(data stored in ACNUC30630 zone)

HOGENOM: ESCOL1_1_PE3299

ID   ESCOL1_1_PE3299                      STANDARD;      PRT;   187 AA.
AC   ESCOL1_1_PE3299; P00903; Q2M726;
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 glutamine amidotransferase
DE   component II; EC=2.6.1 85;AltName: Full=ADC synthase; (ESCOL1_1.PE3299).
GN   Name=pabA; OrderedLocusNames=b3360, JW3323;
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.PE3299.
CC       Escherichia coli str. K-12 substr. MG1655 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PABA_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: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- GENE_FAMILY: HOG000025029 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P00903; Q2M726; -.
DR   EMBL; M28363; AAA23774.1; -; Genomic_DNA.
DR   EMBL; K00030; AAA24260.1; -; Genomic_DNA.
DR   EMBL; M32354; AAA24264.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58157.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76385.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77930.1; -; Genomic_DNA.
DR   PIR; A01124; AGEC2.
DR   RefSeq; AP_004429.1; AC_000091.1.
DR   RefSeq; NP_417819.1; NC_000913.2.
DR   ProteinModelPortal; P00903; -.
DR   SMR; P00903; 1-187.
DR   DIP; DIP-10433N; -.
DR   IntAct; P00903; 4.
DR   EnsemblBacteria; EBESCT00000003028; EBESCP00000003028; EBESCG00000002484.
DR   EnsemblBacteria; EBESCT00000003029; EBESCP00000003029; EBESCG00000002484.
DR   EnsemblBacteria; EBESCT00000015266; EBESCP00000014557; EBESCG00000014326.
DR   GeneID; 947873; -.
DR   GenomeReviews; AP009048_GR; JW3323.
DR   GenomeReviews; U00096_GR; b3360.
DR   KEGG; ecj:JW3323; -.
DR   KEGG; eco:b3360; -.
DR   EchoBASE; EB0676; -.
DR   EcoGene; EG10682; pabA.
DR   eggNOG; COG0512; -.
DR   GeneTree; EBGT00050000009095; -.
DR   OMA; SVDEIMG; -.
DR   ProtClustDB; PRK08007; -.
DR   BioCyc; EcoCyc:PABASYN-COMPII-MON; -.
DR   BioCyc; MetaCyc:PABASYN-COMPII-MON; -.
DR   Genevestigator; P00903; -.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:EC.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:InterPro.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic 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; ESCOL1_1.PE3299; -.
KW   Complete proteome; Folate biosynthesis; Glutamine amidotransferase;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   187 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MILLIDNYDS FTWNLYQYFC ELGADVLVKR NDALTLADID ALKPQKIVIS PGPCTPDEAG
     ISLDVIRHYA GRLPILGVCL GHQAMAQAFG GKVVRAAKVM HGKTSPITHN GEGVFRGLAN
     PLTVTRYHSL VVEPDSLPAC FDVTAWSETR EIMGIRHRQW DLEGVQFHPE SILSEQGHQL
     LANFLHR
//

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