(data stored in ACNUC7421 zone)

HOGENOM: ASFUM1_4_PE364

ID   ASFUM1_4_PE364                       STANDARD;      PRT;   387 AA.
AC   ASFUM1_4_PE364; Q4WNI1;
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; (ASFUM1_4.PE364).
GN   Name=mri1; ORFNames=AFUA_4G05830;
OS   ASPERGILLUS FUMIGATUS AF293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=330879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASFUM1_4.PE364.
CC       Aspergillus fumigatus (strain FGSC A1100 / CBS 101355 / Af293) chromoso
CC       4, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_ASPFU
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   UniProtKB/Swiss-Prot; Q4WNI1; -.
DR   EMBL; AAHF01000005; EAL90203.1; -; Genomic_DNA.
DR   RefSeq; XP_752241.1; XM_747148.1.
DR   ProteinModelPortal; Q4WNI1; -.
DR   STRING; Q4WNI1; -.
DR   EnsemblFungi; CADAFUAT00008095; CADAFUAP00008095; CADAFUAG00008095.
DR   GeneID; 3509012; -.
DR   GenomeReviews; CM000172_GR; mri1.
DR   KEGG; afm:AFUA_4G05830; -.
DR   eggNOG; fuNOG06631; -.
DR   GeneTree; EFGT00050000003245; -.
DR   OMA; EDGWKVI; -.
DR   OrthoDB; EOG4S1XGM; -.
DR   PhylomeDB; Q4WNI1; -.
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; ASFUM1_4.PE364; -.
KW   EAL90203.1g.C_scaffold_1320000031;
KW   Methylthioribose-1-phosphate isomerase ;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus; Reference proteome.
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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