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MTNA_TOBAC
ID   MTNA_TOBAC              Reviewed;         374 AA.
AC   Q948X8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 66.
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   Name=CIG2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=11471724; DOI=10.1271/bbb.65.1275;
RA   Kimura T., Nakano T., Taki N., Ishikawa M., Asami T., Yoshida S.;
RT   "Cytokinin-induced gene expression in cultured green cells of Nicotiana
RT   tabacum identified by fluorescent differential display.";
RL   Biosci. Biotechnol. Biochem. 65:1275-1283(2001).
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   -!- INDUCTION: By cytokinin (kinetin) in suspension cell culture.
CC       {ECO:0000269|PubMed:11471724}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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DR   EMBL; AB031321; BAB63262.1; -; mRNA.
DR   RefSeq; NP_001312120.1; NM_001325191.1.
DR   AlphaFoldDB; Q948X8; -.
DR   SMR; Q948X8; -.
DR   STRING; 4097.Q948X8; -.
DR   GeneID; 107774973; -.
DR   KEGG; nta:107774973; -.
DR   OMA; RLWVDET; -.
DR   PhylomeDB; Q948X8; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000084051; Unplaced.
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..374
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000401991"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            175
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   374 AA;  39570 MW;  155DD34ACBB68B17 CRC64;
     MANGNEGDKT LLSICYNRGS LQLLDQRKLP LETIYLDIQD TKDGWDAIKE MVVRGAPAIA
     IAAALSLAVE VSNLSSFDGT SDDASDFLSN KLDYLVSSRP TAVNLSDAAV KLKEVIKKAA
     TTAKDANSVF QAYIEAAEVM LEDDVTSNKA IGSYGASFLK EHLTDSQKIT ILTHCNTGSL
     ATAGYGTALG VIRALYTDGV LERAFCTETR PFNQGSRLTA FELVHENIPA TLIADSAAAA
     LMNAGRVKAV IVGADRVAAN GDTANKIGTY NLAVSAMHHG IPFYVAAPLT SIDLSLSSGQ
     EIVIEERSPK ELLHTRGGLG EQVAASGISV WNPAFDVTPA NLISGIITEK GVITKKGAET
     FDIAEFVRKT SGNL
 
 
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