ID   MTNA_ANADF              Reviewed;         337 AA.
AC   A7HIG6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
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};
GN   OrderedLocusNames=Anae109_4334;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC       (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC       {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01678}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000305}.
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DR   EMBL; CP000769; ABS28512.1; -; Genomic_DNA.
DR   RefSeq; WP_012099157.1; NC_009675.1.
DR   AlphaFoldDB; A7HIG6; -.
DR   SMR; A7HIG6; -.
DR   STRING; 404589.Anae109_4334; -.
DR   EnsemblBacteria; ABS28512; ABS28512; Anae109_4334.
DR   KEGG; afw:Anae109_4334; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_7; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000006382; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..337
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357138"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         51..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         238..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            148
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   337 AA;  35693 MW;  FBFDAA39EA465C6B CRC64;
     MNPQPLRPVI YDEGRDVVRV LDQRRLPSEE VWLDLASCDE VVQAIKDLTV RGAPAIGVAA
     AYGLALESRR GAEPARLREA SERLVHARPT AVNLAWAVRR MSRRLGLGPA ALLEEAHAIR
     DEDEAACRRI GALGAALLPP RASVLTHCNA GALATAGYGT ALGVVRAAVE GGNPVTVFAD
     ETRPFLQGAR LTAWELKRDG IPVTLLTDNM AGWLMAQGEI ACVVVGADRI AANGDVANKI
     GTYALAVLAA YHHLPFYVAA PWSTVDLATP DGSAIPIEER GDEEVVTLAG QRIAPAGVPA
     RYPAFDVTPE PLVTAIITER GVVRRPFAPG LAALAAR