(data stored in ACNUC30630 zone)

HOGENOM: ESCOL1_1_PE1803

ID   ESCOL1_1_PE1803                      STANDARD;      PRT;   453 AA.
AC   ESCOL1_1_PE1803; P05041;
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; (ESCOL1_1.PE1803).
GN   Name=pabB; OrderedLocusNames=b1812, JW1801;
OS   ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511145;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL1_1.PE1803.
CC       Escherichia coli str. K-12 substr. MG1655 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PABB_ECOLI
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; P05041; -.
DR   EMBL; K02673; AAA24266.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74882.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15619.1; -; Genomic_DNA.
DR   EMBL; U07762; AAC43282.1; -; Genomic_DNA.
DR   EMBL; U07748; AAC43269.1; -; Genomic_DNA.
DR   EMBL; U07749; AAC43270.1; -; Genomic_DNA.
DR   PIR; A30251; AGEC1.
DR   RefSeq; AP_002431.1; AC_000091.1.
DR   RefSeq; NP_416326.1; NC_000913.2.
DR   PDB; 1K0E; X-ray; 2.00 A; A/B=1-453.
DR   PDB; 1K0G; X-ray; 2.05 A; A/B=1-453.
DR   PDBsum; 1K0E; -.
DR   PDBsum; 1K0G; -.
DR   ProteinModelPortal; P05041; -.
DR   SMR; P05041; 3-453.
DR   DIP; DIP-10434N; -.
DR   IntAct; P05041; 5.
DR   EnsemblBacteria; EBESCT00000001432; EBESCP00000001432; EBESCG00000001194.
DR   EnsemblBacteria; EBESCT00000016395; EBESCP00000015686; EBESCG00000015455.
DR   GeneID; 946337; -.
DR   GenomeReviews; AP009048_GR; JW1801.
DR   GenomeReviews; U00096_GR; b1812.
DR   KEGG; ecj:JW1801; -.
DR   KEGG; eco:b1812; -.
DR   EchoBASE; EB0677; -.
DR   EcoGene; EG10683; pabB.
DR   eggNOG; COG0147; -.
DR   GeneTree; EBGT00050000009519; -.
DR   OMA; HNRFDIL; -.
DR   ProtClustDB; PRK15465; -.
DR   BioCyc; EcoCyc:PABASYN-COMPI-MON; -.
DR   BioCyc; MetaCyc:PABASYN-COMPI-MON; -.
DR   DrugBank; DB00634; Sulfacetamide.
DR   Genevestigator; P05041; -.
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   InterPro; IPR005802; Para-NH2Bz_synth_comp_1.
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   TIGRFAMs; TIGR00553; PabB; 1.
DR   HOGENOMDNA; ESCOL1_1.PE1803; -.
KW   3D-structure; Complete proteome; Folate biosynthesis;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   453 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKTLSPAVIT LLWRQDAAEF YFSRLSHLPW AMLLHSGYAD HPYSRFDIVV AEPICTLTTF
     GKETVVSESE KRTTTTDDPL QVLQQVLDRA DIRPTHNEDL PFQGGALGLF GYDLGRRFES
     LPEIAEQDIV LPDMAVGIYD WALIVDHQRH TVSLLSHNDV NARRAWLESQ QFSPQEDFTL
     TSDWQSNMTR EQYGEKFRQV QEYLHSGDCY QVNLAQRFHA TYSGDEWQAF LQLNQANRAP
     FSAFLRLEQG AILSLSPERF ILCDNSEIQT RPIKGTLPRL PDPQEDSKQA VKLANSAKDR
     AENLMIVDLM RNDIGRVAVA GSVKVPELFV VEPFPAVHHL VSTITAQLPE QLHASDLLRA
     AFPGGSITGA PKVRAMEIID ELEPQRRNAW CGSIGYLSFC GNMDTSITIR TLTAINGQIF
     CSAGGGIVAD SQEEAEYQET FDKVNRILKQ LEK
//

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