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Database: UniProt
Entry: A0A0D8FYS6_9ACTN
LinkDB: A0A0D8FYS6_9ACTN
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ID   A0A0D8FYS6_9ACTN        Unreviewed;       418 AA.
AC   A0A0D8FYS6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:KJE77787.1};
GN   ORFNames=FEAC_05360 {ECO:0000313|EMBL:KJE77787.1};
OS   Ferrimicrobium acidiphilum DSM 19497.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Ferrimicrobium.
OX   NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE77787.1, ECO:0000313|Proteomes:UP000032336};
RN   [1] {ECO:0000313|EMBL:KJE77787.1, ECO:0000313|Proteomes:UP000032336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T23 {ECO:0000313|EMBL:KJE77787.1,
RC   ECO:0000313|Proteomes:UP000032336};
RA   Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT   "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT   strain T23.";
RL   Submitted (JAN-2015) 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   -!- 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:KJE77787.1}.
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DR   EMBL; JXUW01000003; KJE77787.1; -; Genomic_DNA.
DR   RefSeq; WP_052565328.1; NZ_JXUW01000003.1.
DR   AlphaFoldDB; A0A0D8FYS6; -.
DR   STRING; 1121877.FEAC_05360; -.
DR   GeneID; 78371850; -.
DR   PATRIC; fig|1121877.4.peg.574; -.
DR   eggNOG; COG0303; Bacteria.
DR   OrthoDB; 3196725at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000032336; 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; 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|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032336};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KJE77787.1}.
FT   DOMAIN          177..315
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   418 AA;  43924 MW;  CA3CF800FB1C3C12 CRC64;
     MRPLQEVIDH TLANIPRLPE VQTPLAEAAG LYLAGSTVVQ TPVPPFDNTA VDGFAVNTSG
     WQSDLKPLLR VTATIPAGVD SSQLSIGSEE AIRIMTGAPI PPSADAVVMV EDTSTEGDYV
     RILKLPQIGD NIRRRGSDME TGQHVFETGV QITPAVRGVL ASLGVKKVTT FRRPKIGIIS
     TGDELSDSAI LAPGKIHDSN RPALLDSVTA LGATAVDLGN VGDDPDEIRR AFKHAVATCD
     ALITSGGVSV GDFDYTKAVL NELSDNQITW FQVAIKPAKP FAFGAISDIP VFGLPGNPVS
     ALVSFELFVR PSILRMQGAS QLFRPTLSAI STAAIHHEPD GKLHLLRATI GSDRNGGLTA
     TPQNQQGSHM LTGLARANGL ILSPDGARIG PGERVDVLLI GNLGADTFSV PAPVPTDK
//
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