(data stored in ACNUC30630 zone)

HOGENOM: VIPAR1_1_PE1957

ID   VIPAR1_1_PE1957                      STANDARD;      PRT;   196 AA.
AC   VIPAR1_1_PE1957; P22101;
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=Anthranilate synthase component II; EC=4.1.3 27;AltName:
DE   Full=Glutamine amido-transferase; (VIPAR1_1.PE1957).
GN   Name=trpG; OrderedLocusNames=VP1957;
OS   VIBRIO PARAHAEMOLYTICUS RIMD 2210633.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS VIPAR1_1.PE1957.
CC       Vibrio parahaemolyticus RIMD 2210633 chromosome chromosome 1, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPG_VIBPA
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Contains 2 chains with different activities: component I
CC       catalyzes the formation of anthranilate using ammonia rather than
CC       glutamine, whereas component II provides glutamine
CC       amidotransferase activity.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- GENE_FAMILY: HOG000025029 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P22101; -.
DR   EMBL; X17149; CAA35032.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60220.1; -; Genomic_DNA.
DR   RefSeq; NP_798336.1; NC_004603.1.
DR   ProteinModelPortal; P22101; -.
DR   SMR; P22101; 2-193.
DR   GeneID; 1189468; -.
DR   GenomeReviews; BA000031_GR; VP1957.
DR   KEGG; vpa:VP1957; -.
DR   NMPDR; fig|223926.1.peg.1957; -.
DR   OMA; YGGKVER; -.
DR   ProtClustDB; PRK05670; -.
DR   BioCyc; VPAR223926:VP1957-MON; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic 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; VIPAR1_1.PE1957; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Glutamine amidotransferase; Lyase;
KW   Tryptophan biosynthesis.
SQ   SEQUENCE   196 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MANIVFIDNF DSFTYNLVDQ FRSLGHSVKI YRNHIPAETI EQAINELENP VVLLSPGPGA
     PSEAGSMPEL IQRMKGKVPM IGICLGHQAI VEAYGGTVAG AGEIIHGKVS MMEHQDHAIY
     QNLPSPLAIA RYHSLVATKV PDSLTITAEV DNLVMSVVHE QDKVCGFQFH PESIMTTYGA
     TLLGNAIEWA LEKNNA
//

If you have problems or comments...

PBIL Back to PBIL home page