ID   MOG_ECO57               Reviewed;         195 AA.
AC   P0AF04; P28694; Q8KMY3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Molybdopterin adenylyltransferase;
DE            Short=MPT adenylyltransferase;
DE            EC=2.7.7.75;
GN   Name=mog; OrderedLocusNames=Z0009, ECs0009;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of the
CC       biosynthesis of the molybdenum-cofactor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; EC=2.7.7.75;
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG54309.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33432.1; -; Genomic_DNA.
DR   PIR; A85481; A85481.
DR   PIR; A90630; A90630.
DR   RefSeq; NP_308036.1; NC_002695.1.
DR   RefSeq; WP_001295414.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AF04; -.
DR   SMR; P0AF04; -.
DR   STRING; 155864.EDL933_0009; -.
DR   EnsemblBacteria; AAG54309; AAG54309; Z0009.
DR   EnsemblBacteria; BAB33432; BAB33432; ECs_0009.
DR   GeneID; 58461422; -.
DR   GeneID; 913401; -.
DR   KEGG; ece:Z0009; -.
DR   KEGG; ecs:ECs_0009; -.
DR   PATRIC; fig|386585.9.peg.106; -.
DR   eggNOG; COG0521; Bacteria.
DR   HOGENOM; CLU_077358_1_0_6; -.
DR   OMA; EYLTSEW; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..195
FT                   /note="Molybdopterin adenylyltransferase"
FT                   /id="PRO_0000170983"
SQ   SEQUENCE   195 AA;  21222 MW;  3610EBDB4BE97872 CRC64;
     MNTLRIGLVS ISDRASSGVY QDKGIPALEE WLTSALTTPF ELETRLIPDE QAIIEQTLCE
     LVDEMSCHLV LTTGGTGPAR RDVTPDATLA VADREMPGFG EQMRQISLHF VPTAILSRQV
     GVIRKQALIL NLPGQPKSIK ETLEGVKDAE GNVVVHGIFA SVPYCIQLLE GPYVETAPEV
     VAAFRPKSAR RDVSE