MTNA_MAGMM
ID MTNA_MAGMM Reviewed; 352 AA.
AC A0L909;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Mmc1_1944;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK44452.1; -; Genomic_DNA.
DR RefSeq; WP_011713596.1; NC_008576.1.
DR AlphaFoldDB; A0L909; -.
DR SMR; A0L909; -.
DR STRING; 156889.Mmc1_1944; -.
DR EnsemblBacteria; ABK44452; ABK44452; Mmc1_1944.
DR KEGG; mgm:Mmc1_1944; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_5; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000002586; 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..352
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000357202"
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 352 AA; 38030 MW; C94A917BD96671F0 CRC64;
MSIFDVAVWD EAEHCARMLD QRRLPNEVVN LYYRSAAEMA DGIRDMVVRG APAIGCACAY
GVAVEAKRLA KQGIPSHWPT AMAEGMATLR QSRPTAVNLT WALERMAPLL ETTPPHEVPQ
RLLQEAHAIR EEDIASCRAM GAHGAALLPT NSQRPTVIMT HCNAGALATA GYGTALGVIR
AAHTAQQGNL RVIANETRPY LQGARLTAWE LLQDHIDTTL ITDNMAGWLM ANGEVDAVVV
GSDRVAANGD VANKIGTYTL AVLARRHDIP FFVAAPLSTV DLRCPTGREI PIEERSANEV
THCMGIRSAA DGVKVRNPAF DVTPAELITA FICEKGVAKA PDQEKIAKLF QI