ID A0A133SIK0_9FIRM Unreviewed; 339 AA.
AC A0A133SIK0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=HMPREF3201_00966 {ECO:0000313|EMBL:KXA69505.1};
OS Megasphaera sp. MJR8396C.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1603888 {ECO:0000313|EMBL:KXA69505.1, ECO:0000313|Proteomes:UP000070314};
RN [1] {ECO:0000313|EMBL:KXA69505.1, ECO:0000313|Proteomes:UP000070314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR9396C {ECO:0000313|EMBL:KXA69505.1,
RC ECO:0000313|Proteomes:UP000070314};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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|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;
CC Evidence={ECO:0000256|RuleBase:RU365090};
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|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family.
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:KXA69505.1}.
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DR EMBL; LRVC01000039; KXA69505.1; -; Genomic_DNA.
DR RefSeq; WP_062411940.1; NZ_KQ958170.1.
DR AlphaFoldDB; A0A133SIK0; -.
DR STRING; 1603888.HMPREF3201_00966; -.
DR PATRIC; fig|1603888.3.peg.932; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000070314; 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; cd03522; MoeA_like; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR038987; MoeA-like.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR10192:SF28; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR SMART; SM00852; MoCF_biosynth; 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 173..306
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 339 AA; 36739 MW; 3C7E8E8A39A21FA3 CRC64;
MKMMKTEDAV GHILCHDITQ IIRGVTKDPV FRKGHIITKE DIPVLLSVGK DHVYIWENDD
TVFHENEGAA ILRDICMGAH MHGSEPKEGK IELIADCDGV LTVRRQALQA VNSVGEMMIA
TRHGGFTVRK GDKLAGTRVI PLIIKKEKMA RAKEAAGPLP LLDVHPFKKK RAGVVTTGNE
VFHGRIEDTF TPVIECKLAE FDAEMAMHKV LADDPAAITA AIQEMLDAGM DMVFCTGGMS
VDPDDQTPLA IKNTGARIVS YGAPVLPGAM FLLAYTEDNR PIVGLPGCVM YSKRTIFDLV
LPSLMADVPV TASDLSRLGE GGLCLNCPVC TFPNCGFGK
//
