PYRC_ECOLI
ID PYRC_ECOLI Reviewed; 348 AA.
AC P05020;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000303|PubMed:2876892};
GN OrderedLocusNames=b1062, JW1049;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2876892; DOI=10.1111/j.1432-1033.1986.tb09942.x;
RA Baeckstroem D., Sjoeberg R.-M., Lundberg L.G.;
RT "Nucleotide sequence of the structural gene for dihydroorotase of
RT Escherichia coli K12.";
RL Eur. J. Biochem. 160:77-82(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=2885307; DOI=10.1128/jb.169.7.3051-3058.1987;
RA Wilson H.R., Chan P.T., Turnbough C.L. Jr.;
RT "Nucleotide sequence and expression of the pyrC gene of Escherichia coli K-
RT 12.";
RL J. Bacteriol. 169:3051-3058(1987).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-348.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Ohmori H.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=6142052; DOI=10.1016/s0021-9258(17)43293-5;
RA Washabaugh M.W., Collins K.D.;
RT "Dihydroorotase from Escherichia coli. Purification and characterization.";
RL J. Biol. Chem. 259:3293-3298(1984).
RN [9]
RP COFACTOR, AND ZINC-BINDING.
RX PubMed=1671037; DOI=10.1016/s0021-9258(18)52336-x;
RA Brown D.C., Collins K.D.;
RT "Dihydroorotase from Escherichia coli. Substitution of Co(II) for the
RT active site Zn(II).";
RL J. Biol. Chem. 266:1597-1604(1991).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND MUTAGENESIS OF ARG-21; ASN-45; ASP-251 AND HIS-255.
RX PubMed=15610022; DOI=10.1021/bi048308g;
RA Porter T.N., Li Y., Raushel F.M.;
RT "Mechanism of the dihydroorotase reaction.";
RL Biochemistry 43:16285-16292(2004).
RN [11] {ECO:0007744|PDB:1J79}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-348 IN COMPLEX WITH OROTATE AND
RP ZINC, COFACTOR, SUBUNIT, AND CARBOXYLATION AT LYS-103.
RX PubMed=11401542; DOI=10.1021/bi010682i;
RA Thoden J.B., Phillips G.N. Jr., Neal T.M., Raushel F.M., Holden H.M.;
RT "Molecular structure of dihydroorotase: a paradigm for catalysis through
RT the use of a binuclear metal center.";
RL Biochemistry 40:6989-6997(2001).
RN [12] {ECO:0007744|PDB:1XGE}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-348 IN COMPLEX WITH
RP L-DIHYDROOROTATE AND ZINC, COFACTOR, SUBUNIT, DOMAIN, AND CARBOXYLATION AT
RP LYS-103.
RX PubMed=15826651; DOI=10.1016/j.jmb.2005.01.067;
RA Lee M., Chan C.W., Mitchell Guss J., Christopherson R.I., Maher M.J.;
RT "Dihydroorotase from Escherichia coli: loop movement and cooperativity
RT between subunits.";
RL J. Mol. Biol. 348:523-533(2005).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219,
CC ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219,
CC ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219,
CC ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15610022,
CC ECO:0000269|PubMed:15826651, ECO:0000269|PubMed:1671037,
CC ECO:0000269|PubMed:6142052};
CC Note=Binds 2 Zn(2+) ions per subunit (PubMed:6142052, PubMed:11401542,
CC PubMed:15826651). In vitro, can also use Co(2+) or Cd(2+)
CC (PubMed:1671037, PubMed:15610022). {ECO:0000269|PubMed:11401542,
CC ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:15826651,
CC ECO:0000269|PubMed:1671037, ECO:0000269|PubMed:6142052};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0756 mM for dihydroorotate {ECO:0000269|PubMed:6142052};
CC KM=0.080 mM for dihydroorotate (in the presence of Zn(2+))
CC {ECO:0000269|PubMed:15610022};
CC KM=0.70 mM for dihydroorotate (in the presence of Co(2+))
CC {ECO:0000269|PubMed:15610022};
CC KM=0.23 mM for dihydroorotate (in the presence of Cd(2+))
CC {ECO:0000269|PubMed:15610022};
CC KM=1.07 mM for N-carbamoyl-DL-aspartate {ECO:0000269|PubMed:6142052};
CC KM=1.70 mM for carbamoyl aspartate (in the presence of Zn(2+))
CC {ECO:0000269|PubMed:15610022};
CC KM=15 mM for carbamoyl aspartate (in the presence of Co(2+))
CC {ECO:0000269|PubMed:15610022};
CC KM=4.0 mM for carbamoyl aspartate (in the presence of Cd(2+))
CC {ECO:0000269|PubMed:15610022};
CC Note=kcat is 127 sec(-1) with dihydroorotate as substrate and 195
CC sec(-1) with N-carbamoyl-DL-aspartate as substrate (PubMed:6142052).
CC kcat is 100 sec(-1) with dihydroorotate as substrate and 160 sec(-1)
CC with carbamoyl aspartate as substrate in the presence of Zn(2+). kcat
CC is 15 sec(-1) with dihydroorotate as substrate and 25 sec(-1) with
CC carbamoyl aspartate as substrate in the presence of Co(2+). kcat is
CC 1.9 sec(-1) with dihydroorotate as substrate and 8.2 sec(-1) with
CC carbamoyl aspartate as substrate in the presence of Cd(2+)
CC (PubMed:15610022). {ECO:0000269|PubMed:15610022,
CC ECO:0000269|PubMed:6142052};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00219, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219,
CC ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
CC ECO:0000269|PubMed:6142052}.
CC -!- INDUCTION: Induced by pyrimidine limitation.
CC {ECO:0000269|PubMed:2885307}.
