ID A0A291GZ91_9MICO Unreviewed; 417 AA.
AC A0A291GZ91;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=CFK41_12650 {ECO:0000313|EMBL:ATG55528.1};
OS Brachybacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1331682 {ECO:0000313|EMBL:ATG55528.1, ECO:0000313|Proteomes:UP000217889};
RN [1] {ECO:0000313|EMBL:ATG55528.1, ECO:0000313|Proteomes:UP000217889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY80 {ECO:0000313|EMBL:ATG55528.1,
RC ECO:0000313|Proteomes:UP000217889};
RX PubMed=24944333; DOI=10.1099/ijs.0.058388-0;
RA Hoang V.A., Kim Y.J., Nguyen N.L., Yang D.C.;
RT "Brachybacterium ginsengisoli sp. nov., isolated from soil of a ginseng
RT field.";
RL Int. J. Syst. Evol. Microbiol. 64:3063-3068(2014).
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; CP023564; ATG55528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GZ91; -.
DR KEGG; bgg:CFK41_12650; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000217889; 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 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, ECO:0000313|EMBL:ATG55528.1}.
FT DOMAIN 190..335
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 417 AA; 42663 MW; DF126B25D7F92838 CRC64;
MSGAPRIPLA DHVADAVALL AAVRGTEVLP LDGRAAGRVA IAEQRSRVDV PGHDNSQMDG
YALAAADLAG ADQEVSLPLG PMIAAGDAPG TLEPGTARPI MTGAPIPAGA DLVVPVEESG
PGRFTPDLGS RVTLAPTSVA RGRFVRTRGS DTHRGDAVLR EGRLLTPARI AHLAACGILD
VEVQAPVRAI VLSTGSEVRR ADADLPDPGA LFDANGPGLA AALTEAGAEV VRTGAVPDDA
AALLDHLREQ IRAHDADLVV TSGGVSMGAV EVVRHAAERD GVLLAFPTIA MQPGGPQGIG
TLEVDGRRVP WLAFPGNPVS ALLSCELIAR PALGAPARRR LHLPIQLEAE ESSPPALDQY
RRARVLPSGR VRLVGGASSH LLGGYAAADA LVLVPRGTSA VHDGDTLETL LIPGGES
//