GAL7_ECOLI
ID GAL7_ECOLI Reviewed; 348 AA.
AC P09148; P78270;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12 {ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:10820011, ECO:0000269|PubMed:321007};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=galT; Synonyms=galB; OrderedLocusNames=b0758, JW0741;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3022232; DOI=10.1093/nar/14.19.7705;
RA Lemaire H.-G., Mueller-Hill B.;
RT "Nucleotide sequences of the gal E gene and the gal T gene of E. coli.";
RL Nucleic Acids Res. 14:7705-7711(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-348.
RX PubMed=3158881; DOI=10.1093/nar/13.6.1841;
RA Debouck C., Riccio A., Schumperli D., McKenney K., Jeffers J., Hughes C.,
RA Rosenberg M., Heusterspreute M., Brunel F., Davison J.;
RT "Structure of the galactokinase gene of Escherichia coli, the last (?) gene
RT of the gal operon.";
RL Nucleic Acids Res. 13:1841-1853(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-38.
RX PubMed=2823224; DOI=10.1093/nar/15.19.8116;
RA Cornwell T.L., Adhya S.L., Reznikoff W.S., Frey P.A.;
RT "The nucleotide sequence of the gal T gene of Escherichia coli.";
RL Nucleic Acids Res. 15:8116-8116(1987).
RN [7]
RP CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RX PubMed=321007; DOI=10.1021/bi00624a032;
RA Wong L.J., Sheu K.F., Lee S.L., Frey P.A.;
RT "Galactose-1-phosphate uridylyltransferase: isolation and properties of a
RT uridylyl-enzyme intermediate.";
RL Biochemistry 16:1010-1016(1977).
RN [8]
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-52; CYS-55; HIS-115;
RP HIS-164 AND GLU-182.
RX PubMed=10529216; DOI=10.1021/bi9910631;
RA Geeganage S., Frey P.A.;
RT "Significance of metal ions in galactose-1-phosphate uridylyltransferase:
RT an essential structural zinc and a nonessential structural iron.";
RL Biochemistry 38:13398-13406(1999).
RN [9]
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND MUTAGENESIS OF CYS-160 AND
RP SER-161.
RX PubMed=10820011; DOI=10.1021/bi992594s;
RA Geeganage S., Ling V.W., Frey P.A.;
RT "Roles of two conserved amino acid residues in the active site of
RT galactose-1-phosphate uridylyltransferase: an essential serine and a
RT nonessential cysteine.";
RL Biochemistry 39:5397-5404(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH IRON;
RP URIDINE-5'-MONOPHOSPHATE AND ZINC, AND ACTIVE SITE HIS-166.
RX PubMed=8794735; DOI=10.1021/bi9612677;
RA Wedekind J.E., Frey P.A., Rayment I.;
RT "The structure of nucleotidylated histidine-166 of galactose-1-phosphate
RT uridylyltransferase provides insight into phosphoryl group transfer.";
RL Biochemistry 35:11560-11569(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7669762; DOI=10.1021/bi00035a010;
RA Wedekind J.E., Frey P.A., Rayment I.;
RT "Three-dimensional structure of galactose-1-phosphate uridylyltransferase
RT from Escherichia coli at 1.8-A resolution.";
RL Biochemistry 34:11049-11061(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH IRON;
RP UDP-ALPHA-D-GLUCOSE AND ZINC, MUTAGENESIS OF HIS-166, AND ACTIVE SITE.
RX PubMed=9063869; DOI=10.1021/bi9626517;
RA Thoden J.B., Ruzicka F.J., Frey P.A., Rayment I., Holden H.M.;
RT "Structural analysis of the H166G site-directed mutant of galactose-1-
RT phosphate uridylyltransferase complexed with either UDP-glucose or UDP-
RT galactose: detailed description of the nucleotide sugar binding site.";
RL Biochemistry 36:1212-1222(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-
CC glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989,
CC ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:66914; EC=2.7.7.12;
CC Evidence={ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:10820011,
CC ECO:0000269|PubMed:321007};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10529216, ECO:0000269|PubMed:8794735,
CC ECO:0000269|PubMed:9063869};
CC Note=Binds 1 zinc ion per subunit. Zinc binding seems to play a
CC structural role. {ECO:0000269|PubMed:10529216,
CC ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.200 mM for uridine 5'-diphosphate glucose
CC {ECO:0000269|PubMed:10820011};
CC KM=0.303 mM for galactose-1-phosphate {ECO:0000269|PubMed:10820011};
CC KM=0.121 mM for uridine 5'-diphosphate galactose
CC {ECO:0000269|PubMed:10820011};
CC KM=0.157 mM for glucose-1-phosphate {ECO:0000269|PubMed:10820011};
CC Vmax=180 umol/min/mg enzyme {ECO:0000269|PubMed:10820011};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: Iron binding is not required for protein folding or
CC enzyme activity. {ECO:0000269|PubMed:10820011}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
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DR EMBL; X06226; CAA29574.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73845.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35420.1; -; Genomic_DNA.
DR EMBL; X02306; CAA26171.1; -; Genomic_DNA.
DR PIR; S00722; XNECUD.
