ID A0A0E0KWA6_ORYPU Unreviewed; 615 AA.
AC A0A0E0KWA6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC04G25870.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC04G25870.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC04G25870.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 AlphaFoldDB; A0A0E0KWA6; -.
DR STRING; 4537.A0A0E0KWA6; -.
DR EnsemblPlants; OPUNC04G25870.2; OPUNC04G25870.2; OPUNC04G25870.
DR Gramene; OPUNC04G25870.2; OPUNC04G25870.2; OPUNC04G25870.
DR eggNOG; KOG2371; Eukaryota.
DR HOGENOM; CLU_010186_6_1_1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000026962; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:EnsemblPlants.
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:0008940; F:nitrate reductase activity; IEA:EnsemblPlants.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010038; P:response to metal ion; IEA:EnsemblPlants.
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; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 2.
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; 2.
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:UP000026962};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 208..356
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 441..571
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 576..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 64226 MW; 86FF00AF3FF994CA CRC64;
MLPVEEALAA VLSAAAAASA ARPTAEAVPL HDALGLVLAE DVRAPDPLPP FRASIKDGYA
VVASDGPGEY PVITESRAGD DALGVVVTPG TVAYVTTGGE VAHAIPSDAA AVIELLTVVS
RAGPIPDGAD AVVQVEDTEQ LAGAPDGSKR VRILVRPTQG QDIRNVGCDI EKDSVVLKSG
EHIGPAEIGL LATVGVTTVK VYRRPTIAVF STGDELVQPV TASLSRGQIR DSNRAMLLAA
AIQHKCKVVD LGIAKDTEES LKEHMDAALS SDADIILTSG GVSMGDRDLV KPCLANMGKI
HFEKIRMKPG KPLTFAEIVT KDTSKPSKKV LAFGLPGNPV IPTDEIGLGR YVAESTGQQA
SSRLLSMKSA NALLEVPLVG QMLEAGTSMQ AILISDMTSS PFDKLPTASN PLPSHLFPPA
KSVSTDLSQV PASQNTEVKV AILTVSDTVS SGAGPDRSGP RAISVVNSSS EKLGGATVVA
TAVVPDDVEK IKNILVKWSD IDRVSLILTL GGTGFTPRDV TPEATKSVIE KEAPGLTYVM
LQESLKIINM PGNPNAVAEC MEALLPALKH ALKQIKGDKR EKHPRHVPHA EAAPVDQWDR
SFRAASSGRG CSCEP
//