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Database: UniProt
Entry: A0A0M8KRD3_9MICO
LinkDB: A0A0M8KRD3_9MICO
Original site: A0A0M8KRD3_9MICO 
ID   A0A0M8KRD3_9MICO        Unreviewed;       437 AA.
AC   A0A0M8KRD3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-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=Y09_2350 {ECO:0000313|EMBL:GAP79502.1};
OS   Brachybacterium sp. SW0106-09.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1704590 {ECO:0000313|EMBL:GAP79502.1, ECO:0000313|Proteomes:UP000037781};
RN   [1] {ECO:0000313|EMBL:GAP79502.1, ECO:0000313|Proteomes:UP000037781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW0106-09 {ECO:0000313|EMBL:GAP79502.1,
RC   ECO:0000313|Proteomes:UP000037781};
RA   Qin Q.L., Li Y., Zhang Y.Z.;
RT   "Genome Sequencing of Brachybacterium sp. SW0106-09.";
RL   Submitted (SEP-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}.
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:GAP79502.1}.
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DR   EMBL; BCAK01000025; GAP79502.1; -; Genomic_DNA.
DR   RefSeq; WP_053917834.1; NZ_BCAK01000025.1.
DR   AlphaFoldDB; A0A0M8KRD3; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000037781; 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   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          210..355
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          122..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  43859 MW;  50A006E38A5B14D2 CRC64;
     MTGAQRSPLA DHVADAVALL AAVRATEPVA LDGRAVGRVA ARPLRSHVDV PGVDNSQMDG
     FAVASTDLAG PGAAVTLPLG PTIAAGDAPG RLEPGQARPI MTGAPVPDGA DLVVPVEESA
     QGRFDTGGAG AEGGGTSAGG PDAAHGADPA TVTLTPADAA PGRFVRRRGS DTHRGDTVLR
     EGQMLTPARI AHLAACGLSE VEVGAPVRVV VLSTGSEVRG PSGAEPAPGT LHDANGPGLA
     AALTEAGAEV VHRGAVPDDA TLLLERLRDE VLAHDADLIV TSGGVSMGAF EVVRHAAALP
     GTTLAFPTLA MQPGGPQGIG TLEVDGRRVP WLAFPGNPVS ALLSCELIAR PALGAPPRRR
     LRLPVRLEAE ESSPAQLEQY RRARVLPSGA VRLVGGASSH LIGGYAAADA LAIVPVGTAV
     VRDGDLLETL LIPGGDS
//
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