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Q39054 (CNX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Molybdopterin biosynthesis protein CNX1
Alternative name(s):
Molybdenum cofactor biosynthesis enzyme CNX1

Including the following 2 domains:

  1. Molybdopterin molybdenumtransferase
    Short name=MPT Mo-transferase
    EC=2.10.1.1
    Alternative name(s):
    Domain E
  2. Molybdopterin adenylyltransferase
    Short name=MPT adenylyltransferase
    EC=2.7.7.75
    Alternative name(s):
    Domain G
Gene names
Name:CNX1
Ordered Locus Names:At5g20990
ORF Names:F22D1.6, T10F18.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.10 Ref.11

Catalytic activity

Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP. Ref.7 Ref.8

ATP + molybdopterin = diphosphate + adenylyl-molybdopterin. Ref.7 Ref.8

Cofactor

Magnesium. Ref.7 Ref.11

Enzyme regulation

Inhibited by copper and tungsten. Ref.11

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis.

Subunit structure

The G domain: homotrimer or homohexamer. The E domain: homodimer. Ref.5 Ref.9 Ref.10 Ref.11

Sequence similarities

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

In the C-terminal section; belongs to the MoeA family.

Biophysicochemical properties

Kinetic parameters:

KM=62 µM for ATP for domain G Ref.7 Ref.8

KM=133 µM for Zn2+ for domain E

KM=255 µM for Mg2+ for domain E

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 670670Molybdopterin biosynthesis protein CNX1
PRO_0000170963

Regions

Region19 – 439421MPT Mo-transferase
Region466 – 620155MPT adenylyltransferase
Region542 – 5432Substrate binding
Compositional bias8 – 125Poly-Gly

Sites

Binding site4851AMP
Binding site4861AMP; via amide nitrogen
Binding site5411AMP; via amide nitrogen
Binding site5731Substrate
Binding site6001AMP; via carbonyl oxygen
Binding site6001Substrate; via amide nitrogen
Binding site6071Substrate

Experimental info

Mutagenesis4751S → D: Reduced molybdopterin binding. Loss of adenylation activity. Ref.10
Mutagenesis4851D → S: Reduced molybdopterin binding. Loss of adenylation activity. Ref.10
Mutagenesis5151D → H or N: Almost normal molybdopterin binding. Loss adenylation activity. Ref.6 Ref.10
Mutagenesis5421T → A: Strongly reduced molybdopterin binding. Reduced activity. Ref.10
Mutagenesis5421T → D or N: Loss of molybdopterin binding. Loss of activity. Ref.10
Mutagenesis5421T → S: Reduced molybdopterin binding. No effect on activity. Ref.10
Mutagenesis5421T → V: Strongly reduced molybdopterin binding. No effect on activity. Ref.10
Mutagenesis5471R → E: No effect on molybdopterin binding. Clear reduction in adenylation activity. Ref.10
Mutagenesis5571V → G: Impaired folding. Loss of activity. Ref.6
Mutagenesis5731S → A: Loss of molybdopterin binding. Loss of activity. Ref.10
Mutagenesis5831S → A: No effect on activity.
Mutagenesis5971N → L: Loss of molybdopterin binding. Loss of activity. Ref.6
Sequence conflict1131D → V Ref.1
Sequence conflict1131D → V Ref.2
Sequence conflict1341S → A Ref.1
Sequence conflict1341S → A Ref.2
Sequence conflict6531S → L Ref.1
Sequence conflict6531S → L Ref.2

Secondary structure

............................. 670
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q39054 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 4405722BB9C5EF02

FASTA67071,279
        10         20         30         40         50         60 
MEGQGCCGGG GGKTEMIPTE EALRIVFGVS KRLPPVIVSL YEALGKVLAE DIRAPDPLPP 

        70         80         90        100        110        120 
YPASVKDGYA VVASDGPGEY PVITESRAGN DGLGVTVTPG TVAYVTTGGP IPDGADAVVQ 

       130        140        150        160        170        180 
VEDTKVIGDV STESKRVKIL IQTKKGTDIR RVGCDIEKDA TVLTTGERIG ASEIGLLATA 

       190        200        210        220        230        240 
GVTMVKVYPM PIVAILSTGD ELVEPTAGTL GRGQIRDSNR AMLVAAVMQQ QCKVVDLGIV 

       250        260        270        280        290        300 
RDDRKELEKV LDEAVSSGVD IILTSGGVSM GDRDFVKPLL EEKGKVYFSK VLMKPGKPLT 

       310        320        330        340        350        360 
FAEIRAKPTE SMLGKTVLAF GLPGNPVSCL VCFNIFVVPT IRQLAGWTSP HPLRVRLRLQ 

       370        380        390        400        410        420 
EPIKSDPIRP EFHRAIIKWK DNDGSGTPGF VAESTGHQMS SRLLSMRSAN ALLELPATGN 

       430        440        450        460        470        480 
VLSAGSSVSA IIVSDISAFS IDKKASLSEP GSIRKEKKYD EVPGPEYKVA ILTVSDTVSA 

       490        500        510        520        530        540 
GAGPDRSGPR AVSVVDSSSE KLGGAKVVAT AVVPDEVERI KDILQKWSDV DEMDLILTLG 

       550        560        570        580        590        600 
GTGFTPRDVT PEATKKVIER ETPGLLFVMM QESLKITPFA MLSRSAAGIR GSTLIINMPG 

       610        620        630        640        650        660 
NPNAVAECME ALLPALKHAL KQIKGDKREK HPKHIPHAEA TLPTDTWDQS YKSAYETGEK 

       670 
KEEAGCSCTH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_197599.1. NM_122108.3.
UniGeneAt.23035.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray1.45A462-628[»]
ProteinModelPortalQ39054.
SMRQ39054. Positions 20-416, 464-623.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17499. 2 interactions.
MINTMINT-8070811.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Proteomic databases

PaxDbQ39054.
PRIDEQ39054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G20990.1; AT5G20990.1; AT5G20990.
GeneID832224.
KEGGath:AT5G20990.

Organism-specific databases

TAIRAT5G20990.

Phylogenomic databases

eggNOGCOG0303.
HOGENOMHOG000280651.
InParanoidQ39054.
KOK15376.
OMAICDDDPE.
PhylomeDBQ39054.
ProtClustDBPLN02699.

Enzyme and pathway databases

UniPathwayUPA00344.

Gene expression databases

GenevestigatorQ39054.

Family and domain databases

Gene3D2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]
PfamPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsTIGR00177. molyb_syn. 2 hits.
PROSITEPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ39054.
PROQ39054.

Entry information

Entry nameCNX1_ARATH
AccessionPrimary (citable) accession number: Q39054
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 6, 2002
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names