ID   MTNA_SULSY              Reviewed;         339 AA.
AC   B2V8N9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=SYO3AOP1_0676;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(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; CP001080; ACD66312.1; -; Genomic_DNA.
DR   RefSeq; WP_012459389.1; NC_010730.1.
DR   AlphaFoldDB; B2V8N9; -.
DR   SMR; B2V8N9; -.
DR   STRING; 436114.SYO3AOP1_0676; -.
DR   EnsemblBacteria; ACD66312; ACD66312; SYO3AOP1_0676.
DR   KEGG; sul:SYO3AOP1_0676; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_0; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
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..339
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357243"
FT   ACT_SITE        227
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         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         237..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            147
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   339 AA;  38147 MW;  5984760D1123ABEF CRC64;
     MRKLKDIKPL ELKDDVLYVI NQLKLPHELV WEKLETLADY EKAIKDMIVR GAPLIGIVGA
     YGFYTGIKEG IDYIQVYERL KQTRPTAVNL FWALDRMKSI YEKYGNDLNL LLKEAKRIEV
     EDYHANRSIG GYGEVLIPKK ANILTHCNTG ALATAGWGTA LGIIRSAFEN DKDITVYVDE
     TRPYLQGSRL TAWELLREGI PHYIITDSSA GFLMKKGMID VIVVGADRIT LNGDVANKIG
     TYSLSILAKH HNIPFYVAAP SSSLDFNLES GDEIPIEERN EDEVKNCHCC KVAPQQSHAL
     NYSFDITPAD NITAIITEKG IIEKPNKEKI LKFFGRKLS