MTNA_MAIZE
ID MTNA_MAIZE Reviewed; 367 AA.
AC B6TZD1; B6TL88; B8A2A0; Q5XTZ5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Protein IRON DEFICIENCY INDUCIBLE 2;
DE Short=ZmIDI2;
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 Name=IDI2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root;
RA Holtgraewe D.L., Heuer S., Scheibe R.;
RT "Zea mays isopentenyl-diphosphate delta isomerase 2 mRNA.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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 -!- 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=ACL54299.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY738148; AAU86895.1; -; mRNA.
DR EMBL; EU965753; ACG37871.1; -; mRNA.
DR EMBL; EU970346; ACG42464.1; -; mRNA.
DR EMBL; BT055692; ACL54299.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001105275.1; NM_001111805.1.
DR AlphaFoldDB; B6TZD1; -.
DR SMR; B6TZD1; -.
DR STRING; 4577.GRMZM2G139533_P01; -.
DR PaxDb; B6TZD1; -.
DR PRIDE; B6TZD1; -.
DR EnsemblPlants; Zm00001eb168430_T001; Zm00001eb168430_P001; Zm00001eb168430.
DR GeneID; 542191; -.
DR Gramene; Zm00001eb168430_T001; Zm00001eb168430_P001; Zm00001eb168430.
DR KEGG; zma:542191; -.
DR eggNOG; KOG1468; Eukaryota.
DR HOGENOM; CLU_016218_1_3_1; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; B6TZD1; baseline and differential.
DR Genevisible; B6TZD1; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW Nucleus; Reference proteome.
FT CHAIN 1..367
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000401998"
FT ACT_SITE 250
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT CONFLICT 2..3
FT /note="AA -> VG (in Ref. 2; ACG37871)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="F -> V (in Ref. 1; AAU86895 and 2; ACG37871)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> A (in Ref. 1; AAU86895 and 2; ACG37871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 38622 MW; CD154B4515A3C79F CRC64;
MAASDALQSI VYSRGSLRLL DQRKLPLEME YIDVKSSADG WNAIRDMVVR GAPAIAIAAA
LALAVEVSDL DFIGTPEEAA SFVSKKLEYL VSSRPTAVNL SDAATKLQTL VSKAAETAKD
SKSIFQVYIE AAETMLVDDV ADNKAIGSHG AVFLQRQLAN SKKISVLTHC NTGSLATAGY
GTALGVIRAL HSGGVLEKAF CTETRPFNQG SRLTAFELVH EKIPATLIAD SAAAALMKQG
HVQAVIVGAD RIAANGDTAN KIGTYNLAIS AKHHSVQFYV SAPVTSIDLS LPSGDEIVIE
ERSPKELLNS EGGLGKQVAA SGISVWNPAF DVTPANLITA IITEKGVITK TDADGSFDIK
GFLLPAK