CC -!- DOMAIN: There is an asymmetry between active sites in the dimer, with
CC dihydroorotate bound to the active site of subunit A and N-carbamoyl-L-
CC aspartate bound to the active site of subunit B.
CC {ECO:0000269|PubMed:15826651}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00219, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X04469; CAA28157.1; -; Genomic_DNA.
DR EMBL; M16752; AAA24482.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74146.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35870.1; -; Genomic_DNA.
DR EMBL; D31709; BAA06514.1; -; Genomic_DNA.
DR PIR; A25008; DEECOO.
DR RefSeq; NP_415580.1; NC_000913.3.
DR RefSeq; WP_000126534.1; NZ_SSZK01000053.1.
DR PDB; 1J79; X-ray; 1.70 A; A/B=2-348.
DR PDB; 1XGE; X-ray; 1.90 A; A/B=2-348.
DR PDB; 2E25; X-ray; 2.70 A; A=2-348.
DR PDB; 2EG6; X-ray; 1.70 A; A/B=2-348.
DR PDB; 2EG7; X-ray; 2.00 A; A/B=2-348.
DR PDB; 2EG8; X-ray; 2.20 A; A/B=2-348.
DR PDB; 2Z24; X-ray; 1.90 A; A/B=2-348.
DR PDB; 2Z25; X-ray; 1.87 A; A/B=2-348.
DR PDB; 2Z26; X-ray; 1.29 A; A/B=2-348.
DR PDB; 2Z27; X-ray; 1.87 A; A/B=2-348.
DR PDB; 2Z28; X-ray; 1.87 A; A/B=2-348.
DR PDB; 2Z29; X-ray; 1.90 A; A/B=2-348.
DR PDB; 2Z2A; X-ray; 1.87 A; A/B=2-348.
DR PDB; 2Z2B; X-ray; 1.85 A; A=2-348.
DR PDB; 6HG1; X-ray; 2.12 A; A=107-119.
DR PDBsum; 1J79; -.
DR PDBsum; 1XGE; -.
DR PDBsum; 2E25; -.
DR PDBsum; 2EG6; -.
DR PDBsum; 2EG7; -.
DR PDBsum; 2EG8; -.
DR PDBsum; 2Z24; -.
DR PDBsum; 2Z25; -.
DR PDBsum; 2Z26; -.
DR PDBsum; 2Z27; -.
DR PDBsum; 2Z28; -.
DR PDBsum; 2Z29; -.
DR PDBsum; 2Z2A; -.
DR PDBsum; 2Z2B; -.
DR PDBsum; 6HG1; -.
DR AlphaFoldDB; P05020; -.
DR SMR; P05020; -.
DR BioGRID; 4261761; 32.
DR BioGRID; 850154; 4.
DR DIP; DIP-10624N; -.
DR IntAct; P05020; 6.
DR STRING; 511145.b1062; -.
DR BindingDB; P05020; -.
DR DrugBank; DB02129; Dihydroorotic Acid.
DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR DrugBank; DB04252; N-Carbamoylaspartic acid.
DR DrugBank; DB02262; Orotic acid.
DR MEROPS; M38.A02; -.
DR jPOST; P05020; -.
DR PaxDb; P05020; -.
DR PRIDE; P05020; -.
DR EnsemblBacteria; AAC74146; AAC74146; b1062.
DR EnsemblBacteria; BAA35870; BAA35870; BAA35870.
DR GeneID; 945787; -.
DR KEGG; ecj:JW1049; -.
DR KEGG; eco:b1062; -.
DR PATRIC; fig|1411691.4.peg.1206; -.
DR EchoBASE; EB0799; -.
DR eggNOG; COG0418; Bacteria.
DR HOGENOM; CLU_041558_1_0_6; -.
DR InParanoid; P05020; -.
DR OMA; TLHHISM; -.
DR PhylomeDB; P05020; -.
DR BioCyc; EcoCyc:DIHYDROOROT-MON; -.
DR BioCyc; MetaCyc:DIHYDROOROT-MON; -.
DR BRENDA; 3.5.2.3; 2026.
DR SABIO-RK; P05020; -.
DR UniPathway; UPA00070; UER00117.
DR EvolutionaryTrace; P05020; -.
DR PRO; PR:P05020; -.
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:0004151; F:dihydroorotase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:EcoCyc.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd01294; DHOase; 1.
DR HAMAP; MF_00219; PyrC_classII; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43137; PTHR43137; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00856; pyrC_dimer; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW Pyrimidine biosynthesis; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..348
FT /note="Dihydroorotase"
FT /id="PRO_0000147205"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:15610022"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:15826651, ECO:0007744|PDB:1XGE"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000305|PubMed:11401542, ECO:0000305|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT MOD_RES 103
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219,
FT ECO:0000269|PubMed:11401542, ECO:0000269|PubMed:15826651,
FT ECO:0007744|PDB:1J79, ECO:0007744|PDB:1XGE"
FT MUTAGEN 21
FT /note="R->K: 9-fold decrease in catalytic efficiency with
FT carbamoyl aspartate as substrate."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 21
FT /note="R->M,Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 45
FT /note="N->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 251
FT /note="D->A,H,N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 251
FT /note="D->E: 24-fold decrease in catalytic efficiency with
FT carbamoyl aspartate as substrate."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 251
FT /note="D->S: 3500-fold decrease in catalytic efficiency
FT with carbamoyl aspartate as substrate."
FT /evidence="ECO:0000269|PubMed:15610022"
FT MUTAGEN 255
FT /note="H->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15610022"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6HG1"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2Z26"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2E25"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:2Z26"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:2Z26"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2Z26"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:2Z26"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:2Z26"
SQ SEQUENCE 348 AA; 38827 MW; 179B35324204A111 CRC64;
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSI
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
