(data stored in ACNUC7421 zone)

HOGENOM: PERMH_2_PE487

ID   PERMH_2_PE487                        STANDARD;      PRT;   353 AA.
AC   PERMH_2_PE487; C0QUC0;
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; (PERMH_2.PE487).
GN   Name=mtnA; OrderedLocusNames=PERMA_0495;
OS   PERSEPHONELLA MARINA EX-H1.
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX   NCBI_TaxID=123214;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PERMH_2.PE487.
CC       Persephonella marina EX-H1 chromosome, complete genome.
CC       1255) contig Pc00c12, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_PERMH
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   -!- 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; C0QUC0; -.
DR   EMBL; CP001230; ACO03726.1; -; Genomic_DNA.
DR   RefSeq; YP_002730285.1; NC_012440.1.
DR   ProteinModelPortal; C0QUC0; -.
DR   STRING; C0QUC0; -.
DR   GeneID; 7675251; -.
DR   GenomeReviews; CP001230_GR; PERMA_0495.
DR   KEGG; pmx:PERMA_0495; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; CLSK2479518; -.
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   HAMAP; MF_01678; Salvage_MtnA; 1; -.
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; PERMH_2.PE487; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   353 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRKIKDIRPI QLKDHKLYVI NQLKLPKEKE WLELSTYQQV AEAIEKMIIR GAPLIGIVGA
     YGFAIGVKQI LDEGRSLDDV RDVFDRLKNT RPTAVNLFWA LERVWKKFER WTEEGRSGEE
     LVNLLFKEAE RIDLEDYHAN KAIGGYGQVL LPERCNVLTH CNTGALATSG WGTALGVIRS
     AFENGKDITV YVDETRPYLQ GSRLTAWELV EEGIPHYLIT DNSAGFLMSK GIIDAIIVGA
     DRITANGDVA NKIGTYTLAV LAEAHGIPFY VAAPTSTFDL DTDSGKDIPI EERSQLEVKK
     CGGCDIAPEE TEALNYSFDV TPASKITAII TEKGIISHVD KEHITKFLRY RGV
//

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