IMDH_MYCTU
ID IMDH_MYCTU Reviewed; 529 AA.
AC P9WKI7; L0TCG3; P65167; Q50715;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964};
DE Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964};
DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:20491506, ECO:0000269|PubMed:21081761};
DE AltName: Full=IMPDH2 {ECO:0000303|PubMed:26440283};
GN Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964};
GN Synonyms=guaB2 {ECO:0000303|PubMed:20491506, ECO:0000303|PubMed:21081761,
GN ECO:0000312|EMBL:CCP46233.1}; OrderedLocusNames=Rv3411c;
GN ORFNames=MTCY78.17;
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA Sassetti C.M., Boyd D.H., Rubin E.J.;
RT "Genes required for mycobacterial growth defined by high density
RT mutagenesis.";
RL Mol. Microbiol. 48:77-84(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=H37Rv;
RX PubMed=20491506; DOI=10.1021/jm100424m;
RA Chen L., Wilson D.J., Xu Y., Aldrich C.C., Felczak K., Sham Y.Y.,
RA Pankiewicz K.W.;
RT "Triazole-linked inhibitors of inosine monophosphate dehydrogenase from
RT human and Mycobacterium tuberculosis.";
RL J. Med. Chem. 53:4768-4778(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21081761; DOI=10.1099/mic.0.042549-0;
RA Usha V., Gurcha S.S., Lovering A.L., Lloyd A.J., Papaemmanouil A.,
RA Reynolds R.C., Besra G.S.;
RT "Identification of novel diphenyl urea inhibitors of Mt-GuaB2 active
RT against Mycobacterium tuberculosis.";
RL Microbiology 157:290-299(2011).
RN [5]
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 [6]
RP ACTIVITY REGULATION.
RC STRAIN=H37Rv;
RX PubMed=22479467; DOI=10.1371/journal.pone.0033886;
RA Usha V., Hobrath J.V., Gurcha S.S., Reynolds R.C., Besra G.S.;
RT "Identification of novel Mt-Guab2 inhibitor series active against M.
RT tuberculosis.";
RL PLoS ONE 7:E33886-E33886(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-125 AND 253-529 IN COMPLEXES
RP WITH POTASSIUM; XMP; NAD(+); IMP AND INHIBITORS WITH ANTITUBERCULAR
RP ACTIVITY, ACTIVITY REGULATION, REACTION MECHANISM, ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=26440283; DOI=10.1371/journal.pone.0138976;
RA Makowska-Grzyska M., Kim Y., Gorla S.K., Wei Y., Mandapati K., Zhang M.,
RA Maltseva N., Modi G., Boshoff H.I., Gu M., Aldrich C., Cuny G.D.,
RA Hedstrom L., Joachimiak A.;
RT "Mycobacterium tuberculosis IMPDH in complexes with substrates, products
RT and antitubercular compounds.";
RL PLoS ONE 10:E0138976-E0138976(2015).
CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to
CC xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC step in the de novo synthesis of guanine nucleotides, and therefore
CC plays an important role in the regulation of cell growth
CC (PubMed:20491506, PubMed:21081761). Does not catalyze the reverse
CC reaction, i.e. the conversion of XMP to IMP (PubMed:21081761). Appears
CC to be essential for the optimal growth of M.tuberculosis
CC (PubMed:12657046). {ECO:0000255|HAMAP-Rule:MF_01964,
CC ECO:0000269|PubMed:12657046, ECO:0000269|PubMed:20491506,
CC ECO:0000269|PubMed:21081761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964,
CC ECO:0000269|PubMed:20491506, ECO:0000269|PubMed:21081761};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01964,
CC ECO:0000269|PubMed:21081761};
CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC inhibitor that prevents formation of the closed enzyme conformation by
CC binding to the same site as the amobile flap. In contrast, mizoribine
CC monophosphate (MZP) is a competitive inhibitor that induces the closed
CC conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC bacterial IMPDH (By similarity). Inhibited by the products XMP and
CC NADH. Significantly inhibited in vitro by a panel of diphenyl urea-
CC based derivatives and a series of novel classes of inhibitors, which
CC are also potent anti-mycobacterial agents against M.tuberculosis and
CC M.smegmatis (PubMed:21081761) (PubMed:22479467). Is also inhibited by a
CC mycophenolic adenine dinucleotide (MAD) derivative in which a 1,2,3-
CC triazole linker was incorporated as isosteric replacement of the
CC pyrophosphate linker, thereby mimicking NAD (PubMed:20491506). Other
CC inhibitors with modular structures consisting of two aromatic moieties
CC connected by different linkers (such as urea and amide) have been
CC identified and shown to exhibit antitubercular activity
CC (PubMed:26440283). {ECO:0000255|HAMAP-Rule:MF_01964,
CC ECO:0000269|PubMed:20491506, ECO:0000269|PubMed:21081761,
CC ECO:0000269|PubMed:22479467, ECO:0000269|PubMed:26440283}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=78 uM for inosine 5'-phosphate {ECO:0000269|PubMed:20491506};
CC KM=1005 uM for NAD(+) {ECO:0000269|PubMed:20491506};
CC KM=128.1 uM for inosine 5'-phosphate {ECO:0000269|PubMed:21081761};
CC KM=610.5 uM for NAD(+) {ECO:0000269|PubMed:21081761};
CC Note=kcat is 0.53 sec(-1). {ECO:0000269|PubMed:20491506};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:21081761};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:21081761};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964,
CC ECO:0000305|PubMed:26440283}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display impaired growth.
