PYRF_METTH
ID PYRF_METTH Reviewed; 228 AA.
AC O26232;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
GN Name=pyrF; OrderedLocusNames=MTH_129;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10930842; DOI=10.1107/s090744490000576x;
RA Wu N., Christendat D., Dharamsi A., Pai E.F.;
RT "Purification, crystallization and preliminary X-ray study of orotidine 5'-
RT monophosphate decarboxylase.";
RL Acta Crystallogr. D 56:912-914(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP 6-AZAUMP, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10681441; DOI=10.1073/pnas.050417797;
RA Wu N., Mo Y., Gao J., Pai E.F.;
RT "Electrostatic stress in catalysis: structure and mechanism of the enzyme
RT orotidine monophosphate decarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2017-2022(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANTS ALA-42; GLY-70; ALA-70;
RP ALA-72; ALA-70/ALA-72; ASN-75; ALA-127 AND ALA-185 IN COMPLEX WITH
RP DIFFERENT LIGANDS, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=11900543; DOI=10.1021/bi015758p;
RA Wu N., Gillon W., Pai E.F.;
RT "Mapping the active site-ligand interactions of orotidine 5'-monophosphate
RT decarboxylase by crystallography.";
RL Biochemistry 41:4002-4011(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF COMPLEXES WITH BMP; CMP; UMP; XMP
RP AND OF MUTANT DELTA ALA-203 IN COMPLEX WITH 6-AZAUMP, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=12011084; DOI=10.1074/jbc.m202362200;
RA Wu N., Pai E.F.;
RT "Crystal structures of inhibitor complexes reveal an alternate binding mode
RT in orotidine-5'-monophosphate decarboxylase.";
RL J. Biol. Chem. 277:28080-28087(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF COMPLEX WITH BMP, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=16248642; DOI=10.1021/ja054865u;
RA Fujihashi M., Bello A.M., Poduch E., Wei L., Annedi S.C., Pai E.F.,
RA Kotra L.P.;
RT "An unprecedented twist to ODCase catalytic activity.";
RL J. Am. Chem. Soc. 127:15048-15050(2005).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10681441,
CC ECO:0000269|PubMed:11900543, ECO:0000269|PubMed:12011084,
CC ECO:0000269|PubMed:16248642}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000666; AAB84635.1; -; Genomic_DNA.
DR PIR; F69038; F69038.
DR PDB; 1DV7; X-ray; 1.80 A; A=2-228.
DR PDB; 1DVJ; X-ray; 1.50 A; A/B/C/D=2-226.
DR PDB; 1KLY; X-ray; 1.50 A; A=1-228.
DR PDB; 1KLZ; X-ray; 1.50 A; A=1-228.
DR PDB; 1KM0; X-ray; 1.70 A; A/B/C/D=1-226.
DR PDB; 1KM1; X-ray; 1.60 A; A/B=1-226.
DR PDB; 1KM2; X-ray; 1.50 A; A=1-226.
DR PDB; 1KM3; X-ray; 1.50 A; A=1-226.
DR PDB; 1KM4; X-ray; 1.50 A; A=1-226.
DR PDB; 1KM5; X-ray; 1.50 A; A=1-226.
DR PDB; 1KM6; X-ray; 1.50 A; A=1-226.
DR PDB; 1LOL; X-ray; 1.90 A; A/B=1-226.
DR PDB; 1LOQ; X-ray; 1.50 A; A=1-228.
DR PDB; 1LOR; X-ray; 1.60 A; A=1-228.
DR PDB; 1LOS; X-ray; 1.90 A; A/B/C/D=1-228.
DR PDB; 1LP6; X-ray; 1.90 A; A/B=1-226.
DR PDB; 1X1Z; X-ray; 1.45 A; A/B=1-228.
DR PDB; 2E6Y; X-ray; 1.60 A; A/B=1-228.
DR PDB; 2ZZ1; X-ray; 1.57 A; A/B=1-228.
DR PDB; 2ZZ2; X-ray; 1.53 A; A/B=1-228.
DR PDB; 2ZZ3; X-ray; 1.80 A; A/B=1-228.
DR PDB; 2ZZ4; X-ray; 1.67 A; A/B=1-228.
