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Conserved domains on  [gi|24665102|ref|NP_730120|]
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lethal (3) 72Dr [Drosophila melanogaster]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 10109835)

type 1 glutamine amidotransferase (GATase1) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 23-313 3.34e-152

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


:

Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 428.66  E-value: 3.34e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102  23 IDIATQLQQNFS--GAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGAVFIDeadrqanpdvTS 100
Cdd:cd01747   1 IGILTQPVDGAGsnKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID----------TS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 101 DCVRSAELIYQLAMERNmrakkldDRGAYFPVWGTCLGFQLILIHAAEAPNVRIACQPMREAMPVTLTDDYQQSQLLGSL 180
Cdd:cd01747  71 GYARTAKIIYNLALERN-------DAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRF 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 181 PKSVADEMEKHPFACHQHRYCITKESLESYGLAKDWHPLATQK-DTSGLEFITIVEHRRFPIFGCQFHPERAAFEQLFNs 259
Cdd:cd01747 144 PPDLLKSLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNdDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKS- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665102 260 pdkCYMAHSRMGIDLSQIFGSRFVDFCRRNNNQFESDKLKTRHLIWNWQPVFSG 313
Cdd:cd01747 223 ---SSIPHSEEAIRLTQYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 23-313 3.34e-152

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 428.66  E-value: 3.34e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102  23 IDIATQLQQNFS--GAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGAVFIDeadrqanpdvTS 100
Cdd:cd01747   1 IGILTQPVDGAGsnKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID----------TS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 101 DCVRSAELIYQLAMERNmrakkldDRGAYFPVWGTCLGFQLILIHAAEAPNVRIACQPMREAMPVTLTDDYQQSQLLGSL 180
Cdd:cd01747  71 GYARTAKIIYNLALERN-------DAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRF 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 181 PKSVADEMEKHPFACHQHRYCITKESLESYGLAKDWHPLATQK-DTSGLEFITIVEHRRFPIFGCQFHPERAAFEQLFNs 259
Cdd:cd01747 144 PPDLLKSLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNdDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKS- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665102 260 pdkCYMAHSRMGIDLSQIFGSRFVDFCRRNNNQFESDKLKTRHLIWNWQPVFSG 313
Cdd:cd01747 223 ---SSIPHSEEAIRLTQYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 16-249 1.97e-21

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 90.78  E-value: 1.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102    16 PTVGVMCiDIATQLQQNFSGAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGAVfIDEADRQAN 95
Cdd:pfam07722   1 PVIGITA-NEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPN-VDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102    96 PDVTSDCVRSAELIYQLAMERNMRAkklddrgAYFPVWGTCLGFQLIlihaaeapNVriacqpmreAMPVTLtddYQQSQ 175
Cdd:pfam07722  79 PSESGGPYDPARDAYELALIRAALA-------RGKPILGICRGFQLL--------NV---------ALGGTL---YQDIQ 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102   176 LLGSLPKSVADEMEKHPFACHQ-----------------------HRYCITKeslesygLAKDWHPLATQKDtsGL-EFI 231
Cdd:pfam07722 132 EQPGFTDHREHCQVAPYAPSHAvnvepgsllasllgseefrvnslHHQAIDR-------LAPGLRVEAVAPD--GTiEAI 202

                         250
                  ....*....|....*...
gi 24665102   232 TIVEHRRFpIFGCQFHPE 249
Cdd:pfam07722 203 ESPNAKGF-ALGVQWHPE 219
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 131-249 6.61e-04

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 40.70  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 131 PVWGTCLGFQLIlIHAAEApnvRIACQPMREA--MPVTLTDDyqqSQLLGSLPKsvademekhPFACHQ-HRYCITKesl 207
Cdd:COG0518  84 PVLGICYGAQLL-AHALGG---KVEPGPGREIgwAPVELTEA---DPLFAGLPD---------EFTVWMsHGDTVTE--- 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24665102 208 esygLAKDWHPLAtqkdTSGLEFITIVEHRRfPIFGCQFHPE 249
Cdd:COG0518 145 ----LPEGAEVLA----SSDNCPNQAFRYGR-RVYGVQFHPE 177
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 23-313 3.34e-152

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 428.66  E-value: 3.34e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102  23 IDIATQLQQNFS--GAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGAVFIDeadrqanpdvTS 100
Cdd:cd01747   1 IGILTQPVDGAGsnKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDID----------TS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 101 DCVRSAELIYQLAMERNmrakkldDRGAYFPVWGTCLGFQLILIHAAEAPNVRIACQPMREAMPVTLTDDYQQSQLLGSL 180
Cdd:cd01747  71 GYARTAKIIYNLALERN-------DAGDYFPVWGTCLGFELLTYLTSGETLLLEATEATNSALPLNFTEDALQSRLFKRF 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 181 PKSVADEMEKHPFACHQHRYCITKESLESYGLAKDWHPLATQK-DTSGLEFITIVEHRRFPIFGCQFHPERAAFEQLFNs 259
Cdd:cd01747 144 PPDLLKSLATEPLTMNNHRYGISPENFTENGLLSDFFNVLTTNdDWNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKS- 222

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665102 260 pdkCYMAHSRMGIDLSQIFGSRFVDFCRRNNNQFESDKLKTRHLIWNWQPVFSG 313
Cdd:cd01747 223 ---SSIPHSEEAIRLTQYFANFFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 16-249 1.97e-21

