Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495200772   2 SALPATACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSL 48
Cdd:cd01743  138 DLLEVTASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495200772   2 SALPATACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSL 48
Cdd:cd01743  138 DLLEVTASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184

anthranilate synthase component II; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495200772   7 TACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSLALA 51
Cdd:PRK05670 144 TAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFLELA 188

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495200772   2 SALPATACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSL 48
Cdd:cd01743  138 DLLEVTASTEDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184

anthranilate synthase component II; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495200772   7 TACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSLALA 51
Cdd:PRK05670 144 TAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFLELA 188

anthranilate synthase component II;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495200772   4 LPATACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRNSLAL 50
Cdd:PRK06895 142 LEITAVCDENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWLAI 188

anthranilate synthase component I;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495200772   4 LPATACPDDGVNRAARQRTRPIESVPFHPESI---GTDYGIKMIRNSLALA 51
Cdd:PRK13566 668 LLVTAETEDGVIMAIEHKTLPVAAVQFHPESImtlGGDVGLRIIENVVRLL 718

aminodeoxychorismate/anthranilate synthase component II;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495200772   6 ATACPDDGVNRAARQRTRPIESVPFHPESIGTDYGIKMIRN 46
Cdd:PRK07649 143 VTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQN 183

anthranilate synthase component 2

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495200772   2 SALPATACPDDGVNRAARQRTRP-IESVPFHPESIGTDYGIKMIRNSLALAN 52
Cdd:CHL00101 139 SPLEITAWTEDGLIMACRHKKYKmLRGIQFHPESLLTTHGQQILRNFLSLSS 190

aminodeoxychorismate synthase component II;

                         10        20        30
                 ....*....|....*....|....*....|
gi 495200772  19 RQRTRPIESVPFHPESIGTDYGIKMIRNSL 48
Cdd:PRK06774 160 RHRTLPLEGVQFHPESILSEQGHQLLDNFL 189

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.

                         10        20        30
                 ....*....|....*....|....*....|
gi 495200772  17 AARQRTRPIESVPFHPESIGTDYGIKMIRN 46
Cdd:cd01742  150 AIANEEKKIYGVQFHPEVTHTEKGKEILKN 179