ID I3KML1_ORENI Unreviewed; 353 AA.
AC I3KML1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000256|HAMAP-Rule:MF_03119};
GN Name=mri1 {ECO:0000313|Ensembl:ENSONIP00000022356.1};
GN Synonyms=MRI1 {ECO:0000256|HAMAP-Rule:MF_03119};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000022356.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000022356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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_03119}.
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_03119};
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:0000256|HAMAP-Rule:MF_03119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_03119}.
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DR RefSeq; XP_003455807.1; XM_003455759.3.
DR AlphaFoldDB; I3KML1; -.
DR STRING; 8128.ENSONIP00000022356; -.
DR Ensembl; ENSONIT00000022376.2; ENSONIP00000022356.1; ENSONIG00000017732.2.
DR GeneID; 100708933; -.
DR KEGG; onl:100708933; -.
DR CTD; 84245; -.
DR eggNOG; KOG1468; Eukaryota.
DR GeneTree; ENSGT00390000013732; -.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; I3KML1; -.
DR OMA; TDNMAGY; -.
DR OrthoDB; 4853at2759; -.
DR TreeFam; TF300852; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000005207; Linkage group LG6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03119}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03119};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03119}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03119};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
FT SITE 161
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
SQ SEQUENCE 353 AA; 37949 MW; 68C3A81042FE03AF CRC64;
MTLEAIRYRT GSLQILNQLL LPHQTVYDDI RSVQDAYEAI KSMKVRGAPA IAIVGCLSLA
VELRAGAGGD DPVTFIRESL CHLTSARPTA VNMGRAAREL MEFAENESME KNSEQLRESV
IAWIEDMLER DVNDNRKIGN YGAQHILSGV PRDSVTILTH CNTGSLATAG YGTALGVVRS
LHALGRLKRV YCTETRPYNQ GSRLTAYEAV AEGIPATLIT DSMAALTMRE MDITAVVVGA
DRVVANGDTA NKVGTYQLAI AAKHHGIPFY VAAPSTSCDL SLESGRDIII EVRPPEELTS
INGVPIAAPG IEVWNPAFDV TPHQLITGGI ITELGVFLPS ELQAALTGRL TAL
//
