BIOD1_ECOLI
ID BIOD1_ECOLI Reviewed; 225 AA.
AC P13000; Q2MBJ1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD 1 {ECO:0000255|HAMAP-Rule:MF_00336};
DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336};
DE AltName: Full=DTB synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00336};
DE Short=DTBS 1 {ECO:0000255|HAMAP-Rule:MF_00336};
DE AltName: Full=Dethiobiotin synthase 1 {ECO:0000255|HAMAP-Rule:MF_00336};
GN Name=bioD1 {ECO:0000255|HAMAP-Rule:MF_00336};
GN OrderedLocusNames=b0778, JW0761;
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=3058702; DOI=10.1016/s0021-9258(19)77675-3;
RA Otsuka A.J., Buoncristiani M.R., Howard P.K., Flamm J., Johnson O.,
RA Yamamoto R., Uchida K., Cook C., Ruppert J., Matsuzaki J.;
RT "The Escherichia coli biotin biosynthetic enzyme sequences predicted from
RT the nucleotide sequence of the bio operon.";
RL J. Biol. Chem. 263:19577-19585(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20 AND
RP 224-225.
RX PubMed=8289297; DOI=10.1006/jmbi.1994.1030;
RA Alexeev D., Bury S.M., Boys C.W.G., Turner M.A., Sawyer L., Ramsey A.J.,
RA Baxter H.C., Baxter R.L.;
RT "Sequence and crystallization of Escherichia coli dethiobiotin synthetase,
RT the penultimate enzyme of biotin biosynthesis.";
RL J. Mol. Biol. 235:774-776(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pearson B.M., McKee R.A.;
RT "Genetic material for expression of biotin synthetase enzymes.";
RL Patent number GB2216530, 11-OCT-1989.
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 FUNCTION IN BIOTIN BIOSYNTHESIS.
RX PubMed=4892372; DOI=10.1128/jb.98.3.1227-1231.1969;
RA Eisenberg M.A., Krell K.;
RT "Synthesis of desthiobiotin from 7,8-diaminopelargonic acid in biotin
RT auxotrophs of Escherichia coli K-12.";
RL J. Bacteriol. 98:1227-1231(1969).
RN [7]
RP FUNCTION AS A DETHIOBIOTIN SYNTHETASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=4921568; DOI=10.1016/s0021-9258(18)62570-0;
RA Krell K., Eisenberg M.A.;
RT "The purification and properties of dethiobiotin synthetase.";
RL J. Biol. Chem. 245:6558-6566(1970).
RN [8]
RP ACTIVE SITE, AND MUTAGENESIS OF THR-12; GLU-13; LYS-16; LYS-38 AND SER-42.
RX PubMed=9125495; DOI=10.1021/bi9631677;
RA Yang G., Sandalova T., Lohman K., Lindqvist Y., Rendina A.R.;
RT "Active site mutants of Escherichia coli dethiobiotin synthetase: effects
RT of mutations on enzyme catalytic and structural properties.";
RL Biochemistry 36:4751-4760(1997).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-176.
RC STRAIN=K12;
RX PubMed=25801336; DOI=10.1016/j.tube.2015.02.046;
RA Salaemae W., Yap M.Y., Wegener K.L., Booker G.W., Wilce M.C., Polyak S.W.;
RT "Nucleotide triphosphate promiscuity in Mycobacterium tuberculosis
RT dethiobiotin synthetase.";
RL Tuberculosis 95:259-266(2015).
RN [10] {ECO:0007744|PDB:1DTS}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RX PubMed=8081756; DOI=10.1016/s0969-2126(00)00042-3;
RA Huang W., Lindqvist Y., Schneider G., Gibson K.J., Flint D., Lorimer G.;
RT "Crystal structure of an ATP-dependent carboxylase, dethiobiotin
RT synthetase, at 1.65-A resolution.";
RL Structure 2:407-414(1994).
RN [11] {ECO:0007744|PDB:1DBS}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ATP AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=7881906; DOI=10.1016/s0969-2126(94)00109-x;
RA Alexeev D., Baxter R.L., Sawyer L.;
RT "Mechanistic implications and family relationships from the structure of
RT dethiobiotin synthetase.";
RL Structure 2:1061-1072(1994).
RN [12] {ECO:0007744|PDB:1DAD, ECO:0007744|PDB:1DAE, ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAI}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-224 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, ATP AND MAGNESIUM IONS, AND REACTION MECHANISM.
RX PubMed=7669756; DOI=10.1021/bi00035a004;
RA Huang W., Jia J., Gibson K.J., Taylor W.S., Rendina A.R., Schneider G.,
RA Lindqvist Y.;
RT "Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based
RT on crystallographic studies of complexes with substrates and a reaction
RT intermediate.";
RL Biochemistry 34:10985-10995(1995).
