GenomeNet

Database: UniProt
Entry: A0A0U3KYZ1_9BURK
LinkDB: A0A0U3KYZ1_9BURK
Original site: A0A0U3KYZ1_9BURK 
ID   A0A0U3KYZ1_9BURK        Unreviewed;       423 AA.
AC   A0A0U3KYZ1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   Name=moeA {ECO:0000313|EMBL:ALU88968.1};
GN   ORFNames=Hrubri_1764 {ECO:0000313|EMBL:ALU88968.1};
OS   Herbaspirillum rubrisubalbicans M1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU88968.1, ECO:0000313|Proteomes:UP000069903};
RN   [1] {ECO:0000313|EMBL:ALU88968.1, ECO:0000313|Proteomes:UP000069903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1 {ECO:0000313|EMBL:ALU88968.1,
RC   ECO:0000313|Proteomes:UP000069903};
RA   Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA   Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA   Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT   "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL   Submitted (DEC-2015) 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   ---------------------------------------------------------------------------
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; CP013737; ALU88968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U3KYZ1; -.
DR   STRING; 1078773.Hrubri_1764; -.
DR   KEGG; hrb:Hrubri_1764; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000069903; Chromosome.
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; 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.
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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          193..334
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   423 AA;  45106 MW;  4477F5D09A27713E CRC64;
     MHDIVSCISG YDPHAMTVAS AQAVIQEFIT PIDTVEKLAI RSALSRVLAQ DIISRIDVPA
     HDNSAMDGYA LRGAEVAAGQ QVRLQIIGAV HAGERFSGTV GPGQCVRIMT GAPMPTGCDT
     VIPQELTTDA DAQAVTLPAG RVRPGDNRRL RGEDLALGSV ALPRGRVLRP SDIGLLASLG
     IAEVPVQRRL RVAFFSTGDE LRSVGEPLEP GCVYDSNRYT LHGMLTRLGC DVLDMGVVPD
     DPAALEAAFR NACEEADAVI TSGGVSVGEA DYTKQIMASL GEMTFWKIAM RPGRPLAFGR
     IQSRGRAAYL FGLPGNPVAV TVSFSFFVRD ALLRLAGAEP KPLPRLRAKT ATAIRKKAGR
     TEYQRGILAP DDHGTWQVRL TGMQGSGILR SMSDANCIIE LEHERGDVAA GEEVAVVLFD
     GLV
//
DBGET integrated database retrieval system