UniProt: A0A2S8ER40

Database: UniProt
Entry: A0A2S8ER40_9RHOB

LinkDB:  A0A2S8ER40_9RHOB 
Original site:  A0A2S8ER40_9RHOB

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

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ID   A0A2S8ER40_9RHOB        Unreviewed;       712 AA.
AC   A0A2S8ER40;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=C2I36_13695 {ECO:0000313|EMBL:PQO22311.1};
OS   Rhodobacteraceae bacterium WD3A24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO22311.1, ECO:0000313|Proteomes:UP000237945};
RN   [1] {ECO:0000313|EMBL:PQO22311.1, ECO:0000313|Proteomes:UP000237945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WD3A24 {ECO:0000313|EMBL:PQO22311.1,
RC   ECO:0000313|Proteomes:UP000237945};
RA   Wang S.;
RT   "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL   Submitted (JAN-2018) 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:PQO22311.1}.
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DR   EMBL; PUHN01000053; PQO22311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8ER40; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000237945; 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   Reference proteome {ECO:0000313|Proteomes:UP000237945};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:PQO22311.1}.
FT   DOMAIN          488..626
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   712 AA;  74358 MW;  EED3F2DB90EE1B74 CRC64;
     MFDRVAILDW SAAGTPKSGR DSIWLGVAGA GGVEVENPRT RVEAERRLAR LIDDSIGAGE
     RLLIGMDFAF GYPAGFAARL TGRAHAPAVW EWLAAHVSDT PDNRSTYRDA AARMNAYFAG
     DGPFWGNNEA TATAGLPRRK PALPEGLAEL RATDRAAGGS GGTPKPVWQL AYSGAVGAQT
     LTAQPMLHRL RAGFAGRLAV WPFDPPADAR VVVAEVYPSM LSAEVRAFCR DNSGVVPDEA
     QVRLMASAFL QLATTGRLSA MFDPPAAPDL LAEEGWILAA GHEMALRSAL PARTAPPRLR
     DDCFAMPQGV DWVPVDTALE KLRAGLHPVA GTLQLPPAQA DGHVLAEAAI ARRANPPAPN
     SAVDGYGFAH LATGEGPQRL PLLEGRAAAG QPWTTPVPEG AAIRILTGAI LPPGVDTVVL
     DEDTARDGAA IVFDGPVRAG ANTRRAGEDV AAGSPALPAG RRLTPPDLAL LTALGVGEVT
     VRRRLRVAVL STGDELVADP ARPAETHQIF DANRPMLLAT VARWGHEPVD LGHAPDDEAA
     IAAALDRGAD GADVILTSGG ASAGDEDHVS KLLQTRAQLT SWRIALKPGR PLALAVWNGA
     AVFGLPGNPV AAFVCTLIFA RPALSLMAGA GWLAPQGFTV PAAFSKSKKP GRREYLRARL
     DAEGRAEVFA SEGSGRISGL SWADGLVELA DGAAEIGPGA PVRYIPYASF GL
//

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