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Database: UniProt
Entry: A0A099LEX3_9GAMM
LinkDB: A0A099LEX3_9GAMM
Original site: A0A099LEX3_9GAMM 
ID   A0A099LEX3_9GAMM        Unreviewed;       415 AA.
AC   A0A099LEX3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=ND16A_3383 {ECO:0000313|EMBL:KGK00623.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGK00623.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGK00623.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGK00623.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-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}.
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:KGK00623.1}.
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DR   EMBL; JQDZ01000012; KGK00623.1; -; Genomic_DNA.
DR   RefSeq; WP_033076162.1; NZ_JQDZ01000012.1.
DR   AlphaFoldDB; A0A099LEX3; -.
DR   STRING; 1535422.ND16A_3383; -.
DR   PATRIC; fig|1535422.3.peg.503; -.
DR   eggNOG; COG0303; Bacteria.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000029848; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000029848};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          188..325
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   415 AA;  44142 MW;  5F2BDDDE0B1A6EC4 CRC64;
     MSDCCSAPGL MAFDLALKQL LDNVPAPENS QHVAIENALG KVLAGDVISP VFVPPHNNSA
     MDGYAFNSQL SVQAINTNSG LEIVGRSFAG EPFTGQTQAG QSIRIMTGAK MPRCCDTVVM
     QENTEVKDGQ LHFTKAPVAN SNVRKQGEDI QLNDKVLTKG HKLTAIDIGV LASLGIAKIE
     VFAPLTVAVL STGDELRSPG EPLNDGDIYE SNRFAIIALL EKLNVNILDL GIIRDDKTAI
     TNAFIQADIE ADVVISSGGV SVGEADYTKE VLAELGEINF WKIAMKPGKP FAFGKLANSI
     FFGLPGNPVS ALVTFYQLAT PGIEKMQGLT FKAKPKFLAK STSKLKKSPG RMDFQRAILY
     FSESGEAQVT STGSQGSGIL SSLGAANSFI VLDSEQGSVE AGEMVFVEPY SALFQ
//
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