ID A0A498CSE3_9FIRM Unreviewed; 341 AA.
AC A0A498CSE3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=D4A47_04830 {ECO:0000313|EMBL:RLL12739.1};
OS Anaerotruncus massiliensis (ex Liu et al. 2021).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=2321404 {ECO:0000313|EMBL:RLL12739.1, ECO:0000313|Proteomes:UP000276301};
RN [1] {ECO:0000313|EMBL:RLL12739.1, ECO:0000313|Proteomes:UP000276301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22A2-44 {ECO:0000313|EMBL:RLL12739.1,
RC ECO:0000313|Proteomes:UP000276301};
RA Wang Y.-J.;
RT "Anaerotruncus faecis sp. nov., isolated from human feces.";
RL Submitted (OCT-2018) 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:RLL12739.1}.
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DR EMBL; RCHT01000005; RLL12739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498CSE3; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000276301; 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 Reference proteome {ECO:0000313|Proteomes:UP000276301};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 173..305
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 341 AA; 36618 MW; B395330A6B1CAE1A CRC64;
MKRIKTEDAV GQVLCHDMTQ IIPGVTKDAR FRKGHVVTAE DIPVLLSMGK DYLYIWEKQE
GMLHENEGAR ILCDLCKNEH MSESPVKEGK IELTATCDGL FSIDVERLDA INSLGEIMIA
ARSNHLPVKA GDKLAGTRVI PLVISEEKMN EAKRIAGDKP LLSLLPYQKK RCGIVTTGNE
VFYGRIKDAF SPVVAAKLEE YGGEVMGVTL CGDDPAGITA AIEAFLADGA DLVVCTGGMS
VDPDDRTPAA IKATGARIVS YGAPVLPGAM FLLSYLDGKP IMGLPGCVMY ARRTIFDLVL
PRVMADDPVT AKDLARLGNG GLCLNCETCH YPNCGFGKGG V
//
