OTC1_ECOLI
ID OTC1_ECOLI Reviewed; 334 AA.
AC P04391; Q2M655;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ornithine carbamoyltransferase subunit I {ECO:0000303|PubMed:6369246};
DE Short=OTCase-1 {ECO:0000303|PubMed:6369246};
DE EC=2.1.3.3 {ECO:0000305|PubMed:3072022};
GN Name=argI {ECO:0000303|PubMed:6369246}; OrderedLocusNames=b4254, JW4211;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX PubMed=6369246; DOI=10.1093/nar/11.23.8509;
RA Bencini D.A., Houghton J.E., Hoover T.A., Foltermann K.F., Wild J.R.,
RA O'Donovan G.A.;
RT "The DNA sequence of argI from Escherichia coli K12.";
RL Nucleic Acids Res. 11:8509-8518(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ARG-58, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3072022; DOI=10.1021/bi00424a021;
RA Kuo L.C., Miller A.W., Lee S., Kozuma C.;
RT "Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase:
RT role of arginine-57 in substrate binding and catalysis.";
RL Biochemistry 27:8823-8832(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 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 [7]
RP SUBUNIT.
RX PubMed=4558857; DOI=10.1111/j.1432-1033.1972.tb01814.x;
RA Legrain C., Halleux P., Stalon V., Glansdorff N.;
RT "The dual genetic control of ornithine carbamolytransferase in Escherichia
RT coli. A case of bacterial hybrid enzymes.";
RL Eur. J. Biochem. 27:93-102(1972).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=789338; DOI=10.1128/jb.128.1.35-38.1976;
RA Legrain C., Stalon V., Glansdorff N.;
RT "Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary
RT significance and the isolation of lambdaargF and lambdaargI transducing
RT bacteriophages.";
RL J. Bacteriol. 128:35-38(1976).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=7048313; DOI=10.1073/pnas.79.7.2250;
RA Kuo L.C., Lipscomb W.N., Kantrowitz E.R.;
RT "Zn(II)-induced cooperativity of Escherichia coli ornithine
RT transcarbamoylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2250-2254(1982).
RN [10]
RP MUTAGENESIS OF ARG-58.
RX PubMed=2674127; DOI=10.1016/s0021-9258(18)71613-x;
RA Kuo L.C., Seaton B.A.;
RT "X-ray diffraction analysis on single crystals of recombinant Escherichia
RT coli ornithine transcarbamoylase.";
RL J. Biol. Chem. 264:16246-16248(1989).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=2105398; DOI=10.1016/0022-2836(90)90025-h;
RA Lee S., Shen W.H., Miller A.W., Kuo L.C.;
RT "Zn2+ regulation of ornithine transcarbamoylase. I. Mechanism of action.";
RL J. Mol. Biol. 211:255-269(1990).
RN [12]
RP MUTAGENESIS OF CYS-274, AND ACTIVITY REGULATION.
RX PubMed=2405164; DOI=10.1016/0022-2836(90)90026-i;
RA Kuo L.C., Caron C., Lee S., Herzberg W.;
RT "Zn2+ regulation of ornithine transcarbamoylase. II. Metal binding site.";
RL J. Mol. Biol. 211:271-280(1990).
RN [13]
RP MUTAGENESIS OF SER-56; LYS-87; ARG-320 AND ALA-326, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8845761; DOI=10.1002/pro.5560050416;
RA Murata L.B., Schachman H.K.;
RT "Structural similarity between ornithine and aspartate transcarbamoylases
RT of Escherichia coli: characterization of the active site and evidence for
RT an interdomain carboxy-terminal helix in ornithine transcarbamoylase.";
RL Protein Sci. 5:709-718(1996).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=9253409; DOI=10.1038/nsb0897-622;
RA Jin L., Seaton B.A., Head J.F.;
RT "Crystal structure at 2.8-A resolution of anabolic ornithine
RT transcarbamylase from Escherichia coli.";
RL Nat. Struct. Biol. 4:622-625(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=9275160; DOI=10.1073/pnas.94.18.9550;
RA Ha Y., McCann M.T., Tuchman M., Allewell N.M.;
RT "Substrate-induced conformational change in a trimeric ornithine
RT transcarbamoylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9550-9555(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-333 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=10747936; DOI=10.1074/jbc.m000585200;
RA Langley D.B., Templeton M.D., Fields B.A., Mitchell R.E., Collyer C.A.;
RT "Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-
RT Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue?
