ID A0A075JPI4_9BACI Unreviewed; 421 AA.
AC A0A075JPI4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=X953_12860 {ECO:0000313|EMBL:AIF43931.1};
OS Virgibacillus sp. SK37.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43931.1, ECO:0000313|Proteomes:UP000027985};
RN [1] {ECO:0000313|EMBL:AIF43931.1, ECO:0000313|Proteomes:UP000027985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK37 {ECO:0000313|EMBL:AIF43931.1,
RC ECO:0000313|Proteomes:UP000027985};
RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT halophilic bacterium isolated from Thai fish sauce fermentation.";
RL Submitted (FEB-2014) 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}.
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DR EMBL; CP007161; AIF43931.1; -; Genomic_DNA.
DR RefSeq; WP_040955829.1; NZ_CP007161.1.
DR AlphaFoldDB; A0A075JPI4; -.
DR STRING; 403957.X953_12860; -.
DR KEGG; vir:X953_12860; -.
DR HOGENOM; CLU_010186_7_1_9; -.
DR OrthoDB; 9804758at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000027985; Chromosome.
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|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|RuleBase:RU365090};
KW Reference proteome {ECO:0000313|Proteomes:UP000027985};
KW Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AIF43931.1}.
FT DOMAIN 189..327
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 421 AA; 46243 MW; 13822DF247E4C13F CRC64;
MVEIRKPIPV ETAIRKVMNY ASIGVVEEVP IENSHQRRLA QQVVATNNVP SFHKSPYDGF
ALRSIDTSEA SLESPIEFEV VEHIGAGQVP KKKLQSNQAT RIMTGAQIPE GADCVAMFEI
CKTYEKDGKN YISLKRKMEK GQNIIKEGSE VVKGEVLIEK GTWINPGVIA SLATFGYSSV
KVARKPVIGI IATGTELLDV DEDLRPGKIR NSNAYMISSQ IERAGGTPKY LGKLEDELES
SYETIKKALE EVDYLVTTGG VSVGDFDLMP AIYEKLGADV LFNKIAMRPG SVTTVAVLGN
QLLFGLSGNP SACYVGGELF LRPVIQANQF STTPYLKRIK ATLADEFPKP NPFTRFVRCY
VVYKDGKVFT RVAGIDKSNV VTSLAYSDCL MMLPGGTRGF KIGDEVEILL LNNYEGQQDF
N
//