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Database: UniProt
Entry: A0A090ZEA9_PAEMA
LinkDB: A0A090ZEA9_PAEMA
Original site: A0A090ZEA9_PAEMA 
ID   A0A090ZEA9_PAEMA        Unreviewed;       423 AA.
AC   A0A090ZEA9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|ARBA:ARBA00021108, ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|ARBA:ARBA00013269, ECO:0000256|RuleBase:RU365090};
GN   ORFNames=DJ90_4927 {ECO:0000313|EMBL:KFN08773.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN08773.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFN08773.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFN08773.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-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:KFN08773.1}.
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DR   EMBL; JMQA01000026; KFN08773.1; -; Genomic_DNA.
DR   RefSeq; WP_036623045.1; NZ_UGSI01000001.1.
DR   AlphaFoldDB; A0A090ZEA9; -.
DR   STRING; 44252.DJ90_4927; -.
DR   GeneID; 77007280; -.
DR   PATRIC; fig|44252.3.peg.2843; -.
DR   HOGENOM; CLU_010186_7_1_9; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000029278; 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   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.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU365090};
KW   Metal-binding {ECO:0000256|RuleBase:RU365090};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029278};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          196..334
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   423 AA;  45562 MW;  582FB35CFE9C1D91 CRC64;
     MTTDSQQDKF RRKALQVPDA QGRILPYARR LPAETVALPD AQGRILAERV TAPHPYPHFR
     RSGMDGFAIL SRDTQGCGAN RPALLEVVDE IPCGSLPSVP LAPGTAARIM TGAKVPDEAD
     AVVMFEMTET IRQDGKTYIR LIREIDPGKN ITPVGLELAA GEVILEPGRK VGAGEISVLA
     TFGIDRVPVV RKPRIAVFST GSELLAISEP LQDGRIRNSN AYMLASQIKD AGAEPFMLEA
     IPDDLELARQ RVRAAFADYD AVITTGGVSV GDFDIMADLV SGGEVEMLFN KVTMRPGSVT
     TAAVKDGNLL FALSGNPGAC FVGFELFVRP AIGRMLGVLQ PFLPEMTAEL GRPYKKINNF
     TRFVRGRLEA REGKLYAYPA ELDESGVMIT IKDSDALIVI PPSGEAREAG EMVTVLKLPG
     ASL
//
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