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 779978590   5 TLVLLYPGAISYEVMYAIECLGAYGKVDITT--PENHNHTDSSGLRICPTVNFEDVCITDYQALLVPGGNPDSIMGSDQI 82
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYEGFEVRTvsPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779978590  83 ASFIQKAHESSLVIGGICAGVLVLARAGILKGVKITHN---YTEKYAPessvqltrPYWEGAIYEESLVQVDKRIVTAMP 159
Cdd:cd03140   81 AGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNsldFLKAHAP--------YYGGAEYYDEPQAVSDGNLITANG 152

                        170
                 ....*....|....*.
gi 779978590 160 NGYVDFGLAVAEALEL 175
Cdd:cd03140  153 TAPVEFAAEILRALDV 168

transcriptional activator FtrA; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 779978590  86 IQKAHESSLVIGGICAGVLVLARAGILKGVKI-TH-NYTEKYA---PESSVQ 132
Cdd:PRK09393  99 LRAAHARGARLCSICSGVFVLAAAGLLDGRRAtTHwRYAERLQaryPAIRVD 150

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 779978590   5 TLVLLYPGAISYEVMYAIECLGAYGKVDITT--PENHNHTDSSGLRICPTVNFEDVCITDYQALLVPGGNPDSIMGSDQI 82
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYEGFEVRTvsPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779978590  83 ASFIQKAHESSLVIGGICAGVLVLARAGILKGVKITHN---YTEKYAPessvqltrPYWEGAIYEESLVQVDKRIVTAMP 159
Cdd:cd03140   81 AGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNsldFLKAHAP--------YYGGAEYYDEPQAVSDGNLITANG 152

                        170
                 ....*....|....*.
gi 779978590 160 NGYVDFGLAVAEALEL 175
Cdd:cd03140  153 TAPVEFAAEILRALDV 168

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779978590  42 TDSSGLRICPTVNFEDVCITDYQALLVPGGNPdsimGSDQIAS------FIQKAHESSLVIGGICAGVLVLARAGILKGV 115
Cdd:cd03135   40 GSSHGIKVKADKTLSDVNLDDYDAIVIPGGLP----GAQNLADneklikLLKEFNAKGKLIAAICAAPAVLAKAGLLKGK 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 779978590 116 KITHnytekyAPESSVQLtrpywEGAIYEESLVQVDKRIVTAM-PNGYVDFGLAVAEAL 173
Cdd:cd03135  116 KATC------YPGFEDKL-----GGANYVDEPVVVDGNIITSRgPGTAFEFALKIVEAL 163

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 779978590   8 LLYPgaisyevMYAIECLGAygKVDITTPENH------NHTDSsglrICPTVNFEDVCITDYQALLVPGG-NPDSIMGSD 80
Cdd:cd03134   15 LTYP-------LYRLREAGA--EVVVAGPEAGgeiqgkHGYDT----VTVDLTIADVDADDYDALVIPGGtNPDKLRRDP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779978590  81 QIASFIQKAHESSLVIGGICAGVLVLARAGILKGVKIThnytekyapesSVQLTRPYWE--GAIYEESLVQVDKRIVTA 157
Cdd:cd03134   82 DAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLT-----------SYPSIKDDLInaGANWVDEEVVVDGNLITS 149

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 779978590  42 TDSSGLRICPTVNFEDvcITDYQALLVPGGNPDSI-MGSDQIASFIQKAHESSLVIGGICAGVLVLARAGILKGVKIThn 120
Cdd:cd03139   44 SSRSGLTVLPDTSFAD--PPDLDVLLVPGGGGTRAlVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRAT-- 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779978590 121 yTEKYAPEssvqLTRPYweGAIYEESL-VQVDKRIVTAmpnGYV----DFGLAVAEalELLDRKQKQFI 184
Cdd:cd03139  120 -THWAAID----WLKEF--GAIVVVDArWVVDGNIWTS---GGVsagiDMALALVA--RLFGEELAQAV 176

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. 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 the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779978590  44 SSGLRICPTVNFEDvcITDYQALLVPGGN-PDSIMGSDQIASFIQKAHESSLVIGGICAGVLVLARAGILKGVKIT--HN 120
Cdd:cd03137   48 SSGLSLVADAGLDA--LAAADTVIVPGGPdVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATthWA 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 779978590 121 YTEKYA---PESSVQltrpywEGAIYeeslVQvDKRIVTA 157
Cdd:cd03137  126 YAEDLArrfPAVRVD------PDVLY----VD-DGNVWTS 154

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779978590   6 LVLLYPGAISYEVMYAIECLGAYG-KVDITTPENHNHTDssglricptvnfeDVCITDYQALLVPGG--NPDSIMGSDQI 82
Cdd:cd03128    2 AVLLFGGSEELELASPLDALREAGaEVDVVSPDGGPVES-------------DVDLDDYDGLILPGGpgTPDDLAWDEAL 68

                         90       100
                 ....*....|....*....|....
gi 779978590  83 ASFIQKAHESSLVIGGICAGVLVL 106
Cdd:cd03128   69 LALLREAAAAGKPVLGICLGAQLL 92

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 779978590  56 EDVCITDYQALLVPGG---------NPDSimgsdqiASFIQKAHESSLVIGGICAGVLVLARAG------ILKGVKIT-- 118
Cdd:cd03141   84 SDVDPSDYDAIFIPGGhgpmfdlpdNPDL-------QDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVAGKTVTgf 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779978590 119 HNYTEKYAPESSVQltrPYW-------EGAIYEESL-----VQVDKRIVTAM-PNGYVDFGLAVAEAL 173
Cdd:cd03141  157 TNEEEEAAGLKKVV---PFLledelkeLGANYVKAEpwaefVVVDGRLITGQnPASAAAVAEALVKAL 221