ID   MOEA2_MYCTO             Reviewed;         405 AA.
AC   P9WJQ4; L0T5D3; O53725;
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 2;
DE            Short=MPT Mo-transferase 2;
DE            EC=2.10.1.1;
GN   Name=moaE2; OrderedLocusNames=MT0454;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44677.1; -; Genomic_DNA.
DR   PIR; G70829; G70829.
DR   RefSeq; WP_003898451.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJQ4; -.
DR   SMR; P9WJQ4; -.
DR   EnsemblBacteria; AAK44677; AAK44677; MT0454.
DR   KEGG; mtc:MT0454; -.
DR   PATRIC; fig|83331.31.peg.481; -.
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..405
FT                   /note="Molybdopterin molybdenumtransferase 2"
FT                   /id="PRO_0000427789"
SQ   SEQUENCE   405 AA;  42021 MW;  E21F6BA920EFD889 CRC64;
     MRSVQEHQRV VAEMMRACRP ITVPLTQAQG LVLGGDVVAP LSLPVFDNSA MDGYAVRAED
     TSGATPQNPV MLPVAEDIPA GRADMLTLQP VTAHRIMTGA PVPTGATAIV PVEATDGGVD
     SVAIRQQATP GKHIRRSGED VAAGTTVLHN GQIVTPAVLG LAAALGLAEL PVLPRQRVLV
     ISTGSELASP GTPLQPGQIY ESNSIMLAAA VRDAGAAVVA TATAGDDVAQ FGAILDRYAV
     DADLIITSGG VSAGAYEVVK DAFGSADYRG GDHGVEFVKV AMQPGMPQGV GRVAGTPIVT
     LPGNPVSALV SFEVFIRPPL RMAMGLPDPY RPHRSAVLTA SLTSPRGKRQ FRRAILDHQA
     GTVISYGPPA SHHLRWLASA NGLLDIPEDV VEVAAGTQLQ VWDLT