ID J7U4Y6_MORMO Unreviewed; 369 AA.
AC J7U4Y6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000256|HAMAP-Rule:MF_01678};
GN ORFNames=MU9_3120 {ECO:0000313|EMBL:AGG32164.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG32164.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG32164.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG32164.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01678}.
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
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DR EMBL; CP004345; AGG32164.1; -; Genomic_DNA.
DR RefSeq; WP_004237737.1; NC_020418.1.
DR AlphaFoldDB; J7U4Y6; -.
DR GeneID; 69677845; -.
DR KEGG; mmk:MU9_3120; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_6; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000011834; 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; translation initiation factor eif-2b, domain 1; 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 NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR00512; salvage_mtnA; 1.
DR PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43475:SF1; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Reference proteome {ECO:0000313|Proteomes:UP000011834}.
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 369 AA; 39940 MW; 567AD8563BBE4CA6 CRC64;
MKINGKHYRS VWPADNGIDV CIFDQTKLPF EVSIITLTTM EEAATSIKDM WVRGAPLIGA
VAAYGVALAM HRDSSDAALK NAYDVLVATR PTAINLKWAL DRICGALTPL PAAERGDAAY
RIAAEIADED AEICHRIGEH GLTIIRDIAA RKKPGEPVNI LTHCNAGWLA TVDWGTALSP
IYQAYDEGIN IHVWVDETRP RNQGGLTAFE LGSHGVPHTL IADNAGGHLM QHGEVDMCIV
GTDRTTARGD VCNKIGTYLK ALAAKANNVP FYVALPSPTL DFTVWDGVKE IPIEQRAGEE
QSHVFGITPE GTRSWVNTAP AGTRCGNYAF DVTPAEYVTG LITERGICDA SPAGLKGMFP
EMWPSEYEV
//
