UniProt: A0A1S3UFM5

Database: UniProt
Entry: A0A1S3UFM5_VIGRR

LinkDB:  A0A1S3UFM5_VIGRR 
Original site:  A0A1S3UFM5_VIGRR

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Ontology (5)   
   GO (5)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
All databases (24)   

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ID   A0A1S3UFM5_VIGRR        Unreviewed;       650 AA.
AC   A0A1S3UFM5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Molybdopterin biosynthesis protein CNX1 {ECO:0000256|RuleBase:RU365090};
DE   AltName: Full=Molybdenum cofactor biosynthesis enzyme CNX1 {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT Mo-transferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain E {ECO:0000256|RuleBase:RU365090};
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              Short=MPT adenylyltransferase {ECO:0000256|RuleBase:RU365090};
DE              EC=2.7.7.75 {ECO:0000256|RuleBase:RU365090};
DE     AltName: Full=Domain G {ECO:0000256|RuleBase:RU365090};
GN   Name=LOC106764894 {ECO:0000313|RefSeq:XP_014504816.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014504816.1};
RN   [1] {ECO:0000313|RefSeq:XP_014504816.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014504816.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC       cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC       molybdate is inserted into adenylated molybdopterin and AMP is
CC       released. {ECO:0000256|RuleBase:RU365090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; Evidence={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;
CC         Evidence={ECO:0000256|RuleBase:RU365090};
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.
CC       {ECO:0000256|RuleBase:RU365090}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC       {ECO:0000256|ARBA:ARBA00008339}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00007589}.
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DR   RefSeq; XP_014504816.1; XM_014649330.2.
DR   AlphaFoldDB; A0A1S3UFM5; -.
DR   STRING; 3916.A0A1S3UFM5; -.
DR   EnsemblPlants; Vradi06g03370.1; Vradi06g03370.1; Vradi06g03370.
DR   GeneID; 106764894; -.
DR   Gramene; Vradi06g03370.1; Vradi06g03370.1; Vradi06g03370.
DR   KEGG; vra:106764894; -.
DR   OrthoDB; 275356at2759; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000087766; Chromosome 6.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; 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   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
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; 2.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 2.
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; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 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:UP000087766};
KW   Transferase {ECO:0000256|RuleBase:RU365090}.
FT   DOMAIN          179..324
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
FT   DOMAIN          456..605
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   650 AA;  68764 MW;  70297ACAD880B298 CRC64;
     MIPVTDAIQI VLNASKRLPP LTVPLHDALG KVLAQDVRAP DPHPPYAASV KDGYAVIAAD
     GPGEYPVVAE SRAGDDALGV ILSPGTVAYV TTGGPIPEGA DAVVQVENTE LVNDASDGTK
     RVRILVQTTQ GNDIRPVGVD IEKGAIVLTS GERLGASEIG LLATVGVTMV KVYPLPTVAV
     LSTGDELVEP TTGHLSRGQI RDSNRAMLLA AAVQLQCKVL DLGIAKDDKE CLGRILDKAF
     ASGINILITS GGVSMGDKDF IKPLLEKRGK VHFDKVLIKP GKPFTFAEID FQSSESKILA
     FGLPGNPASS LVCFHLFVVP AIRLLAGWTD PHHLRVQARL HQPIKTDSFR PEYHRASVIW
     TDNDGTGNPG FVAVSTGHQV SSRLLSMKSA NALLEFPATG RVVSAGTAVS AIIISDLRNM
     AFDENHMSSG AAFALPGIKS QKVTTDSSGD AEVRVAILTV SDTVAMGGGP DRSGPRAVSV
     INSSSEKLGG AKVVATAVVP DNVVKIQNIL RRWSDIEQMD LIITLGGTGF TPRDLTPEAT
     KPLIEKETPG LLYVMMQESL KVTPFAMLSR SAAGIRGSTL IINMPGNPNA VAECMGALLP
     ALKHGLKQIR GDKKEKHPRH VPHVDAVPAD VWEQSYRLST ADDVSCSCCN
//

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