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 90.78  E-value: 1.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102    16 PTVGVMCiDIATQLQQNFSGAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGAVfIDEADRQAN 95
Cdd:pfam07722   1 PVIGITA-NEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPN-VDPHFYGEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102    96 PDVTSDCVRSAELIYQLAMERNMRAkklddrgAYFPVWGTCLGFQLIlihaaeapNVriacqpmreAMPVTLtddYQQSQ 175
Cdd:pfam07722  79 PSESGGPYDPARDAYELALIRAALA-------RGKPILGICRGFQLL--------NV---------ALGGTL---YQDIQ 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102   176 LLGSLPKSVADEMEKHPFACHQ-----------------------HRYCITKeslesygLAKDWHPLATQKDtsGL-EFI 231
Cdd:pfam07722 132 EQPGFTDHREHCQVAPYAPSHAvnvepgsllasllgseefrvnslHHQAIDR-------LAPGLRVEAVAPD--GTiEAI 202

                         250
                  ....*....|....*...
gi 24665102   232 TIVEHRRFpIFGCQFHPE 249
Cdd:pfam07722 203 ESPNAKGF-ALGVQWHPE 219
GATase pfam00117
Glutamine amidotransferase class-I;
77-249 3.74e-11

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 61.48  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102    77 GILLPGGavfideadrqanPDVTSDCVRSAELIyQLAMERNmrakklddrgayFPVWGTCLGFQLIlIHAAEAPNVRIAC 156
Cdd:pfam00117  43 GIILSGG------------PGSPGAAGGAIEAI-REARELK------------IPILGICLGHQLL-ALAFGGKVVKAKK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102   157 QPMREA-MPVtltDDYQQSQLLGSLPKSVAdemekhpfaCHQHRYCITKESLEsyglaKDWHPLATQKDTSGLEFItivE 235
Cdd:pfam00117  97 FGHHGKnSPV---GDDGCGLFYGLPNVFIV---------RRYHSYAVDPDTLP-----DGLEVTATSENDGTIMGI---R 156

                         170
                  ....*....|....
gi 24665102   236 HRRFPIFGCQFHPE 249
Cdd:pfam00117 157 HKKLPIFGVQFHPE 170
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 33-144 2.25e-06

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: 46.05  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102  33 FSGAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGavfideadrqanPDVTSDCVRSAELIyql 112
Cdd:cd01653   5 LFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGG------------PGTPDDLARDEALL--- 69

                        90       100       110
                ....*....|....*....|....*....|..
gi 24665102 113 amernMRAKKLDDRGAyfPVWGTCLGFQLILI 144
Cdd:cd01653  70 -----ALLREAAAAGK--PILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 33-142 1.03e-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: 43.34  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102  33 FSGAYHSYLAASYVKFLEASGAHVVPIWIGRERAYYALMMSQLNGILLPGGavfideadrqanPDVTSDCVRSAELIyql 112
Cdd:cd03128   5 LFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGG------------PGTPDDLAWDEALL--- 69

                        90       100       110
                ....*....|....*....|....*....|
gi 24665102 113 amernMRAKKLDDRGAyfPVWGTCLGFQLI 142
Cdd:cd03128  70 -----ALLREAAAAGK--PVLGICLGAQLL 92
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 131-249 3.95e-04

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.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 40.60  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 131 PVWGTCLGFQLIlihaAEAPNVRIACQPMREAMPVTLTDDYQqSQLLGSLPKSV------ADEMEKhpfachqhrycitk 204
Cdd:cd01742  72 PVLGICYGMQLI----AKALGGKVERGDKREYGKAEIEIDDS-SPLFEGLPDEQtvwmshGDEVVK-------------- 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24665102 205 eslesygLAKDWHPLATQKDTSglefITIVEHRRFPIFGCQFHPE 249
Cdd:cd01742 133 -------LPEGFKVIASSDNCP----VAAIANEEKKIYGVQFHPE 166
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 131-249 6.61e-04

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 40.70  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665102 131 PVWGTCLGFQLIlIHAAEApnvRIACQPMREA--MPVTLTDDyqqSQLLGSLPKsvademekhPFACHQ-HRYCITKesl 207
Cdd:COG0518  84 PVLGICYGAQLL-AHALGG---KVEPGPGREIgwAPVELTEA---DPLFAGLPD---------EFTVWMsHGDTVTE--- 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24665102 208 esygLAKDWHPLAtqkdTSGLEFITIVEHRRfPIFGCQFHPE 249
Cdd:COG0518 145 ----LPEGAEVLA----SSDNCPNQAFRYGR-RVYGVQFHPE 177
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 217-249 1.08e-03

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.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 39.44  E-value: 1.08e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24665102 217 HPLATQKDTSGLEFITI----------VEHRRFPIFGCQFHPE 249
Cdd:cd01743 127 HSLVVDPDPLPDLLEVTastedgvimaLRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 234-249 2.56e-03

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 38.48  E-value: 2.56e-03
                        10
                ....*....|....*.
gi 24665102 234 VEHRRFPIFGCQFHPE 249
Cdd:COG0512 154 IRHRELPIEGVQFHPE 169
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 227-250 7.03e-03

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 37.33  E-value: 7.03e-03
                        10        20
                ....*....|....*....|....
gi 24665102 227 GLEFITIVEHRrfPIFGCQFHPER 250
Cdd:COG0118 165 GVPFTAAVERG--NVFGTQFHPEK 186
 
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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