(data stored in ACNUC30630 zone)

HOGENOM: SAENT1_1_PE1763

ID   SAENT1_1_PE1763                      STANDARD;      PRT;   454 AA.
AC   SAENT1_1_PE1763; P12680;
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; (SAENT1_1.PE1763).
GN   Name=pabB; OrderedLocusNames=STM1824;
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.PE1763.
CC       Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:PABB_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: Belongs to the anthranilate synthase component I
CC       family.
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P12680; -.
DR   EMBL; M22079; AAA88618.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20739.1; -; Genomic_DNA.
DR   PIR; A31132; A31132.
DR   RefSeq; NP_460780.1; NC_003197.1.
DR   ProteinModelPortal; P12680; -.
DR   SMR; P12680; 4-453.
DR   PRIDE; P12680; -.
DR   GeneID; 1253343; -.
DR   GenomeReviews; AE006468_GR; STM1824.
DR   KEGG; stm:STM1824; -.
DR   NMPDR; fig|99287.1.peg.1765; -.
DR   OMA; HNRFDIL; -.
DR   ProtClustDB; PRK15465; -.
DR   BioCyc; STYP99287:STM1824-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   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; SAENT1_1.PE1763; -.
KW   para-aminobenzoate synthase component I;
KW   Complete proteome; Folate biosynthesis; Reference proteome;
KW   Transferase.
SQ   SEQUENCE   454 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMKTLSPTVI TLPWRPDAAE HYFAPVNHLP WAMLLHSGDA IHPYNRFDIL VADPVTTLTT
     RAQETTVCTA RTTTVTLDDP LHVLQTQLEA LPFHPQPDPD LPFQGGALGL FGYDLGRRFE
     ILPDTAARDI ALPDMAIGLY DWALIVDHQK QVVSLISYHD ADARYRWLTS QRAPTRTPFR
     LTSAWQSNMT RCEYGEKFRQ VQAWLHSGDC YQVNLSQRFQ ASYEGDEWQA FERLNRANRA
     PFSAFLRLHD GAILSLSPER FIQLENGHIQ TRPIKGTLPR LNDPQADRQQ AQKLANSMKD
     RAENLMIVDL MRNDIGRVAV PGSVKVPELF VVEPFPAVHH LVSTITARLP DSLHATDLLR
     AAFPGGSITG APKVRAMEII DELEPQRRNA WCGSIGYLSF CGKMDTSITI RTVTATQGQL
     YCSAGGGIVA DSNEEAEYQE TFDKVNRILH PLEN
//

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