-ray; 1.60 A; A/B=3-300.
DR PDB; 3IME; X-ray; 2.39 A; A/B=3-300.
DR PDB; 3IMG; X-ray; 1.80 A; A/B=3-300.
DR PDB; 3IOB; X-ray; 1.80 A; A/B=3-300.
DR PDB; 3IOC; X-ray; 2.50 A; A/B=3-300.
DR PDB; 3IOD; X-ray; 1.75 A; A/B=3-300.
DR PDB; 3IOE; X-ray; 1.95 A; A/B=3-300.
DR PDB; 3ISJ; X-ray; 2.20 A; A/B=3-300.
DR PDB; 3IUB; X-ray; 1.50 A; A/B=3-301.
DR PDB; 3IUE; X-ray; 1.73 A; A/B=3-301.
DR PDB; 3IVC; X-ray; 2.13 A; A/B=3-301.
DR PDB; 3IVG; X-ray; 1.95 A; A/B=3-301.
DR PDB; 3IVX; X-ray; 1.73 A; A/B=3-301.
DR PDB; 3LE8; X-ray; 1.70 A; A/B=3-300.
DR PDB; 4DDH; X-ray; 2.07 A; A/B=3-301.
DR PDB; 4DDK; X-ray; 1.75 A; A/B=3-301.
DR PDB; 4DDM; X-ray; 1.83 A; A/B=3-301.
DR PDB; 4DE5; X-ray; 2.25 A; A/B=3-301.
DR PDB; 4EF6; X-ray; 1.94 A; A/B=3-300.
DR PDB; 4EFK; X-ray; 1.70 A; A/B=3-300.
DR PDB; 4FZJ; X-ray; 1.63 A; A/B=3-301.
DR PDB; 4G5F; X-ray; 2.33 A; A/B=3-309.
DR PDB; 4G5Y; X-ray; 1.80 A; A/B=3-300.
DR PDBsum; 1MOP; -.
DR PDBsum; 1N2B; -.
DR PDBsum; 1N2E; -.
DR PDBsum; 1N2G; -.
DR PDBsum; 1N2H; -.
DR PDBsum; 1N2I; -.
DR PDBsum; 1N2J; -.
DR PDBsum; 1N2O; -.
DR PDBsum; 2A7X; -.
DR PDBsum; 2A84; -.
DR PDBsum; 2A86; -.
DR PDBsum; 2A88; -.
DR PDBsum; 3COV; -.
DR PDBsum; 3COW; -.
DR PDBsum; 3COY; -.
DR PDBsum; 3COZ; -.
DR PDBsum; 3IMC; -.
DR PDBsum; 3IME; -.
DR PDBsum; 3IMG; -.
DR PDBsum; 3IOB; -.
DR PDBsum; 3IOC; -.
DR PDBsum; 3IOD; -.
DR PDBsum; 3IOE; -.
DR PDBsum; 3ISJ; -.
DR PDBsum; 3IUB; -.
DR PDBsum; 3IUE; -.
DR PDBsum; 3IVC; -.
DR PDBsum; 3IVG; -.
DR PDBsum; 3IVX; -.
DR PDBsum; 3LE8; -.
DR PDBsum; 4DDH; -.
DR PDBsum; 4DDK; -.
DR PDBsum; 4DDM; -.
DR PDBsum; 4DE5; -.
DR PDBsum; 4EF6; -.
DR PDBsum; 4EFK; -.
DR PDBsum; 4FZJ; -.
DR PDBsum; 4G5F; -.
DR PDBsum; 4G5Y; -.
DR AlphaFoldDB; P9WIL5; -.
DR SMR; P9WIL5; -.
DR STRING; 83332.Rv3602c; -.
DR BindingDB; P9WIL5; -.
DR ChEMBL; CHEMBL6069; -.
DR DrugBank; DB01930; 2,4-Dihydroxy-3,3-Dimethyl-Butyrate.
