UniProt: A0A254QQE9

Database: UniProt
Entry: A0A254QQE9_9RHOB

LinkDB:  A0A254QQE9_9RHOB 
Original site:  A0A254QQE9_9RHOB

All links

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)   

Download RDF

ID   A0A254QQE9_9RHOB        Unreviewed;       711 AA.
AC   A0A254QQE9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=ATO1_13305 {ECO:0000313|EMBL:OWU79057.1};
OS   Phaeobacter sp. 22II1-1F12B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU79057.1, ECO:0000313|Proteomes:UP000197279};
RN   [1] {ECO:0000313|EMBL:OWU79057.1, ECO:0000313|Proteomes:UP000197279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU79057.1,
RC   ECO:0000313|Proteomes:UP000197279};
RA   Lai Q., Li G., Shao Z.;
RT   "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL   Submitted (APR-2013) 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:OWU79057.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AQQP01000007; OWU79057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254QQE9; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000197279; 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:UP000197279};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          489..626
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   711 AA;  76115 MW;  1B834EB77E27CB98 CRC64;
     MSFDTYVVVD WSAGKRAPAK PSKDSIWIGI SRASGDDEPV YCRSRQDAEA HLAELIAAER
     EAGRRMMIGF DFPFGYPKGL ARKITGTDDV FALWAWLEER ISDLTDGSNN RYDVASEMNG
     FFDGPGPFWG KPNEQDWPEI PYRKAGIVFD EVAEKRHCDL AGKASSSCFQ LAFPPTVGGQ
     VLMGLPVLSR LRRLDGVAVW PFEDTSNAPV VLAEIWPGLI EPAVKEIKSQ APEDIRDRVQ
     VRLLARALSR LPNDELADLM AAPPQEAREE GWILGAGHVA RLSELALGGQ DAGEGPEPPP
     LRNDCFALPA GVNWTPVDQA LDLLKTRLNP IAGAERSPIR SALGRVLASD VIAERSNPPA
     ANSAVDGYGF AGGASEGKHR LHLVEGRAAA GAPYIGEVPV CSAIRILTGA PLPAGVDTVI
     LEEDVTTAEG QIAFRGPLRP GANARKAGED VAAGGMVLPA GRRLTPADLA LLSAVGPARV
     DLRRTLRVAV ISTGDELAEP GTPLKPGQIH DANRPMLLAM LARFAFEPVD MGIVPDERQA
     LSARLDAAAE QADVILTSGG ASAGDEDHVS ALLREAGAMQ EWRIAVKPGR PLALGLWAGK
     PVFGLPGNPV AAMVCTLVFA RPALCLLAGE GWQEPQGFTL PAAFEKRKKP GRREYLRARI
     REGRAEVFAS EGSGRISGLS WAEGLVELED GERHIRPGDP VRYIPFGSFA L
//

DBGET integrated database retrieval system