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Database: UniProt
Entry: A0A0A0M937_9GAMM
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ID   A0A0A0M937_9GAMM        Unreviewed;       350 AA.
AC   A0A0A0M937;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=N791_04195 {ECO:0000313|EMBL:KGO99543.1};
OS   Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO99543.1, ECO:0000313|Proteomes:UP000030003};
RN   [1] {ECO:0000313|EMBL:KGO99543.1, ECO:0000313|Proteomes:UP000030003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO99543.1,
RC   ECO:0000313|Proteomes:UP000030003};
RA   Wang Q., Wang G.;
RT   "Genomic analysis of Lysobacter defluvii.";
RL   Submitted (AUG-2013) 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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO99543.1}.
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DR   EMBL; AVBH01000011; KGO99543.1; -; Genomic_DNA.
DR   RefSeq; WP_027068762.1; NZ_AVBH01000011.1.
DR   AlphaFoldDB; A0A0A0M937; -.
DR   STRING; 1385515.GCA_000423325_00183; -.
DR   eggNOG; COG0182; Bacteria.
DR   OrthoDB; 9803436at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000030003; Unassembled WGS sequence.
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:UP000030003}.
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         55..57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         252..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   SITE            162
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   350 AA;  36987 MW;  E3AC77934CF8AA91 CRC64;
     MDDIDFDRYD RIRPIRWTGE ALELLDQRRL PFEVDYVRCL TSSEVAAAIH ALTVRGAPAI
     GIAAAWGVVL ASRAVEALDG GEAAVKLQPA IEELNAARPT AVNLGWALAR MRAALLTAGQ
     DWRAALEAQA HAIAADDLAA NRRMGALGAA LIEPGSNVLT HCNTGSLATA GFGTALGVIR
     AGVAQGRIGQ VYAGETRPWL QGARLTAWEL QQDGIAPTLV ADAAAAHLMR TGRVQWVVVG
     ADRICANGDT ANKIGTYQLA ISARHHGVRF MVAAPSSTVD MATPSGDAID IEERDPGELF
     GLGGVRTAAA DIRAWNPVFD VTPHGLIDAI VTERGVIERP DEEAMRVAFG
//
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