UniProt: A0A062XSG4

Database: UniProt
Entry: A0A062XSG4_9BACT

LinkDB:  A0A062XSG4_9BACT 
Original site:  A0A062XSG4_9BACT

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
All databases (15)   

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ID   A0A062XSG4_9BACT        Unreviewed;       396 AA.
AC   A0A062XSG4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=EG19_02855 {ECO:0000313|EMBL:KDA53773.1};
OS   Thermoanaerobaculum aquaticum.
OC   Bacteria; Acidobacteriota; Thermoanaerobaculia; Thermoanaerobaculales;
OC   Thermoanaerobaculaceae; Thermoanaerobaculum.
OX   NCBI_TaxID=1312852 {ECO:0000313|EMBL:KDA53773.1, ECO:0000313|Proteomes:UP000027284};
RN   [1] {ECO:0000313|EMBL:KDA53773.1, ECO:0000313|Proteomes:UP000027284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP-01 {ECO:0000313|EMBL:KDA53773.1,
RC   ECO:0000313|Proteomes:UP000027284};
RA   Stamps B.W., Losey N.A., Lawson P.A., Stevenson B.S.;
RT   "The Genome Sequence of Thermoanaerobaculum aquaticum MP-01, The First
RT   Cultivated Group 23 Acidobacterium.";
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|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:KDA53773.1}.
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DR   EMBL; JMFG01000017; KDA53773.1; -; Genomic_DNA.
DR   RefSeq; WP_038049041.1; NZ_JMFG01000017.1.
DR   AlphaFoldDB; A0A062XSG4; -.
DR   STRING; 1312852.EG19_02855; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000027284; 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   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; 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:UP000027284};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          172..308
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   396 AA;  41333 MW;  D7D9880D706282FC CRC64;
     MIHPDHALEL LASTAKPLPA RAVSLSRAAG HVLAQEVRAR VSFPPAPVAA MDGYAVRLPE
     ACGQALPMLF TVAAGDDPPP LPAGGCARIF TGAVVPEGAT AVVAQEDVEL VGGQVRFPAQ
     ISPGDNIRQK GEVFAQGEVL AEAGVVLTPA HLALLAAAGK KRLVVHPKPR VAVVATGSEL
     ADEKLTRGKI FDSNTPMLES FLLLSGFAVA AKARVPDQLD ALQKTLTSLL AHADVVITTG
     GVSVGDLDLL PQAVQELGGE VIFHKVAMQP GKPVLAAKVG ERFILGLPGN PVSALVGFRL
     FALPLLRALA GFAQAFHEPW TPLPLAGPVS NRGQRVQFRP ARELPSETGK AVEVLPWKGS
     HDLKAAAQAT HLARLDAGFA GQAGDRVLAV ELYRPR
//

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