ID E1J1M1_ECOLX Unreviewed; 251 AA.
AC E1J1M1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Thiazole biosynthesis adenylyltransferase ThiF {ECO:0000313|EMBL:EFK70118.1};
GN Name=thiF {ECO:0000313|EMBL:EFK70118.1};
GN ORFNames=HMPREF9347_00769 {ECO:0000313|EMBL:EFK70118.1};
OS Escherichia coli MS 124-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK70118.1, ECO:0000313|Proteomes:UP000003390};
RN [1] {ECO:0000313|EMBL:EFK70118.1, ECO:0000313|Proteomes:UP000003390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK70118.1,
RC ECO:0000313|Proteomes:UP000003390};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR612731-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR612731-3};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFK70118.1}.
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DR EMBL; ADWT01000004; EFK70118.1; -; Genomic_DNA.
DR RefSeq; WP_000999737.1; NZ_ADWT01000004.1.
DR AlphaFoldDB; E1J1M1; -.
DR SMR; E1J1M1; -.
DR GeneID; 75205510; -.
DR Proteomes; UP000003390; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR012731; Adenyl_ThiF.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR NCBIfam; TIGR02356; adenyl_thiF; 1.
DR PANTHER; PTHR10953:SF240; SULFUR CARRIER PROTEIN THIS ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR612731-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR612731-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR612731-2};
KW Nucleotidyltransferase {ECO:0000313|EMBL:EFK70118.1};
KW Transferase {ECO:0000313|EMBL:EFK70118.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR612731-3}.
FT DOMAIN 9..242
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT ACT_SITE 184
FT /note="Glycyl persulfide ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-1"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 127..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT CROSSLNK 184
FT /note="Glycyl cysteine dithioester (Cys-Gly) (interchain
FT with G-Cter in ThiS)"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-4"
SQ SEQUENCE 251 AA; 26970 MW; 9CB9E20FD094F12D CRC64;
MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA GVGTLVLADD
DDVHLSNLQR QILFTTEDID RPKSQVSQQR LTQLNPDIQL TALQQRLTGE ALKDAVARAD
VVLDCTDNMA TRQEINAACV ALNTPLITAS AVGFGGQLMV LTPPWEQGCY RCLWPDNQEP
ERNCRTAGVV GPVVGVMGTL QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRASGC
PVCGGSNADP V
//
