ID   MTNA_GEOTN              Reviewed;         355 AA.
AC   A4ILL1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=GTNG_0837;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000305}.
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DR   EMBL; CP000557; ABO66215.1; -; Genomic_DNA.
DR   RefSeq; WP_011887032.1; NC_009328.1.
DR   AlphaFoldDB; A4ILL1; -.
DR   SMR; A4ILL1; -.
DR   STRING; 420246.GTNG_0837; -.
DR   EnsemblBacteria; ABO66215; ABO66215; GTNG_0837.
DR   KEGG; gtn:GTNG_0837; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_9; -.
DR   OMA; GDVIMTH; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001578; 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.
FT   CHAIN           1..355
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357186"
FT   ACT_SITE        239
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         50..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         249..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            159
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   355 AA;  38737 MW;  D0412FAF4DF8FBC6 CRC64;
     MSTFAIPRSV EWHETHVTIL NQQKLPSVTE YLDLHTLEDV HDAIVTLKVR GAPAIGITAA
     YGLALAASRY ETESVDEFQR RLKQDRDYLA SARPTAVNLF WALDRLVAAA KSAASVNEAK
     TTLVHEAIRI QIEDEDVCRR IGEHALSLFH RGDRIMTICN AGSIATARYG TALAPFYLAK
     EKGIELSVYA LETRPVLQGA RLTAWELMQA GVDVTLITDN MAAQTIKAKN INAIIVGADR
     IAQNGDTANK IGTFGLALLA QSFGIPFYVA APLSTIDLAT KTGADIPIEE RHPDEVTHLN
     GVRIAPEGVN VYNPAFDVTP NELITAIITE KGIVYGDYET ELPSLVAKEE HHETA