DR PDB; 2ZZ5; X-ray; 1.56 A; A/B=1-228.
DR PDB; 2ZZ6; X-ray; 1.66 A; A/B=1-228.
DR PDB; 2ZZ7; X-ray; 1.58 A; A=1-228.
DR PDB; 3G18; X-ray; 1.60 A; A/B=1-228.
DR PDB; 3G1A; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3G1D; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3G1F; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-228.
DR PDB; 3G1H; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-228.
DR PDB; 3G1S; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3G1V; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3G1X; X-ray; 1.55 A; A/B=1-228.
DR PDB; 3G1Y; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3G22; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3G24; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3LHT; X-ray; 1.35 A; A/B=1-228.
DR PDB; 3LHU; X-ray; 1.60 A; A/B=1-228.
DR PDB; 3LHV; X-ray; 1.35 A; A/B/C/D=1-228.
DR PDB; 3LHW; X-ray; 1.35 A; A/B=1-228.
DR PDB; 3LHY; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3LHZ; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3LI0; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3LI1; X-ray; 1.35 A; A/B=1-228.
DR PDB; 3LLD; X-ray; 1.45 A; A/B=1-228.
DR PDB; 3LLF; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3LTP; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3LTS; X-ray; 1.43 A; A/B=1-228.
DR PDB; 3LTY; X-ray; 1.50 A; A/B=1-228.
DR PDB; 3LV5; X-ray; 1.44 A; A/B=1-228.
DR PDB; 3LV6; X-ray; 1.45 A; A/B=1-228.
DR PDB; 3M1Z; X-ray; 1.42 A; A/B=1-228.
DR PDB; 3M41; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3M43; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3M44; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3M47; X-ray; 1.20 A; A/B=1-228.
DR PDB; 3M5X; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3M5Y; X-ray; 1.46 A; A/B=1-228.
DR PDB; 3M5Z; X-ray; 1.35 A; A/B=1-228.
DR PDB; 3NQ6; X-ray; 1.49 A; A/B=1-228.
DR PDB; 3NQ7; X-ray; 1.44 A; A/B=1-228.
DR PDB; 3NQA; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3NQC; X-ray; 1.53 A; A/B=1-228.
DR PDB; 3NQD; X-ray; 1.42 A; A/B=1-228.
DR PDB; 3NQE; X-ray; 1.42 A; A/B=1-228.
DR PDB; 3NQF; X-ray; 1.31 A; A/B=1-228.
DR PDB; 3NQG; X-ray; 1.42 A; A/B=1-228.
DR PDB; 3NQM; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3P5Y; X-ray; 1.60 A; A/B=1-228.
DR PDB; 3P5Z; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3P60; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3P61; X-ray; 1.40 A; A/B=1-228.
DR PDB; 3PBU; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3PBV; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3PBW; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3PBY; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3PC0; X-ray; 1.30 A; A/B=1-228.
DR PDB; 3QEZ; X-ray; 1.54 A; A/B=1-228.
DR PDB; 3QF0; X-ray; 1.34 A; A/B=1-228.
DR PDB; 3QMR; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3QMS; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3QMT; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3RLU; X-ray; 1.49 A; A/B=1-228.
DR PDB; 3RLV; X-ray; 1.42 A; A/B=1-228.
DR PDB; 3SEC; X-ray; 1.70 A; A=1-226.
DR PDB; 3SGU; X-ray; 1.70 A; A=1-226.
DR PDB; 3SIZ; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3SJ3; X-ray; 1.26 A; A/B=1-228.
DR PDB; 3SSJ; X-ray; 1.40 A; A=1-226.
DR PDB; 3SW6; X-ray; 1.50 A; A=1-226.
DR PDB; 3SY5; X-ray; 1.32 A; A/B=1-228.
DR PDB; 3THQ; X-ray; 1.50 A; A/B=1-226.
DR PDB; 3V1P; X-ray; 1.37 A; A/B=1-228.
DR PDB; 3W07; X-ray; 1.03 A; A=1-228.
DR PDB; 3WJW; X-ray; 1.59 A; A=1-228.
DR PDB; 3WJX; X-ray; 1.23 A; A=1-228.
