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Protein

Molybdopterin biosynthesis protein CNX1

Gene

CNX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.4 Publications

Catalytic activityi

Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.

Cofactori

Mg2+2 Publications

Enzyme regulationi

Inhibited by copper and tungsten.1 Publication

Kineticsi

  1. KM=62 µM for ATP for domain G2 Publications
  2. KM=133 µM for Zn2+ for domain E2 Publications
  3. KM=255 µM for Mg2+ for domain E2 Publications

    Pathwayi: molybdopterin biosynthesis

    This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei485AMP1
    Binding sitei486AMP; via amide nitrogen1
    Binding sitei541AMP; via amide nitrogen1
    Binding sitei573Substrate1 Publication1
    Binding sitei600AMP; via carbonyl oxygen1
    Binding sitei600Substrate; via amide nitrogen1 Publication1
    Binding sitei607Substrate1 Publication1

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • molybdenum ion binding Source: TAIR
    • molybdopterin adenylyltransferase activity Source: GO_Central
    • molybdopterin molybdotransferase activity Source: GO_Central
    • nitrate reductase activity Source: CAFA

    GO - Biological processi

    • auxin-activated signaling pathway Source: TAIR
    • molybdenum incorporation into molybdenum-molybdopterin complex Source: GO_Central
    • molybdopterin cofactor biosynthetic process Source: GO_Central
    • Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW
    • response to metal ion Source: CAFA

    Keywordsi

    Molecular functionTransferase
    Biological processMolybdenum cofactor biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.10.1.1. 399.
    2.7.7.75. 399.
    ReactomeiR-ATH-947581. Molybdenum cofactor biosynthesis.
    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdopterin biosynthesis protein CNX1
    Alternative name(s):
    Molybdenum cofactor biosynthesis enzyme CNX1
    Including the following 2 domains:
    Molybdopterin molybdenumtransferase (EC:2.10.1.1)
    Short name:
    MPT Mo-transferase
    Alternative name(s):
    Domain E
    Molybdopterin adenylyltransferase (EC:2.7.7.75)
    Short name:
    MPT adenylyltransferase
    Alternative name(s):
    Domain G
    Gene namesi
    Name:CNX1
    Ordered Locus Names:At5g20990
    ORF Names:F22D1.6, T10F18.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRilocus:2147157. AT5G20990.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi475S → D: Reduced molybdopterin binding. Loss of adenylation activity. 1 Publication1
    Mutagenesisi485D → S: Reduced molybdopterin binding. Loss of adenylation activity. 1 Publication1
    Mutagenesisi515D → H or N: Almost normal molybdopterin binding. Loss adenylation activity. 2 Publications1
    Mutagenesisi542T → A: Strongly reduced molybdopterin binding. Reduced activity. 1 Publication1
    Mutagenesisi542T → D or N: Loss of molybdopterin binding. Loss of activity. 1 Publication1
    Mutagenesisi542T → S: Reduced molybdopterin binding. No effect on activity. 1 Publication1
    Mutagenesisi542T → V: Strongly reduced molybdopterin binding. No effect on activity. 1 Publication1
    Mutagenesisi547R → E: No effect on molybdopterin binding. Clear reduction in adenylation activity. 1 Publication1
    Mutagenesisi557V → G: Impaired folding. Loss of activity. 1 Publication1
    Mutagenesisi573S → A: Loss of molybdopterin binding. Loss of activity. 1 Publication1
    Mutagenesisi583S → A: No effect on activity. 1 Publication1
    Mutagenesisi597N → L: Loss of molybdopterin binding. Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001709631 – 670Molybdopterin biosynthesis protein CNX1Add BLAST670

    Proteomic databases

    PaxDbiQ39054.
    PRIDEiQ39054.

    PTM databases

    iPTMnetiQ39054.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ39054. baseline and differential.
    GenevisibleiQ39054. AT.

    Interactioni

    Subunit structurei

    The G domain: homotrimer or homohexamer. The E domain: homodimer.4 Publications

    Protein-protein interaction databases

    BioGridi17499. 3 interactors.
    MINTiMINT-8070811.
    STRINGi3702.AT5G20990.1.

