(data stored in ACNUC8465 zone)

HOGENOM: BASUB1_1_PE3516

ID   BASUB1_1_PE3516                      STANDARD;      PRT;   226 AA.
AC   BASUB1_1_PE3516; O06995;
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=Putative beta-phosphoglucomutase; Short=Beta-PGM; EC=5.4.2
DE   6; (BASUB1_1.PE3516).
GN   Name=yvdM; OrderedLocusNames=BSU34550;
OS   BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BASUB1_1.PE3516.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PGMB_BACSU
CC   -!- FUNCTION: Reversible transformation of glucose 6-phosphate and
CC       beta-glucose 1-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Beta-D-glucose 1-phosphate = beta-D-glucose 6-
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family.
CC   -!- GENE_FAMILY: HOG000248341 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; O06995; -.
DR   EMBL; Z94043; CAB08042.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15460.1; -; Genomic_DNA.
DR   PIR; E70034; E70034.
DR   RefSeq; NP_391335.1; NC_000964.3.
DR   PDB; 3NAS; X-ray; 3.00 A; A/B=2-224.
DR   PDBsum; 3NAS; -.
DR   ProteinModelPortal; O06995; -.
DR   SMR; O06995; 1-223.
DR   EnsemblBacteria; EBBACT00000000589; EBBACP00000000589; EBBACG00000000587.
DR   GeneID; 938624; -.
DR   GenomeReviews; AL009126_GR; BSU34550.
DR   KEGG; bsu:BSU34550; -.
DR   NMPDR; fig|224308.1.peg.3461; -.
DR   GenoList; BSU34550; -.
DR   GeneTree; EBGT00050000000474; -.
DR   OMA; YIVDANE; -.
DR   PhylomeDB; O06995; -.
DR   ProtClustDB; CLSK537154; -.
DR   BioCyc; BSUB:BSU34550-MON; -.
DR   GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR   InterPro; IPR010972; Beta-phosphoglucomutase.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006402; HAD-SF_hydro_IA_v3.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01990; BPGM; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
DR   HOGENOMDNA; BASUB1_1.PE3516; -.
KW   3D-structure; Complete proteome; Isomerase; Reference proteome.
SQ   SEQUENCE   226 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKAVIFDLDG VITDTAEYHF LAWKHIAEQI DIPFDRDMNE RLKGISREES LESILIFGGA
     ETKYTNAEKQ ELMHRKNRDY QMLISKLTPE DLLPGIGRLL CQLKNENIKI GLASSSRNAP
     KILRRLAIID DFHAIVDPTT LAKGKPDPDI FLTAAAMLDV SPADCAAIED AEAGISAIKS
     AGMFAVGVGQ GQPMLGADLV VRQTSDLTLE LLHEEWEQYR IRESIP
//

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