(data stored in ACNUC7421 zone)

HOGENOM: DEHAN1_1_PE51

ID   DEHAN1_1_PE51                        STANDARD;      PRT;   406 AA.
AC   DEHAN1_1_PE51; Q6BZH5;
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; (DEHAN1_1.PE51).
GN   Name=MRI1; OrderedLocusNames=DEHA2A01276g;
OS   DEBARYOMYCES HANSENII CBS767.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHAN1_1.PE51.
CC       Debaryomyces hansenii (strain IGC 2968 / CBS 767 / ATCC 36239 / JCM 199
CC       / IFO 0083) chromosome A, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_DEBHA
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; Q6BZH5; -.
DR   EMBL; CR382133; CAG84341.2; -; Genomic_DNA.
DR   RefSeq; XP_456394.2; XM_456394.1.
DR   ProteinModelPortal; Q6BZH5; -.
DR   STRING; Q6BZH5; -.
DR   GeneID; 2899313; -.
DR   GenomeReviews; CR382133_GR; DEHA2A01276g.
DR   KEGG; dha:DEHA2A01276g; -.
DR   eggNOG; fuNOG06631; -.
DR   OMA; EDGWKVI; -.
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   TIGRFAMs; TIGR00512; Salvage_mtnA; 1.
DR   HOGENOMDNA; DEHAN1_1.PE51; -.
KW   CAG84341.2000191865old_1320000031;
KW   Methylthioribose-1-phosphate isomerase ;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus.
SQ   SEQUENCE   406 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSEAKTLQA IKFDRETKTL DILDQLLIPY ATEYISIKSI EDAYQAIKLM QVRGAPAIAI
     VGAFSIVVDV YNNLKETKEK SRTIGDLVES IHYLITARPT AVNLSNACLD IEKLILTEFK
     KDELVNQHTF DIVYQYSVAL YDDDLDNNFK IGDNGLHYIV ETLKSQSFTG PFSIITICNT
     GSLATSGHGT ALGIIRTVFK KLSKDAGEKF WLEHVYPCET RPYNQGARLT TYELNYEGIP
     STLVCDSMAS SLIATLSKQR KVKSSTAPVK FIIAGADRIV ENGDTANKIG TFQLSTIADY
     FNSRAEKENT IKFIIAAPRT TIDFKTKTGD GIIIEERPSQ ELTTLNGPVL TNNGVLEKQT
     VGIATPGIDV WNPAFDVTPH ELIDCIVTED TNAFVKNSEG DFNLKV
//

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