CC {ECO:0000269|PubMed:12657046}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
CC Rule:MF_01964}.
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DR EMBL; AL123456; CCP46233.1; -; Genomic_DNA.
DR PIR; H70736; H70736.
DR RefSeq; NP_217928.1; NC_000962.3.
DR RefSeq; WP_003900682.1; NZ_NVQJ01000027.1.
DR PDB; 4ZQM; X-ray; 1.60 A; A=1-125, A=253-529.
DR PDB; 4ZQN; X-ray; 2.00 A; A=1-125, A=253-529.
DR PDB; 4ZQO; X-ray; 1.76 A; A=1-125, A=253-529.
DR PDB; 4ZQP; X-ray; 1.90 A; A=1-125, A=253-529.
DR PDB; 4ZQR; X-ray; 1.69 A; A/B/C/D=1-125, A/B/C/D=253-529.
DR PDB; 5UPU; X-ray; 2.90 A; A=1-125, A=256-529.
DR PDB; 5UPV; X-ray; 1.63 A; A=1-125, A=256-529.
DR PDBsum; 4ZQM; -.
DR PDBsum; 4ZQN; -.
DR PDBsum; 4ZQO; -.
DR PDBsum; 4ZQP; -.
DR PDBsum; 4ZQR; -.
DR PDBsum; 5UPU; -.
DR PDBsum; 5UPV; -.
DR AlphaFoldDB; P9WKI7; -.
DR SMR; P9WKI7; -.
DR STRING; 83332.Rv3411c; -.
DR BindingDB; P9WKI7; -.
DR ChEMBL; CHEMBL4295586; -.
DR PaxDb; P9WKI7; -.
DR DNASU; 887498; -.
DR GeneID; 45427407; -.
DR GeneID; 887498; -.
DR KEGG; mtu:Rv3411c; -.
DR TubercuList; Rv3411c; -.
DR eggNOG; COG0516; Bacteria.
DR eggNOG; COG0517; Bacteria.
DR OMA; MGYCGAK; -.
DR PhylomeDB; P9WKI7; -.
DR BRENDA; 1.1.1.205; 3445.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MTBBASE.
DR GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006204; P:IMP catabolic process; IDA:MTBBASE.
DR GO; GO:0097293; P:XMP biosynthetic process; IDA:MTBBASE.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01964; IMPDH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR11911; PTHR11911; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CBS domain; GMP biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..529
FT /note="Inosine-5'-monophosphate dehydrogenase"
FT /id="PRO_0000093702"
FT DOMAIN 129..185
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT DOMAIN 189..246
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT ACT_SITE 341
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000305|PubMed:26440283"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000305|PubMed:26440283"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26440283"
FT BINDING 334..336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 336
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 338
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 339
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 341
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26440283"
FT BINDING 374..376
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 397..398
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 421..425
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 458
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 458
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:26440283"
FT BINDING 511
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 512
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT BINDING 513
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964,
FT ECO:0000269|PubMed:26440283"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4ZQR"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4ZQM"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:4ZQM"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:4ZQM"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 470..488
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:4ZQM"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:4ZQM"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:4ZQR"
SQ SEQUENCE 529 AA; 54867 MW; 689A7C7C53993C0A CRC64;
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV LLLPAASDVV
PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA GGMGVLHRNL PVAEQAGQVE
MVKRSEAGMV TDPVTCRPDN TLAQVDALCA RFRISGLPVV DDDGALVGII TNRDMRFEVD
QSKQVAEVMT KAPLITAQEG VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE
QHPLATKDSD GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG APQITAILEA
VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL AGTAEAPGEL IFVNGKQYKS
YRGMGSLGAM RGRGGATSYS KDRYFADDAL SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG
LRAAMGYTGS PTIEVLQQAQ FVRITPAGLK ESHPHDVAMT VEAPNYYAR
