UniProt: A0A098F3M5

Database: UniProt
Entry: A0A098F3M5_9BACI

LinkDB:  A0A098F3M5_9BACI 
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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 (15)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (21)   

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ID   A0A098F3M5_9BACI        Unreviewed;       639 AA.
AC   A0A098F3M5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=BN1002_04192 {ECO:0000313|EMBL:CEG29260.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG29260.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG29260.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG29260.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-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   -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC       {ECO:0000256|ARBA:ARBA00003487}.
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}.
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DR   EMBL; CCXR01000001; CEG29260.1; -; Genomic_DNA.
DR   RefSeq; WP_048827311.1; NZ_CCXR01000001.1.
DR   AlphaFoldDB; A0A098F3M5; -.
DR   STRING; 1476857.BN1002_04192; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000042335; 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   InterPro; IPR024370; PBP_domain.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF16; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   Pfam; PF12727; PBP_like; 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   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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|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:UP000042335};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          179..316
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   639 AA;  70447 MW;  4A4C036AAD79AA8B CRC64;
     MDQKQYKRKI YLEDKPRIQA RDELLAAFGL PSQKEWVKVD DALGRITAEP VFATTSMPHY
     HASAMDGIAV QASETYSAHE QRPLRLSLGE QFAYVDTGNA IPPQYNAVIM IENVNVIDDH
     TLEIIEPATP WQHIRPIGED IVQEEMIFPQ GHKLRPADLG SLLAARITEV EVIKKPVVAI
     IPTGNELIEV TAEPQSGKII EFNGTVFANF VKEWGGEPHL RGIVKDEPEK IREALLNAAE
     SSDIVVINAG SSAGSKDFTV HIIHEIGEVF THGVAARPGK PVILGKIKGK PVVGVPGYPV
     SAYLALEWFV RPLICKYLQI PEPKRQTIQV KLGRRIVSTM GQEDFIRVNI GYVNGQFVAN
     PLTRAAGVTM SYVRADGLLV VPVNVLGYEQ GDMAEAELLR PLEEVAGSIV FSGSHDLTID
     LLSSQIKKKR TDMKIISSHV GSMAGLLAIR KGEAHVAGVH LLDPETKEYN LSYVKKLLDG
     MEIVLYPFLK RKQGWFLPPG NPLGIESVMD VAEKKAHFVN RQRGAGTRIL FDLLLKEAVL
     TPDQITGYNR EMFSHLSVAA EVKGNPEAVG IGIFPAARAM GLSFVPIADE EYDLVMTKEF
     FESEKGRMLI SVIQSDEFRQ NVEKIGGYEV VAGAMPKIC
//

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