MTNA_OLEA2
ID MTNA_OLEA2 Reviewed; 355 AA.
AC Q317L9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Dde_0076;
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB36877.1; -; Genomic_DNA.
DR RefSeq; WP_011366261.1; NC_007519.1.
DR AlphaFoldDB; Q317L9; -.
DR SMR; Q317L9; -.
DR STRING; 207559.Dde_0076; -.
DR EnsemblBacteria; ABB36877; ABB36877; Dde_0076.
DR KEGG; dde:Dde_0076; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_7; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000002710; 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..355
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000357178"
FT ACT_SITE 240
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 91
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 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 355 AA; 38380 MW; 7F004AB825087C51 CRC64;
METHIRYSRQ DRTLILLDQR VLPTVEEDFY CNDVADTIYA LQTMVVRGAP AIGVTAAYGC
CLAAYEAGHP APHAQWQKEL DTLLEKLAQA RPTAVNLRWA VERMRSVWKS MGDPDLNTLI
ARWLDEAEAI HEEDKSINRA IGRHGATLIQ DNDCIMTHCN AGALATAGYG TALGVVRGAV
DAGRTGITVI ANETRPFLQG ARLTAYELHK DGIPVTVACD NACGLLMQRG MVQKVVVGAD
RIAANGDAAN KIGTYSVALL AREHGIPFYV AAPLSTIDRA TPSGKQIPIE ERPAEEVTHV
GETRITPEGV PVYNYAFDVT PAHLIAGIVT EQGVLRPPYT ASIARAFAAA DKDRS