RN [13] {ECO:0007744|PDB:1A82, ECO:0007744|PDB:1DAK}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ATP, AND MAGNESIUM IONS.
RX PubMed=9576910; DOI=10.1073/pnas.95.10.5495;
RA Kaeck H., Gibson K.J., Lindqvist Y., Schneider G.;
RT "Snapshot of a phosphorylated substrate intermediate by kinetic
RT crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5495-5500(1998).
RN [14] {ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAM}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ATP AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=9865950; DOI=10.1002/pro.5560071209;
RA Kaeck H., Sandmark J., Gibson K.J., Schneider G., Lindqvist Y.;
RT "Crystal structure of two quaternary complexes of dethiobiotin synthetase,
RT enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-
RT phosphate; implications for catalysis.";
RL Protein Sci. 7:2560-2566(1998).
RN [15] {ECO:0007744|PDB:1BYI}
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS).
RX PubMed=10089457; DOI=10.1107/s090744499801381x;
RA Sandalova T., Schneider G., Kack H., Lindqvist Y.;
RT "Structure of dethiobiotin synthetase at 0.97-A resolution.";
RL Acta Crystallogr. D 55:610-624(1999).
CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC form a ureido ring. Only CTP can partially replace ATP while
CC diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid
CC (PubMed:4892372, PubMed:4921568). In another study both CTP and GTP
CC (but not ITP, TTP or UTP) can partially replace ATP (PubMed:25801336).
CC {ECO:0000269|PubMed:25801336, ECO:0000269|PubMed:4892372,
CC ECO:0000269|PubMed:4921568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00336, ECO:0000269|PubMed:4921568};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336,
CC ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:7881906,
CC ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950};
CC Note=Binds 1 Mg(2+) per subunit, in one structure a second Mg(2+) was
CC seen. {ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:7881906,
CC ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.2 uM for DAPA (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=600 uM for NaHCO3 (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=10.5 uM for ATP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=1.10 mM for CTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC KM=1.56 mM for GTP (at pH 7.5, 37 degrees Celsius)
CC {ECO:0000269|PubMed:25801336};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00336,
CC ECO:0000269|PubMed:4921568, ECO:0000269|PubMed:7669756,
CC ECO:0000269|PubMed:7881906, ECO:0000269|PubMed:8081756,
CC ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00336}.
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DR EMBL; J04423; AAA23518.1; -; Genomic_DNA.
DR EMBL; S68059; AAB29683.2; -; Genomic_DNA.
DR EMBL; A11538; CAA00967.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73865.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76365.1; -; Genomic_DNA.
DR PIR; B64814; SYECDB.
DR RefSeq; NP_415299.1; NC_000913.3.
DR RefSeq; WP_000044843.1; NZ_LN832404.1.
DR PDB; 1A82; X-ray; 1.80 A; A=2-225.
DR PDB; 1BS1; X-ray; 1.80 A; A=2-225.
DR PDB; 1BYI; X-ray; 0.97 A; A=2-225.
DR PDB; 1DAD; X-ray; 1.60 A; A=2-225.
DR PDB; 1DAE; X-ray; 1.70 A; A=2-225.
DR PDB; 1DAF; X-ray; 1.70 A; A=2-225.
DR PDB; 1DAG; X-ray; 1.64 A; A=2-225.
DR PDB; 1DAH; X-ray; 1.64 A; A=2-225.
DR PDB; 1DAI; X-ray; 1.64 A; A=2-225.
DR PDB; 1DAK; X-ray; 1.60 A; A=2-225.
DR PDB; 1DAM; X-ray; 1.80 A; A=2-225.
DR PDB; 1DBS; X-ray; 1.80 A; A=2-225.
DR PDB; 1DTS; X-ray; 1.65 A; A=1-224.
DR PDBsum; 1A82; -.
DR PDBsum; 1BS1; -.
DR PDBsum; 1BYI; -.
DR PDBsum; 1DAD; -.
DR PDBsum; 1DAE; -.
DR PDBsum; 1DAF; -.
DR PDBsum; 1DAG; -.
DR PDBsum; 1DAH; -.
DR PDBsum; 1DAI; -.
DR PDBsum; 1DAK; -.
DR PDBsum; 1DAM; -.
DR PDBsum; 1DBS; -.
DR PDBsum; 1DTS; -.
DR AlphaFoldDB; P13000; -.
DR SMR; P13000; -.
DR BioGRID; 4259956; 20.
DR IntAct; P13000; 3.
DR STRING; 511145.b0778; -.
DR DrugBank; DB02941; 3-(1-Aminoethyl)Nonanedioic Acid.
DR DrugBank; DB01715; 7,8-Diamino-Nonanoic Acid.
DR DrugBank; DB03624; 7-(Carboxyamino)-8-Amino-Nonanoic Acid.
DR DrugBank; DB03775; Dethiobiotin.
DR DrugBank; DB02927; Mixed Carbamic Phosphoric Acid Anhydride of 7,8-Diaminononanic Acid.
