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Database: UniProt
Entry: A0A0F8BC26_LARCR
LinkDB: A0A0F8BC26_LARCR
Original site: A0A0F8BC26_LARCR 
ID   A0A0F8BC26_LARCR        Unreviewed;       353 AA.
AC   A0A0F8BC26;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:0000256|HAMAP-Rule:MF_03119};
GN   ORFNames=D5F01_LYC01015 {ECO:0000313|EMBL:KAE8300866.1};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358 {ECO:0000313|EMBL:KAE8300866.1, ECO:0000313|Proteomes:UP000424527};
RN   [1] {ECO:0000313|EMBL:KAE8300866.1, ECO:0000313|Proteomes:UP000424527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8300866.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAE8300866.1};
RA   Xiao S.;
RT   "Chromosome genome assembly for large yellow croaker.";
RL   Submitted (JUL-2019) 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_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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAE8300866.1}.
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DR   EMBL; REGW02000001; KAE8300866.1; -; Genomic_DNA.
DR   RefSeq; XP_010740335.1; XM_010742033.2.
DR   AlphaFoldDB; A0A0F8BC26; -.
DR   GeneID; 104927856; -.
DR   KEGG; lco:104927856; -.
DR   CTD; 84245; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   OrthoDB; 4853at2759; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000424527; Unassembled WGS sequence.
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|HAMAP-Rule:MF_03119};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_03119, ECO:0000313|EMBL:KAE8300866.1};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03119};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000424527}.
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;  37921 MW;  742BC02776243A71 CRC64;
     MTLEAIRYRA GSLQILNQLL LPHQTVYDEI RSVQDAYEAI KSMKVRGAPA IAIVGCLSLA
     VELRAGAGGD DPVTFIRESL CHLTSARPTA VNMGRAAREL MEFAENESME KNSEQLRESV
     IAWIEDMLER DVNDNKKIGN YGAQHILSGV PRDSVTILTH CNTGSLATAG YGTALGVVRS
     LHSLGRLKRV YCTETRPYNQ GSRLTAYEAV AEGIPATLIT DSMAALTMRE MDITAVVVGA
     DRVVANGDTA NKVGTYQLAI AAKHHGIPFY VAAPSTSCDL SLESGRDIII EVRPPEELTS
     INGVPIAAPG IEVWNPAFDV TPHQLITGGI ITELGVFLPS ELQAALTGRL TAL
//
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