(data stored in ACNUC30630 zone)

HOGENOM: BASUB1_1_PE75

ID   BASUB1_1_PE75                        STANDARD;      PRT;   194 AA.
AC   BASUB1_1_PE75; P28819;
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=Para-aminobenzoate/anthranilate synthase glutamine
DE   amidotransferase component II;Includes: RecName: Full=Para-aminobenzoate
DE   synthase glutamine amidotransferase component II; EC=2.6.1.85; AltName:
DE   Full=ADC synthase;Includes: RecName: Full=Anthranilate synthase component
DE   II; EC=4.1.3 27; (BASUB1_1.PE75).
GN   Name=pabA; Synonyms=trpG; OrderedLocusNames=BSU00750;
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.PE75.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PABA_BACSU
CC   -!- FUNCTION: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate
CC       (ADC) from chorismate and glutamine and also involved in the
CC       synthesis of anthranilate.
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = 4-amino-4-
CC       deoxychorismate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 1/2.
CC   -!- SUBUNIT: Consists of two non-identical chains: component I
CC       catalyzes the formation of ADC by binding chorismate and ammonia;
CC       component II provides the glutamine amidotransferase activity.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- GENE_FAMILY: HOG000025029 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P28819; -.
DR   EMBL; M34053; AAA22695.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05310.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11851.1; -; Genomic_DNA.
DR   PIR; B37854; B37854.
DR   RefSeq; NP_387956.1; NC_000964.3.
DR   ProteinModelPortal; P28819; -.
DR   SMR; P28819; 1-188.
DR   EnsemblBacteria; EBBACT00000003162; EBBACP00000003162; EBBACG00000003155.
DR   GeneID; 936441; -.
DR   GenomeReviews; AL009126_GR; BSU00750.
DR   KEGG; bsu:BSU00750; -.
DR   NMPDR; fig|224308.1.peg.75; -.
DR   GenoList; BSU00750; -.
DR   GeneTree; EBGT00050000001033; -.
DR   OMA; SVDEIMG; -.
DR   PhylomeDB; P28819; -.
DR   ProtClustDB; PRK07649; -.
DR   BioCyc; BSUB:BSU00750-MON; -.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:EC.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase_dom.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR006221; TrpG_papA.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR00566; TrpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   HOGENOMDNA; BASUB1_1.PE75; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Folate biosynthesis; Glutamine amidotransferase;
KW   Lyase; Reference proteome; Transferase; Tryptophan biosynthesis.
SQ   SEQUENCE   194 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MILMIDNYDS FTYNLVQYLG ELGEELVVKR NDSITIDEIE ELSPDFLMIS PGPCSPDEAG
     ISLEAIKHFA GKIPIFGVCL GHQSIAQVFG GDVVRAERLM HGKTSDIEHD GKTIFEGLKN
     PLVATRYHSL IVKPETLPSC FTVTAQTKEG EIMAIRHNDL PIEGVQFHPE SIMTSFGKEM
     LRNFIETYRK EVIA
//

If you have problems or comments...

PBIL Back to PBIL home page