MOAB_METJA
ID MOAB_METJA Reviewed; 163 AA.
AC Q57631;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Probable molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75;
GN Name=moaB; OrderedLocusNames=MJ0167;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98149.1; -; Genomic_DNA.
DR PIR; H64320; H64320.
DR RefSeq; WP_010869662.1; NC_000909.1.
DR AlphaFoldDB; Q57631; -.
DR SMR; Q57631; -.
DR STRING; 243232.MJ_0167; -.
DR EnsemblBacteria; AAB98149; AAB98149; MJ_0167.
DR GeneID; 1451014; -.
DR KEGG; mja:MJ_0167; -.
DR eggNOG; arCOG00214; Archaea.
DR HOGENOM; CLU_077358_2_3_2; -.
DR InParanoid; Q57631; -.
DR OMA; TGWDGIL; -.
DR OrthoDB; 108340at2157; -.
DR PhylomeDB; Q57631; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IPR012245; MoaB.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR PANTHER; PTHR43232; PTHR43232; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF006443; MoaB; 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..163
FT /note="Probable molybdopterin adenylyltransferase"
FT /id="PRO_0000170981"
SQ SEQUENCE 163 AA; 18247 MW; 5B7FA49A5A223435 CRC64;
MHKRIKNIKY AVVTVSDSRY NDLIKGKEVD DKSGKLLKKE LNAKVYTIIP DNKNMIKGIV
EHIVEFFDVD CIVFTGGTGI AERDVTVEAL KEIIEKELDG FKIIFQKLSY EEVGFSAMLS
RAMAGIYKGK IIYALPGSVN ACRTALKIIK EETGHILGHL REG