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Database: UniProt
Entry: A0A0S1S6E3_9FLAO
LinkDB: A0A0S1S6E3_9FLAO
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ID   A0A0S1S6E3_9FLAO        Unreviewed;       392 AA.
AC   A0A0S1S6E3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=SB49_10790 {ECO:0000313|EMBL:ALM08234.1};
OS   Sediminicola sp. YIK13.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sediminicola.
OX   NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM08234.1, ECO:0000313|Proteomes:UP000063759};
RN   [1] {ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA   Kwon Y.M., Kim S.-J.;
RT   "Genome sequence of Sediminicola sp. YIK13.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALM08234.1, ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|EMBL:ALM08234.1,
RC   ECO:0000313|Proteomes:UP000063759};
RX   PubMed=26823585;
RA   Kwon Y.M., Kim S.J.;
RT   "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT   Bacterium Sediminicola sp. YIK13.";
RL   Genome Announc. 4:e01635-15(2016).
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; CP010535; ALM08234.1; -; Genomic_DNA.
DR   RefSeq; WP_062056455.1; NZ_CP010535.1.
DR   AlphaFoldDB; A0A0S1S6E3; -.
DR   STRING; 1453352.SB49_10790; -.
DR   KEGG; syi:SB49_10790; -.
DR   PATRIC; fig|1453352.4.peg.2244; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000063759; 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; 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: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.
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:UP000063759};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          171..309
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   392 AA;  42154 MW;  901FA58DBB32E551 CRC64;
     MVSVEEALQI IAKNTTTLQS VTLPLSKARG MVTAQDVHAP IDLPPFDQSA MDGYAINIHP
     VKKYAIIGEV AAGDGKEVLL KAGEAVRIFT GAMVPETAKA VVMQEKVIRL ADSITLMEDA
     VAGSNIRPRG EQITKGDLAL RKGTELTPPA IGFLAGMGIM EVNVFDKPRV GIVITGNELA
     EGGETLKPGQ IYEGNSKMLL AAVEGYGIDG CNTYRVADNF MATCEVLSKA FQENDVVLVN
     GGISVGDHDY VYKALKALEV EPLFYKVRQK PGKPLFFGKR GNKIVFALPG NPAAALTCFY
     LYVYPALQKI MGQLGKGLER RKLMVSTSVA NTYNRALLLK ARILENGEVE ILEGQSSAML
     HTYSLANALV YVPESVSEIH QGSGVEVLVL PN
//
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