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Database: UniProt
Entry: A0A0C5VYE1_9FLAO
LinkDB: A0A0C5VYE1_9FLAO
Original site: A0A0C5VYE1_9FLAO 
ID   A0A0C5VYE1_9FLAO        Unreviewed;       392 AA.
AC   A0A0C5VYE1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=AW14_11050 {ECO:0000313|EMBL:AJR04096.1};
OS   Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Siansivirga.
OX   NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR04096.1, ECO:0000313|Proteomes:UP000032229};
RN   [1] {ECO:0000313|EMBL:AJR04096.1, ECO:0000313|Proteomes:UP000032229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR04096.1,
RC   ECO:0000313|Proteomes:UP000032229};
RA   Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL   Submitted (FEB-2014) 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}.
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DR   EMBL; CP007202; AJR04096.1; -; Genomic_DNA.
DR   RefSeq; WP_044638805.1; NZ_CP007202.1.
DR   AlphaFoldDB; A0A0C5VYE1; -.
DR   STRING; 1454006.AW14_11050; -.
DR   KEGG; sze:AW14_11050; -.
DR   PATRIC; fig|1454006.5.peg.2190; -.
DR   HOGENOM; CLU_010186_7_1_10; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000032229; 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:UP000032229};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          172..310
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   392 AA;  43584 MW;  BC31558D689809DB CRC64;
     MIIIESALNI IKANTTPLLK ETKKQVEKAG GYKLCKDVYA PINMPPFRQS AMDGYAVCLH
     DKQIYNVIDE IKAGDNHQPI LKKGDAVRIF TGAPVPDTAN CVIMQEKVMV NGKSIKITDP
     MNLQDNIRSI GEQVKKGQVA LKKDTKLTPA AIGYLSSLGI TEVAVYKKPQ IAIITTGNEL
     VEAGTYLEYG QIYESNSKML LSALYSLKFY EVTIHNIKDD YQQTVKALSK VIENNDLLLI
     TGGISVGDYD FVGKALAELK VEELFYKVKQ KPGKPFFFGK KESTLVFALP GNPAASLTCF
     YMYVYVSLQK LINNEREDLQ RVQAKSASKF IKRGDRPQFL KAIYNNGNVE ILEGQSSAMQ
     QTFALSNALV FVSEEQTKIK INDIVETILL PV
//
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