ID B7NFT3_ECOLU Unreviewed; 251 AA.
AC B7NFT3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Thiamin (Thiazole moiety) biosynthesis protein {ECO:0000313|EMBL:CAR15640.1};
DE EC=2.7.7.- {ECO:0000313|EMBL:CAR15640.1};
GN Name=thiF {ECO:0000313|EMBL:CAR15640.1};
GN OrderedLocusNames=ECUMN_4516 {ECO:0000313|EMBL:CAR15640.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR15640.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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};
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DR EMBL; CU928163; CAR15640.1; -; Genomic_DNA.
DR RefSeq; WP_000999730.1; NC_011751.1.
DR RefSeq; YP_002415130.1; NC_011751.1.
DR AlphaFoldDB; B7NFT3; -.
DR STRING; 585056.ECUMN_4516; -.
DR KEGG; eum:ECUMN_4516; -.
DR PATRIC; fig|585056.7.peg.4686; -.
DR HOGENOM; CLU_013325_10_3_6; -.
DR Proteomes; UP000007097; Chromosome.
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; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
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:CAR15640.1};
KW Transferase {ECO:0000313|EMBL:CAR15640.1};
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; 26996 MW; A5E37B7EB6855BBB CRC64;
MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA GVGTLVLADD
DDVHLSNLQR QILFTTEDID RPKSQVSHQR LTQLNPDIQL TALQQRLTGE ALKDAVARAD
VVLDCTDNMA TRQEINTACV ALNTPLITAS AVGFGGQLMV LTPPWEQGCY RCLWPDTQDP
ERNCRTAGVV GPVVGVMGTL QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRATGC
PVCGGSNADP V
//
