CNX3_ARATH
ID CNX3_ARATH Reviewed; 270 AA.
AC Q39056; Q1ECR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase, mitochondrial;
DE EC=4.6.1.17 {ECO:0000250|UniProtKB:P0A738};
DE AltName: Full=Molybdenum cofactor biosynthesis enzyme CNX3;
DE AltName: Full=Molybdenum cofactor biosynthesis protein C;
DE AltName: Full=Molybdopterin biosynthesis protein CNX3;
DE Flags: Precursor;
GN Name=CNX3; OrderedLocusNames=At1g01290; ORFNames=F6F3.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7890743; DOI=10.1074/jbc.270.11.6100;
RA Hoff T., Schnorr K.M., Meyer C., Caboche M.;
RT "Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum
RT cofactor biosynthesis by functional complementation of Escherichia coli
RT mutants.";
RL J. Biol. Chem. 270:6100-6107(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20164445; DOI=10.1105/tpc.109.068478;
RA Teschner J., Lachmann N., Schulze J., Geisler M., Selbach K.,
RA Santamaria-Araujo J., Balk J., Mendel R.R., Bittner F.;
RT "A novel role for Arabidopsis mitochondrial ABC transporter ATM3 in
RT molybdenum cofactor biosynthesis.";
RL Plant Cell 22:468-480(2010).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000250|UniProtKB:P0A738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000250|UniProtKB:P0A738};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:20164445}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:20164445}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the roots.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000305}.
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DR EMBL; Z48046; CAA88106.1; -; mRNA.
DR EMBL; AC023628; AAF97327.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27266.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27267.1; -; Genomic_DNA.
DR EMBL; BT025641; ABF74702.1; -; mRNA.
DR PIR; T46961; T46961.
DR RefSeq; NP_001154299.1; NM_001160827.2.
DR RefSeq; NP_171636.1; NM_100011.4.
DR AlphaFoldDB; Q39056; -.
DR SMR; Q39056; -.
DR BioGRID; 24680; 1.
DR STRING; 3702.AT1G01290.1; -.
DR PaxDb; Q39056; -.
DR PRIDE; Q39056; -.
DR ProteomicsDB; 241247; -.
DR EnsemblPlants; AT1G01290.1; AT1G01290.1; AT1G01290.
DR EnsemblPlants; AT1G01290.2; AT1G01290.2; AT1G01290.
DR GeneID; 839445; -.
DR Gramene; AT1G01290.1; AT1G01290.1; AT1G01290.
DR Gramene; AT1G01290.2; AT1G01290.2; AT1G01290.
DR KEGG; ath:AT1G01290; -.
DR Araport; AT1G01290; -.
DR TAIR; locus:2035277; AT1G01290.
DR eggNOG; KOG2876; Eukaryota.
DR HOGENOM; CLU_074693_0_0_1; -.
DR InParanoid; Q39056; -.
DR OMA; EASCTGK; -.
DR OrthoDB; 1436523at2759; -.
DR PhylomeDB; Q39056; -.
DR BioCyc; ARA:AT1G01290-MON; -.
DR BioCyc; MetaCyc:AT1G01290-MON; -.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q39056; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39056; baseline and differential.
DR Genevisible; Q39056; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR Gene3D; 3.30.70.640; -; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; SSF55040; 1.
DR TIGRFAMs; TIGR00581; moaC; 1.
PE 1: Evidence at protein level;
KW Lyase; Mitochondrion; Molybdenum cofactor biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..270
FT /note="Cyclic pyranopterin monophosphate synthase,
FT mitochondrial"
FT /id="PRO_0000097868"
FT ACT_SITE 240
FT /evidence="ECO:0000255"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
SQ SEQUENCE 270 AA; 29513 MW; 16808C377900667E CRC64;
MISTLRRAVF LRRFPAVVSP IKRAFSSRID DEFDPQIMNI NELNQEMQSI FGQEPSPDGP
GTMDFSELKS SKIEPLRSKN IDFRQQIEYH KSTHSSKNDS QAIEQYAKVA SDMSKLTHVG
IAGEAQMVDV SSKDNSKRTA LACCKVILGK RVFDLVLANQ MGKGDVLGVA KIAGINGAKQ
TSSLIPLCHN IALTHVRVDL RLNPEDFSVD IEGEASCTGK TGVEMEAMTA VSVAGLTVYD
MCKAASKDIS ITDVRLERKT GGKSGSWSRL
