ID A7GLF9_BACCN Unreviewed; 339 AA.
AC A7GLF9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Thiazole biosynthesis adenylyltransferase ThiF {ECO:0000313|EMBL:ABS20967.1};
GN OrderedLocusNames=Bcer98_0620 {ECO:0000313|EMBL:ABS20967.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20967.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS20967.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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DR EMBL; CP000764; ABS20967.1; -; Genomic_DNA.
DR RefSeq; WP_011983723.1; NC_009674.1.
DR AlphaFoldDB; A7GLF9; -.
DR STRING; 315749.Bcer98_0620; -.
DR GeneID; 56416209; -.
DR KEGG; bcy:Bcer98_0620; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_1_9; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000002300; Chromosome.
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:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 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 Nucleotidyltransferase {ECO:0000313|EMBL:ABS20967.1};
KW Transferase {ECO:0000313|EMBL:ABS20967.1}.
FT DOMAIN 5..241
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 339 AA; 37945 MW; C9374B2967A9E904 CRC64;
MNNRYSRQEL FSSIGEKGQK KIGKKHVFII GAGALGSANA EMLVRAGVGN VTIVDRDYID
WSNLQRQQLY AEEDVKNHLP KAIAAKQRLK AINSSVVVKA FVKDITAEEL EELVTNVDVI
IDATDNFETR FIINDISQKY SIPWIYGACV GSYGLSYTIL PGKTPCLSCL LQSIPLGGAT
CDTAGIISPA VSIVVSHQVT ETLKLLVEDY KALRDGLVSF DVWKNEYSCM NVQKLKKDHC
PSCGEKAIYP YLNKENTSKT AVLCGRNTVQ IRPPHKEKLD FHRYKELLRD RVADLTVNPY
LLSFRADGKR LVAFQDGRVL VYGTKEIAEA KTIYHRYFG
//
