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Database: UniProt
Entry: A0A0P7YAJ0_9RHOB
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Original site: A0A0P7YAJ0_9RHOB 
ID   A0A0P7YAJ0_9RHOB        Unreviewed;       418 AA.
AC   A0A0P7YAJ0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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   Name=moeA-2 {ECO:0000313|EMBL:KPP87367.1};
GN   ORFNames=HLUCCA08_05390 {ECO:0000313|EMBL:KPP87367.1};
OS   Rhodobacteraceae bacterium HLUCCA08.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP87367.1, ECO:0000313|Proteomes:UP000050293};
RN   [1] {ECO:0000313|Proteomes:UP000050293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KPP87367.1, ECO:0000313|Proteomes:UP000050293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP87367.1};
RX   PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA   Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT   "Identification and Resolution of Microdiversity through Metagenomic
RT   Sequencing of Parallel Consortia.";
RL   Appl. Environ. Microbiol. 82:255-267(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}.
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:KPP87367.1}.
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DR   EMBL; LJSF01000028; KPP87367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7YAJ0; -.
DR   STRING; 1666913.HLUCCA08_05390; -.
DR   PATRIC; fig|1666913.4.peg.1839; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000050293; 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: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   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:KPP87367.1}.
FT   DOMAIN          191..330
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   418 AA;  43267 MW;  D5B6B24E83411C02 CRC64;
     MATAVSCSAG TSGPTLSVDA ARLRAIAAAC PVAGQEVLAL DEASGRVIAA PIMAAHALPP
     FDNSAMDGYA LRLSDLAGDG PWHLPVSARI AAGDACALTL AAGTAARILT GAPVPLGADT
     VVMQERVTRA GDMISLRERP RLGQNIRRQG EDVARGAPVL AAGLALTPPR LALLAGCGVA
     SVAVRARVRV AILSTGNELS EPGRALGPGQ IHNSNRVLLR ATLSRFPWVD LTDLGIVPDD
     AAGIRTAIRH AAQTHDVVIS SGGVSAGEED HILDALRLEA AEPDVLKVAI RPGKPLTVAR
     LGPALYVGLP GNPYAAAITF SQIARPALRR AAGLMEEPDT WLPAVAGFSY RRTTGRREFV
     PVTWTSRDSL GRPVLMRLGK GASASMSPMA QARGIAVIAP DIDDVRPGQP LPVDPLCE
//
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