DR RefSeq; NP_415279.1; NC_000913.3.
DR RefSeq; WP_000191497.1; NZ_SSZK01000002.1.
DR PDB; 1GUP; X-ray; 1.80 A; A/B/C/D=1-348.
DR PDB; 1GUQ; X-ray; 1.80 A; A/B/C/D=1-348.
DR PDB; 1HXP; X-ray; 1.80 A; A/B=1-348.
DR PDB; 1HXQ; X-ray; 1.86 A; A/B=1-348.
DR PDBsum; 1GUP; -.
DR PDBsum; 1GUQ; -.
DR PDBsum; 1HXP; -.
DR PDBsum; 1HXQ; -.
DR AlphaFoldDB; P09148; -.
DR SMR; P09148; -.
DR BioGRID; 4261703; 397.
DR DIP; DIP-9735N; -.
DR IntAct; P09148; 1.
DR STRING; 511145.b0758; -.
DR DrugBank; DB01861; Uridine diphosphate glucose.
DR DrugBank; DB03685; Uridine monophosphate.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR jPOST; P09148; -.
DR PaxDb; P09148; -.
DR PRIDE; P09148; -.
DR EnsemblBacteria; AAC73845; AAC73845; b0758.
DR EnsemblBacteria; BAA35420; BAA35420; BAA35420.
DR GeneID; 945357; -.
DR KEGG; ecj:JW0741; -.
DR KEGG; eco:b0758; -.
DR PATRIC; fig|1411691.4.peg.1520; -.
DR EchoBASE; EB0361; -.
DR eggNOG; COG1085; Bacteria.
DR HOGENOM; CLU_029960_0_0_6; -.
DR InParanoid; P09148; -.
DR OMA; HAIYYPP; -.
DR PhylomeDB; P09148; -.
DR BioCyc; EcoCyc:GALACTURIDYLYLTRANS-MON; -.
DR BioCyc; MetaCyc:GALACTURIDYLYLTRANS-MON; -.
DR BRENDA; 2.7.7.12; 2026.
DR SABIO-RK; P09148; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; P09148; -.
DR PRO; PR:P09148; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0004335; F:galactokinase activity; IMP:CACAO.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:EcoCyc.
DR CDD; cd00608; GalT; 1.
DR Gene3D; 3.30.428.10; -; 2.
DR InterPro; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR019779; GalP_UDPtransf1_His-AS.
DR InterPro; IPR005850; GalP_Utransf_C.
DR InterPro; IPR005849; GalP_Utransf_N.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR11943; PTHR11943; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF000808; GalT; 1.
DR SUPFAM; SSF54197; SSF54197; 2.
DR TIGRFAMs; TIGR00209; galT_1; 1.
DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Galactose metabolism; Iron;
KW Metal-binding; Nucleotidyltransferase; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1..348
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169894"
FT ACT_SITE 166
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033,
FT ECO:0000269|PubMed:8794735, ECO:0000269|PubMed:9063869"
FT BINDING 28..31
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 61
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 77..78
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 153
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 159..161
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 168
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:8794735,
FT ECO:0000269|PubMed:9063869, ECO:0007744|PDB:1GUQ,
FT ECO:0007744|PDB:1HXQ"
FT BINDING 311..312
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 316..317
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT BINDING 323
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9063869,
FT ECO:0007744|PDB:1GUQ"
FT MUTAGEN 52
FT /note="C->S: Decreases enzyme activity 3000-fold."
FT /evidence="ECO:0000269|PubMed:10529216"
FT MUTAGEN 55
FT /note="C->S: Decreases enzyme activity 600-fold."
FT /evidence="ECO:0000269|PubMed:10529216"
FT MUTAGEN 115
FT /note="H->N: Decreases enzyme activity by 98%."
FT /evidence="ECO:0000269|PubMed:10529216"
FT MUTAGEN 160
FT /note="C->S,A: Slight inhibition of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10820011"
FT MUTAGEN 161
FT /note="S->A: 7000-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:10820011"
FT MUTAGEN 164
FT /note="H->N: Decreases enzyme activity 10000-fold."
FT /evidence="ECO:0000269|PubMed:10529216"
FT MUTAGEN 166
FT /note="H->G: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:9063869"
FT MUTAGEN 182
FT /note="E->A: Decreases enzyme activity by about 50%.
FT Abolishes iron binding, but has no effect on zinc binding."
FT /evidence="ECO:0000269|PubMed:10529216"
FT CONFLICT 29..31
FT /note="AKR -> LS (in Ref. 1; CAA29574)"
FT /evidence="ECO:0000305"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1GUP"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 124..144
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 249..270
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:1GUP"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:1GUP"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:1GUP"
SQ SEQUENCE 348 AA; 39646 MW; 3D55D2CB38D8C9A2 CRC64;
MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP DCFLCAGNVR
VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ SARGTSRVIC FSPDHSKTLP
ELSVAALTEI VKTWQEQTAE LGKTYPWVQV FENKGAAMGC SNPHPHGQIW ANSFLPNEAE
REDRLQKEYF AEQKSPMLVD YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH
VLRITDLTDA QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV
