ID A0A380NPA3_9FIRM Unreviewed; 329 AA.
AC A0A380NPA3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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 Name=moeA_2 {ECO:0000313|EMBL:SUP44397.1};
GN ORFNames=NCTC12020_01639 {ECO:0000313|EMBL:SUP44397.1};
OS Veillonella criceti.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=103891 {ECO:0000313|EMBL:SUP44397.1, ECO:0000313|Proteomes:UP000255367};
RN [1] {ECO:0000313|EMBL:SUP44397.1, ECO:0000313|Proteomes:UP000255367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12020 {ECO:0000313|EMBL:SUP44397.1,
RC ECO:0000313|Proteomes:UP000255367};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UHIO01000001; SUP44397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380NPA3; -.
DR OrthoDB; 9767940at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000255367; 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:UP000255367};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SUP44397.1}.
FT DOMAIN 178..311
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 329 AA; 35417 MW; EBCAAFC838318AFB CRC64;
MKRVSVAEAV GQVLAHDIAR IVIGEVKDTP FRRGHVISSE DIELLLTLGK EHVFVQEAGD
EEAFAHKLHE EDVALGLYEV CAHESLYASE IREGKIEALA AWDGMLSIDV NRLNMINSIG
ELTIVTKYNH QAVRKGDKVA GMRCIPLWLE GVQLEQARRI GQGAPLMQIK PFVRKRIGLV
TTGSEVAKGR IKDAFRPRIE ERAASFGMTV IAQEIVTDDT EAIMKAIETV KQAGADIIFC
TGGMSVDPDD LTPGAIARSA AQVVTYGLPV LPGSMVCIAY MADGTPLIGL PGGVLFSQPT
AFDILLPRLA ADDPITKADC VALGHGGLQ
//
