(data stored in ACNUC30630 zone)

HOGENOM: SAENT1_1_PE3347

ID   SAENT1_1_PE3347                      STANDARD;      PRT;   187 AA.
AC   SAENT1_1_PE3347; P06193;
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; (SAENT1_1.PE3347).
GN   Name=pabA; OrderedLocusNames=STM3469;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SAENT1_1.PE3347.
CC       Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:PABA_SALTY
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; P06193; -.
DR   EMBL; X02603; CAA26450.1; -; Genomic_DNA.
DR   EMBL; M32355; AAA27177.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22331.1; -; Genomic_DNA.
DR   PIR; S09636; S09636.
DR   RefSeq; NP_462372.1; NC_003197.1.
DR   ProteinModelPortal; P06193; -.
DR   PRIDE; P06193; -.
DR   GeneID; 1254992; -.
DR   GenomeReviews; AE006468_GR; STM3469.
DR   KEGG; stm:STM3469; -.
DR   NMPDR; fig|99287.1.peg.3349; -.
DR   OMA; SVDEIMG; -.
DR   ProtClustDB; PRK08007; -.
DR   BioCyc; STYP99287:STM3469-MON; -.
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; SAENT1_1.PE3347; -.
KW   Complete proteome; Folate biosynthesis; Glutamine amidotransferase;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   187 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MILLIDNYDS FTWNLYQYFC ELGAEVQVRR NDALTLAHID ALNPQKIVIS PGPCTPNDAG
     ISLAVIRHYA GRIPMLGVCL GHQAMAQAFG ASVVRAAKVM HGKTSPVTHN GQGVFRGLPS
     PLTVTRYHSL IVDPATLPEC FEITAWSETQ EIMGIRHREW DLEGVQFHPE SILSEQGHAL
     LKNFLRR
//

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