XGPT_ECOLI
ID XGPT_ECOLI Reviewed; 152 AA.
AC P0A9M5; P00501;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000303|PubMed:23927482, ECO:0000303|PubMed:3886014, ECO:0000303|PubMed:6324103};
DE Short=XGPRT {ECO:0000303|PubMed:23927482};
DE EC=2.4.2.- {ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006};
DE EC=2.4.2.22 {ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006};
DE AltName: Full=Xanthine phosphoribosyltransferase {ECO:0000303|PubMed:9100006};
GN Name=gpt; Synonyms=gpp, gxu; OrderedLocusNames=b0238, JW0228;
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=6324103; DOI=10.1093/nar/11.24.8817;
RA Pratt D., Subramani S.;
RT "Nucleotide sequence of the Escherichia coli xanthine-guanine
RT phosphoribosyl transferase gene.";
RL Nucleic Acids Res. 11:8817-8823(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6324102; DOI=10.1093/nar/11.24.8809;
RA Richardson K.K., Fostel J., Skopek T.R.;
RT "Nucleotide sequence of the xanthine guanine phosphoribosyl transferase
RT gene of E. coli.";
RL Nucleic Acids Res. 11:8809-8816(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6397401; DOI=10.1016/0378-1119(84)90052-0;
RA Nueesch J., Schuemperli D.;
RT "Structural and functional organization of the gpt gene region of
RT Escherichia coli.";
RL Gene 32:243-249(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6396164; DOI=10.1016/0378-1119(84)90228-2;
RA Jagadeeswaran P., Ashman C.R., Roberts S., Langenberg J.;
RT "Nucleotide sequence and analysis of deletion mutants of the Escherichia
RT coli gpt gene in plasmid pSV2 gpt.";
RL Gene 31:309-313(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3540961; DOI=10.1073/pnas.84.2.344;
RA Richardson K.K., Richardson F.C., Crosby R.M., Swenberg J.A., Skopek T.R.;
RT "DNA base changes and alkylation following in vivo exposure of Escherichia
RT coli to N-methyl-N-nitrosourea or N-ethyl-N-nitrosourea.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:344-348(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RX PubMed=6100966; DOI=10.1128/mcb.1.5.449-459.1981;
RA Mulligan R.C., Berg P.;
RT "Factors governing the expression of a bacterial gene in mammalian cells.";
RL Mol. Cell. Biol. 1:449-459(1981).
RN [11] {ECO:0007744|PDB:1NUL}
RP PROTEIN SEQUENCE OF 66-76, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT
RP ALA-59 IN COMPLEX WITH MAGNESIUM, COFACTOR, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, AND PATHWAY.
RX PubMed=9100006; DOI=10.1021/bi962640d;
RA Vos S., de Jersey J., Martin J.L.;
RT "Crystal structure of Escherichia coli xanthine
RT phosphoribosyltransferase.";
RL Biochemistry 36:4125-4134(1997).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=3886014; DOI=10.1016/0304-4165(85)90003-0;
RA Deo S.S., Tseng W.C., Saini R., Coles R.S., Athwal R.S.;
RT "Purification and characterization of Escherichia coli xanthine-guanine
RT phosphoribosyltransferase produced by plasmid pSV2gpt.";
RL Biochim. Biophys. Acta 839:233-239(1985).
RN [13]
RP MUTAGENESIS OF CYS-59, AND CRYSTALLIZATION OF WILD-TYPE AND OF MUTANT
RP ALA-59.
RX PubMed=8812991; DOI=10.1006/jsbi.1996.0050;
RA Vos S., de Jersey J., Martin J.L.;
RT "Crystallization and preliminary X-ray crystallographic studies of
RT Escherichia coli xanthine phosphoribosyltransferase.";
RL J. Struct. Biol. 116:330-334(1996).
RN [14] {ECO:0007744|PDB:1A95, ECO:0007744|PDB:1A96, ECO:0007744|PDB:1A97, ECO:0007744|PDB:1A98}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT ALA-59 AND WILD-TYPE IN
RP COMPLEXES WITH GUANINE; XANTHINE; GMP;
RP 5-PHOSPHO-ALPHA-D-RIBOSE-1-DIPHOSPHATE ANALOG AND MAGNESIUM, AND SUBUNIT.
RX PubMed=9743633; DOI=10.1006/jmbi.1998.2051;
RA Vos S., Parry R.J., Burns M.R., de Jersey J., Martin J.L.;
RT "Structures of free and complexed forms of Escherichia coli xanthine-
RT guanine phosphoribosyltransferase.";
RL J. Mol. Biol. 282:875-889(1998).
