COABC_ECOLI
ID COABC_ECOLI Reviewed; 406 AA.
AC P0ABQ0; P24285; P76718; Q2M7V3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE AltName: Full=Phosphopantothenoylcysteine synthetase/decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPCS-PPCDC {ECO:0000255|HAMAP-Rule:MF_02225};
DE Includes:
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:10922366};
DE Short=PPC decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:10922366};
DE Short=PPC-DC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
DE EC=4.1.1.36 {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11358972};
DE AltName: Full=CoaC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
DE Includes:
DE RecName: Full=Phosphopantothenate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305};
DE EC=6.3.2.5 {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000269|PubMed:11278255, ECO:0000269|PubMed:12140293, ECO:0000269|PubMed:14686929};
DE AltName: Full=CoaB {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
DE AltName: Full=Phosphopantothenoylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
DE Short=PPC synthetase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPC-S {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
GN Name=coaBC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000303|PubMed:11278255};
GN Synonyms=dfp {ECO:0000303|PubMed:10922366};
GN OrderedLocusNames=b3639, JW5642;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-11, CHARACTERIZATION OF COAC ACTIVITY, COFACTOR,
RP SUBUNIT, PATHWAY, AND MUTAGENESIS OF PHE-46; HIS-75; PRO-89; THR-91;
RP MET-124; ASN-125 AND MET-128.
RX PubMed=10922366; DOI=10.1074/jbc.m004273200;
RA Kupke T., Uebele M., Schmid D., Jung G., Blaesse M., Steinbacher S.;
RT "Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals
RT a function for bacterial Dfp proteins in coenzyme A biosynthesis.";
RL J. Biol. Chem. 275:31838-31846(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-406.
RC STRAIN=K12;
RX PubMed=6139280; DOI=10.1002/j.1460-2075.1983.tb01529.x;
RA Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O.;
RT "Nucleotide sequence of the structural gene for dUTPase of Escherichia coli
RT K-12.";
RL EMBO J. 2:967-971(1983).
RN [6]
RP CHARACTERIZATION OF COAB ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=11278255; DOI=10.1074/jbc.c100033200;
RA Strauss E., Kinsland C., Ge Y., McLafferty F.W., Begley T.P.;
RT "Phosphopantothenoylcysteine synthetase from Escherichia coli.
RT Identification and characterization of the last unidentified coenzyme A
RT biosynthetic enzyme in bacteria.";
RL J. Biol. Chem. 276:13513-13516(2001).
RN [7]
RP CHARACTERIZATION OF COAC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF
RP GLY-11; GLY-14; GLY-15; ILE-16; ALA-17; TYR-19; LYS-20 AND ASN-125.
RX PubMed=11358972; DOI=10.1074/jbc.m103342200;
RA Kupke T.;
RT "Molecular characterization of the 4'-phosphopantothenoylcysteine
RT decarboxylase domain of bacterial Dfp flavoproteins.";
RL J. Biol. Chem. 276:27597-27604(2001).
RN [8]
RP CHARACTERIZATION OF COAB ACTIVITY, SUBUNIT, AND MUTAGENESIS OF THR-194;
RP THR-198; ASP-203; ASN-210; SER-212; LYS-215; ALA-275; LYS-289; LYS-291 AND
RP LYS-292.
RX PubMed=12140293; DOI=10.1074/jbc.m206188200;
RA Kupke T.;
RT "Molecular characterization of the 4'-phosphopantothenoylcysteine
RT synthetase domain of bacterial dfp flavoproteins.";
RL J. Biol. Chem. 277:36137-36145(2002).
RN [9]
RP CHARACTERIZATION OF COAB ACTIVITY, AND MUTAGENESIS OF ASN-210 AND ALA-275.
RX PubMed=14686929; DOI=10.1046/j.1432-1033.2003.03916.x;
RA Kupke T.;
RT "Active-site residues and amino acid specificity of the bacterial 4'-
RT phosphopantothenoylcysteine synthetase CoaB.";
RL Eur. J. Biochem. 271:163-172(2004).
RN [10] {ECO:0007744|PDB:1U7U, ECO:0007744|PDB:1U7W, ECO:0007744|PDB:1U7Z, ECO:0007744|PDB:1U80}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 181-406 OF MUTANT ASP-210
RP APOENZYME AND OF COMPLEX WITH SUBSTRATE; CTP AND CALCIUM IONS.
