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Database: UniProt
Entry: A0A0Q5E8I8_9MICO
LinkDB: A0A0Q5E8I8_9MICO
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ID   A0A0Q5E8I8_9MICO        Unreviewed;       417 AA.
AC   A0A0Q5E8I8;
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   ORFNames=ASF68_09520 {ECO:0000313|EMBL:KQQ52543.1};
OS   Plantibacter sp. Leaf314.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Plantibacter.
OX   NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52543.1, ECO:0000313|Proteomes:UP000051200};
RN   [1] {ECO:0000313|EMBL:KQQ52543.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52543.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ52543.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52543.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|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:KQQ52543.1}.
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DR   EMBL; LMOB01000001; KQQ52543.1; -; Genomic_DNA.
DR   RefSeq; WP_056009632.1; NZ_LMOB01000001.1.
DR   AlphaFoldDB; A0A0Q5E8I8; -.
DR   STRING; 1736333.ASF68_09520; -.
DR   OrthoDB; 3196725at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000051200; 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; 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; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 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:UP000051200};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          183..333
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   417 AA;  42188 MW;  BB06E5837DFBA203 CRC64;
     MTRSSWSDAR RIAHAAGVEQ RSQVVDSVEL ATALGHVLAA PLVSPIAIPH YASSAMDGWA
     VAGAGPWELV RGAAADRARS VGLEVGTAVE VLTGGLIPTG AVAVLQREHG IVEETADALR
     LGLSPQAPRE EPVAGRHIRD AGTESPAGTI LLDQGTRLGP VHLAVAAGGG FDRVPVVPRP
     KVRLVLTGDE VVTSGVPGAG FVRDSFGPSL PGVIASLGGV VTSSVRVRDD ASATAEALGT
     TTLGTTALTE PPARRAGEVI VTTGGTGGSR ADHVRALLRD AGAEFLVDGV EVRPGGPALL
     ARLPDGRLVV GLPGNPLAAL LSVLTLVQPL LAGQQGLGLP PLRPVVLASP VDPTRSETVL
     RPYRAVLDAE TAAVTAEPSP WHGAAMLRGL ADADGVLVHS GTGAAAGTVV PSLDLPW
//
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