(data stored in ACNUC7421 zone)

HOGENOM: EMENI_35_PE888

ID   EMENI_35_PE888                       STANDARD;      PRT;   379 AA.
AC   EMENI_35_PE888; Q5B590; C8V9A3;
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; (EMENI_35.PE888).
GN   Name=mri1; ORFNames=AN4290;
OS   EMERICELLA NIDULANS.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiales;
OC   Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=162425;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS EMENI_35.PE888.
CC       Aspergillus nidulans chromosome III CADRE2 full sequence 1..3412996
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNA_EMENI
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_nidulans;CADANIAG00006174;CADANIAT00006174;CADANIAP00006174.
DR   EMBL_PREDICTED; AACD01000072; - ;
DR   EMBL; BN001303; - ;
DR   UniProtKB/Swiss-Prot; Q5B590; C8V9A3; -.
DR   EMBL; AACD01000072; EAA60042.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77829.1; -; Genomic_DNA.
DR   RefSeq; XP_661894.1; XM_656802.1.
DR   ProteinModelPortal; Q5B590; -.
DR   SMR; Q5B590; 198-378.
DR   STRING; Q5B590; -.
DR   GeneID; 2872088; -.
DR   KEGG; ani:AN4290.2; -.
DR   OMA; RPRNQGA; -.
DR   OrthoDB; EOG4S1XGM; -.
DR   PhylomeDB; Q5B590; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:RefGenome.
DR   GO; GO:0005634; C:nucleus; ISS:RefGenome.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; ISS:RefGenome.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:RefGenome.
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; EMENI_35.PE888; -.
KW   CADANIAG00006174575old_1320000031; CADANIAP00006174631old_1320000031;
KW   BN001303;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus; Reference proteome.
SQ   SEQUENCE   379 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVLEAIRYKD GKLSIIDQLQ LPFTERYIEI RTSEEGWQAI KNMQVRGAPA IAIVAALSLA
     SELHELSIRN KISTTAEDVT AFIRERLGHL VSSRPTAVNL SDAARKLEVI VSERSQTPGS
     TAQDIVNVFI QAAEGMLAKD VEDNTRIGEN GAKWISMNAL PTDHDKAVVL THCNTGSLAT
     AGYGTALGVI RSLMANNTLQ HAYCTETRPY NQGSRLTAFE LVHDKIPATL ITDSMAAALL
     SRPETRVNAI VVGADRVAAN GDTANKIGTY GLAVLARYHG VKFLVAAPLT TIDLATKSGG
     DIVIEERPPS EVTRVKGSRE DDTTGDVRLE TISIAAEGIN VWNPAFDVTP SELIDGIITE
     KGVAEKDTDG RFHLEELFD
//

If you have problems or comments...

PBIL Back to PBIL home page