ID   MTNA_SYNY3              Reviewed;         351 AA.
AC   P74497;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Methylthioribose-1-phosphate isomerase;
DE            Short=MTR-1-P isomerase;
DE            Short=M1Pi;
DE            EC=5.3.1.23;
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase;
GN   Name=mtnA; OrderedLocusNames=slr1938;
OS   Synechocystis sp. (strain PCC 6803).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-
CC       phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate =
CC       S-methyl-5-thio-D-ribulose 1-phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from (S)-methyl-5-thio-alpha-D-
CC       ribose 1-phosphate: step 1/6.
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits
CC       family. MtnA subfamily.
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DR   EMBL; BA000022; BAA18601.1; -; Genomic_DNA.
DR   PIR; S76472; S76472.
DR   RefSeq; NP_441923.1; -.
DR   IntAct; P74497; 2.
DR   GeneID; 953317; -.
DR   GenomeReviews; BA000022_GR; slr1938.
DR   KEGG; syn:slr1938; -.
DR   NMPDR; fig|1148.1.peg.2024; -.
DR   HOGENOM; P74497; -.
DR   OMA; P74497; NAGWLAT.
DR   BioCyc; SSP1148:SLR1938-MON; -.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase...; IEA:HAMAP.
DR   GO; GO:0019284; P:methionine biosynthetic process from S-aden...; IEA:HAMAP.
DR   HAMAP; MF_01678; -; 1.
DR   InterPro; IPR000649; IF-2B_related.
DR   InterPro; IPR005251; IF-2BI_MTNA.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   PANTHER; PTHR10233; IF-2B_related; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
FT   CHAIN         1    351       Methylthioribose-1-phosphate isomerase.
FT                                /FTId=PRO_0000156093.
FT   REGION       53     55       Substrate binding (By similarity).
FT   REGION      256    257       Substrate binding (By similarity).
FT   ACT_SITE    246    246       Proton donor (By similarity).
FT   BINDING      96     96       Substrate (By similarity).
FT   BINDING     205    205       Substrate (By similarity).
FT   SITE        166    166       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   351 AA;  38282 MW;  8EF513650BE5A3C3 CRC64;
     MTQSTNFDDV YPVQWRDDQV ILIDQTRLPL EYKEVAIADY EAMGHAIKSM VVRGAPAIGV
     AAAYGMYLGA RRIQTTELRE FVVQLEFVAD QLRQTRPTAV NLFWAIDQML NVAYHSGENV
     EQIKANLLSQ AQQIQLDDLR TCQAIGAAGL EVLPREPHQL TILTHCNAGA LATAGYGTAI
     GVIRAAWSAG RLARVYADET RPRLQGAKLT VWECVQAGIP VTLITDNMAA HCMQQQRIDA
     VVVGADRIAR NGDIANKIGT YGLAVLAKMH AIPFFVAAPL STVDFALDDG SQIPIEERDP
     VEIYQPEGNR ITPEGAEFYN PAFDVTPASL ITAIITEQGA IAPEKLADLQ A
//