RT Crystal structure and implications for catalytic mechanism.";
RL J. Biol. Chem. 275:20012-20019(2000).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline, which is a substrate for argininosuccinate
CC synthetase, the enzyme involved in the final step in arginine
CC biosynthesis. {ECO:0000269|PubMed:3072022, ECO:0000269|PubMed:789338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000305|PubMed:3072022};
CC -!- ACTIVITY REGULATION: Reversely inhibited by N-(N-
CC Sulfodiaminophosphinyl)-L-ornithine (PubMed:10747936). Zinc is an
CC allosteric regulator of the substrate-bound enzyme and a competitive
CC inhibitor of the free enzyme (PubMed:7048313, PubMed:2105398,
CC PubMed:2405164). {ECO:0000269|PubMed:10747936,
CC ECO:0000269|PubMed:2105398, ECO:0000269|PubMed:2405164,
CC ECO:0000269|PubMed:7048313}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for carbamoyl phosphate {ECO:0000269|PubMed:789338};
CC KM=50 uM for carbamoyl phosphate {ECO:0000269|PubMed:3072022};
CC KM=0.18 mM for L-ornithine {ECO:0000269|PubMed:8845761};
CC KM=0.32 mM for L-ornithine {ECO:0000269|PubMed:3072022};
CC KM=5 mM for L-ornithine {ECO:0000269|PubMed:789338};
CC Vmax=0.29 umol/min/ug enzyme {ECO:0000269|PubMed:8845761};
CC Note=kcat is 14000 min(-1) for L-ornithine. kcat is 13000 min(-1) for
CC carbamoyl phosphate. {ECO:0000269|PubMed:3072022};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
CC -!- SUBUNIT: In E.coli strain K12, trimer of identical or non-identical
CC chains are composed of ArgI (I) and/or ArgF (F) (PubMed:6369246,
CC PubMed:4558857, PubMed:789338). The trimer has the following
CC composition: FFI, FFF, FII, III (PubMed:6369246, PubMed:4558857,
CC PubMed:789338). E.coli strains B and W, which are known to contain only
CC ArgI, produce only a trimer of identical chains (III).
CC {ECO:0000269|PubMed:10747936, ECO:0000269|PubMed:4558857,
CC ECO:0000269|PubMed:6369246, ECO:0000269|PubMed:789338,
CC ECO:0000269|PubMed:9253409, ECO:0000269|PubMed:9275160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; X00210; CAA25037.1; -; Genomic_DNA.
DR EMBL; J02842; AAA23483.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97150.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77211.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78251.1; -; Genomic_DNA.
DR PIR; A31314; OWECI.
DR RefSeq; NP_418675.1; NC_000913.3.
DR RefSeq; WP_000012931.1; NZ_LN832404.1.
DR PDB; 1AKM; X-ray; 2.80 A; A/B/C=2-334.
DR PDB; 1DUV; X-ray; 1.70 A; G/H/I=2-334.
DR PDB; 2OTC; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I=2-334.
DR PDBsum; 1AKM; -.
DR PDBsum; 1DUV; -.
DR PDBsum; 2OTC; -.
DR AlphaFoldDB; P04391; -.
DR SMR; P04391; -.
DR BioGRID; 4262723; 6.
DR ComplexPortal; CPX-5624; Ornithine transcarbamoylase complex, argIII variant.
DR ComplexPortal; CPX-5625; Ornithine transcarbamoylase complex, argFII variant.
DR ComplexPortal; CPX-5626; Ornithine transcarbamoylase complex, argFFI variant.
DR DIP; DIP-9143N; -.
DR IntAct; P04391; 7.
DR STRING; 511145.b4254; -.
