ID A0A0F2PRB9_9FIRM Unreviewed; 401 AA.
AC A0A0F2PRB9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=VR69_11080 {ECO:0000313|EMBL:KJS16030.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS16030.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS16030.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS16030.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS16030.1}.
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DR EMBL; LADO01000043; KJS16030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PRB9; -.
DR STRING; 1629717.VR69_11080; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000033446; 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 177..316
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 401 AA; 42475 MW; 65049F538B2DDFFC CRC64;
MLTNINVEEA RDLLLEVIMP LPAETVPLLQ SLRRVTALDL TADNDLPDCP RSAVDGFAVH
EADLMGGTSL TIMERLKPGE VPSAALTPGK TIGVATGGPL PRDAAAVLPW EATSTENNKL
SFDREIRPGT NIKPQGEDFK KGDTLIRRGA RISPGGVGLL AAFGHSSIEV YRRPRVAIIC
LGSEIIPHDT SPQEGQVRDS NGPLLKSLVE QDGGQAIGLS YINGYQNDSI KEFLHESFRR
ADLVLTVGGA ASGEYDQALA LLREAGARML FWGVRAKPGS HSGGGIRRST TVISLSGNPS
ACVTGYHLLA APVLRAMQGL SPGPVVITAT CSNSFARGGD TRRFLRGYLE CGTEGRQVTI
LPGQKSSMIK SLAGCNALIE IPAGHPPVQE GDMVTVYPVN S
//