MTNA_ECO45
ID MTNA_ECO45 Reviewed; 371 AA.
AC B7MMH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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, ECO:0000269|PubMed:31950558};
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, ECO:0000303|PubMed:31950558};
GN OrderedLocusNames=ECS88_4902;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 25922 / DSM 1103 / NCIB 12210 / ExPEC;
RX PubMed=31950558; DOI=10.1111/mmi.14459;
RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA Tabita F.R.;
RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT products that is widespread in bacteria, including pathogenic Escherichia
RT coli.";
RL Mol. Microbiol. 113:923-937(2020).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC (PubMed:31950558). Also catalyzes the interconversion of 5-deoxyribose
CC 1-phosphate and 5-deoxyribulose 1-phosphate (PubMed:31950558). Part of
CC a bifunctional DHAP-shunt salvage pathway for SAM by-products
CC (PubMed:31950558). {ECO:0000269|PubMed:31950558}.
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, ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19990;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-
CC phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749,
CC ChEBI:CHEBI:144504; Evidence={ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 5-methylthioribose-1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC KM=222 uM for 5-deoxyribose 1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC Note=kcat is 0.49 sec(-1) with 5-methylthioribose-1-phosphate as
CC substrate. kcat is 2.02 sec(-1) with 5-deoxyribose 1-phosphate as
CC substrate. kcat is 0.67 sec(-1) with ribose-1-phosphate as substrate.
CC {ECO:0000269|PubMed:31950558};
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 -!- DISRUPTION PHENOTYPE: Inactivation of the gene precludes growth of the
CC strain with 5-deoxyribose. {ECO:0000269|PubMed:31950558}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; CU928161; CAR06048.1; -; Genomic_DNA.
DR RefSeq; WP_001022014.1; NC_011742.1.
DR AlphaFoldDB; B7MMH6; -.
DR SMR; B7MMH6; -.
DR PRIDE; B7MMH6; -.
DR EnsemblBacteria; CAR06048; CAR06048; ECS88_4902.
DR KEGG; ecz:ECS88_4902; -.
DR HOGENOM; CLU_016218_1_2_6; -.
DR OMA; RLWVDET; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000000747; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Isomerase; Methionine biosynthesis.
FT CHAIN 1..371
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_1000187357"
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 203
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 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 371 AA; 40361 MW; 47F168302DEEFA6E CRC64;
MNIKGKHYRT VWVSGDGKAV EIIDQTKLPF KFEVVALTSA EMAATAIQDM WVRGAPLIGV
VAAYGIALGM NHDASDMGLQ RYYDLLIKTR PTAINLKWAL DRMIDTLKDL CVSERKDVAW
ALAAEIAEED VALCEQIGLH GAEVIREIAQ KKPAGSVVNI LTHCNAGWLA TVDWGTALSP
IYKAHENGIP VHVWVDETRP RNQGGLTAFE LGSHGIPHTL IADNAGGHLM QHGDVDLCIV
GTDRTTARGD VCNKIGTYLK ALAAHDNHVP FYVALPSPTI DWTIEDGKSI PIEQRDGKEQ
SHVYGINPQG ELSWVNTAPE GTRCGNYAFD VTPARYITGF ITERGVCAAS KSALADMFAD
LKSKALQGEQ H
