GenomeNet

Database: UniProt
Entry: A0A0J1F9G2_9FIRM
LinkDB: A0A0J1F9G2_9FIRM
Original site: A0A0J1F9G2_9FIRM 
ID   A0A0J1F9G2_9FIRM        Unreviewed;       414 AA.
AC   A0A0J1F9G2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   Name=moeA_3 {ECO:0000313|EMBL:KLU59972.1};
GN   ORFNames=CEB3_c34030 {ECO:0000313|EMBL:KLU59972.1};
OS   Peptococcaceae bacterium CEB3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU59972.1, ECO:0000313|Proteomes:UP000035957};
RN   [1] {ECO:0000313|EMBL:KLU59972.1, ECO:0000313|Proteomes:UP000035957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEB3 {ECO:0000313|EMBL:KLU59972.1,
RC   ECO:0000313|Proteomes:UP000035957};
RA   Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA   Muehling M.;
RT   "Genome sequence of the moderately acidophilic sulfate reducing
RT   Peptococcaceae bacterium strain CEB3.";
RL   Submitted (JUN-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:KLU59972.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LDXJ01000061; KLU59972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1F9G2; -.
DR   STRING; 999898.CEB3_c34030; -.
DR   PATRIC; fig|999898.3.peg.3848; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000035957; 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:UP000035957};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KLU59972.1}.
FT   DOMAIN          191..330
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   414 AA;  44447 MW;  90C2B2E5E3584CB3 CRC64;
     MGWGKELFSV ITLAEALEVL EPYVQPLYER KEEVSLSTSL GRVVAVDVPA RGPLPHFRKS
     TVDGLAVRAQ DTFGASESLP ALVQVRGEVM MGRAPRETLD LGQGLLIPTG GMLPAEADAV
     VMLEHLEDFG EGLYGVTKAV APGENVIDIG EDLQAGEVIL PQYTVIRAQE MGLLASQGIL
     SVPVLTRVRV GILSTGDEIV SPESEPLPAQ ARDINGYTLL GQAIEAGFEA HYYGIAADEP
     AELRSILEHM LAENDVVILS GGSSVGARDL TAQMMGELGQ PGLLFHGLAL RPGKPTIGGV
     VGDKIIIGLP GHPASAMVVF DTLVRPLLDG SRRRSEFPWP EVKLSQNVYS GTGREEFVRV
     RLEQEDGNWL AEPVRGKSGL IRTMVLANGL VHIPLNVEGI QAGEKVKVRP LRRY
//
DBGET integrated database retrieval system