Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q39054

- CNX1_ARATH

UniProt

Q39054 - CNX1_ARATH

Protein

Molybdopterin biosynthesis protein CNX1

Gene

CNX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (06 Dec 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Magnesium.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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei485 – 4851AMP
    Binding sitei486 – 4861AMP; via amide nitrogen
    Binding sitei541 – 5411AMP; via amide nitrogen
    Binding sitei573 – 5731Substrate1 Publication
    Binding sitei600 – 6001AMP; via carbonyl oxygen
    Binding sitei600 – 6001Substrate; via amide nitrogen1 Publication
    Binding sitei607 – 6071Substrate1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. molybdenum ion binding Source: TAIR
    3. molybdopterin adenylyltransferase activity Source: UniProtKB-EC
    4. molybdopterin molybdotransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. auxin-activated signaling pathway Source: TAIR
    2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_187830. 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
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G20990.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi475 – 4751S → D: Reduced molybdopterin binding. Loss of adenylation activity. 2 Publications
    Mutagenesisi485 – 4851D → S: Reduced molybdopterin binding. Loss of adenylation activity. 2 Publications
    Mutagenesisi515 – 5151D → H or N: Almost normal molybdopterin binding. Loss adenylation activity. 3 Publications
    Mutagenesisi542 – 5421T → A: Strongly reduced molybdopterin binding. Reduced activity. 2 Publications
    Mutagenesisi542 – 5421T → D or N: Loss of molybdopterin binding. Loss of activity. 2 Publications
    Mutagenesisi542 – 5421T → S: Reduced molybdopterin binding. No effect on activity. 2 Publications
    Mutagenesisi542 – 5421T → V: Strongly reduced molybdopterin binding. No effect on activity. 2 Publications
    Mutagenesisi547 – 5471R → E: No effect on molybdopterin binding. Clear reduction in adenylation activity. 2 Publications
    Mutagenesisi557 – 5571V → G: Impaired folding. Loss of activity. 2 Publications
    Mutagenesisi573 – 5731S → A: Loss of molybdopterin binding. Loss of activity. 2 Publications
    Mutagenesisi583 – 5831S → A: No effect on activity. 1 Publication
    Mutagenesisi597 – 5971N → L: Loss of molybdopterin binding. Loss of activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 670670Molybdopterin biosynthesis protein CNX1PRO_0000170963Add
    BLAST

    Proteomic databases

    PaxDbiQ39054.
    PRIDEiQ39054.

    Expressioni

    Gene expression databases

    GenevestigatoriQ39054.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi17499. 2 interactions.
    MINTiMINT-8070811.

    Structurei

    Secondary structure

    1
    670
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi466 – 4749
    Helixi476 – 4794
    Helixi487 – 49711
    Turni498 – 5036
    Beta strandi504 – 51310
    Helixi517 – 52913
    Beta strandi534 – 5407
    Beta strandi543 – 5453
    Helixi550 – 5578
    Beta strandi559 – 5613
    Helixi563 – 57614
    Helixi578 – 5825
    Beta strandi587 – 5904
    Beta strandi593 – 5986
    Helixi604 – 62320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ39054.
    SMRiQ39054. Positions 20-416, 464-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ39054.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 439421MPT Mo-transferaseAdd
    BLAST
    Regioni466 – 620155MPT adenylyltransferaseAdd
    BLAST
    Regioni542 – 5432Substrate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 125Poly-Gly

    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

    eggNOGiCOG0303.
    HOGENOMiHOG000280651.
    InParanoidiQ39054.
    KOiK15376.
    OMAiICDDDPE.
    PhylomeDBiQ39054.

