ID   MTNA_GEMAT              Reviewed;         344 AA.
AC   C1A6J9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=GAU_0817;
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA   Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA   Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT   novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009153; BAH37859.1; -; Genomic_DNA.
DR   RefSeq; WP_012682306.1; NC_012489.1.
DR   AlphaFoldDB; C1A6J9; -.
DR   SMR; C1A6J9; -.
DR   STRING; 379066.GAU_0817; -.
DR   PRIDE; C1A6J9; -.
DR   EnsemblBacteria; BAH37859; BAH37859; GAU_0817.
DR   KEGG; gau:GAU_0817; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_0; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000002209; 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;
KW   Reference proteome.
FT   CHAIN           1..344
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_1000215897"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         55..57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         253..254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            163
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   344 AA;  35957 MW;  04DF9153AFF9FC61 CRC64;
     MPVPPLPLHV PAVGWSPDLR ALRILDQRLL PGAQEVRDLV QLEEIVEAIR TLAVRGAPAI
     GVAAAIGLVV ALEVDSGGQE TRARALLADY AARLQRARPT AVNLGWAIDR LVRTAHRTAV
     GSMLAALRAE AEAIRAEDVA MCEAIGQHGL AVVPDGARVL THCNAGALAT AGIGTALAPL
     YMAHARGRAL TVYADETRPL RQGARLTAWE LSRAGISVSV LPDGAAASLL SQGLVDLVIV
     GADRIAANGD VANKVGTYGV ALAAAAHHVP FYVAAPGSTI DPHTATGRDI VIEHRDADEL
     GELPPGVPAW NPAFDVTPRA LIRGYITDRG FVEPPFTLAD YAGR