FADE5_MYCTU
ID FADE5_MYCTU Reviewed; 611 AA.
AC O53666; I6Y372; Q7DA67;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Broad-specificity linear acyl-CoA dehydrogenase FadE5 {ECO:0000305};
DE AltName: Full=Long-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.8 {ECO:0000269|PubMed:32601219};
DE AltName: Full=Medium-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.7 {ECO:0000269|PubMed:32601219};
DE AltName: Full=Short-chain-acyl-CoA dehydrogenase {ECO:0000305};
DE EC=1.3.8.1 {ECO:0000269|PubMed:32601219};
GN Name=fadE5 {ECO:0000303|PubMed:32601219};
GN OrderedLocusNames=Rv0244c {ECO:0000312|EMBL:CCP42973.1};
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 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 [3] {ECO:0007744|PDB:6KSE}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-447 IN COMPLEX WITH
RP FAD AND OCTADECANOYL-COA, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-171; LYS-225; PHE-294; ARG-301; GLU-447 AND ARG-460.
RC STRAIN=H37Rv;
RX PubMed=32601219; DOI=10.1073/pnas.2002835117;
RA Chen X., Chen J., Yan B., Zhang W., Guddat L.W., Liu X., Rao Z.;
RT "Structural basis for the broad substrate specificity of two acyl-CoA
RT dehydrogenases FadE5 from mycobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:16324-16332(2020).
CC -!- FUNCTION: Acyl-CoA dehydrogenase that exhibits broad specificity for
CC linear acyl-CoA substrates, with a preference for long-chain
CC substrates. {ECO:0000269|PubMed:32601219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC ChEBI:CHEBI:87488; EC=1.3.8.1;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:32601219};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:32601219};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=358.7 uM for butanoyl-CoA {ECO:0000269|PubMed:32601219};
CC KM=353.0 uM for hexanoyl-CoA {ECO:0000269|PubMed:32601219};
CC KM=162.5 uM for octadecanoyl-CoA {ECO:0000269|PubMed:32601219};
CC Note=kcat is 1.07 sec(-1) with butanoyl-CoA as substrate. kcat is
CC 0.80 sec(-1) with hexanoyl-CoA as substrate. kcat is 0.61 sec(-1)
CC with octadecanoyl-CoA as substrate. {ECO:0000269|PubMed:32601219};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:32601219}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32601219}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42973.1; -; Genomic_DNA.
DR RefSeq; NP_214758.1; NC_000962.3.
DR RefSeq; WP_003401312.1; NZ_NVQJ01000001.1.
DR PDB; 6KSE; X-ray; 2.00 A; A/B=1-611.
DR PDBsum; 6KSE; -.
DR AlphaFoldDB; O53666; -.
DR SMR; O53666; -.
DR STRING; 83332.Rv0244c; -.
DR PaxDb; O53666; -.
DR PRIDE; O53666; -.
DR DNASU; 886698; -.
DR GeneID; 886698; -.
DR KEGG; mtu:Rv0244c; -.
DR PATRIC; fig|83332.111.peg.277; -.
DR TubercuList; Rv0244c; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; MWAKMAK; -.
DR PhylomeDB; O53666; -.
DR BioCyc; MetaCyc:G185E-4366-MON; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR CDD; cd01153; ACAD_fadE5; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034188; FadE5-like.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..611
FT /note="Broad-specificity linear acyl-CoA dehydrogenase
FT FadE5"
FT /id="PRO_0000452498"
FT ACT_SITE 447
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:32601219"
FT BINDING 162..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 171
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 224..225
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 301
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 338
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 420..424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 447
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 456
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT BINDING 460..461
FT /ligand="a 2,3-saturated acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:65111"
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 171
FT /note="S->A: Decreases affinity for eicosanoyl-CoA; when
FT associated with A-447."
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 225
FT /note="K->A: Decreases affinity for eicosanoyl-CoA; when
FT associated with A-447."
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 294
FT /note="F->A: Increases affinity for eicosanoyl-CoA; when
FT associated with A-447."
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 301
FT /note="R->A: Increases affinity for eicosanoyl-CoA; when
FT associated with A-447."
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 447
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:32601219"
FT MUTAGEN 460
FT /note="R->A: Decreases affinity for eicosanoyl-CoA; when
FT associated with A-447."
FT /evidence="ECO:0000269|PubMed:32601219"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 289..325
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6KSE"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 349..373
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 389..421
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 460..467
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 468..481
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 491..517
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 525..560
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 565..584
FT /evidence="ECO:0007829|PDB:6KSE"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 588..597
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:6KSE"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:6KSE"
SQ SEQUENCE 611 AA; 66046 MW; 768532A48AD4875C CRC64;
MSHYRSNVRD QVFNLFEVLG VDKALGHGEF SDVDVDTARD MLAEVSRLAE GPVAESFVEG
DRNPPVFDPK THSVMLPESF KKSVNAMLEA GWDKVGIDEA LGGMPMPKAV VWALHEHILG
ANPAVWMYAG GAGFAQILYH LGTEEQKKWA VLAAERGWGS TMVLTEPDAG SDVGAARTKA
VQQADGSWHI DGVKRFITSG DSGDLFENIF HLVLARPEGA GPGTKGLSLY FVPKFLFDVE
TGEPGERNGV FVTNVEHKMG LKVSATCELA FGQHGVPAKG WLVGEVHNGI AQMFEVIEQA
RMMVGTKAIA TLSTGYLNAL QYAKSRVQGA DLTQMTDKTA PRVTITHHPD VRRSLMTQKA
YAEGLRALYL YTATFQDAAV AEVVHGVDAK LAVKVNDLML PVVKGVGSEQ AYAKLTESLQ
TLGGSGFLQD YPIEQYIRDA KIDSLYEGTT AIQAQDFFFR KIVRDKGVAL AHVSGQIQEF
VDSGAGNGRL KTERALLAKA LTDVQGMAAA LTGYLMAAQQ DVTSLYKVGL GSVRFLMSVG
DLIIGWLLQR QAAVAVAALD AGATGDERSF YEGKVAVASF FAKNFLPLLT STREVIETLD
NDIMELDEAA F