RX PubMed=15530362; DOI=10.1016/j.str.2004.08.007;
RA Stanitzek S., Augustin M.A., Huber R., Kupke T., Steinbacher S.;
RT "Structural basis of CTP-dependent peptide bond formation in coenzyme A
RT biosynthesis catalyzed by Escherichia coli PPC synthetase.";
RL Structure 12:1977-1988(2004).
CC -!- FUNCTION: Catalyzes two sequential steps in the biosynthesis of
CC coenzyme A. In the first step cysteine is conjugated to 4'-
CC phosphopantothenate to form 4-phosphopantothenoylcysteine
CC (PubMed:11278255, PubMed:12140293, PubMed:14686929). In the second step
CC the latter compound is decarboxylated to form 4'-phosphopantotheine
CC (PubMed:10922366, PubMed:11358972). {ECO:0000269|PubMed:10922366,
CC ECO:0000269|PubMed:11278255, ECO:0000269|PubMed:11358972,
CC ECO:0000269|PubMed:12140293, ECO:0000269|PubMed:14686929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-
CC phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11358972};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP +
CC diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine;
CC Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:59458, ChEBI:CHEBI:60377; EC=6.3.2.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:11278255, ECO:0000269|PubMed:12140293,
CC ECO:0000269|PubMed:14686929};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:11278255};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11278255,
CC ECO:0000269|PubMed:11358972};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:10922366};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:11278255}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_02225,
CC ECO:0000269|PubMed:10922366}.
CC -!- SUBUNIT: Homododecamer (PubMed:10922366, PubMed:11358972). The CoaC
CC domain is responsible for dodecamer formation (PubMed:11358972). The
CC CoaB domain forms homodimers (PubMed:12140293).
CC {ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11358972,
CC ECO:0000269|PubMed:12140293}.
CC -!- INTERACTION:
CC P0ABQ0; P0A7L0: rplA; NbExp=2; IntAct=EBI-548929, EBI-543771;
CC P0ABQ0; P0A7Z4: rpoA; NbExp=2; IntAct=EBI-548929, EBI-544985;
CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC oligomeric flavin containing Cys decarboxylase) superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61992.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L10328; AAA61992.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76663.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77653.1; -; Genomic_DNA.
DR EMBL; V01578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_418096.4; NC_000913.3.
DR RefSeq; WP_000050139.1; NZ_SSZK01000022.1.
DR PDB; 1U7U; X-ray; 2.40 A; A=181-406.
DR PDB; 1U7W; X-ray; 2.50 A; A/B/C=181-406.
DR PDB; 1U7Z; X-ray; 2.30 A; A/B/C=181-406.
DR PDB; 1U80; X-ray; 2.85 A; A/B/C=181-406.
DR PDBsum; 1U7U; -.
DR PDBsum; 1U7W; -.
DR PDBsum; 1U7Z; -.
DR PDBsum; 1U80; -.
DR AlphaFoldDB; P0ABQ0; -.
DR SMR; P0ABQ0; -.
DR BioGRID; 4261256; 26.
DR DIP; DIP-48472N; -.
DR IntAct; P0ABQ0; 2.
DR STRING; 511145.b3639; -.
DR DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR jPOST; P0ABQ0; -.
DR PaxDb; P0ABQ0; -.
DR PRIDE; P0ABQ0; -.
DR EnsemblBacteria; AAC76663; AAC76663; b3639.
DR EnsemblBacteria; BAE77653; BAE77653; BAE77653.
DR GeneID; 66672466; -.
DR GeneID; 949047; -.
DR KEGG; ecj:JW5642; -.
DR KEGG; eco:b3639; -.
DR PATRIC; fig|1411691.4.peg.3067; -.
DR EchoBASE; EB0004; -.
DR eggNOG; COG0452; Bacteria.
DR HOGENOM; CLU_033319_0_1_6; -.
DR InParanoid; P0ABQ0; -.
DR OMA; LDMIVAN; -.
DR PhylomeDB; P0ABQ0; -.
DR BioCyc; EcoCyc:EG10004-MON; -.
DR BioCyc; MetaCyc:EG10004-MON; -.
DR BRENDA; 6.3.2.5; 2026.
DR SABIO-RK; P0ABQ0; -.
DR UniPathway; UPA00241; UER00353.
DR UniPathway; UPA00241; UER00354.
DR EvolutionaryTrace; P0ABQ0; -.
