CNX2_ARATH
ID CNX2_ARATH Reviewed; 390 AA.
AC Q39055; F4IRV0; Q8LBF4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=GTP 3',8-cyclase, mitochondrial;
DE EC=4.1.99.22 {ECO:0000250|UniProtKB:P69848};
DE AltName: Full=Molybdenum cofactor biosynthesis enzyme CNX2;
DE AltName: Full=Molybdopterin biosynthesis protein CNX2;
DE AltName: Full=Molybdopterin precursor Z synthase;
DE Flags: Precursor;
GN Name=CNX2; OrderedLocusNames=At2g31955; ORFNames=F20M17.1, F22D22.30;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-45.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate. {ECO:0000250|UniProtKB:P69848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:131766; EC=4.1.99.22;
CC Evidence={ECO:0000250|UniProtKB:P69848};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P69848};
CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1
CC [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived
CC substrate. {ECO:0000250|UniProtKB:P69848};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20164445}.
CC -!- INTERACTION:
CC Q39055; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-4446408, EBI-963665;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:20164445, ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q39055-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q39055-2; Sequence=VSP_044629;
CC -!- TISSUE SPECIFICITY: Expressed in all organs, with an abundant
CC expression in the roots.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC {ECO:0000305}.
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DR EMBL; Z48047; CAA88107.1; -; mRNA.
DR EMBL; AC006223; AAM15155.1; -; Genomic_DNA.
DR EMBL; AC006533; AAM15276.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08608.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08609.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08610.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62583.1; -; Genomic_DNA.
DR EMBL; AY065265; AAL38741.1; -; mRNA.
DR EMBL; AY096557; AAM20207.1; -; mRNA.
DR EMBL; AY087242; AAM64798.1; -; mRNA.
DR PIR; B84727; B84727.
DR RefSeq; NP_001031461.1; NM_001036384.2. [Q39055-1]
DR RefSeq; NP_001189652.1; NM_001202723.1. [Q39055-2]
DR RefSeq; NP_001324731.1; NM_001336358.1. [Q39055-1]
DR RefSeq; NP_850177.2; NM_179846.4. [Q39055-1]
DR AlphaFoldDB; Q39055; -.
DR SMR; Q39055; -.
DR BioGRID; 3101; 3.
DR IntAct; Q39055; 3.
DR STRING; 3702.AT2G31955.2; -.
DR SwissPalm; Q39055; -.
DR PaxDb; Q39055; -.
DR PRIDE; Q39055; -.
DR ProteomicsDB; 220397; -. [Q39055-1]
DR EnsemblPlants; AT2G31955.1; AT2G31955.1; AT2G31955. [Q39055-1]
DR EnsemblPlants; AT2G31955.2; AT2G31955.2; AT2G31955. [Q39055-1]
DR EnsemblPlants; AT2G31955.3; AT2G31955.3; AT2G31955. [Q39055-2]
DR EnsemblPlants; AT2G31955.5; AT2G31955.5; AT2G31955. [Q39055-1]
DR GeneID; 817754; -.
DR Gramene; AT2G31955.1; AT2G31955.1; AT2G31955. [Q39055-1]
DR Gramene; AT2G31955.2; AT2G31955.2; AT2G31955. [Q39055-1]
DR Gramene; AT2G31955.3; AT2G31955.3; AT2G31955. [Q39055-2]
DR Gramene; AT2G31955.5; AT2G31955.5; AT2G31955. [Q39055-1]
DR KEGG; ath:AT2G31955; -.
DR Araport; AT2G31955; -.
DR TAIR; locus:2827337; AT2G31955.
DR eggNOG; KOG2876; Eukaryota.
DR HOGENOM; CLU_009273_0_0_1; -.
DR InParanoid; Q39055; -.
DR OMA; IEFMPIG; -.
DR PhylomeDB; Q39055; -.
DR BioCyc; ARA:AT2G31955-MON; -.
DR BioCyc; MetaCyc:AT2G31955-MON; -.
DR BRENDA; 4.1.99.22; 399.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q39055; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q39055; baseline and differential.
DR Genevisible; Q39055; 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:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01225_B; MoaA_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; Mob_synth_C.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR02666; moaA; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Alternative splicing; GTP-binding; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Mitochondrion; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Reference proteome; S-adenosyl-L-methionine;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 46..390
FT /note="GTP 3',8-cyclase, mitochondrial"
FT /id="PRO_0000153032"
FT DOMAIN 69..290
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT BINDING 322..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 333..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044629"
FT CONFLICT 124
FT /note="V -> A (in Ref. 5; AAM64798)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> M (in Ref. 5; AAM64798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43413 MW; 0E8C012F57D035BB CRC64;
MRRCFSKITD CHLGFKNSNF LLVGSEVGSG SVTRTITTTT SERLFSSSYA AHQVDQIKDN
PVSDMLIDKF GRLHTYLRIS LTERCNLRCQ YCMPSEGVEL TPKPQLLSQS EIVRLAGLFV
SAGVNKIRLT GGEPTVRKDI EEICLQLSSL KGLKNLAITT NGITLAKKLP RLKECGLDSL
NISLDTLVPA KFEFLTRRKG HDRVMKSIDT AIELGYNPVK VNCVIMRGLN DDEICDFVEL
TRDKPINVRF IEFMPFDGNV WNVKKLVPYA EVMDKVVKRF PSIKRMQDHP TETAKNFTID
GHCGSVSFIT SMTEHFCAGC NRLRLLADGN FKVCLFGPSE VSLRDPLRSG ADDEALREII
GAAVKRKKAA HAGMLDIAKT ANRPMIHIGG