Q39054 (CNX1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	670 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Molybdenum Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW auxin mediated signaling pathway Inferred from mutant phenotype PubMed 15710899. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from direct assay Ref.5. Source: TAIR transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 670

670

Molybdopterin biosynthesis protein CNX1

PRO_0000170963

Regions

Region

19 – 439

421

MPT Mo-transferase

Region

466 – 620

155

MPT adenylyltransferase

Region

542 – 543

2

Substrate binding

Compositional bias

8 – 12

5

Poly-Gly

Sites

Binding site

485

1

AMP

Binding site

486

1

AMP; via amide nitrogen

Binding site

541

1

AMP; via amide nitrogen

Binding site

573

1

Substrate

Binding site

600

1

AMP; via carbonyl oxygen

Binding site

600

1

Substrate; via amide nitrogen

Binding site

607

1

Substrate

Experimental info

Mutagenesis

475

1

S → D: Reduced molybdopterin binding. Loss of adenylation activity. Ref.10

Mutagenesis

485

1

D → S: Reduced molybdopterin binding. Loss of adenylation activity. Ref.10

Mutagenesis

515

1

D → H or N: Almost normal molybdopterin binding. Loss adenylation activity. Ref.6 Ref.10

Mutagenesis

542

1

T → A: Strongly reduced molybdopterin binding. Reduced activity. Ref.10

Mutagenesis

542

1

T → D or N: Loss of molybdopterin binding. Loss of activity. Ref.10

Mutagenesis

542

1

T → S: Reduced molybdopterin binding. No effect on activity. Ref.10

Mutagenesis

542

1

T → V: Strongly reduced molybdopterin binding. No effect on activity. Ref.10

Mutagenesis

547

1

R → E: No effect on molybdopterin binding. Clear reduction in adenylation activity. Ref.10

Mutagenesis

557

1

V → G: Impaired folding. Loss of activity. Ref.6

Mutagenesis

573

1

S → A: Loss of molybdopterin binding. Loss of activity. Ref.10

Mutagenesis

583

1

S → A: No effect on activity.

Mutagenesis

597

1

N → L: Loss of molybdopterin binding. Loss of activity. Ref.6

Sequence conflict

113

1

D → V Ref.1

Sequence conflict

113

1

D → V Ref.2

Sequence conflict

134

1

S → A Ref.1

Sequence conflict

134

1

S → A Ref.2

Sequence conflict

653

1

S → L Ref.1

Sequence conflict

653

1

S → L Ref.2

Secondary structure

1

.

.

.

.

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.

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.

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.

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.

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.

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670

Helix Strand Turn

Details...

Beta strand

466 – 474

9

Helix

476 – 479

4

Helix

487 – 497

11

Turn

498 – 503

6

Beta strand

504 – 513

10

Helix

517 – 529

13

Beta strand

534 – 540

7

Beta strand

543 – 545

3

Helix

550 – 557

8

Beta strand

559 – 561

3

Helix

563 – 576

14

Helix

578 – 582

5

Beta strand

587 – 590

4

Beta strand

593 – 598

6

Helix

604 – 623

20

Sequences

	Sequence		Length	Mass (Da)
	Q39054 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: 4405722BB9C5EF02	FASTA	670	71,279
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

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.

IPI

IPI00530587.

RefSeq

NP_197599.1. NM_122108.3.

UniGene

At.23035.

3D structure databases

PDBe
RCSB PDB
PDBj

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	462-628	[»]

ProteinModelPortal

Q39054.

SMR

Q39054. Positions 20-416, 464-623.

ModBase

Search...

Proteomic databases

PaxDb

Q39054.

PRIDE

Q39054.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G20990.1; AT5G20990.1; AT5G20990.

GeneID

832224.

KEGG

ath:AT5G20990.

Organism-specific databases

TAIR

At5g20990.

Phylogenomic databases

eggNOG

COG0303.

HOGENOM

HOG000280651.

InParanoid

Q39054.

KO

K15376.

OMA

KDSHDVV.

PhylomeDB

Q39054.

ProtClustDB

PLN02699.

Enzyme and pathway databases

UniPathway

UPA00344.

Gene expression databases

ArrayExpress

Q39054.

Genevestigator

Q39054.

GermOnline

AT5G20990. Arabidopsis thaliana.

Family and domain databases

Gene3D

2.40.340.10. 1 hit.
3.40.980.10. 2 hits.

InterPro

IPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]

Pfam

PF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]

SMART

SM00852. MoCF_biosynth. 2 hits.
[Graphical view]

SUPFAM

SSF53218. MoCF_biosynth. 2 hits.
SSF63867. MoeA_C. 1 hit.
SSF63882. MoeA_N. 1 hit.

TIGRFAMs

TIGR00177. molyb_syn. 2 hits.

PROSITE

PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

Q39054.

Entry information

Entry name

CNX1_ARATH

Accession

Primary (citable) accession number: Q39054

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 6, 2002
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program