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Database: UniProt
Entry: A0A0F7FT50_9ACTN
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ID   A0A0F7FT50_9ACTN        Unreviewed;       435 AA.
AC   A0A0F7FT50;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=SXIM_20030 {ECO:0000313|EMBL:AKG43387.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG43387.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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; CP009922; AKG43387.1; -; Genomic_DNA.
DR   RefSeq; WP_046723680.1; NZ_CP009922.3.
DR   AlphaFoldDB; A0A0F7FT50; -.
DR   STRING; 408015.SXIM_20030; -.
DR   KEGG; sxi:SXIM_20030; -.
DR   PATRIC; fig|408015.6.peg.2033; -.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000034034; 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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          198..335
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   435 AA;  44729 MW;  787557B9F8FAD5AA CRC64;
     MSDLWSVDDH LADILRAIRP LDPIALPLLE ADGCVLTEDV TVPTALPPFD NSSMDGYAVR
     CADVAAATTE RPVALTVTGD IAAGSGEPPT LRPGQALRIM TGAPLPPGAE AVVPVEWTDG
     GLGGGPVRAM PAGQVRGGER VRVHRPAERG AHIRERGSDA AAGALALPAG TVLGPPQLGL
     LAAVGRASVE VRPRPRVVVL STGSELVPPG TALRPGQIHD SNSFTLTAAA RAAGAAAYRA
     ATVADDPERL RAALEDQLSR ADLVITSGGV SVGAYDVVKE ALRGSVEFRR LAMQPGKPQG
     FGLVGKQRIP LLALPGNPVS SYVSFELFVR PALRALAGHP QVERARVRAR LECDEPLVSP
     AGRRQYLRGS YTPPAPGERL GTVRPVGGAS SHLLAALARA DALIEIPEAA TGAASGAELT
     VVPLGGGAQE YGSSS
//
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