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Database: UniProt
Entry: A0A086YSB1_9FIRM
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Original site: A0A086YSB1_9FIRM 
ID   A0A086YSB1_9FIRM        Unreviewed;       412 AA.
AC   A0A086YSB1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN   ORFNames=DK28_0202440 {ECO:0000313|EMBL:KFD41935.1};
OS   Peptococcaceae bacterium SCADC1_2_3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD41935.1, ECO:0000313|Proteomes:UP000027084};
RN   [1] {ECO:0000313|EMBL:KFD41935.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41935.1};
RA   Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFD41935.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41935.1};
RA   Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT   "Draft genome sequence of an unculturable Firmicutes affiliated with
RT   Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT   degrading cultures.";
RL   Submitted (JUL-2014) 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:KFD41935.1}.
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DR   EMBL; JJNX02000013; KFD41935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086YSB1; -.
DR   STRING; 1487582.HY00_11155; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000027084; 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   Reference proteome {ECO:0000313|Proteomes:UP000027084};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          187..326
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   412 AA;  43950 MW;  80B1FCA31F210A92 CRC64;
     MTELFKAVTI TEARKIISAH YSGPKKTEMI PLLSAQGRRL AEEVRAKEDV PGFTRSTVDG
     FAVQARDTFG ASEGLPDYLE IAGEVFMGEE PKGRLETGQV WQIATGGMLP AGADAVVMVE
     YTENLEEKII GVVRPVAPGE NVIRQGEDIA AGSLVLPFSH CVKAHDLGVL AAAGVTAVKV
     FCPLRVGIVS TGDEVVPPEE KPVPGKVRDI NSYALYGAVT EAGGQPHLYG IVRDDFHRVR
     ESLSAALSEN DLVMLSGGSS VGTRDVAREA INSLGNPGVL FHGLSIQPGK PTIGAAIEGK
     LVFGLPGHPA SALVVFHLLV APLLYKGSYY EEENGFWEFP LTAQITRNIR SAPGREDFIR
     VKLFLRQGNL YAEPILGKSG LITTLVKANG LARITAGKEG VEAGETVEVK LF
//
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