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Conserved domains on  [gi|6323984|ref|NP_014055|]
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glutathione-independent methylglyoxalase family protein [Saccharomyces cerevisiae S288C]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-235 4.20e-114

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.


The actual alignment was detected with superfamily member cd03147:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 231  Bit Score: 325.82  E-value: 4.20e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    5 RALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKA 84
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   85 LARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITG 164
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPKTGKPLIKGKTVTG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323984  165 FPLEGEIALGVDDILRSRKLTTVERVANKNRAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINAL 235
Cdd:cd03147 161 FTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
 
Name Accession Description Interval E-value
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 5-235 4.20e-114

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 325.82  E-value: 4.20e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    5 RALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKA 84
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   85 LARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITG 164
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPKTGKPLIKGKTVTG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323984  165 FPLEGEIALGVDDILRSRKLTTVERVANKNRAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINAL 235
Cdd:cd03147 161 FTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-224 3.00e-19

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 81.69  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    1 MTpKRALISLTSyhgpfykdgaktGVFVVEILRSFDTFEKHGFEVDFVSETGGfgwdehylpksfiggedkmnfETKNSA 80
Cdd:COG0693   1 MM-KKVLILLTD------------GFEDEELTVPYDALREAGAEVDVASPEGG---------------------PPVTSK 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   81 FNKALARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLfdgLIDIkttrPLIEGK 160
Cdd:COG0693  47 HGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAV---LAAA----GLLKGR 119

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323984  161 AITGFPlegeialGVDDILRsrklttvervanKNRAKYLapihpwDDYSITDGKLVTGVNANSS 224
Cdd:COG0693 120 KVTSFP-------NIEDDLK------------NAGATYV------DEEVVVDGNLITSRGPGDA 158
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 29-166 9.59e-06

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]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 44.33  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984     29 VEILRSFDTFEKHGFEVDFVSETGGFGWDEHylpksfiggEDKMNFEtknsafnkalariKTANEVNASDYKIFFASAGH 108
Cdd:TIGR01382  13 SELLYPLDRLREAGHEVDTVSKEAGTTVGKH---------GYSVTVD-------------ATIDEVNPEEYDALVIPGGR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323984    109 GAlfDYPKA-KNLQDIASKIYANGGVIAAICHGPLLfdgLIDIKTTRplieGKAITGFP 166
Cdd:TIGR01382  71 AP--EYLRLnNKAVRLVREFVEKGKPVAAICHGPQL---LISAGVLR----GKKLTSYP 120
PRK04155 PRK04155
protein deglycase HchA;
24-166 1.11e-03

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 39.21  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    24 TGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHY-LPKsfiggEDkmnfETKNSAFNKALARIKT--------ANEV 94
Cdd:PRK04155  72 TGNHPVETLLPMYHLHKAGFEFDVATLSGNPVKFEYWaMPH-----ED----EAVMGFYEKYKSKFKQpkkladvvANLL 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323984    95 NA-SDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGP--LLFDGLIDiktTRPLIEGKAITGFP 166
Cdd:PRK04155 143 APdSDYAAVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPaaLLAAGVDH---GDNPLNGYSICAFP 214
 
Name Accession Description Interval E-value
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 5-235 4.20e-114

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 325.82  E-value: 4.20e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    5 RALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKA 84
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   85 LARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITG 164
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPKTGKPLIKGKTVTG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323984  165 FPLEGEIALGVDDILRSRKLTTVERVANKNRAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINAL 235
Cdd:cd03147 161 FTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 6-235 5.10e-65

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.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 200.86  E-value: 5.10e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    6 ALISLTSYHGPfYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGF-GWDEHYLPKSFiggEDKMNFETKNSAFNKA 84
Cdd:cd03141   1 ILIVLTSADKL-GGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKvPLDPRSLDAED---DDDASVFDNDEEFKKK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   85 LARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDiKTTRPLIEGKAITG 164
Cdd:cd03141  77 LANTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKL-SDGKSLVAGKTVTG 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323984  165 FPLEGEIALGVDDILrsrkLTTVERVANKNRAKYLAPiHPWDDYSITDGKLVTGVNANSSYSTTIRAINAL 235
Cdd:cd03141 156 FTNEEEEAAGLKKVV----PFLLEDELKELGANYVKA-EPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-224 3.00e-19

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 81.69  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    1 MTpKRALISLTSyhgpfykdgaktGVFVVEILRSFDTFEKHGFEVDFVSETGGfgwdehylpksfiggedkmnfETKNSA 80
Cdd:COG0693   1 MM-KKVLILLTD------------GFEDEELTVPYDALREAGAEVDVASPEGG---------------------PPVTSK 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   81 FNKALARIKTANEVNASDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLfdgLIDIkttrPLIEGK 160
Cdd:COG0693  47 HGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAV---LAAA----GLLKGR 119

