UniProt: A0A0W8JD38

Database: UniProt
Entry: A0A0W8JD38_9VIBR

LinkDB:  A0A0W8JD38_9VIBR 
Original site:  A0A0W8JD38_9VIBR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (19)   

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ID   A0A0W8JD38_9VIBR        Unreviewed;       411 AA.
AC   A0A0W8JD38;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE            EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN   ORFNames=VRK_26510 {ECO:0000313|EMBL:KUI97950.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI97950.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI97950.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI97950.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
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   -!- 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:KUI97950.1}.
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DR   EMBL; LQIY01000022; KUI97950.1; -; Genomic_DNA.
DR   RefSeq; WP_059121687.1; NZ_KQ947475.1.
DR   AlphaFoldDB; A0A0W8JD38; -.
DR   STRING; 1761910.VRK_26510; -.
DR   PATRIC; fig|1761910.3.peg.2680; -.
DR   OrthoDB; 9804758at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000054473; 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; 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; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR10192:SF34; MOLYBDOPTERIN MOLYBDENUMTRANSFERASE; 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   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          184..321
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   411 AA;  44169 MW;  E8DAB715D7B8DB7E CRC64;
     MGCCDTQGLL PIEDAIQTML ADVSPLKISQ KLPLETALGH VLAEDVRSPI DVPPFDNSAM
     DGYAVRTQDL TTTDTLPLAG KAFAGQPFSG EWPEKTCIRI MTGAPVPTGC DAVIMQEKTE
     ATPEGIHFLT SQVKAQANIR PQGDDLKQNE VVLPAGSRLT VRDLPLLASL GISQVLVLRK
     PKVAIFSTGD ELKPVGEKLD AGQIYDSNRY AIRPILENFG CDVIDLGIIP DNQTQLTETF
     QQAQSLADVV ITSGGVSVGE ADYTKTILES LGKINFWKIA IKPGKPFAFG KLNHSLFCGL
     PGNPVSAVVT LYVLVQPMLA KLAGHTQWRA PAQMQAVSKV SFKKSPGRTD YQRGIFSVKN
     GQIVVDNAGN QSSGAFRAMS TANCFIVLEQ QRGSVEAGET VTIEPFNPAL Y
//

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