(data stored in ACNUC30630 zone)

HOGENOM: METTM_1_PE232

ID   METTM_1_PE232                        STANDARD;      PRT;   193 AA.
AC   METTM_1_PE232; P26923; D9PUE6;
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; (METTM_1.PE232).
GN   Name=trpG; OrderedLocusNames=MTBMA_c02350;
OS   METHANOTHERMOBACTER MARBURGENSIS STR. MARBURG.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS METTM_1.PE232.
CC       Methanothermobacter marburgensis str. Marburg chromosome, complete geno
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:TRPG_METTM
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   -!- SEQUENCE CAUTION:
CC       Sequence=ADL57844.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -!- GENE_FAMILY: HOG000025029 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P26923; D9PUE6; -.
DR   EMBL; M65060; AAA73029.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL57844.1; ALT_INIT; Genomic_DNA.
DR   PIR; G40362; G40362.
DR   RefSeq; YP_003849157.1; NC_014408.1.
DR   ProteinModelPortal; P26923; -.
DR   GeneID; 9703941; -.
DR   GenomeReviews; CP001710_GR; MTBMA_c02350.
DR   KEGG; mmg:MTBMA_c02350; -.
DR   OMA; LAHQVMH; -.
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; METTM_1.PE232; -.
KW   anthranilate synthase component II;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Glutamine amidotransferase; Lyase;
KW   Tryptophan biosynthesis.
SQ   SEQUENCE   193 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MILIIDNYDS FTHNLYQMAG EIMMEMDSAD IMVVRNDEVD IDYVRGLDPE RIIISPGPGN
     PIKREDFGIC SEVIGEFTDR PILGVCLGHQ GIFHYFGGVV GYGEPVHGKI SEVFHDGSEL
     FRGVPNPFRA TRYHSLRCEC SGVPEDILVS ASAPDGTIMA IRHRQYPVYG LQFHPESAGT
     PHGRDILENF LRM
//

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