ID A0A2N5T488_9BASI Unreviewed; 405 AA.
AC A0A2N5T488;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PCANC_10474 {ECO:0000313|EMBL:PLW49725.1}, PCASD_19738
GN {ECO:0000313|EMBL:PLW20296.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW20296.1, ECO:0000313|Proteomes:UP000235392};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW49725.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW20296.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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:PLW20296.1}.
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DR EMBL; PGCI01000701; PLW20296.1; -; Genomic_DNA.
DR EMBL; PGCJ01000094; PLW49725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5T488; -.
DR STRING; 200324.A0A2N5T488; -.
DR OrthoDB; 4853at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.420; translation initiation factor eif-2b, domain 1; 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388}.
SQ SEQUENCE 405 AA; 43906 MW; 4195034FF61BCEC2 CRC64;
MSSENEKTPS GLLSIRLVDG KPLEETHAVE IIDQLLLPHE FQWITIRDPA EAHRAIKAMN
IRGAPAIGSL AAIALACGLL RLADTKPQLS RQELEEYMHH SSALLVSARP TAVNLQEAIE
RVNALLVKTD QDPPEDTASL IKKIVELCKL IWTEDLERNK KIGRLGADWL IDNLGLKPTQ
KISVLTVCNT GSLATSGYGT ALGIITALHE LGRLEHTYFM QTTPFLQGAR LTSLELHALS
IPCSMVCDSA VGWLVQSGKV DAFVAGADRI ASNGDTANKI STYQISLICK HGNNASLHAK
IPVVIAAPRT TIDLKIKTGG EIRIEERPSW EACTVRGKVV GSDQPMKKEG ELNVATVLVT
PENTVALNPA FDVTPALLID AIATELGVIV KDSNRDQFDL RSYLA
//
