Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCPGKKAGDHIATAIHDFEGHQTYTEKPGHNFTLNATFAEIKPESYDAL 84
Cdd:cd03169    1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  85 VIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADipvDQAVTD 164
Cdd:cd03169   81 VIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVD---DGVVVD 157

                        170       180
                 ....*....|....*....|...
gi 501039978 165 GNLVTSPAWPAHPAWLSQFLTVL 187
Cdd:cd03169  158 GNLVTAQAWPDHPAFLREFLKLL 180

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCPGKKAGDHIATAIHDFEGHQTYTEKPGHNFTLNATFAEIKPESYDAL 84
Cdd:cd03169    1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  85 VIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADipvDQAVTD 164
Cdd:cd03169   81 VIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVD---DGVVVD 157

                        170       180
                 ....*....|....*....|...
gi 501039978 165 GNLVTSPAWPAHPAWLSQFLTVL 187
Cdd:cd03169  158 GNLVTAQAWPDHPAFLREFLKLL 180

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978    5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCpgKKAGdhiataihdfeghqTYTEKPGHNFTLNATFAEIKPESYDAL 84
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAG--------------TTVGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   85 VIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADIpvDQAVTD 164
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDI--EVVVVD 142

                         170       180
                  ....*....|....*....|....
gi 501039978  165 GNLVTSPAWPAHPAWLSQFLTVLG 188
Cdd:TIGR01382 143 GNLVTSRVPDDLPAFNREFLKLLG 166

isoprenoid biosynthesis glyoxalase ElbB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  74 AEIKPESYDALVIPGG-----------RAPEYLRLDDKVIAVVKHFFEANKPVAAVChGAQLLaAARVLEGR---TCSAY 139
Cdd:PRK11780  79 AEADAEDFDALIVPGGfgaaknlsnfaVKGAECTVNPDVKALVRAFHQAGKPIGFIC-IAPAM-LPKILGAGvklTIGND 156

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501039978 140 PACRPEVELAGGKYADIPVDQAVTD--GNLVTSPAW 173
Cdd:PRK11780 157 EDTAAAIEKMGGEHVDCPVDDIVVDeeNKVVTTPAY 192

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCPGKKAGDHIATAIHDFEGHQTYTEKPGHNFTLNATFAEIKPESYDAL 84
Cdd:cd03169    1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  85 VIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADipvDQAVTD 164
Cdd:cd03169   81 VIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVD---DGVVVD 157

                        170       180
                 ....*....|....*....|...
gi 501039978 165 GNLVTSPAWPAHPAWLSQFLTVL 187
Cdd:cd03169  158 GNLVTAQAWPDHPAFLREFLKLL 180

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978    5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCpgKKAGdhiataihdfeghqTYTEKPGHNFTLNATFAEIKPESYDAL 84
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAG--------------TTVGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   85 VIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADIpvDQAVTD 164
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDI--EVVVVD 142

                         170       180
                  ....*....|....*....|....
gi 501039978  165 GNLVTSPAWPAHPAWLSQFLTVLG 188
Cdd:TIGR01382 143 GNLVTSRVPDDLPAFNREFLKLLG 166

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   5 KILMLCGDFGEDYETMVPFQTLLTVGHTVHAVCPgkkagdhiataihdfEGHQTYTEKPGHN-FTLNATFAEIKPESYDA 83
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGP---------------EAGGEIQGKHGYDtVTVDLTIADVDADDYDA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  84 LVIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAGGKYADIPVdqaVT 163
Cdd:cd03134   66 LVIPGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEV---VV 142

                 ....*..
gi 501039978 164 DGNLVTS 170
Cdd:cd03134  143 DGNLITS 149

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  18 ETMVPFQTLLTVGHTVHAVCP-GKKAGdhiataiHDFEGHQTYTEKPGHNFTLNATF----------AEIKPESYDALVI 86
Cdd:cd03141   24 ELAHPYDVFTEAGYEVDFASPkGGKVP-------LDPRSLDAEDDDDASVFDNDEEFkkklantkklSDVDPSDYDAIFI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  87 PGGRAPEY-LRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAAR------VLEGRTCSAYPAC-------------RPEV 146
Cdd:cd03141   97 PGGHGPMFdLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVAGKTVTGFTNEeeeaaglkkvvpfLLED 176

                        170       180       190
                 ....*....|....*....|....*....|..
gi 501039978 147 EL--AGGKY--ADIPVDQAVTDGNLVT--SPA 172
Cdd:cd03141  177 ELkeLGANYvkAEPWAEFVVVDGRLITgqNPA 208

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        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501039978  74 AEIKPESYDALVIPGGRA-PEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLL 125
Cdd:cd03128   40 SDVDLDDYDGLILPGGPGtPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  63 PGHNFTLNATFAEikPESYDALVIPGGRAPEYLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPAC 142
Cdd:cd03139   47 SGLTVLPDTSFAD--PPDLDVLLVPGGGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAA 124

