(data stored in ACNUC7421 zone)

HOGENOM: GEOSW_2_PE784

ID   GEOSW_2_PE784                        STANDARD;      PRT;   356 AA.
AC   GEOSW_2_PE784; C5D7U5;
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; (GEOSW_2.PE784).
GN   Name=mtnA; OrderedLocusNames=GWCH70_0846;
OS   GEOBACILLUS SP. WCH70.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS GEOSW_2.PE784.
CC       Geobacillus sp. WCH70, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_GEOSW
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   -!- SUBUNIT: Homodimer.
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; C5D7U5; -.
DR   EMBL; CP001638; ACS23726.1; -; Genomic_DNA.
DR   RefSeq; YP_002948992.1; NC_012793.1.
DR   ProteinModelPortal; C5D7U5; -.
DR   SMR; C5D7U5; 1-347.
DR   STRING; C5D7U5; -.
DR   GeneID; 7977854; -.
DR   GenomeReviews; CP001638_GR; GWCH70_0846.
DR   KEGG; gwc:GWCH70_0846; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
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; GEOSW_2.PE784; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   356 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAEPFAIPRS VEWNDTHITI LNQQKLPLVT EYLELKNIED VWDAIAALKV RGAPAIGITA
     AYGLALSAQQ YETESLEKFK EHVRKDRDYL ASSRPTAVNL FWALDRLVSS IAHVSSVNEA
     KTTLIHEAIR IQIEDEDVCR RIGEHALSLF QNGDRVLTIC NAGSIATARY GTALAPFYLA
     KEKGMNLHVY ASETRPVLQG ARLTTWELMQ AGVDVTLITD NMAAQTIKAK NITAVIVGAD
     RIAANGDTAN KIGTFGLALL AKAFGIPFYV AAPLSTIDLA TKTGEEIPIE ERNPEEVTHI
     AGTRIAPEGV NVYNPAFDVT PHDLITAIIT EKGIVRGNYE TELPALFAKE ARHEAI
//

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