UniProt: A0A498RDN4

Database: UniProt
Entry: A0A498RDN4_9FIRM

LinkDB:  A0A498RDN4_9FIRM 
Original site:  A0A498RDN4_9FIRM

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (20)   

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ID   A0A498RDN4_9FIRM        Unreviewed;       662 AA.
AC   A0A498RDN4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=LUCI_4909 {ECO:0000313|EMBL:VBB09614.1};
OS   Lucifera butyrica.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Lucifera.
OX   NCBI_TaxID=1351585 {ECO:0000313|EMBL:VBB09614.1, ECO:0000313|Proteomes:UP000277811};
RN   [1] {ECO:0000313|EMBL:VBB09614.1, ECO:0000313|Proteomes:UP000277811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LUCI {ECO:0000313|EMBL:VBB09614.1};
RA   Strepis N.;
RL   Submitted (JUN-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   -!- 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; UPPP01000127; VBB09614.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498RDN4; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000277811; 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|RuleBase:RU365090};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|RuleBase:RU365090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277811};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          190..327
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   662 AA;  70781 MW;  EE6086D693DD9910 CRC64;
     MKILRSNKAY LNCVERSEVQ KLWRQKLMEN GFFHNPPAEV VPVQASLGRV TARSVYAKQS
     VPHYNGAAMD GIAVWAQDTF GAQETDPKCL TLLPPAKTFG SGCCYMVDTG DVLPDGTNAV
     VMIEDVHIRG NMAEIIAAAA PWQHVRIIGE DIVANEMVIP EHHEIAPVDI AALLAAGIED
     VEVVQRPKVT IIPTGDELVA SRGELKPGTI LDVNSHMLAA AIQEWRGEAV RSAIVKDDRQ
     AIKQAILASL QGNDMVIINA GTSAGRDDYT VDVLSELGEV FVHGVAIKPG KPVVMAVCQG
     KPVIGLPGYP VAAMLTAELF VRDILFARQK LPRPEAATVE ASLVKQVPST VGVEEYIRVS
     LGNVQGKMVA APLSRGAGLI SSLTKAQGSI SIAAISSGLS AGTAVPVVLL RKGKPANTLL
     AVGSHDLALE LLGVFLRRRM ENVSLSCANV GSMGGIMAIR NNEAHLAGVH LLEADTGLYN
     TPYVEKFLPD GNWRLIHLAM RLQGLMVMPG NPKVITGLSD LTRDDVSFIN RQRGSGTRML
     LDYQLRKLGI RPEQIAGYEK EVGTHMAVAA SVLAGAADAG LGVQAAAQAL GLDFIPVSPE
     QYDLILNFTG EDERLYQIMD VLLSEEFRSE VESLGGYDLS NAGKLIAAGP NLRLNECGTR
     GE
//

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