    Structurei

    Secondary structure

    1670
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi19 – 29Combined sources11
    Beta strandi36 – 39Combined sources4
    Helixi41 – 43Combined sources3
    Beta strandi46 – 48Combined sources3
    Beta strandi58 – 61Combined sources4
    Beta strandi63 – 71Combined sources9
    Turni73 – 75Combined sources3
    Beta strandi77 – 86Combined sources10
    Beta strandi102 – 105Combined sources4
    Beta strandi117 – 120Combined sources4
    Helixi121 – 123Combined sources3
    Beta strandi124 – 127Combined sources4
    Beta strandi136 – 139Combined sources4
    Turni145 – 148Combined sources4
    Beta strandi154 – 156Combined sources3
    Beta strandi161 – 163Combined sources3
    Helixi171 – 179Combined sources9
    Beta strandi184 – 188Combined sources5
    Beta strandi193 – 198Combined sources6
    Helixi219 – 229Combined sources11
    Beta strandi234 – 240Combined sources7
    Helixi244 – 256Combined sources13
    Beta strandi260 – 266Combined sources7
    Beta strandi269 – 271Combined sources3
    Helixi276 – 283Combined sources8
    Beta strandi284 – 292Combined sources9
    Beta strandi298 – 306Combined sources9
    Beta strandi315 – 322Combined sources8
    Helixi326 – 335Combined sources10
    Helixi337 – 344Combined sources8
    Beta strandi353 – 361Combined sources9
    Beta strandi367 – 369Combined sources3
    Beta strandi371 – 382Combined sources12
    Beta strandi384 – 387Combined sources4
    Beta strandi389 – 394Combined sources6
    Helixi403 – 406Combined sources4
    Beta strandi411 – 415Combined sources5
    Beta strandi427 – 432Combined sources6
    Beta strandi466 – 474Combined sources9
    Helixi476 – 479Combined sources4
    Helixi487 – 497Combined sources11
    Turni498 – 503Combined sources6
    Beta strandi504 – 513Combined sources10
    Helixi517 – 529Combined sources13
    Beta strandi534 – 540Combined sources7
    Beta strandi543 – 545Combined sources3
    Helixi550 – 557Combined sources8
    Beta strandi559 – 561Combined sources3
    Helixi563 – 576Combined sources14
    Helixi578 – 582Combined sources5
    Beta strandi587 – 590Combined sources4
    Beta strandi593 – 598Combined sources6
    Helixi604 – 623Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EAVX-ray2.60A/B/C/D/E/F/G/H462-623[»]
    1O8NX-ray2.80A/B/C462-628[»]
    1O8OX-ray2.70A/B/C462-628[»]
    1O8QX-ray2.60A/B/C/D/E/F/G/H462-628[»]
    1UUXX-ray1.60A462-623[»]
    1UUYX-ray1.45A462-624[»]
    5G2RX-ray2.45A1-451[»]
    5G2SX-ray2.84A1-451[»]
    ProteinModelPortaliQ39054.
    SMRiQ39054.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ39054.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni19 – 439MPT Mo-transferaseAdd BLAST421
    Regioni466 – 620MPT adenylyltransferaseAdd BLAST155
    Regioni542 – 543Substrate binding2

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi8 – 12Poly-Gly5

    Sequence similaritiesi

    In the N-terminal section; belongs to the MoaB/Mog family.Curated
    In the C-terminal section; belongs to the MoeA family.Curated

    Phylogenomic databases

    eggNOGiKOG2371. Eukaryota.
    COG0303. LUCA.
    COG0521. LUCA.
    HOGENOMiHOG000280651.
    InParanoidiQ39054.
    KOiK15376.
    OMAiRPVGCDI.
    OrthoDBiEOG093605YJ.
    PhylomeDBiQ39054.

