ID M4YU26_THEXX Unreviewed; 333 AA.
AC M4YU26;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=TALC_00247 {ECO:0000313|EMBL:AGI47261.1};
OS Thermoplasmatales archaeon (strain BRNA1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales.
OX NCBI_TaxID=1054217 {ECO:0000313|EMBL:AGI47261.1, ECO:0000313|Proteomes:UP000012076};
RN [1] {ECO:0000313|EMBL:AGI47261.1, ECO:0000313|Proteomes:UP000012076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRNA1 {ECO:0000313|EMBL:AGI47261.1,
RC ECO:0000313|Proteomes:UP000012076};
RA Denman S.E., Evans P., Bragg L., Padmanahba J., McKenzie M., Edwards D.,
RA Krzycki J., McSweeney C., Morrison M.;
RT "Thermoplasmatales-like gut symbionts are pyrrolysine dependent-
RT methanogens.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002916; AGI47261.1; -; Genomic_DNA.
DR AlphaFoldDB; M4YU26; -.
DR STRING; 1054217.TALC_00247; -.
DR KEGG; tar:TALC_00247; -.
DR PATRIC; fig|1054217.5.peg.238; -.
DR eggNOG; arCOG01123; Archaea.
DR HOGENOM; CLU_016218_1_2_2; -.
DR Proteomes; UP000012076; 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:AGI47261.1};
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:AGI47261.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012076}.
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 56..58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 149
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 333 AA; 36202 MW; 53A4C2B830AE139A CRC64;
MKARMENGET KDIKAVWFED GKCRMIDQRE LPLKLVIVDF DDYKAVAEAI RNMTTRGAPS
IGASAAYAMC LAAIQKADID EAAKHVKAAR PTAFDLFYAT DWMVKKLKAG ADPVEAADEY
ANITVDKCRR IGEFGGALIK DGMKLMTHCN AGALATVDVG TALAPMRNAH DAGKKFFVYA
SETRPRLQGM QLTAWELNQE GIDHAIIPDG SAAYYMSQGV DMIIVGADRI AANGDFANKI
GTYDKAIVAK KFGIPFYVAA PVSTFDFSTK TGKDIVIEQR SETEMTEVQG IRIAPVGSKA
LNPAFDVTTS DLVTGFITEK GIFKPSEIAE MKE
//