    Family and domain databases

    Gene3Di2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProiIPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view]
    PfamiPF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view]
    SMARTiSM00852. MoCF_biosynth. 2 hits.
    [Graphical view]
    SUPFAMiSSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
    PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q39054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGQGCCGGG GGKTEMIPTE EALRIVFGVS KRLPPVIVSL YEALGKVLAE    50
    DIRAPDPLPP YPASVKDGYA VVASDGPGEY PVITESRAGN DGLGVTVTPG 100
    TVAYVTTGGP IPDGADAVVQ VEDTKVIGDV STESKRVKIL IQTKKGTDIR 150
    RVGCDIEKDA TVLTTGERIG ASEIGLLATA GVTMVKVYPM PIVAILSTGD 200
    ELVEPTAGTL GRGQIRDSNR AMLVAAVMQQ QCKVVDLGIV RDDRKELEKV 250
    LDEAVSSGVD IILTSGGVSM GDRDFVKPLL EEKGKVYFSK VLMKPGKPLT 300
    FAEIRAKPTE SMLGKTVLAF GLPGNPVSCL VCFNIFVVPT IRQLAGWTSP 350
    HPLRVRLRLQ EPIKSDPIRP EFHRAIIKWK DNDGSGTPGF VAESTGHQMS 400
    SRLLSMRSAN ALLELPATGN VLSAGSSVSA IIVSDISAFS IDKKASLSEP 450
    GSIRKEKKYD EVPGPEYKVA ILTVSDTVSA GAGPDRSGPR AVSVVDSSSE 500
    KLGGAKVVAT AVVPDEVERI KDILQKWSDV DEMDLILTLG GTGFTPRDVT 550
    PEATKKVIER ETPGLLFVMM QESLKITPFA MLSRSAAGIR GSTLIINMPG 600
    NPNAVAECME ALLPALKHAL KQIKGDKREK HPKHIPHAEA TLPTDTWDQS 650
    YKSAYETGEK KEEAGCSCTH 670
    Length:670
    Mass (Da):71,279
    Last modified:December 6, 2002 - v2
    Checksum:i4405722BB9C5EF02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131D → V(PubMed:8528286)Curated
    Sequence conflicti113 – 1131D → V1 PublicationCurated
    Sequence conflicti134 – 1341S → A(PubMed:8528286)Curated
    Sequence conflicti134 – 1341S → A1 PublicationCurated
    Sequence conflicti653 – 6531S → L(PubMed:8528286)Curated
    Sequence conflicti653 – 6531S → L1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_122108.3.
    UniGeneiAt.23035.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_197599.1. NM_122108.3.
    UniGenei At.23035.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EAV X-ray 2.60 A/B/C/D/E/F/G/H 462-623 [» ]
    1O8N X-ray 2.80 A/B/C 462-628 [» ]
    1O8O X-ray 2.70 A/B/C 462-628 [» ]
    1O8Q X-ray 2.60 A/B/C/D/E/F/G/H 462-628 [» ]
    1UUX X-ray 1.60 A 462-623 [» ]
    1UUY X-ray 1.45 A 462-624 [» ]
    ProteinModelPortali Q39054.
    SMRi Q39054. Positions 20-416, 464-623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 17499. 2 interactions.
    MINTi MINT-8070811.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Proteomic databases

    PaxDbi Q39054.
    PRIDEi Q39054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G20990.1 ; AT5G20990.1 ; AT5G20990 .
    GeneIDi 832224.
    KEGGi ath:AT5G20990.

    Organism-specific databases

    TAIRi AT5G20990.

    Phylogenomic databases

    eggNOGi COG0303.
    HOGENOMi HOG000280651.
    InParanoidi Q39054.
    KOi K15376.
    OMAi ICDDDPE.
    PhylomeDBi Q39054.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    Reactomei REACT_187830. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q39054.
    PROi Q39054.

    Gene expression databases

    Genevestigatori Q39054.

    Family and domain databases

    Gene3Di 2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProi IPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view ]
    Pfami PF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view ]
    SMARTi SM00852. MoCF_biosynth. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsi TIGR00177. molyb_syn. 2 hits.
    PROSITEi PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins."
      Stallmeyer B., Nerlich A., Schiemann J., Brinkmann H., Mendel R.R.
      Plant J. 8:751-762(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Sequence of the Arabidopsis thaliana gene cnx1 that is involved in the last step of molybdenum cofactor biosynthesis."
      Brinkmann H., Schledzewski K., Nerlich A., Bollmann G., Stallmeyer B., Mendel R.R.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Molybdenum cofactor biosynthesis. The plant protein Cnx1 binds molybdopterin with high affinity."
      Schwarz G., Boxer D.H., Mendel R.R.
      J. Biol. Chem. 272:26811-26814(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING OF MPT TO DOMAIN G, SUBUNIT.
    6. "Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilization."
      Kuper J., Palmer T., Mendel R.R., Schwarz G.
      Proc. Natl. Acad. Sci. U.S.A. 97:6475-6480(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-515; VAL-557 AND ASN-597.
    7. "Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion."
      Llamas A., Mendel R.R., Schwarz G.
      J. Biol. Chem. 279:55241-55246(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF DOMAIN G AS MPT ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, MUTAGENESIS, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly."
      Llamas A., Otte T., Multhaup G., Mendel R.R., Schwarz G.
      J. Biol. Chem. 281:18343-18350(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF DOMAIN E AS MOLYBDENUM--MPT-AMP LIGASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
    9. "Crystal structures of human gephyrin and plant Cnx1 G domains: comparative analysis and functional implications."
      Schwarz G., Schrader N., Mendel R.R., Hecht H.-J., Schindelin H.
      J. Mol. Biol. 312:405-418(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 462-623, SUBUNIT.
    10. "The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G."
      Kuper J., Winking J., Hecht H.-J., Mendel R.R., Schwarz G.
      Arch. Biochem. Biophys. 411:36-46(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 462-628 OF MUTANTS ALA/ASP-542 AND ALA-573, FUNCTION, MUTAGENESIS OF SER-475; ASP-485; ASP-515; THR-542; ARG-547 AND SER-573, SUBUNIT.
    11. "Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism."
      Kuper J., Llamas A., Hecht H.-J., Mendel R.R., Schwarz G.
      Nature 430:803-806(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 462-623 OF WILD-TYPE AND MUTANT ALA-583 IN COMPLEX WITH SUBSTRATE, FUNCTION, COFACTOR, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiCNX1_ARATH
    AccessioniPrimary (citable) accession number: Q39054
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 6, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [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

    External Data

    Dasty 3