GGT_ECOLI
ID GGT_ECOLI Reviewed; 580 AA.
AC P18956; Q2M7B0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glutathione hydrolase proenzyme;
DE EC=3.4.19.13 {ECO:0000305|PubMed:2877974};
DE AltName: Full=Gamma-glutamyltranspeptidase proenzyme {ECO:0000303|PubMed:2570061};
DE Short=GGT;
DE EC=2.3.2.2 {ECO:0000269|PubMed:1360205};
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain;
DE Flags: Precursor;
GN Name=ggt; OrderedLocusNames=b3447, JW3412;
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 26-41 AND
RP 391-403.
RC STRAIN=K12;
RX PubMed=2570061; DOI=10.1128/jb.171.9.5169-5172.1989;
RA Suzuki H., Kumagai H., Echigo T., Tochikura T.;
RT "DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase
RT gene, ggt.";
RL J. Bacteriol. 171:5169-5172(1989).
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 [LARGE SCALE GENOMIC DNA] OF 1-362.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=2877974; DOI=10.1128/jb.168.3.1325-1331.1986;
RA Suzuki H., Kumagai H., Tochikura T.;
RT "gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and
RT properties.";
RL J. Bacteriol. 168:1325-1331(1986).
RN [6]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ARG-513
RP AND ARG-571, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=1360205; DOI=10.1016/0006-291x(92)91540-7;
RA Hashimoto W., Suzuki H., Nohara S., Kumagai H.;
RT "Escherichia coli gamma-glutamyltranspeptidase mutants deficient in
RT processing to subunits.";
RL Biochem. Biophys. Res. Commun. 189:173-178(1992).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8104180; DOI=10.1128/jb.175.18.6038-6040.1993;
RA Suzuki H., Hashimoto W., Kumagai H.;
RT "Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as
RT an amino acid source, for which gamma-glutamyltranspeptidase is
RT essential.";
RL J. Bacteriol. 175:6038-6040(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-580 IN COMPLEX WITH GLUTAMATE,
RP SUBUNIT, ACTIVE SITE, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=16618936; DOI=10.1073/pnas.0511020103;
RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.;
RT "Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli,
RT a key enzyme in glutathione metabolism, and its reaction intermediate.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6471-6476(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-580 OF MUTANT ALA-391,
RP SUBUNIT, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF THR-391.
RX PubMed=17135273; DOI=10.1074/jbc.m607490200;
RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.;
RT "Crystal structure of the gamma-glutamyltranspeptidase precursor protein
RT from Escherichia coli. Structural changes upon autocatalytic processing and
RT implications for the maturation mechanism.";
RL J. Biol. Chem. 282:2433-2439(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-580 IN COMPLEXES WITH
RP AZASERINE AND ACIVICIN, ACTIVE SITE, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=18555071; DOI=10.1016/j.jmb.2008.05.007;
RA Wada K., Hiratake J., Irie M., Okada T., Yamada C., Kumagai H., Suzuki H.,
RA Fukuyama K.;
RT "Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in
RT complex with azaserine and acivicin: novel mechanistic implication for
RT inhibition by glutamine antagonists.";
RL J. Mol. Biol. 380:361-372(2008).
CC -!- FUNCTION: Cleaves the gamma-glutamyl bond of periplasmic glutathione
CC (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl
CC compounds. The metabolism of glutathione releases free glutamate and
CC the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and
CC glycine by dipeptidases; it may function in amino acid uptake/salvage,
CC or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and
CC transpeptidation of many gamma-glutamyl compounds (including some D-
CC gamma-glutamyl substrates), with a preference for basic and aromatic
CC amino acids as acceptors (PubMed:2877974). The KM values for gamma-
CC glutamyl acceptors are so high that it has been proposed
CC transpeptidation is not the physiological role in E.coli
CC (PubMed:2877974, PubMed:8104180). {ECO:0000269|PubMed:2877974,
CC ECO:0000305|PubMed:8104180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000269|PubMed:1360205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC Evidence={ECO:0000305|PubMed:2877974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC Evidence={ECO:0000305|PubMed:2877974};
CC -!- ACTIVITY REGULATION: Transferase and hydrolase activities are inhibited
CC by L-Ala and L-Gln, and also by GGT affinity labeling reagents such as
CC azaserine and 6-diazo-5-oxo-nor-leucine. {ECO:0000269|PubMed:2877974}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for glutathione transfer to glycylglycine (gly-gly)
CC {ECO:0000269|PubMed:2877974};
CC KM=35 uM for gamma-glutamyl-p-nitroanilide (gamma-GpNA) transfer to
CC gly-gly {ECO:0000269|PubMed:2877974};
CC KM=29 uM for glutathione hydrolysis {ECO:0000269|PubMed:2877974};
CC KM=68 uM for gamma-GpNA hydrolysis {ECO:0000269|PubMed:2877974};
CC pH dependence:
CC Optimum pH is 8.73 for transfer of p-nitroanilide from gamma-GpNA to
CC gly-gly and 9.25 for hydrolysis of gamma-GpNA.
CC {ECO:0000269|PubMed:2877974};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius for both transferase and
CC hydrolase activities. {ECO:0000269|PubMed:2877974};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide.
CC {ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936,
CC ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071,
CC ECO:0000269|PubMed:2877974}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1360205,
CC ECO:0000269|PubMed:2877974}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936,
CC ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071,
CC ECO:0000269|PubMed:2570061}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth using exogenous gamma-glutamyl
CC peptides as amino acid sources. {ECO:0000269|PubMed:8104180}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M28722; AAA23869.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58245.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76472.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77846.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18422.1; -; Genomic_DNA.
