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Q39054

- CNX1_ARATH

UniProt

Q39054 - CNX1_ARATH

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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

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

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

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 [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)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.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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