MOG_ECOLI
ID MOG_ECOLI Reviewed; 195 AA.
AC P0AF03; P28694; Q8KMY3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75 {ECO:0000269|PubMed:15632135};
GN Name=mog; Synonyms=chlG, mogA, yaaG; OrderedLocusNames=b0009, JW0008;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8400364; DOI=10.3109/10425179309020832;
RA James R., Dean D.O., Debbage J.;
RT "Five open reading frames upstream of the dnaK gene of E. coli.";
RL DNA Seq. 3:327-332(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INTERACTION WITH MOEA AND MOBB.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12372836; DOI=10.1074/jbc.m205806200;
RA Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.;
RT "In vivo interactions between gene products involved in the final stages of
RT molybdenum cofactor biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 277:48199-48204(2002).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15632135; DOI=10.1074/jbc.m413783200;
RA Nichols J.D., Rajagopalan K.V.;
RT "In vitro molybdenum ligation to molybdopterin using purified components.";
RL J. Biol. Chem. 280:7817-7822(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ASP-49
RP AND ASP-82.
RX PubMed=10636880; DOI=10.1074/jbc.275.3.1814;
RA Liu M.T.W., Wuebbens M.M., Rajagopalan K.V., Schindelin H.;
RT "Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis
RT protein MogA from Escherichia coli.";
RL J. Biol. Chem. 275:1814-1822(2000).
CC -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of the
CC biosynthesis of the molybdenum-cofactor. {ECO:0000269|PubMed:15632135}.
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 Evidence={ECO:0000269|PubMed:15632135};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homotrimer. Interacts with MoeA and MobB in vivo.
CC {ECO:0000269|PubMed:10636880, ECO:0000269|PubMed:12372836}.
CC -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR EMBL; X67700; CAA47930.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73120.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96587.2; -; Genomic_DNA.
DR PIR; B56688; B56688.
DR RefSeq; NP_414550.1; NC_000913.3.
DR RefSeq; WP_001295414.1; NZ_LN832404.1.
DR PDB; 1DI6; X-ray; 1.45 A; A=3-195.
DR PDB; 1DI7; X-ray; 1.60 A; A=3-195.
DR PDBsum; 1DI6; -.
DR PDBsum; 1DI7; -.
DR AlphaFoldDB; P0AF03; -.
DR SMR; P0AF03; -.
DR BioGRID; 4261931; 17.
DR BioGRID; 849162; 1.
DR DIP; DIP-35784N; -.
DR IntAct; P0AF03; 9.
DR STRING; 511145.b0009; -.
DR SWISS-2DPAGE; P0AF03; -.
DR jPOST; P0AF03; -.
DR PaxDb; P0AF03; -.
DR PRIDE; P0AF03; -.
DR EnsemblBacteria; AAC73120; AAC73120; b0009.
DR EnsemblBacteria; BAB96587; BAB96587; BAB96587.
DR GeneID; 58461422; -.
DR GeneID; 944760; -.
DR KEGG; ecj:JW0008; -.
DR KEGG; eco:b0009; -.
DR PATRIC; fig|1411691.4.peg.2274; -.
DR EchoBASE; EB1473; -.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_077358_1_0_6; -.
DR InParanoid; P0AF03; -.
DR OMA; EYLTSEW; -.
DR PhylomeDB; P0AF03; -.
DR BioCyc; EcoCyc:EG11511-MON; -.
DR BioCyc; MetaCyc:EG11511-MON; -.
DR BRENDA; 2.7.7.75; 2026.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; P0AF03; -.
DR PRO; PR:P0AF03; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IDA:EcoCyc.
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 3D-structure; ATP-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Molybdopterin adenylyltransferase"
FT /id="PRO_0000170982"
FT MUTAGEN 49
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10636880"
FT MUTAGEN 82
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10636880"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1DI6"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:1DI6"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1DI6"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1DI6"
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
