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Conserved domains on  [gi|669033298|ref|NP_001288166|]
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CTP synthase 1 isoform b [Homo sapiens]

Protein Classification

CTP synthase( domain architecture ID 1000862)

cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis

CATH:  3.40.50.880
EC:  6.3.4.2
Gene Ontology:  GO:0003883|GO:0005524|GO:0006241|GO:0042802

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02327 super family cl33465
CTP synthase
 1-400 0e+00

CTP synthase


The actual alignment was detected with superfamily member PLN02327:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 615.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:PLN02327 157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYA 159
Cdd:PLN02327 237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYL 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPF 239
Cdd:PLN02327 315 SVLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPY 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 240 LGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLE 319
Cdd:PLN02327 395 LGICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVD 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYL 399
Cdd:PLN02327 475 ERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVL 554


                 .
gi 669033298 400 Q 400
Cdd:PLN02327 555 N 555
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-400 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 615.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:PLN02327 157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYA 159
Cdd:PLN02327 237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYL 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPF 239
Cdd:PLN02327 315 SVLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPY 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 240 LGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLE 319
Cdd:PLN02327 395 LGICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVD 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYL 399
Cdd:PLN02327 475 ERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVL 554


                 .
gi 669033298 400 Q 400
Cdd:PLN02327 555 N 555
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-394 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 555.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:COG0504  151 LPFLEAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNV 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYAS 160
Cdd:COG0504  231 PEEAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKS 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 161 VIKALEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFL 240
Cdd:COG0504  308 VVEALKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFL 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 241 GVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYL 318
Cdd:COG0504  378 GICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEI 454

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669033298 319 EERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 394
Cdd:COG0504  455 SERHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-390 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 519.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298    1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:TIGR00337 151 LPFLEAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDV 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYAS 160
Cdd:TIGR00337 231 EEEAVISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLS 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  161 VIKALEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFL 240
Cdd:TIGR00337 308 VIEALKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFL 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  241 GVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLE 319
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVY 454

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669033298  320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 390
Cdd:TIGR00337 455 ERHRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 143-388 5.79e-142

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 404.63  E-value: 5.79e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 143 CSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITsqeepvryheAWQKLCSAHGVLVPGGFGVRGT 222
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 223 EGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLF 301
Cdd:cd01746   71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 302 QtKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPS 381
Cdd:cd01746  151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                 ....*..
gi 669033298 382 PPYFGLL 388
Cdd:cd01746  229 PLFVGFV 235
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-116 3.13e-73

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 230.69  E-value: 3.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298    1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:pfam06418 150 LPFLEAIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNV 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 669033298   81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 116
Cdd:pfam06418 230 PKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-400 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 615.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:PLN02327 157 MPFIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHV 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYA 159
Cdd:PLN02327 237 PAENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYL 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPF 239
Cdd:PLN02327 315 SVLKALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPY 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 240 LGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLE 319
Cdd:PLN02327 395 LGICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVD 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYL 399
Cdd:PLN02327 475 ERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVL 554


                 .
gi 669033298 400 Q 400
Cdd:PLN02327 555 N 555
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-394 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 555.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:COG0504  151 LPFLEAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNV 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYAS 160
Cdd:COG0504  231 PEEAVISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKS 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 161 VIKALEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFL 240
Cdd:COG0504  308 VVEALKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFL 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 241 GVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYL 318
Cdd:COG0504  378 GICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEI 454

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669033298 319 EERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 394
Cdd:COG0504  455 SERHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
pyrG PRK05380
CTP synthetase; Validated
 1-394 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 555.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:PRK05380 150 LPFLEAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNV 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIeRQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYAS 160
Cdd:PRK05380 230 PEEAVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPD--LSEWEELVERLKNPKGEVTIALVGKYVELPDAYKS 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 161 VIKALEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFL 240
Cdd:PRK05380 307 VIEALKHAGIANDVKVNIKWIDSEDLEE----------ENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFL 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 241 GVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLFQtKNSVMRKLYGdADYLE 319
Cdd:PRK05380 377 GICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEIYG-KEEIY 454

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669033298 320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 394
Cdd:PRK05380 455 ERHRHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-390 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 519.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298    1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:TIGR00337 151 LPFLEAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDV 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYAS 160
Cdd:TIGR00337 231 EEEAVISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLS 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  161 VIKALEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFL 240
Cdd:TIGR00337 308 VIEALKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFL 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  241 GVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLE 319
Cdd:TIGR00337 377 GICLGMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVY 454

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 669033298  320 ERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 390
Cdd:TIGR00337 455 ERHRHRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 143-388 5.79e-142

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 404.63  E-value: 5.79e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 143 CSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITsqeepvryheAWQKLCSAHGVLVPGGFGVRGT 222
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 223 EGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLF 301
Cdd:cd01746   71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 302 QtKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPS 381
Cdd:cd01746  151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                 ....*..
gi 669033298 382 PPYFGLL 388
Cdd:cd01746  229 PLFVGFV 235
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 1-116 3.13e-73