DR DrugBank; DB02965; Ndelta-(N'-Sulphodiaminophosphinyl)-L-Ornithine.
DR SWISS-2DPAGE; P04391; -.
DR PaxDb; P04391; -.
DR PRIDE; P04391; -.
DR EnsemblBacteria; AAC77211; AAC77211; b4254.
DR EnsemblBacteria; BAE78251; BAE78251; BAE78251.
DR GeneID; 948774; -.
DR KEGG; ecj:JW4211; -.
DR KEGG; eco:b4254; -.
DR PATRIC; fig|1411691.4.peg.2450; -.
DR EchoBASE; EB0067; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_1_6; -.
DR InParanoid; P04391; -.
DR OMA; KYNGYEQ; -.
DR PhylomeDB; P04391; -.
DR BioCyc; EcoCyc:CHAINI-MON; -.
DR BioCyc; MetaCyc:CHAINI-MON; -.
DR BRENDA; 2.1.3.3; 2026.
DR SABIO-RK; P04391; -.
DR UniPathway; UPA00068; UER00112.
DR EvolutionaryTrace; P04391; -.
DR PRO; PR:P04391; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009348; C:ornithine carbamoyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:EcoCyc.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR InterPro; IPR024904; OTCase_ArgI.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Arginine biosynthesis; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..334
FT /note="Ornithine carbamoyltransferase subunit I"
FT /id="PRO_0000112918"
FT BINDING 56..59
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 83
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 107
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 134..137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 168
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 232
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 236..237
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 274..275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0000269|PubMed:9275160, ECO:0007744|PDB:1DUV,
FT ECO:0007744|PDB:2OTC"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:2405164"
FT BINDING 320
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|PubMed:10747936,
FT ECO:0007744|PDB:1DUV"
FT MUTAGEN 56
FT /note="S->H: Much less active than the wild-type."
FT /evidence="ECO:0000269|PubMed:8845761"
FT MUTAGEN 58
FT /note="R->G: The mutant is drastically inefficient in
FT catalysis, but affects only moderately the binding of
FT carbamoyl phosphate."
FT /evidence="ECO:0000269|PubMed:2674127,
FT ECO:0000269|PubMed:3072022"
FT MUTAGEN 87
FT /note="K->Q: Much less active than the wild-type."
FT /evidence="ECO:0000269|PubMed:8845761"
FT MUTAGEN 274
FT /note="C->A: Zinc ion is no longer a tight-binding
FT inhibitor and does not promote isomerization."
FT /evidence="ECO:0000269|PubMed:2405164"
FT MUTAGEN 320
FT /note="R->A: Much less active than the wild-type."
FT /evidence="ECO:0000269|PubMed:8845761"
FT MUTAGEN 326
FT /note="A->G: Activity greater than the wild-type and Km for
FT ornithwinas increases about twofold."
FT /evidence="ECO:0000269|PubMed:8845761"
FT CONFLICT 12
FT /note="L -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> Q (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="A -> R (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..142
FT /note="LADL -> IEYK (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="E -> Q (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> A (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="D -> G (in Ref. 1; CAA25037)"
FT /evidence="ECO:0000305"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2OTC"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1DUV"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1DUV"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:1DUV"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1AKM"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1DUV"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:1DUV"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2OTC"
FT HELIX 313..332
FT /evidence="ECO:0007829|PDB:1DUV"
SQ SEQUENCE 334 AA; 36907 MW; 75D67EE69C229E5C CRC64;
MSGFYHKHFL KLLDFTPAEL NSLLQLAAKL KADKKSGKEE AKLTGKNIAL IFEKDSTRTR
CSFEVAAYDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGYG QEIVETLAEY
ASVPVWNGLT NEFHPTQLLA DLLTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
GLDLRLVAPQ ACWPEAALVT ECRALAQQNG GNITLTEDVA KGVEGADFIY TDVWVSMGEA
KEKWAERIAL LREYQVNSKM MQLTGNPEVK FLHCLPAFHD DQTTLGKKMA EEFGLHGGME
VTDEVFESAA SIVFDQAENR MHTIKAVMVA TLSK
