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Database: UniProt
Entry: D2NRK1_ROTMD
LinkDB: D2NRK1_ROTMD
Original site: D2NRK1_ROTMD 
ID   D2NRK1_ROTMD            Unreviewed;       496 AA.
AC   D2NRK1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   OrderedLocusNames=RMDY18_04450 {ECO:0000313|EMBL:BAI64277.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64277.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI64277.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64277.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent apical
RT   periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI64277.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64277.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA   Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT   with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT   Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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; AP011540; BAI64277.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2NRK1; -.
DR   STRING; 680646.RMDY18_04450; -.
DR   KEGG; rmu:RMDY18_04450; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001883; 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   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:UP000001883};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          235..392
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   496 AA;  53650 MW;  F5FD0984E57B23F4 CRC64;
     MPRTPPGAYR SLGETAFTSP QKHTYTSHNR RRTIGTAMIA PEFNGTPSTE EYRAYLALLL
     REVFIGTAET VPLYHAAGRI LAQDVTARMD VPSFDNSQMD GYALTAEAAE REDRIFTVGR
     EIPAGRPLQR SRSSDDLTYP IMTGAPMPKG YDAVIPVEQS ERIEYPDLPE SFGRPSEKVK
     LAPGKPGQFV RRRGEDVVTG QVLARAGERI TPAMLGALAS QGYARLTVAA GPRVLVCTGG
     DEILSGVEED GSATTQELGQ GQIFDANGPM LTAMLREDGA EVRRIAIGDD PVELVHRLVA
     EYESFKPDII ITSGGISHGK YEVVRNAIAK AHEADILVPV SWFGHVSQQP GGPQGVNLLD
     FKGHRVPMIS FPGNPVSTLI SYALILRPYL RAGGPYGVPY AVASEQATLN NAPRGVLVTE
     TPLTAPAAKR QFLRGTLAMV EVEPGTYRVE LYPDVLSGSH LLHRAAQADV LIELAPGTTY
     TGGEAVPYHR IRLTDN
//
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