ID A0A1I7F4B8_9BURK Unreviewed; 435 AA.
AC A0A1I7F4B8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=SAMN05216350_101248 {ECO:0000313|EMBL:SFU31061.1};
OS Polaromonas sp. YR568.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFU31061.1, ECO:0000313|Proteomes:UP000217451};
RN [1] {ECO:0000313|EMBL:SFU31061.1, ECO:0000313|Proteomes:UP000217451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR568 {ECO:0000313|EMBL:SFU31061.1,
RC ECO:0000313|Proteomes:UP000217451};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPBM01000001; SFU31061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7F4B8; -.
DR STRING; 1855301.SAMN05216350_101248; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000217451; 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; 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 201..346
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 435 AA; 45685 MW; 57A81C91FB086352 CRC64;
MKTLDQIAAE LQGYDPQALS AGQVLDFLSR LVMPVQDALE LPLMQAFGRV LASDVVSPFD
VPPHDNSAMD GYAFDGSQLA AGTALELQVA PGTALAGKAW QGSVQPGKCV KIMTGAIMPP
GLDTVVPQEF ISVRTGAGNA EFITIPPKLL GAGDNRRLRG EDLMQGRPAL QKGELLTPAR
LGLAASLGLK TLSTWRPLRV AYFSTGDEIL SLGEAPREGA VYDSNRYTVF GMLSRLGCEV
IDMGVVRDDP ALLEAAFTEA AARADAIITS GGVSVGEADF TKAMMKKLGD VAFWRIAMRP
GRPMAVGRIP ATKGGNPNGA ILFGLPGNPV AVMVTFLAFV RPALLQMMGA GAESPLLLKA
RSTEAIRKKA GRTEYQRGWV STAPDGSLQA KTTGSQGSGV LRSMAEANGL IVLHHAQGNV
AVGDEVDVLM FEGAI
//
