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Database: UniProt
Entry: Q1RE99_ECOUT
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Original site: Q1RE99_ECOUT 
ID   Q1RE99_ECOUT            Unreviewed;       249 AA.
AC   Q1RE99;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   SubName: Full=Molybdopterin biosynthesis protein MoeB {ECO:0000313|EMBL:ABE06315.1};
DE            EC=2.7.7.- {ECO:0000313|EMBL:ABE06315.1};
GN   Name=moeB {ECO:0000313|EMBL:ABE06315.1};
GN   OrderedLocusNames=UTI89_C0829 {ECO:0000313|EMBL:ABE06315.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE06315.1};
RN   [1] {ECO:0000313|EMBL:ABE06315.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 {ECO:0000313|EMBL:ABE06315.1};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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DR   EMBL; CP000243; ABE06315.1; -; Genomic_DNA.
DR   RefSeq; WP_000829253.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1RE99; -.
DR   SMR; Q1RE99; -.
DR   KEGG; eci:UTI89_C0829; -.
DR   HOGENOM; CLU_013325_10_3_6; -.
DR   OMA; SAKWKLE; -.
DR   Proteomes; UP000001952; 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   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; 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; IPR012730; Mopterin_Synthase_Sase_MoeB.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   NCBIfam; TIGR02355; moeB; 1.
DR   PANTHER; PTHR10953:SF194; MOLYBDOPTERIN-SYNTHASE 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   Nucleotidyltransferase {ECO:0000313|EMBL:ABE06315.1};
KW   Transferase {ECO:0000313|EMBL:ABE06315.1}.
FT   DOMAIN          12..246
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   249 AA;  26685 MW;  ED44C10BC9F95C43 CRC64;
     MAELSDQEML RYNRQIILRG FDFDGQEALK DSRVLVVGLG GLGCAASQYL ASAGVGNLTL
     LDFDTVSLSN LQRQTLHSDA TVGQPKVESA RDALTRINPH IAITPVNALL DDAELAAMIA
     KHDLVLDCTD NVAVRNQLNA GCFAAKVPLV SGAAIRMEGQ ITVFTYQDGE PCYHCLSRLF
     GENALTCVEA GVMAPLIGVI GSLQAMEAIK LLAGYGKPAS GKIVMYDAMT CQFREMKLMR
     NPGCEVCGQ
//
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