MTNA_CERSK
ID MTNA_CERSK Reviewed; 364 AA.
AC B9KQ55;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=RSKD131_0702;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM00562.1; -; Genomic_DNA.
DR RefSeq; WP_012643899.1; NC_011963.1.
DR AlphaFoldDB; B9KQ55; -.
DR SMR; B9KQ55; -.
DR EnsemblBacteria; ACM00562; ACM00562; RSKD131_0702.
DR GeneID; 67446148; -.
DR KEGG; rsk:RSKD131_0702; -.
DR HOGENOM; CLU_016218_1_2_5; -.
DR OMA; RLWVDET; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000001597; Chromosome 1.
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..364
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_1000187368"
FT ACT_SITE 240
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 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 250..251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 364 AA; 39348 MW; DDA98E58C67C4612 CRC64;
MKINGTPFRS IWCEAGEVRI IDQRWLPHEL RIVPLRTRAE FAAAIRDMWV RGAPLIGATA
AWGMAVQMAE DPSDASLAET WQVLHETRPT AINLRWALNE MRRLLAPLPP SERAAAAARR
AAEICDEDVE INRRIGAHGL TLIREIAERK RGRVNILTHC NAGWLATVDW GTATSPIYHA
LEAGIDVHVF VDETRPRNQG ALLTAWEMNS HGVSHDLIVD NAGGHLMQHG EVDLVIVGTD
RTTAQGDVCN KIGTYLKALA AKANGVPFYV ALPSPTIDWT VRDGVAEIPI EERSSAEVTH
VQGKAPDGSV ISVQISPDGT GARNPAFDVT PASLVTGLIT ERGICAAEAG AMEALFPEAA
RSAA