DR PDB; 3WJY; X-ray; 1.72 A; A=1-228.
DR PDB; 3WJZ; X-ray; 1.39 A; A=1-228.
DR PDB; 3WK0; X-ray; 1.41 A; A=1-228.
DR PDB; 3WK1; X-ray; 1.60 A; A=1-228.
DR PDB; 3WK2; X-ray; 1.69 A; A=1-228.
DR PDB; 3WK3; X-ray; 1.26 A; A=1-228.
DR PDB; 4FX6; X-ray; 1.53 A; M/N=1-228.
DR PDB; 4FX8; X-ray; 1.94 A; A/B=1-228.
DR PDB; 4FXR; X-ray; 1.71 A; A/B=1-228.
DR PDB; 4GC4; X-ray; 1.42 A; A/B=1-228.
DR PDB; 4LC6; X-ray; 1.32 A; A/B=1-228.
DR PDB; 4LC8; X-ray; 1.32 A; A/B=1-228.
DR PDB; 4LW7; X-ray; 1.42 A; A/B=1-228.
DR PDB; 4NT0; X-ray; 1.77 A; A/B=1-228.
DR PDB; 4NUW; X-ray; 1.59 A; A/B=1-228.
DR PDB; 4NX5; X-ray; 1.59 A; A/B=1-228.
DR PDB; 4O11; X-ray; 1.59 A; A/B=1-228.
DR PDB; 4O8R; X-ray; 2.29 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-228.
DR PDBsum; 1DV7; -.
DR PDBsum; 1DVJ; -.
DR PDBsum; 1KLY; -.
DR PDBsum; 1KLZ; -.
DR PDBsum; 1KM0; -.
DR PDBsum; 1KM1; -.
DR PDBsum; 1KM2; -.
DR PDBsum; 1KM3; -.
DR PDBsum; 1KM4; -.
DR PDBsum; 1KM5; -.
DR PDBsum; 1KM6; -.
DR PDBsum; 1LOL; -.
DR PDBsum; 1LOQ; -.
DR PDBsum; 1LOR; -.
DR PDBsum; 1LOS; -.
DR PDBsum; 1LP6; -.
DR PDBsum; 1X1Z; -.
DR PDBsum; 2E6Y; -.
DR PDBsum; 2ZZ1; -.
DR PDBsum; 2ZZ2; -.
DR PDBsum; 2ZZ3; -.
DR PDBsum; 2ZZ4; -.
DR PDBsum; 2ZZ5; -.
DR PDBsum; 2ZZ6; -.
DR PDBsum; 2ZZ7; -.
DR PDBsum; 3G18; -.
DR PDBsum; 3G1A; -.
DR PDBsum; 3G1D; -.
DR PDBsum; 3G1F; -.
DR PDBsum; 3G1H; -.
DR PDBsum; 3G1S; -.
DR PDBsum; 3G1V; -.
DR PDBsum; 3G1X; -.
DR PDBsum; 3G1Y; -.
DR PDBsum; 3G22; -.
DR PDBsum; 3G24; -.
DR PDBsum; 3LHT; -.
DR PDBsum; 3LHU; -.
DR PDBsum; 3LHV; -.
DR PDBsum; 3LHW; -.
DR PDBsum; 3LHY; -.
DR PDBsum; 3LHZ; -.
DR PDBsum; 3LI0; -.
DR PDBsum; 3LI1; -.
DR PDBsum; 3LLD; -.
DR PDBsum; 3LLF; -.
DR PDBsum; 3LTP; -.
DR PDBsum; 3LTS; -.
DR PDBsum; 3LTY; -.
DR PDBsum; 3LV5; -.
DR PDBsum; 3LV6; -.
DR PDBsum; 3M1Z; -.
DR PDBsum; 3M41; -.
DR PDBsum; 3M43; -.
DR PDBsum; 3M44; -.
DR PDBsum; 3M47; -.
DR PDBsum; 3M5X; -.
DR PDBsum; 3M5Y; -.
DR PDBsum; 3M5Z; -.
DR PDBsum; 3NQ6; -.
DR PDBsum; 3NQ7; -.
