(data stored in ACNUC7421 zone)

HOGENOM: ASPFC_5_PE1

ID   ASPFC_5_PE1                          STANDARD;      PRT;   387 AA.
AC   ASPFC_5_PE1; B0Y5C3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Methylthioribose-1-phosphate isomerase; Short=M1Pi;
DE   Short=MTR-1-P isomerase; EC=5.3.1 23;AltName:
DE   Full=S-methyl-5-thioribose-1-phosphate isomerase;AltName:
DE   Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like
DE   protein; (ASPFC_5.PE1).
GN   Name=mri1; ORFNames=AFUB_062900;
OS   ASPERGILLUS FUMIGATUS A1163.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiales;
OC   Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=451804;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASPFC_5.PE1.
CC       Aspergillus fumigatusa1163 scaffold DS499598 CADRE full sequence 1..261
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_ASPFC
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-
CC       phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate =
CC       S-methyl-5-thio-D-ribulose 1-phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family. MtnA subfamily.
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aspergillus_fumigatusa1163;CADAFUBG00006238;CADAFUBT00006238;CADAFUBP00006115.
DR   EMBL; DS499598; - ;
DR   UniProtKB/Swiss-Prot; B0Y5C3; -.
DR   EMBL; DS499598; EDP49958.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0Y5C3; -.
DR   EnsemblFungi; CADAFUBT00006238; CADAFUBP00006115; CADAFUBG00006238.
DR   GeneTree; EFGT00050000003245; -.
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:EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-2BI_MTNA.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   PANTHER; PTHR10233; IF-2B_related; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   TIGRFAMs; TIGR00524; EIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; Salvage_mtnA; 1.
DR   HOGENOMDNA; ASPFC_5.PE1; -.
KW   CADAFUBG00006238affold_1320000031; CADAFUBP00006115affold_1320000031;
KW   DS499598;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   387 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASILQAIRY SHGKLAIIDQ LQLPYVEKFI TIRTSEDAWH AIKEMRVRGA PAIAIVAALA
     LASELNTLII HDKLSSRAEE VKLFIREKLD YLVSSRPTAV NLSDAARKLE STISGHADTP
     GATGRTVAEA FIRAAEEMMT KDLDDNMKIG QNGAEWIIKH ALARHKSTAT VLTHCNTGSL
     ATSGYGTALG VIRSLASKKA LEHAYCTETR PYNQGSRLTA FELVHDRLPA TLITDSMVAA
     LLASTKAEVD AIVVGADRVA ANGDTANKIG TYGLAVLAKY HGVKFLVAAP LTTIDLGTKS
     GEDIVIEERP SAEVTKIRGP VDGDHPADIV KLETVHIAAK GIDVWNPAFD VTPSTLIDGI
     ITEVGVIEKE ADGQFHLERL FIDNSAS
//

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