MTNA_THEAB
ID MTNA_THEAB Reviewed; 346 AA.
AC B7IFW5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000255|HAMAP-Rule:MF_01678}; OrderedLocusNames=THA_488;
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(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_01678}.
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_01678};
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_01678}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; CP001185; ACJ74979.1; -; Genomic_DNA.
DR RefSeq; WP_012579614.1; NC_011653.1.
DR AlphaFoldDB; B7IFW5; -.
DR SMR; B7IFW5; -.
DR STRING; 484019.THA_488; -.
DR PRIDE; B7IFW5; -.
DR EnsemblBacteria; ACJ74979; ACJ74979; THA_488.
DR KEGG; taf:THA_488; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_0; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000002453; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_1000187369"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 48..50
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 247..248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 346 AA; 38047 MW; 6D3FAE1BB046FD85 CRC64;
MKLKTMTMEW TGDELILIDQ RKIPLVEEYV SCKSYKEVAV AIKDMVVRGA PAIGASAAFG
YVLGAREMFV EDFNAFVKKM EEVKEVLANT RPTAVNLFWA LNRMEDSLKK YGKIEGILEY
LEEEAMNIAK EDIEVNKAIG RYGAELLKDG DTVLTHCNAG ALATVDYGTA LGVIRAAVEQ
GKKIKVFADE TRPYLQGARL TAWELMKDGI DVTLISDNMS GWSMKLGKIN AVIVGADRVA
ANGDVANKIG TYMVAVLAKR HGIPFYVAAP TSTIDLNTKT GKDIPIEERK HTEVTHCGGK
QIAPDGVKVF NPAFDVTDAE LVTAIITEKG VVYPPYEENL KKLFEE