DR PDBsum; 3NQA; -.
DR PDBsum; 3NQC; -.
DR PDBsum; 3NQD; -.
DR PDBsum; 3NQE; -.
DR PDBsum; 3NQF; -.
DR PDBsum; 3NQG; -.
DR PDBsum; 3NQM; -.
DR PDBsum; 3P5Y; -.
DR PDBsum; 3P5Z; -.
DR PDBsum; 3P60; -.
DR PDBsum; 3P61; -.
DR PDBsum; 3PBU; -.
DR PDBsum; 3PBV; -.
DR PDBsum; 3PBW; -.
DR PDBsum; 3PBY; -.
DR PDBsum; 3PC0; -.
DR PDBsum; 3QEZ; -.
DR PDBsum; 3QF0; -.
DR PDBsum; 3QMR; -.
DR PDBsum; 3QMS; -.
DR PDBsum; 3QMT; -.
DR PDBsum; 3RLU; -.
DR PDBsum; 3RLV; -.
DR PDBsum; 3SEC; -.
DR PDBsum; 3SGU; -.
DR PDBsum; 3SIZ; -.
DR PDBsum; 3SJ3; -.
DR PDBsum; 3SSJ; -.
DR PDBsum; 3SW6; -.
DR PDBsum; 3SY5; -.
DR PDBsum; 3THQ; -.
DR PDBsum; 3V1P; -.
DR PDBsum; 3W07; -.
DR PDBsum; 3WJW; -.
DR PDBsum; 3WJX; -.
DR PDBsum; 3WJY; -.
DR PDBsum; 3WJZ; -.
DR PDBsum; 3WK0; -.
DR PDBsum; 3WK1; -.
DR PDBsum; 3WK2; -.
DR PDBsum; 3WK3; -.
DR PDBsum; 4FX6; -.
DR PDBsum; 4FX8; -.
DR PDBsum; 4FXR; -.
DR PDBsum; 4GC4; -.
DR PDBsum; 4LC6; -.
DR PDBsum; 4LC8; -.
DR PDBsum; 4LW7; -.
DR PDBsum; 4NT0; -.
DR PDBsum; 4NUW; -.
DR PDBsum; 4NX5; -.
DR PDBsum; 4O11; -.
DR PDBsum; 4O8R; -.
DR AlphaFoldDB; O26232; -.
DR SMR; O26232; -.
DR STRING; 187420.MTH_129; -.
DR BindingDB; O26232; -.
DR ChEMBL; CHEMBL5688; -.
DR EnsemblBacteria; AAB84635; AAB84635; MTH_129.
DR KEGG; mth:MTH_129; -.
DR PATRIC; fig|187420.15.peg.102; -.
DR HOGENOM; CLU_067069_2_0_2; -.
DR OMA; EMSHPGA; -.
DR BRENDA; 4.1.1.23; 7219.
DR UniPathway; UPA00070; UER00120.
DR EvolutionaryTrace; O26232; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01200_A; OMPdecase_type1_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..228
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134612"
FT ACT_SITE 72
FT /note="Proton donor"
FT BINDING 20
FT /ligand="substrate"
FT BINDING 42
FT /ligand="substrate"
FT BINDING 70..79
FT /ligand="substrate"
FT BINDING 127
FT /ligand="substrate"
FT BINDING 180..190
FT /ligand="substrate"
FT BINDING 202
FT /ligand="substrate"
FT BINDING 203
FT /ligand="substrate"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3LI0"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4NT0"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3W07"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3W07"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3W07"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:3W07"
SQ SEQUENCE 228 AA; 24915 MW; A7B65D94C8663D78 CRC64;
MRSRRVDVMD VMNRLILAMD LMNRDDALRV TGEVREYIDT VKIGYPLVLS EGMDIIAEFR
KRFGCRIIAD FKVADIPETN EKICRATFKA GADAIIVHGF RGADSVRACL NVAEEMGREV
FLLTEMSHPG AEMFIQGAAD EIARMGVDLG VKNYVGPSTR PERLSRLREI IGQDSFLISP
GVGAQGGDPG ETLRFADAII VGRSIYLADN PAAAAAGIIE SIKDLLNP
