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Database: UniProt
Entry: F4D0P2_PSEUX
LinkDB: F4D0P2_PSEUX
Original site: F4D0P2_PSEUX 
ID   F4D0P2_PSEUX            Unreviewed;       413 AA.
AC   F4D0P2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=Psed_5714 {ECO:0000313|EMBL:AEA27841.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA27841.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA27841.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
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}.
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DR   EMBL; CP002593; AEA27841.1; -; Genomic_DNA.
DR   RefSeq; WP_013677740.1; NC_015312.1.
DR   AlphaFoldDB; F4D0P2; -.
DR   STRING; 675635.Psed_5714; -.
DR   KEGG; pdx:Psed_5714; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000007809; 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; 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:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          191..329
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   413 AA;  41840 MW;  B4A3EB6D581A2D51 CRC64;
     MTPPEHAPAP GGPRTVDEHR AVVASLVPPA PVVEVPLSQA LGRVLATDVV ATVALPPFDN
     SAMDGYAVRA AEVAAASEDA PVALPVAEDI PAGRTDVPTL QPGTAHRIMT GAPMPAGADA
     VVQVELTDGG VEQVAVRRGP AAGTHVRRAG EDVRPGTTVL TAGTVLGPPQ VGLLAAIGLP
     TVAVRRPPRV LVLSTGSELV EPGAPLAPGQ IYESNGPMLA AAVREAGGEA ELLRFVPDDV
     EVFASLLAEK AGDVDLILTS GGVSAGAYEV VKDALRDRGV EFVRVAMQPG GPQGAGRLDG
     DGPAVVTLPG NPVSSLVSFE VFVRPALRAA MGHPHPLRPV VSAALAEALV SPPDKRQFRR
     GVLDASDGTV AEVGAPASHL LASLALADCL IVVPEGVSAV DKGVAVEVWL LEA
//
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