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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
 
 
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