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Database: UniProt
Entry: A0A1H7DTN5_9RHOB
LinkDB: A0A1H7DTN5_9RHOB
Original site: A0A1H7DTN5_9RHOB 
ID   A0A1H7DTN5_9RHOB        Unreviewed;       390 AA.
AC   A0A1H7DTN5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=SAMN05444007_11410 {ECO:0000313|EMBL:SEK05106.1};
OS   Cribrihabitans marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cribrihabitans.
OX   NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEK05106.1, ECO:0000313|Proteomes:UP000199379};
RN   [1] {ECO:0000313|EMBL:SEK05106.1, ECO:0000313|Proteomes:UP000199379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29340 {ECO:0000313|EMBL:SEK05106.1,
RC   ECO:0000313|Proteomes:UP000199379};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNYD01000014; SEK05106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7DTN5; -.
DR   STRING; 1227549.SAMN05444007_11410; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000199379; 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   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:UP000199379};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:SEK05106.1}.
FT   DOMAIN          173..310
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   390 AA;  40660 MW;  679098B67801EC8B CRC64;
     MITVDEARAR LLQLVTRGPV EKVPVAQAAG RVLGADVTAT RDQPPFAASS MDGYAVHSDE
     VERHAMFKII GEAAAGKRFS GSVQPGQAVR IFTGAPMPAG ADFVVIQEDV SRKGDVITIT
     ETPGTKSNVR PAGVDFTVGT KLSAPRLLMP ADIALLAAMN IAQVPVTRKP VVALIATGDE
     LVMPGEDPGP EQIIASNTFG LRAMLQADGA EVRMLPIARD TEASLRTAFG LAAGADLVVT
     VGGASVGDHD LVAPVAEALG LERSFYKIRM RPGKPLMAGR MGDAAMVGLP GNPVSALVCG
     HLFLRPMVRR MLGLDPGPPP PKNAALAAPI GGNGAREHYM RAHVQDGRIT IFDNQDSSLL
     SVLAASNALV VRPPDDPARA AGDMVSYLAI
//
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