                         90       100       110
                 ....*....|....*....|....*....|
gi 501039978 143 RPEVElaggKYADIPVDQA--VTDGNLVTS 170
Cdd:cd03139  125 IDWLK----EFGAIVVVDArwVVDGNIWTS 150

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  78 PESYDALVIPGGRAPEyLRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPEVELAggkYADIP 157
Cdd:COG4977   64 LAAADTLIVPGGLDPA-AAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAER---FPDVR 139

                         90
                 ....*....|....*.
gi 501039978 158 VDQA---VTDGNLVTS 170
Cdd:COG4977  140 VDPDrlyVDDGDILTS 155

Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  74 AEIKPESYDALVIPGG------------RAPEYlRLDDKVIAVVKHFFEANKPVAAVCHGAQLlaAARVLeGRTCSAYPA 141
Cdd:cd03133   76 AKLKAADFDALIFPGGfgaaknlsdfavKGADC-TVNPEVERLVREFHQAGKPIGAICIAPAL--AAKIL-GEGVEVTIG 151

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501039978 142 CRPEVELA----GGKYADIPVDQAVTD--GNLVTSPAW 173
Cdd:cd03133  152 NDAGTAAAiekmGAEHVNCPVEEIVVDekNKVVTTPAY 189

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501039978  70 NATFAEIKPESYDALVI---PGGraPEYLrldDKVIAVVKHFFEANKPVAAVCHGAQLLAAA 128
Cdd:cd01744   29 NTDAEEILKLDPDGIFLsngPGD--PALL---DEAIKTVRKLLGKKIPIFGICLGHQLLALA 85

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501039978  78 PESYDALVIPGGRA-PEYLRLD--DKVIAVVKHFFEANKPVAAVCHGAQLLAAA 128
Cdd:cd01741   44 LDDYDGLVILGGPMsVDEDDYPwlKKLKELIRQALAAGKPVLGICLGHQLLARA 97

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501039978  78 PESYDALVIPGGRAPEYlRLDDKVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEGRTCSAYPACRPE 145
Cdd:cd03136   62 APPLDYLFVVGGLGARR-AVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEA 128

glutamine amidotransferase subunit PdxT; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978  52 DFEGHQTYTEKPGHNFTLNATFAEIK-----PESyDALVIPGGRAPEYLRLDDK--VIAVVKHFFEANKPVAAVCHGAQL 124
Cdd:PRK13527  11 DVEEHIDALKRALDELGIDGEVVEVRrpgdlPDC-DALIIPGGESTTIGRLMKRegILDEIKEKIEEGLPILGTCAGLIL 89

                 ..
gi 501039978 125 LA 126
Cdd:PRK13527  90 LA 91

ThiJ/PfpI family-like; This is a family of fungal and bacterial ThiJ/PfpI-like proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501039978   12 DFGED-YETMVPFQTLLTVGHTVHAVCP-------------GKKAgdHIATAIHD----FEGHQTYTE--KPGHNFTLNA 71
Cdd:pfam17124   3 DEGYDvTEVCIPWRYFTDHGFMVEFATPhgivpqadqrllsGWKG--KLLGASKEakdiYSRMSTLEEftNPLSWSSEGF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501039978   72 TFaeikpESYDALVIPGGRAP---EYL---RLDDKV---IAVVKHFFEANKPVAAVCHGAQLLAAAR 129
Cdd:pfam17124  81 TL-----TPYDLVLIPGGHDPgvrELVdspRLHSLLvpyLPLCKRIGSPSKVLGAICQGVLALSEAA 142

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        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501039978  69 LNATFAEIKPESYDALVIPGGRAPEYlrlDDKVIAVVKHFFEANKPVAAVCHGAQLLA 126
Cdd:cd01742   30 NTTPLEEIKLKNPKGIILSGGPSSVY---EEDAPRVDPEIFELGVPVLGICYGMQLIA 84

imidazole glycerol phosphate synthase subunit HisH; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501039978  61 EKPGHNFTLNATFAEIKpeSYDALVIPG----GRAPEYLR---LDDkviaVVKHFFEANKPVAAVCHGAQLLA 126
Cdd:PRK13181  20 KRLGVEAVVSSDPEEIA--GADKVILPGvgafGQAMRSLResgLDE----ALKEHVEKKQPVLGICLGMQLLF 86

phosphoribosylformylglycinamidine synthase subunit PurQ;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501039978  73 FAEIKPESYDALVIPGG--------------RAPeylrlddkVIAVVKHFFEANKPVAAVCHGAQLLAAARVLEG 133
Cdd:PRK03619  34 HKETDLDGVDAVVLPGGfsygdylrcgaiaaFSP--------IMKAVKEFAEKGKPVLGICNGFQILTEAGLLPG 100