ID V2YC75_9FIRM Unreviewed; 336 AA.
AC V2YC75;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ECO:0000313|EMBL:USF25532.1};
GN ORFNames=N510_000444 {ECO:0000313|EMBL:USF25532.1}, N510_02497
GN {ECO:0000313|EMBL:ESL13192.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL13192.1};
RN [1] {ECO:0000313|EMBL:ESL13192.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL13192.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF25532.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF25532.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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}.
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DR EMBL; AYJP01000013; ESL13192.1; -; Genomic_DNA.
DR EMBL; CP097573; USF25532.1; -; Genomic_DNA.
DR AlphaFoldDB; V2YC75; -.
DR STRING; 1378168.N510_02497; -.
DR PATRIC; fig|1378168.3.peg.2604; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_9; -.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000017395; 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:UP000017395}.
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 44..46
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 148
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 336 AA; 36174 MW; 36FF4DF1306B4FA1 CRC64;
MEAIRWENSA LYLLDQTRLP AEERWLRYTE YRAVARAIRS MVVRGAPAIG ITAAYAMVLA
AQENACKGDF PAAMSQAKAV LAASRPTAVN LFWTLDRMER CWQTAGPDLP RLEEEARTIH
REDIQMNEAM GKAGAELVPE GARILTHCNA GALATGGYGT ALGVIRAAHA QGKVSMVYAD
ETRPLLQGAR LTACELDKDQ IPVTLICDDM AGYLMSQGKV DLVVVGCDRM AANGDFANKI
GTYSLAVLAK HHGIPFYTAL PSSTIDLSIP DGSHIPVEQR DGQEVACFAG VQTGPLGVQT
WNPAFDVTPH GLLTAVITER GVLRPPFDLA EGQAEA
//
