ID   MTNA_PYRFU              Reviewed;         356 AA.
AC   Q8U178;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative 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=MTNA-like protein {ECO:0000255|HAMAP-Rule:MF_01678};
DE            Short=aMTNA {ECO:0000255|HAMAP-Rule:MF_01678};
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN   OrderedLocusNames=PF1349;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000305}.
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DR   EMBL; AE009950; AAL81473.1; -; Genomic_DNA.
DR   RefSeq; WP_011012495.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U178; -.
DR   SMR; Q8U178; -.
DR   STRING; 186497.PF1349; -.
DR   EnsemblBacteria; AAL81473; AAL81473; PF1349.
DR   GeneID; 41713152; -.
DR   KEGG; pfu:PF1349; -.
DR   PATRIC; fig|186497.12.peg.1412; -.
DR   eggNOG; arCOG01123; Archaea.
DR   HOGENOM; CLU_016218_1_2_2; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 54988at2157; -.
DR   PhylomeDB; Q8U178; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
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..356
FT                   /note="Putative methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000156089"
FT   ACT_SITE        247
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         57..59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         257..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            167
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   356 AA;  39657 MW;  AFF7FC773E5AD9CC CRC64;
     MEIKYRPEEL TKLPRSVEYR EGKVYMINQR LLPREFKVEE FTTVEAVAEA IKNMTVRGAP
     AIGAAAAFGL ALYAETSKAK TKDEFFDGFY RAYETLKNTR PTAVNLFWAL NRIKKLVEEH
     REDSLDEIKR LIVEEAQKIA DEDVEANLRM GHYGAEVLPE GNILTHCNAG SLATVHLGTV
     GAVVRVMHKE GTLKLLWLDE TRPVLQGARL SAWEYSYDGL NVKLIADNAA AFVMQQGKVD
     AIIVGADRIV ANGDFANKIG TYMLAVLAKE HGIPFFTVAP LSSIDMSLSS GKEIPIEERS
     PEEVLTCGGC RIAPDVPVYN PAFDVTPHKY LTGIITDRGV VWPPFKRNLK KLFETL