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Database: UniProt
Entry: A0A1Y3XML6_9FIRM
LinkDB: A0A1Y3XML6_9FIRM
Original site: A0A1Y3XML6_9FIRM 
ID   A0A1Y3XML6_9FIRM        Unreviewed;       329 AA.
AC   A0A1Y3XML6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=B5G06_00085 {ECO:0000313|EMBL:OUN86411.1};
OS   Flavonifractor sp. An52.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Flavonifractor.
OX   NCBI_TaxID=1965642 {ECO:0000313|EMBL:OUN86411.1, ECO:0000313|Proteomes:UP000195424};
RN   [1] {ECO:0000313|Proteomes:UP000195424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An52 {ECO:0000313|Proteomes:UP000195424};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN86411.1}.
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DR   EMBL; NFIB01000001; OUN86411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3XML6; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000195424; 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:UP000195424}.
FT   ACT_SITE        221
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         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         231..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   SITE            141
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   329 AA;  35263 MW;  37AABFC1443450B0 CRC64;
     MDAIRWEGNT LYLLDQTKLP VEETWLPYTD YRPVANAIRT MVVRGAPAIG VTAAYAYCLA
     ALAGEDLAEA KAVLAASRPT AVNLFWALDR MARKAEACGG DPETLIAEAI AIHQEDVAMC
     KAMGLYGASV VPDHAHILTH CNAGALATGG YGTALGVIRA AHEQGKVDMV YADETRPLLQ
     GARLTAYELV TDHIPATLIA DNMAASLMAK GKIDMVVVGC DRMAANGDFA NKIGTYSVAV
     NAHHHGVPFY VALPCSTIDL TIPDGDRIPI EERDKNEVRT LYGVQTAPAT VEVYNPAFDV
     TPHSLVTGII TEKGVIYPPF KENLQKLFG
//
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