ID   MOG_SHIFL               Reviewed;         195 AA.
AC   P0AF05; P28694; Q8KMY3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Molybdopterin adenylyltransferase;
DE            Short=MPT adenylyltransferase;
DE            EC=2.7.7.75;
GN   Name=mog; OrderedLocusNames=SF0010, S0009;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41676.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15555.1; -; Genomic_DNA.
DR   RefSeq; NP_705969.2; NC_004337.2.
DR   RefSeq; WP_001295414.1; NZ_WPGW01000013.1.
DR   AlphaFoldDB; P0AF05; -.
DR   SMR; P0AF05; -.
DR   STRING; 198214.SF0010; -.
DR   PRIDE; P0AF05; -.
DR   EnsemblBacteria; AAN41676; AAN41676; SF0010.
DR   EnsemblBacteria; AAP15555; AAP15555; S0009.
DR   GeneID; 1027511; -.
DR   GeneID; 58461422; -.
DR   KEGG; sfl:SF0010; -.
DR   KEGG; sfx:S0009; -.
DR   PATRIC; fig|198214.7.peg.9; -.
DR   HOGENOM; CLU_077358_1_0_6; -.
DR   OMA; EYLTSEW; -.
DR   OrthoDB; 1877633at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000170987"
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