GenomeNet

Database: UniProt
Entry: K0YT31_9ACTO
LinkDB: K0YT31_9ACTO
Original site: K0YT31_9ACTO 
ID   K0YT31_9ACTO            Unreviewed;       415 AA.
AC   K0YT31;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, 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=HMPREF9240_01135 {ECO:0000313|EMBL:EJZ86761.1};
OS   Winkia neuii BV029A5.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Winkia.
OX   NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ86761.1, ECO:0000313|Proteomes:UP000006075};
RN   [1] {ECO:0000313|EMBL:EJZ86761.1, ECO:0000313|Proteomes:UP000006075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ86761.1,
RC   ECO:0000313|Proteomes:UP000006075};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5.";
RL   Submitted (JUL-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJZ86761.1}.
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; AGWP01000005; EJZ86761.1; -; Genomic_DNA.
DR   RefSeq; WP_004806830.1; NZ_JH815215.1.
DR   AlphaFoldDB; K0YT31; -.
DR   PATRIC; fig|888439.3.peg.1138; -.
DR   eggNOG; COG0303; Bacteria.
DR   HOGENOM; CLU_010186_7_0_11; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006075; 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; 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:UP000006075};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          182..318
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   REGION          355..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   415 AA;  42688 MW;  C44F261FBB66D91B CRC64;
     MKDVAEHYRD VLRLGQALPA ETLPVGEALG RILAEDVTAR LSVPPFTNSA MDGFAVRAQE
     TAAGVGLPVA ADIPAGRTDA LTLEKGTAMR IMTGAPLPQG ADAVIQVELT EGGPANMAPA
     APATVTFTDA VAKGANVRRA GEDIAAGQLL FTAGTRLSAA HLSALVSVGC GQVAVSPQLR
     VGVVTTGEEL RGAGEDLKPG QIPDSNSVLV SGLAREAGAS PILRTFHADT VDGFLKDIDA
     AAGQVDMLVT TGGVSAGAFD VVKAALRERG VTFTRVAMQP GKPQGFGKVG QVPILCLPGN
     PVSVLVSWYL FALPLLGVLA GVDQPAFEDR FVRAQVGTGW KRKTGRVQFL PATAREGEDG
     GTSAQVHVHP ASHGGSKSHF VASLAAATGL VRIPADQAEV KPGEEVPVMW FGRAR
//
DBGET integrated database retrieval system