ID   MOG_HAEIN               Reviewed;         197 AA.
AC   P44645;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Molybdopterin adenylyltransferase;
DE            Short=MPT adenylyltransferase;
DE            EC=2.7.7.75;
GN   Name=mog; Synonyms=mogA; OrderedLocusNames=HI_0336;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
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; L42023; AAC21998.1; -; Genomic_DNA.
DR   PIR; D64148; D64148.
DR   RefSeq; NP_438500.1; NC_000907.1.
DR   RefSeq; WP_005647046.1; NC_000907.1.
DR   AlphaFoldDB; P44645; -.
DR   SMR; P44645; -.
DR   STRING; 71421.HI_0336; -.
DR   EnsemblBacteria; AAC21998; AAC21998; HI_0336.
DR   GeneID; 56956742; -.
DR   KEGG; hin:HI_0336; -.
DR   PATRIC; fig|71421.8.peg.353; -.
DR   eggNOG; COG0521; Bacteria.
DR   HOGENOM; CLU_077358_1_0_6; -.
DR   OMA; EYLTSEW; -.
DR   PhylomeDB; P44645; -.
DR   BioCyc; HINF71421:G1GJ1-352-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000579; 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   1: Evidence at protein level;
KW   ATP-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..197
FT                   /note="Molybdopterin adenylyltransferase"
FT                   /id="PRO_0000170984"
SQ   SEQUENCE   197 AA;  21691 MW;  5F65A75C69DABD8F CRC64;
     MTALLKIGLV SVSDRASAGV YQDQGIPELQ AWLEQALVDP FHLETRLIPD EQPVIEQTLK
     ELVDEQGCHL VLTTGGTGPA KRDVTPDATL AVADREMPGF GEQMRQVSLH FVPTAILSRQ
     VGVIRKESLI LNLPGQPKAI KETLEGVKDK EGNVLVKGIF SAVPYCLQLI NGLYIDTKPE
     IIESFRPKSA RRENLEK