(data stored in ACNUC7421 zone)

HOGENOM: LACTH_5_PE215

ID   LACTH_5_PE215                        STANDARD;      PRT;   417 AA.
AC   LACTH_5_PE215; C5DHL1;
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; (LACTH_5.PE215).
GN   Name=MRI1; OrderedLocusNames=KLTH0E05236g;
OS   LACHANCEA THERMOTOLERANS.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=381046;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LACTH_5.PE215.
CC       Kluyveromyces thermotolerans strain CBS6340 chromosome E complete seque
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_LACTC
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; C5DHL1; -.
DR   EMBL; CU928169; CAR23272.1; -; Genomic_DNA.
DR   RefSeq; XP_002553709.1; XM_002553663.1.
DR   ProteinModelPortal; C5DHL1; -.
DR   STRING; C5DHL1; -.
DR   GeneID; 8291861; -.
DR   GenomeReviews; CU928169_GR; KLTH0E05236g.
DR   KEGG; lth:KLTH0E05236g; -.
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; LACTH_5.PE215; -.
KW   CAR23272.1824841755old_1320000031;
KW   KLTH0E05236p;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   417 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLEAIQFDR SHRDDISVRV LDQLLLPYTT KYVPIYTIDD GYTVINTMQV RGAPAIAIVG
     ALAVLMEIQL LQNDGFARTQ TFYDISSFEL TRSALSQRLD FLLSSRPTAV NLSNALREIR
     VLLAQSAGLA AFGNGVYDFV CRLIDEDLTN NVKMGDNGAA FLLDALQQEG FDEDFAVLTI
     CNTGSLATSG YGTALGVVRS LWNDSLAKSQ APGDGSAKKR KLNQGRAKMV QVYPLETRPY
     NQGARLTAYE LVHDQIPATL IPDSSIAYRI ATSPVPIKAA FVGADRIVRN GDTANKIGTY
     QLALVCKHFG IKFFVTAPKT TIDSKTETGA GIVVEERKPN EFKHVSGTLI DSQTGLPCVD
     NQDKPVSASV GVAPSEIDVW NPAFDITPHE LIDGIVTEDG VFTKSASGSF DLTNLFA
//

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