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323984  161 AITGFPlegeialGVDDILRsrklttvervanKNRAKYLapihpwDDYSITDGKLVTGVNANSS 224
Cdd:COG0693 120 KVTSFP-------NIEDDLK------------NAGATYV------DEEVVVDGNLITSRGPGDA 158
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 89-166 3.45e-06

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.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 45.61  E-value: 3.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   89 KTANEVNASDYKIFFASAGHGA--LFDYPKAknlQDIASKIYANGGVIAAICHGPLLfdgLIDIKttrpLIEGKAITGFP 166
Cdd:cd03134  53 LTIADVDADDYDALVIPGGTNPdkLRRDPDA---VAFVRAFAEAGKPVAAICHGPWV---LISAG----VVRGRKLTSYP 122
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 29-166 9.59e-06

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]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 44.33  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984     29 VEILRSFDTFEKHGFEVDFVSETGGFGWDEHylpksfiggEDKMNFEtknsafnkalariKTANEVNASDYKIFFASAGH 108
Cdd:TIGR01382  13 SELLYPLDRLREAGHEVDTVSKEAGTTVGKH---------GYSVTVD-------------ATIDEVNPEEYDALVIPGGR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323984    109 GAlfDYPKA-KNLQDIASKIYANGGVIAAICHGPLLfdgLIDIKTTRplieGKAITGFP 166
Cdd:TIGR01382  71 AP--EYLRLnNKAVRLVREFVEKGKPVAAICHGPQL---LISAGVLR----GKKLTSYP 120
GATase1_EcHsp31_like cd03148
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ...
 24-166 3.26e-05

Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31); Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. 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 GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. 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. EcHsp31 is a homodimer.


Pssm-ID: 153242 [Multi-domain]  Cd Length: 232  Bit Score: 43.71  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   24 TGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHY-LPK---SFIGGEDKMNFETKNSafnKALARIKTANEVNASDY 99
Cdd:cd03148  21 TGNHPVEMLLPLYHLHAAGFDFDVATLSGLPVKFEYWaMPHedeAVMPFFEKHKSKLRNP---KKLADVVASLNADDSEY 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323984  100 KIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLiDIKTTRPLIEGKAITGFP 166
Cdd:cd03148  98 AAVFIPGGHGALIGIPESQDVAAALQWAIKNDRFVITLCHGPAAFLAA-RHGGGKNPLEGYSVCVFP 163
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 25-143 3.68e-05

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes 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. and, the A4 beta-galactosidase middle domain. 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, 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. 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.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 41.82  E-value: 3.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   25 GVFVVEILRSFDTFEKHGFEVDFVSETGGfgwdehylpksfiggedkmnfetknsafnkalariKTANEVNASDYKIFFA 104
Cdd:cd01653   8 GFEELELASPLDALREAGAEVDVVSPDGG-----------------------------------PVESDVDLDDYDGLIL 52

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323984  105 SAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLL 143
Cdd:cd01653  53 PGGPGTPDDLARDEALLALLREAAAAGKPILGICLGAQL 91
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 25-143 8.54e-05

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.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 40.26  E-value: 8.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   25 GVFVVEILRSFDTFEKHGFEVDFVSETGGfgwdehylpksfiggedkmnfetknsafnkalariKTANEVNASDYKIFFA 104
Cdd:cd03128   8 GSEELELASPLDALREAGAEVDVVSPDGG-----------------------------------PVESDVDLDDYDGLIL 52

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323984  105 SAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLL 143
Cdd:cd03128  53 PGGPGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQL 91
PRK04155 PRK04155
protein deglycase HchA;
24-166 1.11e-03

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 39.21  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984    24 TGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHY-LPKsfiggEDkmnfETKNSAFNKALARIKT--------ANEV 94
Cdd:PRK04155  72 TGNHPVETLLPMYHLHKAGFEFDVATLSGNPVKFEYWaMPH-----ED----EAVMGFYEKYKSKFKQpkkladvvANLL 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323984    95 NA-SDYKIFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGP--LLFDGLIDiktTRPLIEGKAITGFP 166
Cdd:PRK04155 143 APdSDYAAVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPaaLLAAGVDH---GDNPLNGYSICAFP 214
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 36-186 7.66e-03

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.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 35.99  E-value: 7.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323984   36 DTFEKHGFEVDFVSETGGfgwdehylpksfiggedkmnfETKNSAFNKALARIKTANEVNASDYKIFFASAGHGALFDYP 115
Cdd:cd03135  19 DVLRRAGIEVTTASLEKK---------------------LAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323984  116 KAKNLQDIASKIYANGGVIAAICHGPLLFDGLIdikttrpLIEGKAITGFPLEGEIALGV----DDILRSRKLTT 186
Cdd:cd03135  78 DNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAG-------LLKGKKATCYPGFEDKLGGAnyvdEPVVVDGNIIT 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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