ID W0I6L4_9EURY Unreviewed; 362 AA.
AC W0I6L4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Putative methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678};
DE AltName: Full=MTNA-like protein {ECO:0000256|HAMAP-Rule:MF_01678};
DE Short=aMTNA {ECO:0000256|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN ORFNames=TES1_0640 {ECO:0000313|EMBL:AHF80028.1};
OS Thermococcus paralvinellae.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF80028.1, ECO:0000313|Proteomes:UP000019027};
RN [1] {ECO:0000313|EMBL:AHF80028.1, ECO:0000313|Proteomes:UP000019027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES1 {ECO:0000313|EMBL:AHF80028.1,
RC ECO:0000313|Proteomes:UP000019027};
RX PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01678};
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
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DR EMBL; CP006965; AHF80028.1; -; Genomic_DNA.
DR RefSeq; WP_042680181.1; NZ_CP006965.1.
DR AlphaFoldDB; W0I6L4; -.
DR STRING; 582419.TES1_0640; -.
DR GeneID; 24906831; -.
DR KEGG; ths:TES1_0640; -.
DR HOGENOM; CLU_016218_1_2_2; -.
DR OrthoDB; 45195at2157; -.
DR Proteomes; UP000019027; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; translation initiation factor eif-2b, domain 1; 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 NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR00512; salvage_mtnA; 1.
DR PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43475:SF1; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Initiation factor {ECO:0000313|EMBL:AHF80028.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Protein biosynthesis {ECO:0000313|EMBL:AHF80028.1}.
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 362 AA; 40544 MW; ECFAF018D725BE6B CRC64;
MKLKYKPEEL TKLPRSVEYK DKKVYLIDQK LLPWEFKVIH LSTVEQVAKA IKTMQVRGAP
AIGAAAAFGL ALYAERSKAE TKDEFFDGFY RAYEILKNTR PTAVNLFWAL NRIKNLVEEH
REDSLDEIKR LIVEEAQRIA DEDVEANLRM GHIGAEILPE GNVLTHCNAG SLATVHLGTV
GAVLRVMHKE GKLNLLWVDE TRPVLQGARL SAWEYHYDGI PLKLIADNMA GFVMQQGKVD
AIIVGADRIV ANGDFANKIG TYTLAVLAKE HGIPFFTVAP LSTIDMSLKS GKEIPIEERS
REEVLTCGGC KIAPDVDVYN PAFDVTPHKY LTAIITDRGV VYPPFERNLK KLFEDLALED
KL
//