RN [15] {ECO:0007744|PDB:4JIT, ECO:0007744|PDB:4JLS}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH NUCLEOSIDE
RP PHOSPHONATE INHIBITORS, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP 65-HIS--GLU-70.
RX PubMed=23927482; DOI=10.1021/jm400779n;
RA Keough D.T., Hockova D., Rejman D., Spacek P., Vrbkova S., Krecmerova M.,
RA Eng W.S., Jans H., West N.P., Naesens L.M., de Jersey J., Guddat L.W.;
RT "Inhibition of the Escherichia coli 6-oxopurine phosphoribosyltransferases
RT by nucleoside phosphonates: potential for new antibacterial agents.";
RL J. Med. Chem. 56:6967-6984(2013).
CC -!- FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of
CC the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-
CC diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and
CC xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-
CC monophosphate) and XMP (xanthosine 5'-monophosphate), with the release
CC of PPi. To a lesser extent, also acts on hypoxanthine (PubMed:9100006,
CC PubMed:3886014). Does not ribophosphorylate adenine (PubMed:3886014).
CC {ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115;
CC Evidence={ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000305|PubMed:9100006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC Evidence={ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10802;
CC Evidence={ECO:0000305|PubMed:9100006};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053;
CC Evidence={ECO:0000269|PubMed:3886014, ECO:0000269|PubMed:9100006};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000305|PubMed:9100006};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9100006};
CC -!- ACTIVITY REGULATION: Inhibited by thioguanine, GMP and, to a lesser
CC extent, by thioxanthine, azaxanthine and azaguanine (PubMed:3886014).
CC Highly inhibited by nucleoside phosphonates, which are product analogs
CC (PubMed:23927482). {ECO:0000269|PubMed:23927482,
CC ECO:0000269|PubMed:3886014}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for guanine (at pH 8.5) {ECO:0000269|PubMed:9100006};
CC KM=30.5 uM for xanthine (at pH 8.5) {ECO:0000269|PubMed:9100006};
CC KM=90.8 uM for hypoxanthine (at pH 8.5) {ECO:0000269|PubMed:9100006};
CC KM=139 uM for 5-phospho-alpha-D-ribose 1-diphosphate (at pH 8.5)
CC {ECO:0000269|PubMed:9100006};
CC KM=2.5 uM for guanine {ECO:0000269|PubMed:3886014};
CC KM=42 uM for xanthine {ECO:0000269|PubMed:3886014};
CC KM=182 uM for hypoxanthine {ECO:0000269|PubMed:3886014};
CC KM=38.5 uM for 5-phospho-alpha-D-ribose 1-diphosphate (with guanine
CC as cosubstrate) {ECO:0000269|PubMed:3886014};
CC KM=100 uM for 5-phospho-alpha-D-ribose 1-diphosphate (with xanthine
CC as cosubstrate) {ECO:0000269|PubMed:3886014};
CC Note=kcat is 112.0 sec(-1) with guanine as substrate. kcat is 150.1
CC sec(-1) with xanthine as substrate. kcat is 54.8 sec(-1) with
CC hypoxanthine as substrate (at pH 8.5). {ECO:0000269|PubMed:9100006};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1. {ECO:0000305|PubMed:9100006}.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1. {ECO:0000305|PubMed:9100006}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9100006,
CC ECO:0000269|PubMed:9743633}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: E.coli cells express two distinct 6-oxopurine PRTases,
CC with very different specificities for hypoxanthine, guanine, and
CC xanthine. Salvage enzymes allow a more energy efficient synthesis of
CC purine nucleoside monophosphates compared with the de novo pathway. The
CC kinetic analysis suggests that E.coli HPRT is mainly responsible for
CC the synthesis of IMP and that XGPRT primarily salvages guanine and
CC xanthine. {ECO:0000305|PubMed:9100006}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. XGPT subfamily. {ECO:0000305}.
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DR EMBL; X00221; CAA25040.1; -; Genomic_DNA.
DR EMBL; X00222; CAA25041.1; -; Genomic_DNA.
DR EMBL; M13422; AAA23928.1; -; Genomic_DNA.
DR EMBL; M12907; AAA23932.1; -; Genomic_DNA.
DR EMBL; M15035; AAA23933.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08658.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73342.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77907.1; -; Genomic_DNA.
DR EMBL; M10382; AAA23931.1; -; Genomic_DNA.
DR PIR; A00587; RTECGX.
DR RefSeq; NP_414773.1; NC_000913.3.
