ID   MOEA1_MYCTO             Reviewed;         426 AA.
AC   P9WJQ6; L0T705; O05577;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Molybdopterin molybdenumtransferase 1;
DE            Short=MPT Mo-transferase 1;
DE            EC=2.10.1.1;
GN   Name=moeA1; Synonyms=moeA; OrderedLocusNames=MT1023;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45270.1; -; Genomic_DNA.
DR   PIR; E70601; E70601.
DR   RefSeq; WP_003898680.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJQ6; -.
DR   SMR; P9WJQ6; -.
DR   EnsemblBacteria; AAK45270; AAK45270; MT1023.
DR   KEGG; mtc:MT1023; -.
DR   PATRIC; fig|83331.31.peg.1096; -.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Transferase.
FT   CHAIN           1..426
FT                   /note="Molybdopterin molybdenumtransferase 1"
FT                   /id="PRO_0000427788"
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