ID   MTNA_METJA              Reviewed;         329 AA.
AC   Q57896;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=MJ0454;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98443.1; -; Genomic_DNA.
DR   PIR; F64356; F64356.
DR   RefSeq; WP_010869953.1; NC_000909.1.
DR   AlphaFoldDB; Q57896; -.
DR   SMR; Q57896; -.
DR   STRING; 243232.MJ_0454; -.
DR   PRIDE; Q57896; -.
DR   EnsemblBacteria; AAB98443; AAB98443; MJ_0454.
DR   GeneID; 1451315; -.
DR   KEGG; mja:MJ_0454; -.
DR   eggNOG; arCOG01123; Archaea.
DR   HOGENOM; CLU_016218_1_2_2; -.
DR   InParanoid; Q57896; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 54988at2157; -.
DR   PhylomeDB; Q57896; -.
DR   Proteomes; UP000000805; 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; 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..329
FT                   /note="Putative methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000156086"
FT   ACT_SITE        223
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         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         233..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            143
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   329 AA;  36803 MW;  3936298C574730C9 CRC64;
     MTKDLRPIIW DDDKKELILI DQRKLPNKLE YFICKTYEDV AYAIKDMVVR GAPAIGVSAA
     YGLALAEING DDIYKAYEVL KNTRPTAVNL FWALDRCLTA YKEGKSILDE AKKIHEEDIE
     TCKKIGMIGE KLIEDGDTIL THCNAGALAT SAYGTALSVI RFAFYNGKKI RVIADETRPR
     LQGAKLTAFE LNYEGIPVKV ITDNTAGFLM QKGEIDKIIV GADRILADGT VYNKIGTYSL
     AVLAKYHRIP FYVAAPLSTF DLRSSEEDVI IEERDEKEVA YIDGVRIVPE GVGCYNYAFD
     KTPPDLITAI ITEKGIVKPN RDEILKLFR