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   27-MAR-2024, entry version 191.
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; Pseudomonadota; 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=0.2 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; 511145-b0758; -.
DR   EnsemblBacteria; AAC73845; AAC73845; b0758.
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; CFENRGA; -.
DR   OrthoDB; 9769064at2; -.
DR   PhylomeDB; P09148; -.
DR   BioCyc; EcoCyc:GALACTURIDYLYLTRANS-MONOMER; -.
DR   BioCyc; MetaCyc:GALACTURIDYLYLTRANS-MONOMER; -.
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; HIT-like; 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   NCBIfam; TIGR00209; galT_1; 1.
DR   PANTHER; PTHR11943; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR11943:SF1; GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF02744; GalP_UDP_tr_C; 1.
DR   Pfam; PF01087; GalP_UDP_transf; 1.
DR   PIRSF; PIRSF000808; GalT; 1.
DR   SUPFAM; SSF54197; HIT-like; 2.
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
//