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Database: UniProt
Entry: W9H3G7_9PROT
LinkDB: W9H3G7_9PROT
Original site: W9H3G7_9PROT 
ID   W9H3G7_9PROT            Unreviewed;       422 AA.
AC   W9H3G7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=N825_08060 {ECO:0000313|EMBL:EWY39262.1};
OS   Skermanella stibiiresistens SB22.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Skermanella.
OX   NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY39262.1, ECO:0000313|Proteomes:UP000019486};
RN   [1] {ECO:0000313|EMBL:EWY39262.1, ECO:0000313|Proteomes:UP000019486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB22 {ECO:0000313|EMBL:EWY39262.1,
RC   ECO:0000313|Proteomes:UP000019486};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Skermanella stibiiresistens.";
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWY39262.1}.
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DR   EMBL; AVFL01000013; EWY39262.1; -; Genomic_DNA.
DR   RefSeq; WP_037455175.1; NZ_AVFL01000013.1.
DR   AlphaFoldDB; W9H3G7; -.
DR   STRING; 1385369.N825_08060; -.
DR   PATRIC; fig|1385369.3.peg.3795; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000019486; Unassembled WGS sequence.
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: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.
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   Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          196..333
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   422 AA;  44721 MW;  767913A45CB4F04D CRC64;
     MAQLSDDCFA FGGPLMTLDE ARGLLAERLV AVTGSERVAL GEALDRVLAE DVVAGVNVPP
     HDNSAVDGYA VRHEDLAGGA DSVLPIVARV AAGDRPVSRD PAGTAVRIFT GAPMPEGYDT
     VMMQEDCVER DGPGGTRSVL IRPGIKRGAN RRSAGEDVRE GSVILSAGRR LRPQDIGLMA
     AVGLTDALVR APLRVAILST GNELMEPGQP LAPGGIYDAN RFTLSALVRR MGGRVTDFGI
     LRDNPAELRA VLARAAEGHD LIVTTGGVST GEEDHVKGAV EALGGLHFWR LAIKPGRPVA
     LGQVAGKPFI GLPGNPVAAM ITFFCLARPL IQHLAGETVT EPVLFRVRAD FDYKKKEGRR
     EFVRVRLARD GDGGLVATKF ARDGAGVLSS MVESDGLVIL PEDVTRLERG ATVSYMPFTE
     VR
//
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