    Family and domain databases

    CDDicd00886. MogA_MoaB. 1 hit.
    Gene3Di2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProiView protein in InterPro
    IPR001453. MoaB/Mog_dom.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    PfamiView protein in Pfam
    PF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    SMARTiView protein in SMART
    SM00852. MoCF_biosynth. 2 hits.
    SUPFAMiSSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
    PROSITEiView protein in PROSITE
    PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q39054-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEGQGCCGGG GGKTEMIPTE EALRIVFGVS KRLPPVIVSL YEALGKVLAE
    60 70 80 90 100
    DIRAPDPLPP YPASVKDGYA VVASDGPGEY PVITESRAGN DGLGVTVTPG
    110 120 130 140 150
    TVAYVTTGGP IPDGADAVVQ VEDTKVIGDV STESKRVKIL IQTKKGTDIR
    160 170 180 190 200
    RVGCDIEKDA TVLTTGERIG ASEIGLLATA GVTMVKVYPM PIVAILSTGD
    210 220 230 240 250
    ELVEPTAGTL GRGQIRDSNR AMLVAAVMQQ QCKVVDLGIV RDDRKELEKV
    260 270 280 290 300
    LDEAVSSGVD IILTSGGVSM GDRDFVKPLL EEKGKVYFSK VLMKPGKPLT
    310 320 330 340 350
    FAEIRAKPTE SMLGKTVLAF GLPGNPVSCL VCFNIFVVPT IRQLAGWTSP
    360 370 380 390 400
    HPLRVRLRLQ EPIKSDPIRP EFHRAIIKWK DNDGSGTPGF VAESTGHQMS
    410 420 430 440 450
    SRLLSMRSAN ALLELPATGN VLSAGSSVSA IIVSDISAFS IDKKASLSEP
    460 470 480 490 500
    GSIRKEKKYD EVPGPEYKVA ILTVSDTVSA GAGPDRSGPR AVSVVDSSSE
    510 520 530 540 550
    KLGGAKVVAT AVVPDEVERI KDILQKWSDV DEMDLILTLG GTGFTPRDVT
    560 570 580 590 600
    PEATKKVIER ETPGLLFVMM QESLKITPFA MLSRSAAGIR GSTLIINMPG
    610 620 630 640 650
    NPNAVAECME ALLPALKHAL KQIKGDKREK HPKHIPHAEA TLPTDTWDQS
    660 670
    YKSAYETGEK KEEAGCSCTH
    Length:670
    Mass (Da):71,279
    Last modified:December 6, 2002 - v2
    Checksum:i4405722BB9C5EF02
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti113D → V (PubMed:8528286).Curated1
    Sequence conflicti113D → V (Ref. 2) Curated1
    Sequence conflicti134S → A (PubMed:8528286).Curated1
    Sequence conflicti134S → A (Ref. 2) Curated1
    Sequence conflicti653S → L (PubMed:8528286).Curated1
    Sequence conflicti653S → L (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L47323 mRNA. Translation: AAA97413.1.
    AJ236870 Genomic DNA. Translation: CAB38312.1.
    AC069325 Genomic DNA. No translation available.
    AF296834 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92917.1.
    RefSeqiNP_197599.1. NM_122108.4.
    UniGeneiAt.23035.

    Genome annotation databases

    EnsemblPlantsiAT5G20990.1; AT5G20990.1; AT5G20990.
    GeneIDi832224.
    GrameneiAT5G20990.1; AT5G20990.1; AT5G20990.
    KEGGiath:AT5G20990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L47323 mRNA. Translation: AAA97413.1.
    AJ236870 Genomic DNA. Translation: CAB38312.1.
    AC069325 Genomic DNA. No translation available.
    AF296834 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92917.1.
    RefSeqiNP_197599.1. NM_122108.4.
    UniGeneiAt.23035.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EAVX-ray2.60A/B/C/D/E/F/G/H462-623[»]
    1O8NX-ray2.80A/B/C462-628[»]
    1O8OX-ray2.70A/B/C462-628[»]
    1O8QX-ray2.60A/B/C/D/E/F/G/H462-628[»]
    1UUXX-ray1.60A462-623[»]
    1UUYX-ray1.45A462-624[»]
    5G2RX-ray2.45A1-451[»]
    5G2SX-ray2.84A1-451[»]
    ProteinModelPortaliQ39054.
    SMRiQ39054.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi17499. 3 interactors.
    MINTiMINT-8070811.
    STRINGi3702.AT5G20990.1.

    PTM databases

    iPTMnetiQ39054.

    Proteomic databases

    PaxDbiQ39054.
    PRIDEiQ39054.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G20990.1; AT5G20990.1; AT5G20990.
    GeneIDi832224.
    GrameneiAT5G20990.1; AT5G20990.1; AT5G20990.
    KEGGiath:AT5G20990.

    Organism-specific databases

    AraportiAT5G20990.
    TAIRilocus:2147157. AT5G20990.

    Phylogenomic databases

    eggNOGiKOG2371. Eukaryota.
    COG0303. LUCA.
    COG0521. LUCA.
    HOGENOMiHOG000280651.
    InParanoidiQ39054.
    KOiK15376.
    OMAiRPVGCDI.
    OrthoDBiEOG093605YJ.
    PhylomeDBiQ39054.

    Enzyme and pathway databases

    UniPathwayiUPA00344.
    BRENDAi2.10.1.1. 399.
    2.7.7.75. 399.
    ReactomeiR-ATH-947581. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    EvolutionaryTraceiQ39054.
    PROiPR:Q39054.

    Gene expression databases

    ExpressionAtlasiQ39054. baseline and differential.
    GenevisibleiQ39054. AT.

    Family and domain databases

    CDDicd00886. MogA_MoaB. 1 hit.
    Gene3Di2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProiView protein in InterPro
    IPR001453. MoaB/Mog_dom.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    PfamiView protein in Pfam
    PF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    SMARTiView protein in SMART
    SM00852. MoCF_biosynth. 2 hits.
    SUPFAMiSSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
    PROSITEiView protein in PROSITE
    PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCNX1_ARATH
    AccessioniPrimary (citable) accession number: Q39054
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 6, 2002
    Last modified: June 7, 2017
    This is version 147 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.