ID   A6V367_PSEA7            Unreviewed;       405 AA.
AC   A6V367;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA2 {ECO:0000313|EMBL:ABR86388.1};
GN   OrderedLocusNames=PSPA7_2130 {ECO:0000313|EMBL:ABR86388.1};
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR86388.1, ECO:0000313|Proteomes:UP000001582};
RN   [1] {ECO:0000313|EMBL:ABR86388.1, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86388.1,
RC   ECO:0000313|Proteomes:UP000001582};
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR86388.1, ECO:0000313|Proteomes:UP000001582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7 {ECO:0000313|EMBL:ABR86388.1,
RC   ECO:0000313|Proteomes:UP000001582};
RX   PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA   Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA   Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT   "Complete genome sequence of the multiresistant taxonomic outlier
RT   Pseudomonas aeruginosa PA7.";
RL   PLoS ONE 5:E8842-E8842(2010).
CC   -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC       molybdopterin with the concomitant release of AMP.
CC       {ECO:0000256|ARBA:ARBA00002901, ECO:0000256|RuleBase:RU365090}.
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         Evidence={ECO:0000256|ARBA:ARBA00001529};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC       ECO:0000256|RuleBase:RU365090}.
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; CP000744; ABR86388.1; -; Genomic_DNA.
DR   RefSeq; WP_012075137.1; NC_009656.1.
DR   AlphaFoldDB; A6V367; -.
DR   KEGG; pap:PSPA7_2130; -.
DR   HOGENOM; CLU_010186_7_0_6; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001582; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00887; MoeA; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 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   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          185..321
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   405 AA;  43243 MW;  5696BC50AC97A076 CRC64;
     MNGCCDHPGL MPVETALERL LELAAQTPID ACERVPLEQA GGRVLAVDLL AGLDLPPWPN
     SAMDGYALRL ADWTGEPLPV SQKIFAGQAP QPLRAGTCAR IFTGAPLPEG ADLVEMQENA
     EALDDGRVRF TQPLRAGQHV RPRGQEARQG DLVLPAGTRL RPIELGLAAS LGCAALEVRR
     KPRVALLSTG DELVEAGQPL QAGQIYNSNR PLLKDWLQRL GCDVLDAGIL PDDLARTRER
     LAGLAGVDLI LSTGGVSVGE ADFLGMALRE AGELTLWKLA IKPGKPLTVG QFQGIPVIGL
     PGNPASTLVT FALLARPYLL RRLGVAQVAP LRVEVPAGFA WPKAGPRREY LRGRLEQGRA
     VLYPNQSSGV LRSASWAEGL VEVREGRTLA EGEGVAFIPL SELLD
//