ID   MTNA_AQUAE              Reviewed;         456 AA.
AC   O67879;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Methylthioribose-1-phosphate isomerase;
DE            Short=M1Pi;
DE            Short=MTR-1-P isomerase;
DE            EC=5.3.1.23;
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase;
GN   Name=mtnA; OrderedLocusNames=aq_2114;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC       (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC       {ECO:0000250}.
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;
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.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07840.1; -; Genomic_DNA.
DR   PIR; C70481; C70481.
DR   RefSeq; NP_214448.1; NC_000918.1.
DR   AlphaFoldDB; O67879; -.
DR   SMR; O67879; -.
DR   STRING; 224324.aq_2114; -.
DR   EnsemblBacteria; AAC07840; AAC07840; aq_2114.
DR   KEGG; aae:aq_2114; -.
DR   eggNOG; COG0182; Bacteria.
DR   eggNOG; COG2050; Bacteria.
DR   HOGENOM; CLU_016218_1_2_0; -.
DR   InParanoid; O67879; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000000798; Chromosome.
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; IPR029069; HotDog_dom_sf.
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   InterPro; IPR006683; Thioestr_dom.
DR   Pfam; PF03061; 4HBT; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   SUPFAM; SSF54637; SSF54637; 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..456
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000156091"
FT   REGION          40..113
FT                   /note="Thioesterase"
FT   REGION          124..456
FT                   /note="MTR-1-P isomerase"
FT   ACT_SITE        350
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         360..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            270
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  50498 MW;  477F3F6B4BB6E96E CRC64;
     MDIRTHLGIN QELSGKPVKV AEGYAEVLLK TQESMKADDK GLVHGGFIFS AADYASMLAV
     NHPNVVLAGA NVKFLKPVKV GDEIICKARV SEDKGKKKKV LVECFKGEDK VFEGEFFTVF
     LIDMFWRGEK MEVKPFYWKG DKLLLLDQRK LPHQEVWLEL KTYEEVAKAI KEMAVRGAPA
     IGCTAAYGFV LGVKVQKEDP EKVYETLKNT RPTAYNLFWA LDRMMKALKE GKDIEEEAKE
     IEKEDYEANK RMGEIGSEIV PLNAKVLTHC NTGALATAGW GTALGVIRSA HYGGKNIFVW
     VDETRPYLQG ARLTAWELVK ESIPHKIITD STAGFLMKKG MVDLVIVGAD RITAKGDVAN
     KIGTYTLAVL CKEHNVPFYV AAPTSTIDSN IKSGEEIIIE ERSPEEVKVC GGCAIAPKES
     DALHLAFDIT PAELITGIIT EKGIFKPERI TEALKD