MTNA_RHORT
ID MTNA_RHORT Reviewed; 390 AA.
AC Q2RXI0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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, ECO:0000303|PubMed:23042035};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678, ECO:0000269|PubMed:23042035, ECO:0000269|PubMed:31950558};
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, ECO:0000303|PubMed:31950558};
GN OrderedLocusNames=Rru_A0360 {ECO:0000312|EMBL:ABC21165.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=23042035; DOI=10.1038/nchembio.1087;
RA Erb T.J., Evans B.S., Cho K., Warlick B.P., Sriram J., Wood B.M.,
RA Imker H.J., Sweedler J.V., Tabita F.R., Gerlt J.A.;
RT "A RubisCO-like protein links SAM metabolism with isoprenoid
RT biosynthesis.";
RL Nat. Chem. Biol. 8:926-932(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31950558; DOI=10.1111/mmi.14459;
RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA Tabita F.R.;
RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT products that is widespread in bacteria, including pathogenic Escherichia
RT coli.";
RL Mol. Microbiol. 113:923-937(2020).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC (PubMed:23042035, PubMed:31950558). Also catalyzes the interconversion
CC of 5-deoxyribose 1-phosphate and 5-deoxyribulose 1-phosphate
CC (PubMed:31950558, PubMed:23042035). Part of a bifunctional DHAP-shunt
CC salvage pathway for SAM by-products (PubMed:31950558).
CC {ECO:0000269|PubMed:23042035, ECO:0000269|PubMed:31950558}.
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, ECO:0000269|PubMed:23042035,
CC ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19990;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-alpha-D-ribose 1-phosphate = 5-deoxy-D-ribulose 1-
CC phosphate; Xref=Rhea:RHEA:61296, ChEBI:CHEBI:58749,
CC ChEBI:CHEBI:144504; Evidence={ECO:0000269|PubMed:23042035,
CC ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61297;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=134 uM for methylthioribose-1-phosphate
CC {ECO:0000269|PubMed:23042035};
CC KM=171 uM for deoxyribose-1-phosphate {ECO:0000269|PubMed:23042035};
CC Note=kcat is 0.1 sec(-1) with methylthioribose-1-phosphate as
CC substrate. kcat is 0.18 sec(-1) with deoxyribose-1-phosphate as
CC substrate (PubMed:23042035). kcat is 0.03 sec(-1) with ribose-1-
CC phosphate as substrate (PubMed:31950558).
CC {ECO:0000269|PubMed:23042035, ECO:0000269|PubMed:31950558};
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 -!- DISRUPTION PHENOTYPE: Mutant cannot release methanethiol upon 5'-
CC methylthioadenosine (MTA) feeding (PubMed:23042035). Deletion mutant
CC accumulates both S-methyl-5'-thioadenosine and 5'-deoxyadenosine
CC extracellularly (PubMed:31950558). {ECO:0000269|PubMed:23042035,
CC ECO:0000269|PubMed:31950558}.
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_01678}.
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DR EMBL; CP000230; ABC21165.1; -; Genomic_DNA.
DR RefSeq; WP_011388113.1; NC_007643.1.
DR RefSeq; YP_425452.1; NC_007643.1.
DR AlphaFoldDB; Q2RXI0; -.
DR SMR; Q2RXI0; -.
DR STRING; 269796.Rru_A0360; -.
DR EnsemblBacteria; ABC21165; ABC21165; Rru_A0360.
DR KEGG; rru:Rru_A0360; -.
DR PATRIC; fig|269796.9.peg.416; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_5; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR PhylomeDB; Q2RXI0; -.
DR BioCyc; MetaCyc:MON-17870; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000001929; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..390
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000445437"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 258..259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 390 AA; 40656 MW; FAC7D0B6F8B90750 CRC64;
MNVKGTPTRT IWPAREGGAV WIIDQTRLPH EFVTQRLNDL GAVAHAIRAM LVRGAPLIGA
TAAYGVALGM AEDPSDEGLT RACQTLLATR PTAVNLRWAI EAMAESLAAV PPDQRAQAAW
AKAGAICDED VALNEAIGDH GLGIIKDLAR TKGVEKGGEG PINILTHCNA GWLATVDWGT
ALAPLYKAHD AGLPIHVWVD ETRPRNQGAS LTAWELNSHG VPHTVIADNT GGHLMQHGLV
DMVIVGTDRT TATGDVCNKI GTYLKALAAF DNAVPFYVAL PGPTIDWTVN DGLREIPIEQ
RDAAEVTRVW GRTAAGALEW VTITPTGSPA ANYAFDVTPA RLITGLITER GVCAASAAGL
AGLYPERAPA PVPAGSAAGK GAAATADGAL
