GenomeNet

Database: UniProt
Entry: K9RPD7_9CYAN
LinkDB: K9RPD7_9CYAN
Original site: K9RPD7_9CYAN 
ID   K9RPD7_9CYAN            Unreviewed;       410 AA.
AC   K9RPD7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=Riv7116_6849 {ECO:0000313|EMBL:AFY59164.1};
OS   Rivularia sp. PCC 7116.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC   Rivularia.
OX   NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY59164.1, ECO:0000313|Proteomes:UP000010380};
RN   [1] {ECO:0000313|EMBL:AFY59164.1, ECO:0000313|Proteomes:UP000010380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY59164.1,
RC   ECO:0000313|Proteomes:UP000010380};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL   Submitted (AUG-2012) 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; CP003549; AFY59164.1; -; Genomic_DNA.
DR   RefSeq; WP_015122713.1; NC_019678.1.
DR   AlphaFoldDB; K9RPD7; -.
DR   STRING; 373994.Riv7116_6849; -.
DR   KEGG; riv:Riv7116_6849; -.
DR   PATRIC; fig|373994.3.peg.7289; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_1_3; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000010380; 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; 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:UP000010380};
KW   Transferase {ECO:0000256|RuleBase:RU365090, ECO:0000313|EMBL:AFY59164.1}.
FT   DOMAIN          183..324
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   410 AA;  44404 MW;  1AA7D8AC88D732CE CRC64;
     MLSVNEAENI IFNLVKPLNN QTDIETVNLL TATGRVLASP VTSQIDFPHW DNSAMDGYAV
     VYQDVREANE EKPAVLKLVE DIPAGYQPQS NIQSGQAARI FTGAVMPKGA DTVVMQENTR
     REDDKVFILK APESQEFVRH RAAYYQAGTE LLSAGIQLNA PEIAVLAAAQ CTKLNVFRRP
     SVAILSTGDE LITPEQTLQP GQIVDSNQYA LAALVKQCGG EPLILGIIKD DREAIKKAIE
     EAIAKADIVL SSGGVSVGDY DYVEKILESL GGEIKVRAVA MKPGKPLTVA TFNIPNAPIY
     FGLPGNPVSA LVSYWRFVQP VIKKCSSIVE GWQPKFIKAQ TRNNLNSNGK RETYIWGKLN
     LVDGVYQFSA AAGSKSSGNL INLAQTNAFA VLEVGKKSVS TGEEVKVLQV
//
DBGET integrated database retrieval system