Q39055 (CNX2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic pyranopterin monophosphate synthase, mitochondrial
EC=4.1.99.18

Alternative name(s):
Molybdenum cofactor biosynthesis enzyme CNX2
Molybdopterin biosynthesis protein CNX2
Molybdopterin precursor Z synthase

Gene names

Name:	CNX2
Ordered Locus Names:	At2g31955
ORF Names:	F20M17.1, F22D22.30

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	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes, together with CNX3, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) By similarity.
Catalytic activity	GTP = cyclic pyranopterin monophosphate + diphosphate.
Cofactor	Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate By similarity.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homodimer. Ref.6
Subcellular location	Mitochondrion matrix Ref.6.
Tissue specificity	Expressed in all organs, with an abundant expression in the roots.
Sequence similarities	Belongs to the MoaA/NifB/PqqE family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	4Fe-4S GTP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding S-adenosyl-L-methionine
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from genetic interaction Ref.1. Source: TAIR
Cellular_component	chloroplast Inferred from sequence or structural similarity Ref.1. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity Ref.1. Source: TAIR molybdopterin synthase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q39055-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q39055-2)

The sequence of this isoform differs from the canonical sequence as follows:
     333-340: Missing.

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 390		Cyclic pyranopterin monophosphate synthase, mitochondrial		PRO_0000153032
Regions
	Region	322 – 324	3	GTP binding By similarity
	Compositional bias	33 – 40	8	Poly-Thr
Sites
	Metal binding	85	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	89	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	92	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	317	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Metal binding	320	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Metal binding	334	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Binding site	78	1	GTP By similarity
	Binding site	91	1	S-adenosyl-L-methionine By similarity
	Binding site	128	1	GTP By similarity
	Binding site	132	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	159	1	GTP By similarity
	Binding site	183	1	S-adenosyl-L-methionine By similarity
	Binding site	220	1	GTP By similarity
	Binding site	254	1	S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Natural variations
	Alternative sequence	333 – 340	8	Missing in isoform 2.		VSP_044629
Experimental info
	Sequence conflict	124	1	V → A in AAM64798. Ref.5
	Sequence conflict	163	1	I → M in AAM64798. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0E8C012F57D035BB	FASTA	390	43,413
	10 20 30 40 50 60 MRRCFSKITD CHLGFKNSNF LLVGSEVGSG SVTRTITTTT SERLFSSSYA AHQVDQIKDN 70 80 90 100 110 120 PVSDMLIDKF GRLHTYLRIS LTERCNLRCQ YCMPSEGVEL TPKPQLLSQS EIVRLAGLFV 130 140 150 160 170 180 SAGVNKIRLT GGEPTVRKDI EEICLQLSSL KGLKNLAITT NGITLAKKLP RLKECGLDSL 190 200 210 220 230 240 NISLDTLVPA KFEFLTRRKG HDRVMKSIDT AIELGYNPVK VNCVIMRGLN DDEICDFVEL 250 260 270 280 290 300 TRDKPINVRF IEFMPFDGNV WNVKKLVPYA EVMDKVVKRF PSIKRMQDHP TETAKNFTID 310 320 330 340 350 360 GHCGSVSFIT SMTEHFCAGC NRLRLLADGN FKVCLFGPSE VSLRDPLRSG ADDEALREII 370 380 390 GAAVKRKKAA HAGMLDIAKT ANRPMIHIGG
	Isoform 2 [UniParc]. Checksum: 2A7F35D67FFBFC6E	FASTA	382	42,580
	10 20 30 40 50 60 MRRCFSKITD CHLGFKNSNF LLVGSEVGSG SVTRTITTTT SERLFSSSYA AHQVDQIKDN 70 80 90 100 110 120 PVSDMLIDKF GRLHTYLRIS LTERCNLRCQ YCMPSEGVEL TPKPQLLSQS EIVRLAGLFV 130 140 150 160 170 180 SAGVNKIRLT GGEPTVRKDI EEICLQLSSL KGLKNLAITT NGITLAKKLP RLKECGLDSL 190 200 210 220 230 240 NISLDTLVPA KFEFLTRRKG HDRVMKSIDT AIELGYNPVK VNCVIMRGLN DDEICDFVEL 250 260 270 280 290 300 TRDKPINVRF IEFMPFDGNV WNVKKLVPYA EVMDKVVKRF PSIKRMQDHP TETAKNFTID 310 320 330 340 350 360 GHCGSVSFIT SMTEHFCAGC NRLRLLADGN FKVSLRDPLR SGADDEALRE IIGAAVKRKK 370 380 AAHAGMLDIA KTANRPMIHI GG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants." Hoff T., Schnorr K.M., Meyer C., Caboche M. J. Biol. Chem. 270:6100-6107(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in molybdenum cofactor biosynthesis." Teschner J., Lachmann N., Schulze J., Geisler M., Selbach K., Santamaria-Araujo J., Balk J., Mendel R.R., Bittner F. Plant Cell 22:468-480(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48047 mRNA. Translation: CAA88107.1. AC006223 Genomic DNA. Translation: AAM15155.1. AC006533 Genomic DNA. Translation: AAM15276.1. CP002685 Genomic DNA. Translation: AEC08608.1. CP002685 Genomic DNA. Translation: AEC08609.1. CP002685 Genomic DNA. Translation: AEC08610.1. AY065265 mRNA. Translation: AAL38741.1. AY096557 mRNA. Translation: AAM20207.1. AY087242 mRNA. Translation: AAM64798.1.
IPI	IPI00527022. IPI00992640.
PIR	B84727.
RefSeq	NP_001031461.1. NM_001036384.1. NP_001189652.1. NM_001202723.1. NP_850177.2. NM_179846.3.
UniGene	At.19645.
3D structure databases
ProteinModelPortal	Q39055.
SMR	Q39055. Positions 68-383.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q39055. 2 interactions.
STRING	3702.AT2G31955.2-P.
Proteomic databases
PaxDb	Q39055.
PRIDE	Q39055.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G31955.1; AT2G31955.1; AT2G31955. AT2G31955.2; AT2G31955.2; AT2G31955.
GeneID	817754.
KEGG	ath:AT2G31955.
Organism-specific databases
TAIR	At2g31955.
Phylogenomic databases
eggNOG	COG2896.
HOGENOM	HOG000228680.
InParanoid	Q39055.
KO	K03639.
OMA	HRKFYYL.
PhylomeDB	Q39055.
ProtClustDB	PLN02951.
Enzyme and pathway databases
BioCyc	ARA:AT2G31955-MONOMER. MetaCyc:AT2G31955-MONOMER.
UniPathway	UPA00344.
Gene expression databases
ArrayExpress	Q39055.
Genevestigator	Q39055.
GermOnline	AT2G31955. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR013483. MoaA. IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS. IPR010505. Mob_synth_C. IPR007197. rSAM. [Graphical view]
Pfam	PF06463. Mob_synth_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR02666. moaA. 1 hit.
PROSITE	PS01305. MOAA_NIFB_PQQE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CNX2_ARATH

Accession

Primary (citable) accession number: Q39055
Secondary accession number(s): F4IRV0, Q8LBF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program