DR DrugBank; DB02596; alpha,beta-Methyleneadenosine 5'-triphosphate.
DR DrugBank; DB03107; beta-Alanine.
DR DrugBank; DB02694; Pantoyl Adenylate.
DR iPTMnet; P9WIL5; -.
DR PaxDb; P9WIL5; -.
DR DNASU; 885459; -.
DR GeneID; 885459; -.
DR KEGG; mtu:Rv3602c; -.
DR TubercuList; Rv3602c; -.
DR eggNOG; COG0414; Bacteria.
DR OMA; CNHKLEP; -.
DR PhylomeDB; P9WIL5; -.
DR BRENDA; 6.3.2.1; 3445.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IDA:MTBBASE.
DR GO; GO:0019482; P:beta-alanine metabolic process; IDA:MTBBASE.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IDA:MTBBASE.
DR CDD; cd00560; PanC; 1.
DR Gene3D; 3.30.1300.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00158; PanC; 1.
DR InterPro; IPR003721; Pantoate_ligase.
DR InterPro; IPR042176; Pantoate_ligase_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR Pfam; PF02569; Pantoate_ligase; 1.
DR TIGRFAMs; TIGR00018; panC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pantothenate biosynthesis; Reference proteome;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11669627,
FT ECO:0007744|PubMed:21969609"
FT CHAIN 2..309
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128245"
FT ACT_SITE 47
FT /note="Proton donor"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16460002"
FT BINDING 72
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT BINDING 72
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 158..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16460002"
FT BINDING 164
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16460002"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16460002"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MUTAGEN 44
FT /note="H->A: More than 1000-fold reduction in activity and
FT 52-fold decrease in adenylate formation."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 47
FT /note="H->A: More than 1000-fold reduction in activity and
FT 60-fold decrease in adenylate formation. 10-fold decrease
FT in the affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 69
FT /note="N->A: More than 1000-fold reduction in activity and
FT 50-fold decrease in adenylate formation."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 72
FT /note="Q->A: More than 1000-fold reduction in activity and
FT 45-fold decrease in adenylate formation."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 77
FT /note="E->G: No effect."
FT /evidence="ECO:0000269|PubMed:12717031"
FT MUTAGEN 160
FT /note="K->A: More than 1000-fold reduction in activity and
FT 50-fold decrease in the affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 160
FT /note="K->C: More than 1000-fold reduction in activity and
FT 120-fold decrease in adenylate formation. The enzymatic
FT activity and the affinity for beta-alanine can be increased
FT 10- and 3-fold, respectively, by alkylation of cysteine of
FT mutant C-160."
FT /evidence="ECO:0000269|PubMed:15170354"
FT MUTAGEN 164
FT /note="Q->A: 50-fold reduction in activity and slight
FT reduction in the affinity for beta-alanine. 30- and 40-fold
FT decrease in adenylate formation and pantothenate formation,
FT respectively."
FT /evidence="ECO:0000269|PubMed:15170354"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1MOP"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 264..274
FT /evidence="ECO:0007829|PDB:3COV"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:3COV"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3IVC"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3IVC"
SQ SEQUENCE 309 AA; 32678 MW; EB51DBE3485F970A CRC64;
MTIPAFHPGE LNVYSAPGDV ADVSRALRLT GRRVMLVPTM GALHEGHLAL VRAAKRVPGS
VVVVSIFVNP MQFGAGEDLD AYPRTPDDDL AQLRAEGVEI AFTPTTAAMY PDGLRTTVQP
GPLAAELEGG PRPTHFAGVL TVVLKLLQIV RPDRVFFGEK DYQQLVLIRQ LVADFNLDVA
VVGVPTVREA DGLAMSSRNR YLDPAQRAAA VALSAALTAA AHAATAGAQA ALDAARAVLD
AAPGVAVDYL ELRDIGLGPM PLNGSGRLLV AARLGTTRLL DNIAIEIGTF AGTDRPDGYR
AILESHWRN
