(data stored in ACNUC7421 zone)

HOGENOM: ZYGRO_3_PE538

ID   ZYGRO_3_PE538                        STANDARD;      PRT;   414 AA.
AC   ZYGRO_3_PE538; C5DU12;
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; (ZYGRO_3.PE538).
GN   Name=MRI1; OrderedLocusNames=ZYRO0C12936g;
OS   ZYGOSACCHAROMYCES ROUXII.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ZYGRO_3.PE538.
CC       Zygosaccharomyces rouxii strain CBS732 chromosome C complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_ZYGRC
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; C5DU12; -.
DR   EMBL; CU928175; CAR27273.1; -; Genomic_DNA.
DR   RefSeq; XP_002496206.1; XM_002496161.1.
DR   ProteinModelPortal; C5DU12; -.
DR   STRING; C5DU12; -.
DR   GeneID; 8203426; -.
DR   GenomeReviews; CU928175_GR; ZYRO0C12936g.
DR   KEGG; zro:ZYRO0C12936g; -.
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; 1.
DR   TIGRFAMs; TIGR00524; EIF-2B_rel; 1.
DR   HOGENOMDNA; ZYGRO_3.PE538; -.
KW   CAR27273.100026476820036002503210000011;
KW   ZYRO0C12936p;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   414 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLEAIKFDR SEPRKVSVKV LDQLLLPYTT KYIPVHTIDD GYRVIKNMQV RGAPAIAIVG
     SLSILTEVQF LQLDSQKSTQ WFYDLSDWSN VNSKLLQRIE FLLSSRPTAV NLSNSLTEIR
     GILQNSSDLS DFDSKLFQYV CTLIDDDLAN NITMGNNGAE YLLESLVQDG FQGEFGVLTI
     CNTGSLATSG YGTALGVIRS LWAKSQSQGS ENPPSKKQKK DAAPTKMVQV FPLETRPYNQ
     GSRLTAYELV HDEIPATLIT DSMVSYKIKT SPIPIKAAFV GADRIVRNGD TANKIGTFQL
     AIVCKQFGIK FFVVAPKTTI DNVTPSGDQI VVEERKPSEF RLVTGTAVDY VNESPILNDS
     QEPQSAKVGI APPNVNVWNP AFDITPHEFI DGIVTEKGVF TKDDKGNFQL DKLF
//

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