ID   MTNA_KLEP3              Reviewed;         342 AA.
AC   B5XZW2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=KPK_3949;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000964; ACI10456.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XZW2; -.
DR   SMR; B5XZW2; -.
DR   EnsemblBacteria; ACI10456; ACI10456; KPK_3949.
DR   KEGG; kpe:KPK_3949; -.
DR   HOGENOM; CLU_016218_1_2_6; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   BioCyc; MetaCyc:MON-1341; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001734; 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..342
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_1000187361"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         49..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         238..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            148
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   342 AA;  36143 MW;  650C5F483AA8FB30 CRC64;
     MQTLQTTSLR VSENQLFILD QQALPQEKRW LAADNVALLV DHIHALRVRG APLIGLSASL
     LLALLAQRGL NRDALQQALE TLRAARPTAV NLMNNLDRMK QALAREDYPQ ALEAEALRLV
     EEDKQLCDRI AEAGSALVKP GSRLLTHCNT GGLATAGVGT ALGVIALAHR QGKVANVWVD
     ETRPLLQGGR LTAWELGELG VPYQLITDSM AASLMAQGQV DAVWVGADRI AANGDVANKI
     GTYSLAVLAH YHQIPFYVAA PQTTLDRYCP NGAAIPIEQR AAAEVTGVAG SFGAVQWAPM
     GAAVYNPAFD VTPAGLVSGW VLDSGVVTPA QVAAGAFAPD NG