DR PRO; PR:P0ABQ0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:EcoCyc.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:EcoCyc.
DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.10300; -; 1.
DR Gene3D; 3.40.50.1950; -; 1.
DR HAMAP; MF_02225; CoaBC; 1.
DR InterPro; IPR035929; CoaB-like_sf.
DR InterPro; IPR005252; CoaBC.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF04127; DFP; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF102645; SSF102645; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR00521; coaBC_dfp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Flavoprotein; FMN;
KW Ligase; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10922366"
FT CHAIN 2..406
FT /note="Coenzyme A biosynthesis bifunctional protein CoaBC"
FT /id="PRO_0000182022"
FT REGION 2..190
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000305|PubMed:11358972"
FT REGION 191..406
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000305|PubMed:11358972"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225, ECO:0000305"
FT BINDING 273..275
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 279
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 289
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 308..311
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 327
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 341
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT BINDING 345
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225,
FT ECO:0000269|PubMed:15530362, ECO:0007744|PDB:1U7W"
FT MUTAGEN 11
FT /note="G->D: In Dfp-707; temperature-sensitive, impairs
FT folding."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 14
FT /note="G->S: No FMN binding."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 15
FT /note="G->A: Less than 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 16
FT /note="I->L: Severely reduced activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 16
FT /note="I->V: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 17
FT /note="A->D: Less than 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 17
FT /note="A->G,S: Almost wild-type activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 19
FT /note="Y->F: Almost wild-type activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 19
FT /note="Y->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 20
FT /note="K->N,Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 20
FT /note="K->R: Almost wild-type activity."
FT /evidence="ECO:0000269|PubMed:11358972"
FT MUTAGEN 46
FT /note="F->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 75
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 89
FT /note="P->A: Binds FMN, but more loosely than wild-type."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 89
FT /note="P->D: No FMN binding."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 91
FT /note="T->V: Binds FMN."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 124
FT /note="M->L: No effect."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 125
FT /note="N->D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10922366,
FT ECO:0000269|PubMed:11358972"
FT MUTAGEN 128
FT /note="M->L: Severely reduced activity."
FT /evidence="ECO:0000269|PubMed:10922366"
FT MUTAGEN 158
FT /note="C->A,S: Loss of activity."
FT MUTAGEN 194
FT /note="T->V: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 198
FT /note="T->V: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 203
FT /note="D->N: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 210
FT /note="N->D: Loss of activity, reaction intermediate
FT detectable."
FT /evidence="ECO:0000269|PubMed:12140293,
FT ECO:0000269|PubMed:14686929"
FT MUTAGEN 210
FT /note="N->H,K: Loss of activity, reaction intermediate not
FT detectable."
FT /evidence="ECO:0000269|PubMed:12140293,
FT ECO:0000269|PubMed:14686929"
FT MUTAGEN 212
FT /note="S->A: Small effect on activity."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 215
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 275
FT /note="A->V: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:12140293,
FT ECO:0000269|PubMed:14686929"
FT MUTAGEN 289
FT /note="K->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 291
FT /note="K->Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:12140293"
FT MUTAGEN 292
FT /note="K->Q: Small effect on activity."
FT /evidence="ECO:0000269|PubMed:12140293"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:1U7Z"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:1U7Z"
FT HELIX 385..403
FT /evidence="ECO:0007829|PDB:1U7Z"
SQ SEQUENCE 406 AA; 43438 MW; CBD11B9347E8C6AB CRC64;
MSLAGKKIVL GVSGGIAAYK TPELVRRLRD RGADVRVAMT EAAKAFITPL SLQAVSGYPV
SDSLLDPAAE AAMGHIELGK WADLVILAPA TADLIARVAA GMANDLVSTI CLATPAPVAV
LPAMNQQMYR AAATQHNLEV LASRGLLIWG PDSGSQACGD IGPGRMLDPL TIVDMAVAHF
SPVNDLKHLN IMITAGPTRE PLDPVRYISN HSSGKMGFAI AAAAARRGAN VTLVSGPVSL
PTPPFVKRVD VMTALEMEAA VNASVQQQNI FIGCAAVADY RAATVAPEKI KKQATQGDEL
TIKMVKNPDI VAGVAALKDH RPYVVGFAAE TNNVEEYARQ KRIRKNLDLI CANDVSQPTQ
GFNSDNNALH LFWQDGDKVL PLERKELLGQ LLLDEIVTRY DEKNRR
