(data stored in ACNUC7421 zone)

HOGENOM: BACAN0_1_PE10

ID   BACAN0_1_PE10                        STANDARD;      PRT;   196 AA.
AC   BACAN0_1_PE10; Q81W26; Q6I528; Q6KYS2;
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=Glutamine amidotransferase subunit pdxT; EC=2.6.-
DE   -;AltName: Full=Glutamine amidotransferase glutaminase subunit pdxT;
DE   (BACAN0_1.PE10).
GN   Name=pdxT; OrderedLocusNames=BA_0011, GBAA_0011, BAS0014;
OS   BACILLUS ANTHRACIS STR. AMES.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=198094;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACAN0_1.PE10.
CC       Bacillus anthracis str. Ames, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:PDXT_BACAN
CC   -!- FUNCTION: Involved in the hydrolysis of glutamine to glutamate and
CC       ammonia. Channels an ammonia molecule to pdxS (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a complex with pdxS (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamine amidotransferase pdxT/SNO
CC       family.
CC   -!- GENE_FAMILY: HOG000039949 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q81W26; Q6I528; Q6KYS2; -.
DR   EMBL; AE016879; AAP24068.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT29091.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT52353.1; -; Genomic_DNA.
DR   RefSeq; NP_842582.1; NC_003997.3.
DR   RefSeq; YP_016616.1; NC_007530.2.
DR   RefSeq; YP_026302.1; NC_005945.1.
DR   ProteinModelPortal; Q81W26; -.
DR   SMR; Q81W26; 2-192.
DR   EnsemblBacteria; EBBACT00000011343; EBBACP00000011099; EBBACG00000011335.
DR   EnsemblBacteria; EBBACT00000015412; EBBACP00000015033; EBBACG00000015404.
DR   EnsemblBacteria; EBBACT00000020003; EBBACP00000019488; EBBACG00000019994.
DR   GeneID; 1083754; -.
DR   GeneID; 2816387; -.
DR   GeneID; 2850451; -.
DR   GenomeReviews; AE016879_GR; BA_0011.
DR   GenomeReviews; AE017225_GR; BAS0014.
DR   GenomeReviews; AE017334_GR; GBAA_0011.
DR   KEGG; ban:BA_0011; -.
DR   KEGG; bar:GBAA_0011; -.
DR   KEGG; bat:BAS0014; -.
DR   TIGR; BA_0011; -.
DR   TIGR; GBAA_0011; -.
DR   GeneTree; EBGT00050000000582; -.
DR   OMA; ANRTKKG; -.
DR   ProtClustDB; PRK13525; -.
DR   BioCyc; BANT260799:BAS0014-MON; -.
DR   BioCyc; BANT261594:GBAA0011-MON; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01615; PdxT; 1; -.
DR   InterPro; IPR002161; Glutamine_amidoTferase_suPdxT.
DR   InterPro; IPR021196; PdxT/SNO_CS.
DR   Pfam; PF01174; SNO; 1.
DR   PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR   TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1.
DR   PROSITE; PS01236; PDXT_SNO_1; 1.
DR   PROSITE; PS51130; PDXT_SNO_2; 1.
DR   HOGENOMDNA; BACAN0_1.PE10; -.
KW   glutamine amidotransferase subunit PdxT;
KW   Complete proteome; Glutamine amidotransferase; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   196 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVKIGVLGLQ GAVREHVKSV EASGAEAVVV KRIEQLEEID GLILPGGEST TMRRLIDKYD
     FMEPLRTFAK SGKPMFGTCA GMILLAKTLI GYDEAHIGAM DITVERNAFG RQKDSFEAAL
     SIKGVGEDFV GVFIRAPYVV DVADDVEVLS THGDRMVAVK QGPFLAASFH PELTDDHRVT
     AYFVEMVKEA KMKKVV
//

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