ID E1RJP7_METP4 Unreviewed; 346 AA.
AC E1RJP7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Mpet_0927 {ECO:0000313|EMBL:ADN35694.1};
OS Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS (Methanoplanus petrolearius).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN35694.1, ECO:0000313|Proteomes:UP000006565};
RN [1] {ECO:0000313|EMBL:ADN35694.1, ECO:0000313|Proteomes:UP000006565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC {ECO:0000313|Proteomes:UP000006565};
RX PubMed=21304750;
RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
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; CP002117; ADN35694.1; -; Genomic_DNA.
DR RefSeq; WP_013328872.1; NC_014507.1.
DR AlphaFoldDB; E1RJP7; -.
DR STRING; 679926.Mpet_0927; -.
DR GeneID; 9743387; -.
DR KEGG; mpi:Mpet_0927; -.
DR eggNOG; arCOG01123; Archaea.
DR HOGENOM; CLU_016218_1_2_2; -.
DR OrthoDB; 45195at2157; -.
DR Proteomes; UP000006565; 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:ADN35694.1};
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:ADN35694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006565}.
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 48..50
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 346 AA; 37790 MW; 1C937FB9DAA1A278 CRC64;
MEEKTVYWDH DSGSIIFIEQ TALPAEYRTV SCKSVERLAE AIRRLEVRGA PALGVAGAFG
VALAAKLHDD SNMDSFLRLV REDADYLNST RPTAVNLSWG INRTYESIKN AASPEEAAET
ALRVAEEIAA EDEMMCRKIG ETGAKFLPDE CTVLTHCNAG ALACYTWGTA LGVIRSAVEA
GKNVSVISCE TRPLNQGSRL TAWELSRDNI PVKTITDSSA AFLMKRGEID AVVVGADRIT
HDAVFNKIGT YMHAVCAKHH EIPFYVAAPT STFDATLSEK DVVVEQRDRN ELAKCGDRLL
MPDSVDAINY AFDSTPVELV TAIFTEKGAV RPPFSVDEIL QRKVGI
//
