(data stored in ACNUC7421 zone)

HOGENOM: CAGLA1_5_PE196

ID   CAGLA1_5_PE196                       STANDARD;      PRT;   415 AA.
AC   CAGLA1_5_PE196; Q6FVY2;
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; (CAGLA1_5.PE196).
GN   Name=MRI1; OrderedLocusNames=CAGL0D04576g;
OS   CANDIDA GLABRATA CBS 138.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces; mitosporic
OC   Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAGLA1_5.PE196.
CC       Candida glabrata (strain ATCC 2001 / NRRL Y-65 / CBS 138 / IFO 0622)
CC       chromosome D, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_CANGA
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; Q6FVY2; -.
DR   EMBL; CR380950; CAG58523.1; -; Genomic_DNA.
DR   RefSeq; XP_445612.1; XM_445612.1.
DR   ProteinModelPortal; Q6FVY2; -.
DR   SMR; Q6FVY2; 3-212, 226-414.
DR   GeneID; 2887005; -.
DR   GenomeReviews; CR380950_GR; CAGL0D04576g.
DR   KEGG; cgr:CAGL0D04576g; -.
DR   eggNOG; fuNOG06631; -.
DR   OMA; EDGWKVI; -.
DR   OrthoDB; EOG4S1XGM; -.
DR   PhylomeDB; Q6FVY2; -.
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; CAGLA1_5.PE196; -.
KW   CAG58523.149200367fold_1320000031;
KW   Methylthioribose-1-phosphate isomerase ;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   415 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNALRAIDFK RDDPNNVSVS VLDQLLLPYT TKYIPIYTID DGFTVIKKMQ VRGAPAIAIV
     GALSVLMESQ LLLSEGFCKT QYYYNLNDWE NIRSKIDERL AFLLSSRPTA INLSNALDEI
     KIVLDSASDL QTFKNNLFDY VCKLIDDDFA NNKRMGDNGA EFLLNLLKKE NFNEDFAVFT
     ICNTGSLATS GYGTALGVIR SLWNDSKSKT QEGNPNKKVK LTESSPKMVQ VFPLETRPYN
     QGSRLTAYEL VHDDIPATLI PDSSIAYKIM TSKIPIKAAF VGADRIVRNG DTANKIGTLQ
     LAIICKQFGI KFFVVAPRTT IDKVTEEGKD IIVEERNANE FKIVTGSAVD MQTNKPILDE
     KNEPITAKVG IAPENINVWN PAFDITSFEY IDGIVTEVGV FTKNENGNFD LSALH
//

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