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 230.69  E-value: 3.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298    1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:pfam06418 150 LPFLEAIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNV 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 669033298   81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 116
Cdd:pfam06418 230 PKEAVISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 1-112 1.65e-69

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 220.82  E-value: 1.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298   1 MPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHV 80
Cdd:cd03113  150 LPFLEALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNV 229

                         90       100       110
                 ....*....|....*....|....*....|..
gi 669033298  81 EPEQVICVHDVSSIYRVPLLLEEQGVVDYFLR 112
Cdd:cd03113  230 PPEAVISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase pfam00117
Glutamine amidotransferase class-I;
156-390 5.65e-39

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 138.91  E-value: 5.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  156 DSYASVIKALEHSALAINHKLEIKYIDSADLEPItsQEEPvryheawqklcsaHGVLVPGGFGVRGT-EGKIQAIAWARN 234
Cdd:pfam00117   4 DNGDSFTYNLARALRELGVEVTVVPNDTPAEEIL--EENP-------------DGIILSGGPGSPGAaGGAIEAIREARE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  235 QKKPFLGVCLGMQLAVVEFSRNVLgwqdanstefdpttshpvvvdmPEHNPGQMGGTMRLGKRRTlfqtknsvmRKLYGD 314
Cdd:pfam00117  69 LKIPILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVGDDGC---------GLFYGL 117

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669033298  315 ADYLEERHRHRFEVNPVwkkcLEEQGLKFVGQDVEGE-RMEIVELEDhPFFvGVQYHPEFLSRPIKPSPPYFGLLLA 390
Cdd:pfam00117 118 PNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDGtIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 142-394 8.25e-38

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 137.02  E-value: 8.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 142 TCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADlepITSQEEPVRYHEAWqklcsahgvLVPGGfGVRG 221
Cdd:PRK06186   1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPE---ITDPEDLAGFDGIW---------CVPGS-PYRN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 222 TEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMP----EHNpgqmgGTMRLgkr 297
Cdd:PRK06186  68 DDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLScslvEKT-----GDIRL--- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 298 rtlfqTKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGErMEIVELEDHPFFVGVQYHPEFLSRP 377
Cdd:PRK06186 140 -----RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALA 212

                        250
                 ....*....|....*..
gi 669033298 378 IKPSPPYFGLLLASVGR 394
Cdd:PRK06186 213 GRPPPLVRAFLRAARAA 229
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 226-394 5.15e-13

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 68.27  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 226 IQAIAWARNQKKPFLGVCLGMQLAVVefsrnVLG---WQDaNSTEFDPTTSH--PVVVDMPEHnpgqmggTMRLgkrrtl 300
Cdd:COG2071   86 LALIRAALERGKPVLGICRGMQLLNV-----ALGgtlYQD-LPDQVPGALDHrqPAPRYAPRH-------TVEI------ 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 301 fqTKNSVMRKLYGdadyleerhRHRFEVNpvwkkCLEEQGLKFVGQD-----------VEGermeiVELEDHPFFVGVQY 369
Cdd:COG2071  147 --EPGSRLARILG---------EEEIRVN-----SLHHQAVKRLGPGlrvsarapdgvIEA-----IESPGAPFVLGVQW 205

                        170       180
                 ....*....|....*....|....*
gi 669033298 370 HPEFLSRPIKPSPPYFGLLLASVGR 394
Cdd:COG2071  206 HPEWLAASDPLSRRLFEAFVEAARA 230
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 145-251 9.65e-12

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: 61.85  E-value: 9.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 145 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGVRGT-- 222
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTPDDla 63

                         90       100       110
                 ....*....|....*....|....*....|.
gi 669033298 223 --EGKIQAIAWARNQKKPFLGVCLGMQLAVV 251
Cdd:cd01653   64 rdEALLALLREAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 145-248 1.86e-10

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: 57.21  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 145 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGV----R 220
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTpddlA 63

                         90       100
                 ....*....|....*....|....*...
gi 669033298 221 GTEGKIQAIAWARNQKKPFLGVCLGMQL 248
Cdd:cd03128   64 WDEALLALLREAAAAGKPVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 235-372 8.72e-09

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: 55.34  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298  235 QKKPFLGVCLGMQLAVVefsrnVLG---WQDANSTefdpttshPVVVDMPEHNPGQMGGTmrlgkRRTLFQTKNSVMRKL 311
Cdd:pfam07722 104 RGKPILGICRGFQLLNV-----ALGgtlYQDIQEQ--------PGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669033298  312 YGDADyleerhrhrFEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHP-FFVGVQYHPE 372
Cdd:pfam07722 166 LGSEE---------FRVN-----SLHHQAIDRLAPGLRVEAvapdgtIEAIESPNAKgFALGVQWHPE 219
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 160-289 2.66e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 47.85  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHSAlainhkleikyidsADLEP-ITSQEEPVRyheawqklcSAHGVLVPG---------GFGVRGTEGKIQAI 229
Cdd:PRK13146  16 SAAKALERAG--------------AGADVvVTADPDAVA---------AADRVVLPGvgafadcmrGLRAVGLGEAVIEA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669033298 230 AWARNqkKPFLGVCLGMQLAvveFSRNV-------LGWQDANSTEFDPTTSHPVVvdmPehnpgQMG 289
Cdd:PRK13146  73 VLAAG--RPFLGICVGMQLL---FERGLehgdtpgLGLIPGEVVRFQPDGPALKV---P-----HMG 126
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 160-283 7.47e-06

