MTNA_ARATH
ID MTNA_ARATH Reviewed; 374 AA.
AC Q9ZUG4; Q8L5B9; Q8LAU5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000255|HAMAP-Rule:MF_03119};
GN OrderedLocusNames=At2g05830; ORFNames=T6P5.3;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-374 (ISOFORM 1).
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03119};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZUG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZUG4-2; Sequence=VSP_040227;
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20446.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005970; AAC95160.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05975.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05976.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05977.1; -; Genomic_DNA.
DR EMBL; BX820068; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY087601; AAM65143.1; -; mRNA.
DR EMBL; AY099595; AAM20446.1; ALT_INIT; mRNA.
DR EMBL; AY128839; AAM91239.1; -; mRNA.
DR PIR; H84471; H84471.
DR RefSeq; NP_001031339.1; NM_001036262.1. [Q9ZUG4-2]
DR RefSeq; NP_027726.1; NM_126596.4. [Q9ZUG4-1]
DR RefSeq; NP_973428.1; NM_201699.2. [Q9ZUG4-2]
DR AlphaFoldDB; Q9ZUG4; -.
DR SMR; Q9ZUG4; -.
DR BioGRID; 533; 17.
DR IntAct; Q9ZUG4; 7.
DR STRING; 3702.AT2G05830.1; -.
DR iPTMnet; Q9ZUG4; -.
DR PaxDb; Q9ZUG4; -.
DR PRIDE; Q9ZUG4; -.
DR ProteomicsDB; 250968; -. [Q9ZUG4-1]
DR DNASU; 815134; -.
DR EnsemblPlants; AT2G05830.1; AT2G05830.1; AT2G05830. [Q9ZUG4-1]
DR EnsemblPlants; AT2G05830.2; AT2G05830.2; AT2G05830. [Q9ZUG4-2]
DR EnsemblPlants; AT2G05830.3; AT2G05830.3; AT2G05830. [Q9ZUG4-2]
DR GeneID; 815134; -.
DR Gramene; AT2G05830.1; AT2G05830.1; AT2G05830. [Q9ZUG4-1]
DR Gramene; AT2G05830.2; AT2G05830.2; AT2G05830. [Q9ZUG4-2]
DR Gramene; AT2G05830.3; AT2G05830.3; AT2G05830. [Q9ZUG4-2]
DR KEGG; ath:AT2G05830; -.
DR Araport; AT2G05830; -.
DR TAIR; locus:2064717; AT2G05830.
DR eggNOG; KOG1468; Eukaryota.
DR InParanoid; Q9ZUG4; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; Q9ZUG4; -.
DR BioCyc; ARA:AT2G05830-MON; -.
DR UniPathway; UPA00904; UER00874.
DR PRO; PR:Q9ZUG4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUG4; baseline and differential.
DR Genevisible; Q9ZUG4; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Amino-acid biosynthesis; Cytoplasm;
KW Isomerase; Methionine biosynthesis; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..374
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000401989"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 173
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040227"
FT CONFLICT 61
FT /note="A -> T (in Ref. 4; AAM65143)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="K -> R (in Ref. 3; BX820068)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="M -> L (in Ref. 4; AAM65143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 39612 MW; A3987D0DA8D27E37 CRC64;
MSGEGDTTLK AICYKPGSLQ LLDQRKLPLE TIYLEIRDAS DGWSAIQEMV VRGAPAIAIA
AALSLAVEVF NFHGFDGSAS DAVAFLENKL DYLVSSRPTA VNLADAALKL KHVIAKALAT
ATEAKSIFKA YIEASEDMLE DDVVSNKAIG NFGLSLLRQQ AKNPDKLSVL THCNTGSLAT
AGYGTALGVI RALHTQGILE RAYCTETRPF NQGSRLTAFE LVHEKIPATL IADSAAAALM
KDGRVDGVIV GADRVASNGD TANKIGTYSL ALCAKHHGIP FYVAAPLTSV DLSLSSGKEI
VIEERSPKEL MHTHGGLGER IAAPGISVWN PAFDMTPAEL IAGIITEKGV ITKNGNDTFD
ISSFAKKITG NSSR
