(data stored in ACNUC7421 zone)

HOGENOM: CANDC_2_PE106

ID   CANDC_2_PE106                        STANDARD;      PRT;   424 AA.
AC   CANDC_2_PE106; B9WAG5;
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; (CANDC_2.PE106).
GN   Name=MRI1; ORFNames=CD36_16050;
OS   CANDIDA DUBLINIENSIS CD36.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; mitosporic Saccharomycetales; Candida.
OX   NCBI_TaxID=573826;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANDC_2.PE106.
CC       Candida dubliniensis (strain CD36 / CBS 7987 / NCPF 3949 / NRRL Y-17841
CC       chromosome 2, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_CANDC
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; B9WAG5; -.
DR   EMBL; FM992689; CAX43385.1; -; Genomic_DNA.
DR   RefSeq; XP_002418085.1; XM_002418040.1.
DR   ProteinModelPortal; B9WAG5; -.
DR   STRING; B9WAG5; -.
DR   GeneID; 8045655; -.
DR   GenomeReviews; FM992689_GR; MRI1.
DR   KEGG; cdu:CD36_16050; -.
DR   OrthoDB; EOG4S1XGM; -.
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; 2.
DR   TIGRFAMs; TIGR00524; EIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; Salvage_mtnA; 1.
DR   HOGENOMDNA; CANDC_2.PE106; -.
KW   CAX43385.100008510fold_1320000031;
KW   Methylthioribose-1-phosphate isomerase ;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   424 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTTTRTLQA IKFDRNNIKL EILDQLLLPY STTYIPITSI EDAFKAIKLM QVRGAPAIAI
     VGAFSVVVEV SNYLKQSDSN RKTIENLNDS LDYLITSRPT AVNLANALND IKQLLQEFND
     TDIINEKIYQ QIYDYAIALY DEDLANNKKI GENGLKYIIN TLTEQNFKGP FSIMTICNTG
     SLATSGHGTA LGIIRSTYQA LQKNNSKEEF WLDHIYPCET RPYNQGAKLT TYELDYEQIP
     FTLICDNMVS SLINTLSDDD NKKPIKTNQI SPVKFIIVGA DRIVENGDTA NKIGTFQLST
     IANFFNNNKF IQQQSKSNTT KTTINKEIKF IVAAPKTTID LNTKTGDDIV IEERPANELT
     TLVGPLLNEA GDVGEKLTVG IATPGISVWN PAFDVTPHEL IDSIVTEDPH VFTKDENGEF
     NLIK
//

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