ID   MTNA_XANOP              Reviewed;         354 AA.
AC   B2SIW1;
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}; OrderedLocusNames=PXO_00735;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(2008).
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; CP000967; ACD58756.1; -; Genomic_DNA.
DR   RefSeq; WP_011259069.1; NC_010717.2.
DR   AlphaFoldDB; B2SIW1; -.
DR   SMR; B2SIW1; -.
DR   STRING; 360094.PXO_00735; -.
DR   EnsemblBacteria; ACD58756; ACD58756; PXO_00735.
DR   KEGG; xop:PXO_00735; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_6; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001740; 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.
FT   CHAIN           1..354
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357274"
FT   ACT_SITE        245
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         58..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         255..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            165
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   354 AA;  37271 MW;  FD46B64381CBFE33 CRC64;
     MNDSAHIDYA RYDHIRPLLW TGDALELLDQ RKLPFVVEHV RCDTSDAVAE AIHSLAVRGA
     PAIGIAAGWG VALAARDIAA DDGNAALQKL EPALLRLNAA RPTAVNLAWA LMRMRRVLGA
     AGADWRAVIA REAQAIADED LAANRHMGAL GAALIAPGSG VLTHCNTGSL ATAGFGTALG
     VIRAGMAQQR IAKVFAGETR PWLQGARLTV WELQQDGIDA TLIADSAASH LMKSGLVQWV
     IVGADRICAN GDTANKIGTY QLAIAARHHG VKFMVVAPSS TVDMATASGD QIEIEQRDPG
     ELFGVGGVRT VADGIHAWNP VFDVTPGDLI DAIVTERGVI AQPDQARMQA AFGN