DR PaxDb; P13000; -.
DR PRIDE; P13000; -.
DR EnsemblBacteria; AAC73865; AAC73865; b0778.
DR EnsemblBacteria; BAE76365; BAE76365; BAE76365.
DR GeneID; 945387; -.
DR KEGG; ecj:JW0761; -.
DR KEGG; eco:b0778; -.
DR PATRIC; fig|1411691.4.peg.1500; -.
DR EchoBASE; EB0118; -.
DR eggNOG; COG0132; Bacteria.
DR HOGENOM; CLU_072551_0_0_6; -.
DR InParanoid; P13000; -.
DR OMA; SPHWAAE; -.
DR PhylomeDB; P13000; -.
DR BioCyc; EcoCyc:DETHIOBIOTIN-SYN-MON; -.
DR BioCyc; MetaCyc:DETHIOBIOTIN-SYN-MON; -.
DR BRENDA; 6.3.3.3; 2026.
DR SABIO-RK; P13000; -.
DR UniPathway; UPA00078; UER00161.
DR EvolutionaryTrace; P13000; -.
DR PRO; PR:P13000; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43210; PTHR43210; 1.
DR PIRSF; PIRSF006755; DTB_synth; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00347; bioD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin biosynthesis; Cytoplasm;
KW Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8289297"
FT CHAIN 2..225
FT /note="ATP-dependent dethiobiotin synthetase BioD 1"
FT /id="PRO_0000187961"
FT ACT_SITE 38
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000305|PubMed:9125495"
FT BINDING 13..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910,
FT ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82,
FT ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD,
FT ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG,
FT ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAK,
FT ECO:0007744|PDB:1DAM"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9865950,
FT ECO:0007744|PDB:1BS1"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950,
FT ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1,
FT ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910,
FT ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1BS1,
FT ECO:0007744|PDB:1DAE, ECO:0007744|PDB:1DAF,
FT ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH,
FT ECO:0007744|PDB:1DAI, ECO:0007744|PDB:1DAK,
FT ECO:0007744|PDB:1DAM"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:9576910, ECO:0007744|PDB:1A82"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950,
FT ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1,
FT ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM"
FT BINDING 116..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:9576910, ECO:0007744|PDB:1A82,
FT ECO:0007744|PDB:1DAK"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950,
FT ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1,
FT ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM"
FT BINDING 176..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910,
FT ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82,
FT ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD,
FT ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG,
FT ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAK,
FT ECO:0007744|PDB:1DAM"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7669756,
FT ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950,
FT ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1,
FT ECO:0007744|PDB:1DAE, ECO:0007744|PDB:1DAF,
FT ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH,
FT ECO:0007744|PDB:1DAI, ECO:0007744|PDB:1DAK,
FT ECO:0007744|PDB:1DAM"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910,
FT ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82,
FT ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD,
FT ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG,
FT ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAK,
FT ECO:0007744|PDB:1DAM"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336,
FT ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910,
FT ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82,
FT ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD,
FT ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAH,
FT ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM"
FT MUTAGEN 12
FT /note="T->V: Strong decrease in ATP affinity; essential
FT role for this residue in the steady-state affinity for
FT ATP."
FT /evidence="ECO:0000269|PubMed:9125495"
FT MUTAGEN 13
FT /note="E->A,D: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:9125495"
FT MUTAGEN 16
FT /note="K->Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:9125495"
FT MUTAGEN 38
FT /note="K->L,Q,R: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:9125495"
FT MUTAGEN 42
FT /note="S->A,C: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:9125495"
FT MUTAGEN 176
FT /note="N->A: Increases affinity for CTP 3-fold, no change
FT for ATP."
FT /evidence="ECO:0000269|PubMed:25801336"
FT CONFLICT 29
FT /note="A -> R (in Ref. 1; AAA23518)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="QQ -> HK (in Ref. 3; CAA00967)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..225
FT /note="APLLGEIPWLAENPENAATGKYINLALL -> RRCWERSPGLQKIQKMRQPE
FT ST (in Ref. 1; AAA23518)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1DAI"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1DAI"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1DAD"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1BYI"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1BYI"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1DAD"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1BYI"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1BYI"
SQ SEQUENCE 225 AA; 24140 MW; 9AE76F3BE6565780 CRC64;
MSKRYFVTGT DTEVGKTVAS CALLQAAKAA GYRTAGYKPV ASGSEKTPEG LRNSDALALQ
RNSSLQLDYA TVNPYTFAEP TSPHIISAQE GRPIESLVMS AGLRALEQQA DWVLVEGAGG
WFTPLSDTFT FADWVTQEQL PVILVVGVKL GCINHAMLTA QVIQHAGLTL AGWVANDVTP
PGKRHAEYMT TLTRMIPAPL LGEIPWLAEN PENAATGKYI NLALL
