MOG_HELPJ
ID MOG_HELPJ Reviewed; 176 AA.
AC Q9ZL45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75;
GN Name=mog; Synonyms=mogA; OrderedLocusNames=jhp_0735;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06321.1; -; Genomic_DNA.
DR PIR; F71893; F71893.
DR RefSeq; WP_001193339.1; NC_000921.1.
DR PDB; 4XCW; X-ray; 1.80 A; A/B/C/D/E/F=1-176.
DR PDBsum; 4XCW; -.
DR AlphaFoldDB; Q9ZL45; -.
DR SMR; Q9ZL45; -.
DR STRING; 85963.jhp_0735; -.
DR EnsemblBacteria; AAD06321; AAD06321; jhp_0735.
DR KEGG; hpj:jhp_0735; -.
DR eggNOG; COG0521; Bacteria.
DR OMA; EYLTSEW; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000804; 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 3D-structure; ATP-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..176
FT /note="Molybdopterin adenylyltransferase"
FT /id="PRO_0000170986"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4XCW"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4XCW"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:4XCW"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4XCW"
SQ SEQUENCE 176 AA; 19636 MW; 3E113C28E4C05BD9 CRC64;
MQTIHIGVLS ASDRASKGVY EDLSGKAIQE VLSEYLLNPL EFHYEIVADE RDLIEKSLIK
MCDEYQCDLV VTTGGTGPAL RDITPEATKK VCQKMLPGFG ELMRMTSLKY VPTAILSRQS
AGIRNKSLII NLPGKPKSIR ECLEAVFPAI PYCVDLILGN YMQVNEKNIQ AFRPKQ
