ID Q8VMA0_CUPNE Unreviewed; 412 AA.
AC Q8VMA0;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN Name=moeA {ECO:0000313|EMBL:CAC82487.1};
GN ORFNames=I6H87_14535 {ECO:0000313|EMBL:QQB76010.1};
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590 {ECO:0000313|EMBL:CAC82487.1};
RN [1] {ECO:0000313|EMBL:CAC82487.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H16 {ECO:0000313|EMBL:CAC82487.1};
RA Burgdorf T., Boemmer D., Bowien B.;
RT "Involvement of a mol operon in molybdopterin cofactor biosynthesis in
RT Ralstonia eutropha.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QQB76010.1, ECO:0000313|Proteomes:UP000595791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_1030 {ECO:0000313|EMBL:QQB76010.1,
RC ECO:0000313|Proteomes:UP000595791};
RA Kerrigan L., Long C., Tallon L., Sadzewicz L., Zhao X., Boylan J., Ott S.,
RA Bowen H., Vavikolanu K., Mehta A., Aluvathingal J., Nadendla S., Yan Y.,
RA Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ279073; CAC82487.1; -; Genomic_DNA.
DR EMBL; CP066018; QQB76010.1; -; Genomic_DNA.
DR RefSeq; WP_037024094.1; NZ_LVWN01000037.1.
DR AlphaFoldDB; Q8VMA0; -.
DR GeneID; 57644393; -.
DR PATRIC; fig|381666.6.peg.2668; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000595791; Chromosome 1.
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; IPR008284; MoCF_biosynth_CS.
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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 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, ECO:0000313|EMBL:QQB76010.1}.
FT DOMAIN 186..327
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 412 AA; 43525 MW; AECE5AE0DAC608E1 CRC64;
MTQAAAPSRP PMLTMAQALD ALLGAARPLA QLESIDTLHA NGRVLAAPVT STLRVPPADN
TSMDGYAMRA GDVPAAGTRL RVSQRIPAGH VGTALEPGTA ARIFTGGLIP PGADAVVMQE
QCTAEGEDVI VNHVPQSGEW VRRAGEDIEA GSVILPAGTR LTPQALGLAA SVGQAKLDVV
RRVRVAVFFT GDELAMPGEP LKPGAIYNSN RFTLRGLLEN LGCEVSDFGI VPDTLAATRE
TLRRAAQGHD LIITSGGVSV GEEDHIKPAV EAEGRLDMWQ IAIKPGKPLA FGQVNNDAGP
AFFLGLPGNP VSSFVTFLLF VRPFILRLQG VAGVTPRRLP LRADFELNKG DRRNEFLRAR
INAEGGLDLF PNQSSGVLTS TVWGDGLIDN PPNQPIARGD TVQFIPFDGL LA
//
