GenomeNet

Database: UniProt
Entry: A0A0C4Y4I1_9BURK
LinkDB: A0A0C4Y4I1_9BURK
Original site: A0A0C4Y4I1_9BURK 
ID   A0A0C4Y4I1_9BURK        Unreviewed;       425 AA.
AC   A0A0C4Y4I1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=RR42_m2878 {ECO:0000313|EMBL:AJG20252.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG20252.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG20252.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG20252.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
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; CP010536; AJG20252.1; -; Genomic_DNA.
DR   RefSeq; WP_043347929.1; NZ_CP010536.1.
DR   AlphaFoldDB; A0A0C4Y4I1; -.
DR   STRING; 68895.RR42_m2878; -.
DR   KEGG; cbw:RR42_m2878; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000031843; Chromosome main.
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   Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          195..336
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   425 AA;  45025 MW;  3B829B096AC38939 CRC64;
     MPSLQSVISC LSDYDPGALP VAQANQIIGE LVEPVRGTEQ VALRAALDRV LAEDVISRLD
     VPAHDNSAMD GYAFASSELA VGGNVALAVV GSAFAGAACE QAVARGQAAR IMTGAIMPAG
     CDTVIPQEFV DVEGELIRFD AKAVRAGDNR RLRGEDLAIG QPALAAGRIL QPADLGLLAS
     LGVAEVKVRR RLRVAFFSTG DELRSIGEPL DAGCVYDSNR YTLHGMLRRM NVDLIDMGVV
     HDDPAALEAA LRSACENADA VITSGGVSVG EADYTKQIMA QLGDVTFWKI AMRPGRPMAF
     GRIASHGHEA LLFGLPGNPV AVMVTFYHFV RAALHRQMGA KVAPLPLMRV RSAQAIRKKP
     GRTEYQRGIL APAPEGGWQV SITGQQGSGV LRSMSEANCF IVLGHEQGMV AAGDEVEVML
     FDGLM
//
DBGET integrated database retrieval system