ID   MOEA_SYNE7              Reviewed;         403 AA.
AC   Q56207; Q31NQ3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Molybdopterin molybdenumtransferase;
DE            Short=MPT Mo-transferase;
DE            EC=2.10.1.1;
GN   Name=moeA; OrderedLocusNames=Synpcc7942_1286;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9495759; DOI=10.1128/jb.180.5.1200-1206.1998;
RA   Rubio L.M., Flores E., Herrero A.;
RT   "The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster
RT   of molybdopterin biosynthesis genes.";
RL   J. Bacteriol. 180:1200-1206(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; X99625; CAA67944.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57316.1; -; Genomic_DNA.
DR   RefSeq; WP_011377960.1; NC_007604.1.
DR   AlphaFoldDB; Q56207; -.
DR   SMR; Q56207; -.
DR   STRING; 1140.Synpcc7942_1286; -.
DR   PRIDE; Q56207; -.
DR   EnsemblBacteria; ABB57316; ABB57316; Synpcc7942_1286.
DR   KEGG; syf:Synpcc7942_1286; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_2_3; -.
DR   OMA; MTGAMVP; -.
DR   OrthoDB; 651103at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1286-MON; -.
DR   UniPathway; UPA00344; -.
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; IPR008284; MoCF_biosynth_CS.
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   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Transferase.
FT   CHAIN           1..403
FT                   /note="Molybdopterin molybdenumtransferase"
FT                   /id="PRO_0000171002"
SQ   SEQUENCE   403 AA;  43218 MW;  14758195DC12C811 CRC64;
     MILSYSAAIE LLLAEVAQLP LAIERVPLLE TGDRLLAKDL AAPCDLPHWD NSAMDGFALR
     SQDVAAASPD RPVRLPVVGR VMAGEQPPLL ANPTGVACAV MTGAPIPAGF DVIVKVEDVV
     QEENAIAVST PIPAGQFIRR QGEDLRQGSP LLAKGQRLTP MALMLAAAVG MGELPVWSKL
     PVGLISTGTE VVPWSQPTLE LGQIRNSSQP FLIEQLQRLG CEVRAIAHVP DDPEQFAAIA
     QQFWSQGVRL LLTTGAVSMG VADFVPAALE RLGCQTIFHK VAIRPGKPLL FAIAPEHQGL
     VLACPGNPVS TTVTAEFFLK PLLMACRNEV RSPLWLPLAE SVRKPEGLQC FWRSRLTPEG
     KVWVDPQQSS AALKSLVEST HWAILPAGQD FLAAGTPVEV RSL