DR PIR; JV0028; EKECEX.
DR RefSeq; NP_417904.1; NC_000913.3.
DR RefSeq; WP_000595082.1; NZ_SSZK01000008.1.
DR PDB; 2DBU; X-ray; 1.95 A; A/C=25-390, B/D=391-580.
DR PDB; 2DBW; X-ray; 1.80 A; A/C=25-390, B/D=391-580.
DR PDB; 2DBX; X-ray; 1.70 A; A/C=25-390, B/D=391-580.
DR PDB; 2DG5; X-ray; 1.60 A; A/C=25-390, B/D=391-580.
DR PDB; 2E0W; X-ray; 2.55 A; A/B=25-580.
DR PDB; 2E0X; X-ray; 1.95 A; A/C=25-390, B/D=391-580.
DR PDB; 2E0Y; X-ray; 2.02 A; A/C=25-390, B/D=391-580.
DR PDB; 2Z8I; X-ray; 1.65 A; A/C=25-390, B/D=391-580.
DR PDB; 2Z8J; X-ray; 2.05 A; A/C=25-390, B/D=391-580.
DR PDB; 2Z8K; X-ray; 1.65 A; A/C=25-390, B/D=391-580.
DR PDB; 5B5T; X-ray; 1.70 A; A/C=25-390, B/D=391-580.
DR PDBsum; 2DBU; -.
DR PDBsum; 2DBW; -.
DR PDBsum; 2DBX; -.
DR PDBsum; 2DG5; -.
DR PDBsum; 2E0W; -.
DR PDBsum; 2E0X; -.
DR PDBsum; 2E0Y; -.
DR PDBsum; 2Z8I; -.
DR PDBsum; 2Z8J; -.
DR PDBsum; 2Z8K; -.
DR PDBsum; 5B5T; -.
DR AlphaFoldDB; P18956; -.
DR SMR; P18956; -.
DR BioGRID; 4261666; 434.
DR DIP; DIP-9758N; -.
DR IntAct; P18956; 1.
DR STRING; 511145.b3447; -.
DR MEROPS; T03.001; -.
DR jPOST; P18956; -.
DR PaxDb; P18956; -.
DR PRIDE; P18956; -.
DR EnsemblBacteria; AAC76472; AAC76472; b3447.
DR EnsemblBacteria; BAE77846; BAE77846; BAE77846.
DR GeneID; 947947; -.
DR KEGG; ecj:JW3412; -.
DR KEGG; eco:b3447; -.
DR PATRIC; fig|511145.12.peg.3544; -.
DR EchoBASE; EB0369; -.
DR eggNOG; COG0405; Bacteria.
DR HOGENOM; CLU_014813_0_3_6; -.
DR InParanoid; P18956; -.
DR OMA; KATKNMF; -.
DR PhylomeDB; P18956; -.
DR BioCyc; EcoCyc:EG10374-MON; -.
DR BioCyc; MetaCyc:EG10374-MON; -.
DR BRENDA; 2.3.2.2; 2026.
DR BRENDA; 3.4.19.13; 2026.
DR SABIO-RK; P18956; -.
DR UniPathway; UPA00204; -.
DR EvolutionaryTrace; P18956; -.
DR PRO; PR:P18956; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IDA:EcoCyc.
DR GO; GO:0036374; F:glutathione hydrolase activity; IDA:EcoCyc.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043102; P:amino acid salvage; IMP:EcoCyc.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR GO; GO:0097264; P:self proteolysis; IDA:EcoCyc.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing;
KW Glutathione biosynthesis; Hydrolase; Periplasm; Protease;
KW Reference proteome; Signal; Transferase; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2570061"
FT CHAIN 26..390
FT /note="Glutathione hydrolase large chain"
FT /id="PRO_0000011052"
FT CHAIN 391..580
FT /note="Glutathione hydrolase small chain"
FT /id="PRO_0000011053"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16618936,
FT ECO:0000269|PubMed:18555071"
FT BINDING 114
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16618936"
FT BINDING 409
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16618936"
FT BINDING 411
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16618936"
FT BINDING 430
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16618936"
FT BINDING 433
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:16618936"
FT BINDING 462..463
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 483..484
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT MUTAGEN 391
FT /note="T->A: Abolishes autocatalytic cleavage, loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17135273"
FT MUTAGEN 513
FT /note="R->A: Not processed into its subunits, loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:1360205"
FT MUTAGEN 571
FT /note="R->G: Not processed into its subunits, loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:1360205"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2DBU"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:2DG5"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:2DG5"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2E0Y"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 320..340
FT /evidence="ECO:0007829|PDB:2DG5"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:2DG5"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 487..499
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 505..510
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:2DG5"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:2DG5"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:2DG5"
SQ SEQUENCE 580 AA; 61768 MW; 772F652EBA2A5F00 CRC64;
MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM VASVDATATQ
VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML IRSKNGNTTA IDFREMAPAK
ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT VAGFSLALDK YGTMPLNKVV QPAFKLARDG
FIVNDALADD LKTYGSEVLP NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD
EFYKGTIAEQ IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI
VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP WQALTNKAYA
KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD GNAVAVTYTL NTTFGTGIVA
GESGILLNNQ MDDFSAKPGV PNVYGLVGGD ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG
SPGGSRIITT VLQMVVNSID YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK
GQKVALKEAM GSTQSIMVGP DGELYGASDP RSVDDLTAGY
