ID   MTNA_NOSP7              Reviewed;         353 AA.
AC   B2J5P6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=Npun_F5471;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) 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: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; CP001037; ACC83778.1; -; Genomic_DNA.
DR   RefSeq; WP_012411724.1; NC_010628.1.
DR   AlphaFoldDB; B2J5P6; -.
DR   SMR; B2J5P6; -.
DR   STRING; 63737.Npun_F5471; -.
DR   EnsemblBacteria; ACC83778; ACC83778; Npun_F5471.
DR   KEGG; npu:Npun_F5471; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_3; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   PhylomeDB; B2J5P6; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001191; 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..353
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357212"
FT   ACT_SITE        244
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         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            164
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   353 AA;  38206 MW;  7A41F26C56794ABD CRC64;
     MTLSTNHVYP VIWHNGAVSL IDQTRLPNEY TFVEIHRSED MARAIKTMIV RGAPAIGVAA
     AYGMYLGARE IETSDRHEFL QNLDKVAQLL GSTRPTAVNL FWAISRMMKV AKETLGTVED
     IKQTLFQTAQ AINVEDLQTC QAIGDNGLTV LPASPEKLTL LTHCNAGALA TAGYGTALGV
     VRSAWREGRL ERLFADETRP RLQGAKLTAW ECVQEGIPVT LITDNMAAHC MKQGLIHAVV
     VGADRIAANG DTANKIGTYS VAIAAKAHNI PFFVAAPLST VDFELADGSK IPIEERDPTE
     IYQVGDTILT PEGVDFYNPA FDVTPAELIT AIITENGAIA PGELVKLQLK QLV