DR RefSeq; WP_001291990.1; NZ_SSZK01000050.1.
DR PDB; 1A95; X-ray; 2.00 A; A/B/C/D=1-152.
DR PDB; 1A96; X-ray; 2.00 A; A/B/C/D=1-152.
DR PDB; 1A97; X-ray; 2.60 A; A/B/C/D=3-150.
DR PDB; 1A98; X-ray; 2.25 A; A/B=1-152.
DR PDB; 1NUL; X-ray; 1.80 A; A/B=1-152.
DR PDB; 4JIT; X-ray; 2.80 A; A/B/C/D=1-152.
DR PDB; 4JLS; X-ray; 2.20 A; A/B/C/D/E/H/I/J=1-152.
DR PDBsum; 1A95; -.
DR PDBsum; 1A96; -.
DR PDBsum; 1A97; -.
DR PDBsum; 1A98; -.
DR PDBsum; 1NUL; -.
DR PDBsum; 4JIT; -.
DR PDBsum; 4JLS; -.
DR AlphaFoldDB; P0A9M5; -.
DR SMR; P0A9M5; -.
DR BioGRID; 4260989; 10.
DR IntAct; P0A9M5; 1.
DR STRING; 511145.b0238; -.
DR BindingDB; P0A9M5; -.
DR ChEMBL; CHEMBL3988588; -.
DR DrugBank; DB03942; Carboxylic PRPP.
DR DrugBank; DB02377; Guanine.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR DrugBank; DB02134; Xanthine.
DR SWISS-2DPAGE; P0A9M5; -.
DR jPOST; P0A9M5; -.
DR PaxDb; P0A9M5; -.
DR PRIDE; P0A9M5; -.
DR EnsemblBacteria; AAC73342; AAC73342; b0238.
DR EnsemblBacteria; BAA77907; BAA77907; BAA77907.
DR GeneID; 66671444; -.
DR GeneID; 944817; -.
DR KEGG; ecj:JW0228; -.
DR KEGG; eco:b0238; -.
DR PATRIC; fig|1411691.4.peg.2045; -.
DR EchoBASE; EB0409; -.
DR eggNOG; COG2236; Bacteria.
DR HOGENOM; CLU_080904_3_0_6; -.
DR InParanoid; P0A9M5; -.
DR OMA; FHRDCRA; -.
DR PhylomeDB; P0A9M5; -.
DR BioCyc; EcoCyc:GPT-MON; -.
DR BioCyc; MetaCyc:GPT-MON; -.
DR BRENDA; 2.4.2.22; 2026.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR EvolutionaryTrace; P0A9M5; -.
DR PRO; PR:P0A9M5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:RHEA.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0032263; P:GMP salvage; IMP:EcoCyc.
DR GO; GO:0032264; P:IMP salvage; IDA:EcoCyc.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0032265; P:XMP salvage; IMP:EcoCyc.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01903; XGPRT; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR PANTHER; PTHR39563; PTHR39563; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Glycosyltransferase; Magnesium; Membrane;
KW Metal-binding; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..152
FT /note="Xanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139666"
FT BINDING 37..38
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000305|PubMed:9743633,
FT ECO:0007744|PDB:1A95"
FT BINDING 69
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000305|PubMed:9743633,
FT ECO:0007744|PDB:1A95"
FT BINDING 69
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A97"
FT BINDING 88..96
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000305|PubMed:9743633,
FT ECO:0007744|PDB:1A95"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:9100006"
FT BINDING 92..96
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A97"
FT BINDING 92
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A95"
FT BINDING 92
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A96"
FT BINDING 134..135
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A97"
FT BINDING 135
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A95"
FT BINDING 135
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000269|PubMed:9743633,
FT ECO:0007744|PDB:1A96"
FT MUTAGEN 59
FT /note="C->A: No effect on catalytic activity; increased
FT stability."
FT /evidence="ECO:0000269|PubMed:8812991"
FT MUTAGEN 65..70
FT /note="HDNQRE->AAAAAA: No effect on affinity for xanthine
FT and guanine substrates. However, the catalytic activity is
FT highly reduced (200-fold when guanine is used as substrate)
FT and the inhibition by GMP is also affected."
FT /evidence="ECO:0000269|PubMed:23927482"
FT CONFLICT 122
FT /note="V -> G (in Ref. 5; AAA23933)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1NUL"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1A96"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1NUL"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1NUL"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1A95"
SQ SEQUENCE 152 AA; 16971 MW; F0AD813127E7200D CRC64;
MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI REMYPKAHFV TIFAKPAGRP
LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS GR
