ID   MTNA_PARMW              Reviewed;         337 AA.
AC   Q7U4V1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=SYNW1962;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE08477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX569694; CAE08477.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7U4V1; -.
DR   SMR; Q7U4V1; -.
DR   STRING; 84588.SYNW1962; -.
DR   EnsemblBacteria; CAE08477; CAE08477; SYNW1962.
DR   KEGG; syw:SYNW1962; -.
DR   eggNOG; COG0182; Bacteria.
DR   HOGENOM; CLU_016218_1_2_3; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1290468at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001422; 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.
FT   CHAIN           1..337
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000357252"
FT   ACT_SITE        225
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         47..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   BINDING         235..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT   SITE            145
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   337 AA;  35488 MW;  9907DB4D3664226A CRC64;
     MTLPPSLRWT GDHLELLDQR RLPEEVSFLK LHQWRDVAEA IATMAVRGAP AIGVAAAWGV
     VLAAQANEDL DLAVSVLKSS RPTAVNLGWA LDRIKASPAA QEPVDPQGLA AVAAALEADD
     RARTQTLVDH GVGLLASGSR VLHHCHTGAI ATAGVGTALG VIAAGHARGV VRHAWLDETR
     PRLQGAALSA WELGCLGVPC TVIVDGASGL LMRRQEVDAV LVGCDRVAAN GDVANKVGTY
     NLALVARAHG IPFYVCAPGS SMDRSTSDGD AITIEERPQE EITQHRGQRL AAPGAAAWNP
     AFDITPAHLV TALITEFGVI RPPYRDALQA LPLDRQP