ID   MOEA1_MYCTU             Reviewed;         426 AA.
AC   P9WJQ7; L0T705; O05577;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Molybdopterin molybdenumtransferase 1;
DE            Short=MPT Mo-transferase 1;
DE            EC=2.10.1.1;
GN   Name=moeA1; Synonyms=moeA; OrderedLocusNames=Rv0994; ORFNames=MTCI237.08;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC         molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC         ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43744.1; -; Genomic_DNA.
DR   PIR; E70601; E70601.
DR   RefSeq; WP_003898680.1; NZ_NVQJ01000018.1.
DR   RefSeq; YP_177776.1; NC_000962.3.
DR   AlphaFoldDB; P9WJQ7; -.
DR   SMR; P9WJQ7; -.
DR   STRING; 83332.Rv0994; -.
DR   PaxDb; P9WJQ7; -.
DR   DNASU; 885404; -.
DR   GeneID; 885404; -.
DR   KEGG; mtu:Rv0994; -.
DR   TubercuList; Rv0994; -.
DR   eggNOG; COG0303; Bacteria.
DR   OMA; GKPLMHG; -.
DR   PhylomeDB; P9WJQ7; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR   GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 2.40.340.10; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR038987; MoeA-like.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR036135; MoeA_linker/N_sf.
DR   PANTHER; PTHR10192; PTHR10192; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF63867; SSF63867; 1.
DR   SUPFAM; SSF63882; SSF63882; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..426
FT                   /note="Molybdopterin molybdenumtransferase 1"
FT                   /id="PRO_0000170991"
SQ   SEQUENCE   426 AA;  44337 MW;  F6A96255C92B77DB CRC64;
     MRSVEEQQAR ISAAAVAPRP IRVAIAEAQG LMCAEEVVTE RPMPGFDQAA IDGYAVRSVD
     VAGVGDTGGV QVFADHGDLD GRDVLTLPVM GTIEAGARTL SRLQPRQAVR VQTGAPLPTL
     ADAVLPLRWT DGGMSRVRVL RGAPSGAYVR RAGDDVQPGD VAVRAGTIIG AAQVGLLAAV
     GRERVLVHPR PRLSVMAVGG ELVDISRTPG NGQVYDVNSY ALAAAGRDAC AEVNRVGIVS
     NDPTELGEIV EGQLNRAEVV VIAGGVGGAA AEAVRSVLSE LGEMEVVRVA MHPGSVQGFG
     QLGRDGVPTF LLPANPVSAL VVFEVMVRPL IRLSLGKRHP MRRIVSARTL SPITSVAGRK
     GYLRGQLMRD QDSGEYLVQA LGGAPGASSH LLATLAEANC LVVVPTGAEQ IRTGEIVDVA
     FLAQHG