(data stored in ACNUC30630 zone)

HOGENOM: BASUB1_1_PE74

ID   BASUB1_1_PE74                        STANDARD;      PRT;   470 AA.
AC   BASUB1_1_PE74; P28820;
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 synthase component 1; EC=2.6.1
DE   85;AltName: Full=ADC synthase;AltName: Full=Para-aminobenzoate synthase
DE   component I; (BASUB1_1.PE74).
GN   Name=pabB; Synonyms=pab; OrderedLocusNames=BSU00740;
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.PE74.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PABB_BACSU
CC   -!- FUNCTION: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate
CC       (ADC) from chorismate and glutamine.
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = 4-amino-4-
CC       deoxychorismate + L-glutamate.
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: Belongs to the anthranilate synthase component I
CC       family.
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P28820; -.
DR   EMBL; M34053; AAA22694.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05309.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11850.1; -; Genomic_DNA.
DR   PIR; A37854; A37854.
DR   RefSeq; NP_387955.1; NC_000964.3.
DR   ProteinModelPortal; P28820; -.
DR   SMR; P28820; 10-462.
DR   EnsemblBacteria; EBBACT00000001781; EBBACP00000001781; EBBACG00000001778.
DR   GeneID; 936926; -.
DR   GenomeReviews; AL009126_GR; BSU00740.
DR   KEGG; bsu:BSU00740; -.
DR   NMPDR; fig|224308.1.peg.74; -.
DR   GenoList; BSU00740; -.
DR   GeneTree; EBGT00050000001425; -.
DR   OMA; HEYKESF; -.
DR   PhylomeDB; P28820; -.
DR   ProtClustDB; CLSK2752294; -.
DR   BioCyc; BSUB:BSU00740-MON; -.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:EC.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate-bd_C.
DR   Gene3D; G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; TRPE_1_chor_bd; 1.
DR   HOGENOMDNA; BASUB1_1.PE74; -.
KW   Complete proteome; Folate biosynthesis; Reference proteome;
KW   Transferase.
SQ   SEQUENCE   470 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAQRRPAGKK IPFQKDSFLQ QFEKLAQSRK HHVLLESARG GRYSIAGLDP IATVKGKDGI
     TTIKHGDEML FKEGDPLRAF HSWFKTLETE TNHEFPDFQG GAIGFLSYDY ARYIENFKML
     SLDDLETPDI YFLVFDDIAV YDHQEESLWL ITHVNGSDQE TADVKLSELE QMWLTELPAV
     TSREMKPETA GSFAAPFTED GFSQAVEKIK QYIASGDVFQ VNLSIRQSQS LSVHPYQIYK
     TLREVNPSPY MAYLETPDFQ IICGSPELLV SKKGKLLETR PIAGTRSRGK TNEEDEALAN
     ELIHNEKERA EHVMLVDLER NDLGRVSRYG SVRVNEFMAI EKYSHVMHIV SNVQGELQDG
     YDAVDIIHAV FPGGTITGAP KVRTMEIIEE LEPTRRGLYT GSIGWFGYNH DLQFNIVIRT
     IYATGGQAFM QSGAGVVIDS VPKHEYKESF KKAFAMQRAL ELSEEETKIR
//

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