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 488066355   4 ILLFVYPTFAEFEITVATALL--KKKYEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDEIHMKEAKPL 81
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLnsYEGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355  82 FSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTVTIDYQKLDCFP----VENFVYTEVVQHANIITAQGHAFVPFGL 157
Cdd:cd03140   81 AGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPyyggAEYYDEPQAVSDGNLITANGTAPVEFAA 160

                 ....*...
gi 488066355 158 AIASYFGV 165
Cdd:cd03140  161 EILRALDV 168

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 488066355   4 ILLFVYPTFAEFEITVATALL--KKKYEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDEIHMKEAKPL 81
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLnsYEGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355  82 FSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTVTIDYQKLDCFP----VENFVYTEVVQHANIITAQGHAFVPFGL 157
Cdd:cd03140   81 AGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPyyggAEYYDEPQAVSDGNLITANGTAPVEFAA 160

                 ....*...
gi 488066355 158 AIASYFGV 165
Cdd:cd03140  161 EILRALDV 168

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355    2 KKILLFVYPTFAEFEITVATALLKKK-YEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDEI--HMKEA 78
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAgIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGpeRLRDN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488066355   79 KPLFSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTVTIDYQKLDCFPVENFVYTEVVQHANIITAQG 149
Cdd:pfam01965  81 EKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRG 151

protein deglycase YajL;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488066355  40 IISETGLQVQPHIELSEVRVEEYEGIIIPGGdeihMKEAK-----PLF-SVIRQFSEQGKLVAAICAGP 102
Cdd:PRK11574  45 ITCSRGVKLLADAPLVEVADGDFDVIVLPGG----IKGAEcfrdsPLLvETVRQFHRSGRIVAAICAAP 109

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 488066355   4 ILLFVYPTFAEFEITVATALL--KKKYEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDEIHMKEAKPL 81
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLnsYEGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355  82 FSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTVTIDYQKLDCFP----VENFVYTEVVQHANIITAQGHAFVPFGL 157
Cdd:cd03140   81 AGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPyyggAEYYDEPQAVSDGNLITANGTAPVEFAA 160

                 ....*...
gi 488066355 158 AIASYFGV 165
Cdd:cd03140  161 EILRALDV 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 488066355   4 ILLFVYPTFAEFEITVATALLKK-KYEIITAGLT-KEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDE--IHMKEAK 79
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRaGIEVTTASLEkKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPgaQNLADNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355  80 PLFSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTvtidyqkldCFP-------VENFVYTEVVQHANIITAQG--H 150
Cdd:cd03135   81 KLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKAT---------CYPgfedklgGANYVDEPVVVDGNIITSRGpgT 151

                        170
                 ....*....|...
gi 488066355 151 AFvPFGLAIASYF 163
Cdd:cd03135  152 AF-EFALKIVEAL 163

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355    3 KILLFVYPTFAEFE-ITVATALLK--KKYEIITAGLT-KEMIISETGLQVQPHIELSEVRVEEYEGIIIPGGDE--IHMK 76
Cdd:TIGR01383   1 KVLVPLAPGFEEMEaVITVDVLRRagIKVTVAIAGLNgKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPgaENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355   77 EAKPLFSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTvtidyqkldCFP-----VENFVYTE---VVQHANIITAQ 148
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKAT---------CYPgfkekLLNGNYSVnktVVVDGNLITSR 151

                         170
                  ....*....|....*
gi 488066355  149 GHAFV-PFGLAIASY 162
Cdd:TIGR01383 152 GPGTAiEFALELVEL 166

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 488066355   2 KKILLFVYPTFAEFEITVATALL--------KKKYEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYegIIIPGGDEI 73
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFrlanrlagRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADT--LIVPGGLDP 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488066355  74 HMKEAKPLFSVIRQFSEQGKLVAAICAGPYALARAGL 110
Cdd:COG4977   79 AAAADPALLAWLRRAAARGARLASICTGAFLLAAAGL 115

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 488066355  45 GLQVQPHIELSEVRVEEYEGIIIPGG---DEIHMKEAkpLFSVIRQFSEQGKLVAAICAGPYALARAGLFKEISYTvtid 121
Cdd:cd03169   60 GHRFAVTADFDEVDPDDYDALVIPGGrapEYLRLDEK--VLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCT---- 133

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488066355 122 yqkldCFP-----VE----NFVYTEVVQHANIITAQG 149
Cdd:cd03169  134 -----AYPackpeVElaggTVVDDGVVVDGNLVTAQA 165

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 488066355   4 ILLFVYPTFAE------FEITVATALLKKKYEIITAGLTKEMIISETGLQVQPHIELSEVRVEEYegIIIPGG----DEI 73
Cdd:cd03139    1 VGILLFPGVEVldvigpYEVFGRAPRLAAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDV--LLVPGGggtrALV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488066355  74 HMKEakpLFSVIRQFSEQGKLVAAICAGPYALARAGLFKeiSYTVT---IDYQKLDCFPVENFVYTEVVQHANIITAQG 149
Cdd:cd03139   79 NDPA---LLDFIRRQAARAKYVTSVCTGALLLAAAGLLD--GRRATthwAAIDWLKEFGAIVVVDARWVVDGNIWTSGG 152

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488066355  52 IELSEVRVEEYEGIIIPGGdeiH-----MKEAKPLFSVIRQFSEQGKLVAAICAGPYALARAG------LFKeiSYTVT 119
Cdd:cd03141   81 KKLSDVDPSDYDAIFIPGG---HgpmfdLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVA--GKTVT 154

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 488066355  29 EIITAGLTKEMIISETGLQVQPHIELSEVrvEEYEGIIIPG----GDEIHMKEAKPLFSVIRQFSEQGKLVAAICAGPYA 104
Cdd:cd03138   39 EVRLVSLDGGPVLLAGGILILPDATLADV--PAPDLVIVPGlggdPDELLLADNPALIAWLRRQHANGATVAAACTGVFL 116

                 ....*..
gi 488066355 105 LARAGLF 111
Cdd:cd03138  117 LAEAGLL 123

protein deglycase YajL;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488066355  40 IISETGLQVQPHIELSEVRVEEYEGIIIPGGdeihMKEAK-----PLF-SVIRQFSEQGKLVAAICAGP 102
Cdd:PRK11574  45 ITCSRGVKLLADAPLVEVADGDFDVIVLPGG----IKGAEcfrdsPLLvETVRQFHRSGRIVAAICAAP 109

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT 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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488066355  56 EVRVEEYEGIIIPGG----DE-----IHMKeAKPLFSVIRQFSEQGKLVAAICAGPYALARAGLFkeISYTVTIDYQKLD 126
Cdd:cd01740   38 RKDLDDYDGVVLPGGfsygDYlragaIAAA-SPLLMEEVKEFAERGGLVLGICNGFQILVELGLL--PGALIRNKGLKFI 114

                         90       100
                 ....*....|....*....|.
gi 488066355 127 CFPVENFVYTEVVQHANIITA 147
Cdd:cd01740  115 CRWQNRFVTLRVENNDSPFTK 135