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MOEA_SYNY3
ID   MOEA_SYNY3              Reviewed;         390 AA.
AC   Q55368;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Molybdopterin molybdenumtransferase;
DE            Short=MPT Mo-transferase;
DE            EC=2.10.1.1;
GN   Name=moeA; OrderedLocusNames=slr0900;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10450.1; -; Genomic_DNA.
DR   PIR; S75715; S75715.
DR   AlphaFoldDB; Q55368; -.
DR   SMR; Q55368; -.
DR   IntAct; Q55368; 1.
DR   STRING; 1148.1001210; -.
DR   PaxDb; Q55368; -.
DR   EnsemblBacteria; BAA10450; BAA10450; BAA10450.
DR   KEGG; syn:slr0900; -.
DR   eggNOG; COG0303; Bacteria.
DR   InParanoid; Q55368; -.
DR   OMA; MTGAMVP; -.
DR   PhylomeDB; Q55368; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="Molybdopterin molybdenumtransferase"
FT                   /id="PRO_0000171003"
SQ   SEQUENCE   390 AA;  43394 MW;  848183B5610CA314 CRC64;
     MISVAAAVEI IQAHWPNFGD TTMDVDGSYG RVLAESIEAD RDYPPGDRVM MDGVALAWSE
     YHQGRRHFKL LGTVAAGTPQ SSLPDQTGCL EVMTGALLPQ NCDLVIPYEE VAIADNQVKI
     INPRQREPGE FVHPKASDCR AGKVILESSS KLNGPAWNII TSFGKTKVRV KQKPRIQIIS
     TGDELVEITQ KPKIHQLRRS NIYGLQVSLQ SRGFQNVNLT HLADDKEVII RHYQKAKLEY
     RVLIYSGGIS KGKFDYLPEV WSQLGVTKYI HGVAQKPGKP MYFGIDHRSK TVIIGLPGNP
     ISSLVCLHRY FLDSAPIYAQ LTTDFTFKKD LTYFLPVKLS HTPQAVIKAE PLPVKNSGEF
     IALAGSDGFL ELPQHQASFQ AGECFPFYAW
 
 
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