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: 46.57  E-value: 7.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHsalainhkLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG-G-FG-----VRGTEGkIQAIAWA 232
Cdd:COG0118   15 SVAKALER--------LGAEVVVTSDPD----------------EIRAADRLVLPGvGaFGdamenLRERGL-DEAIREA 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669033298 233 RNQKKPFLGVCLGMQL-------------------AVVEFSRNVL-----GWqdaNSTEFdpTTSHPVVVDMPEH 283
Cdd:COG0118   70 VAGGKPVLGICLGMQLlferseengdteglglipgEVVRFPASDLkvphmGW---NTVEI--AKDHPLFAGIPDG 139
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 226-374 2.77e-05

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.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 44.49  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 226 IQAIAWARNQKKPFLGVCLGMQLAVVEFsrnvlgwqdanstefdpttshpvvvdmpehnpgqmGGTmrlgkrrtlfqtkn 305
Cdd:cd01745   90 LALLRAALERGKPILGICRGMQLLNVAL-----------------------------------GGT-------------- 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669033298 306 svmrkLYGDAdyleerhrhrfEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHPFFVGVQYHPEFL 374
Cdd:cd01745  121 -----LYQDI-----------RVN-----SLHHQAIKRLADGLRVEArapdgvIEAIESPDRPFVLGVQWHPEWL 174
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 159-248 2.96e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 44.74  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 159 ASVIKALEhsalainhKLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG--GFGV-------RGTEGKIQAI 229
Cdd:PRK13141  13 RSVEKALE--------RLGAEAVITSDPE----------------EILAADGVILPGvgAFPDamanlreRGLDEVIKEA 68

                         90
                 ....*....|....*....
gi 669033298 230 AwarNQKKPFLGVCLGMQL 248
Cdd:PRK13141  69 V---ASGKPLLGICLGMQL 84
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 226-288 3.43e-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: 41.86  E-value: 3.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 226 IQAIAWARNQKKPFLGVCLGMQL------AVVEFSRNV-LGWqdansTEFDPTTSHPVVVDMPEHNPGQM 288
Cdd:COG0518   72 PALIREAFELGKPVLGICYGAQLlahalgGKVEPGPGReIGW-----APVELTEADPLFAGLPDEFTVWM 136
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 203-272 3.75e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 41.39  E-value: 3.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669033298 203 QKLCSAHGVLVPG----GFGVRGTE--GKIQAIAWARNQKKPFLGVCLGMQL---AVVEFSRNVLGWQDANSTEFDPTT 272
Cdd:PRK13181  33 EEIAGADKVILPGvgafGQAMRSLResGLDEALKEHVEKKQPVLGICLGMQLlfeSSEEGNVKGLGLIPGDVKRFRSEP 111
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 159-248 4.37e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 41.33  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 159 ASVIKALEHsalainhkLEIKYIDSADLEPITSqeepvryheawqklcsAHGVLVPG----GFGVRGTE--GKIQAIAWA 232
Cdd:cd01748   12 RSVANALER--------LGAEVIITSDPEEILS----------------ADKLILPGvgafGDAMANLRerGLIEALKEA 67

                         90
                 ....*....|....*.
gi 669033298 233 RNQKKPFLGVCLGMQL 248
Cdd:cd01748   68 IASGKPFLGICLGMQL 83
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 295-375 4.45e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 41.81  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 295 GKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEV-------------------------NPVWKKCLEEQGLKFVGQDVE 349
Cdd:PRK11366 116 GLQELVVATGGSLHRKLCEQPELLEHREDPELPVeqqyapshevqveeggllsallpecSNFWVNSLHGQGAKVVSPRLR 195

                         90       100       110
                 ....*....|....*....|....*....|..
gi 669033298 350 GER------MEIVELEDHPFFVGVQYHPEFLS 375
Cdd:PRK11366 196 VEArspdglVEAVSVINHPFALGVQWHPEWNS 227
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 160-248 4.50e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 41.39  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669033298 160 SVIKALEHsalainhkleikyidsADLEP-ITSQEEpvryheawqKLCSAHGVLVPG----GFGVRGTEGKIQAIAWARN 234
Cdd:PRK13143  15 SVSKALER----------------AGAEVvITSDPE---------EILDADGIVLPGvgafGAAMENLSPLRDVILEAAR 69

                         90
                 ....*....|....
gi 669033298 235 QKKPFLGVCLGMQL 248
Cdd:PRK13143  70 SGKPFLGICLGMQL 83
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 232-248 6.61e-03

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 37.69  E-value: 6.61e-03
                          10
                  ....*....|....*..
gi 669033298  232 ARNQKKPFLGVCLGMQL 248
Cdd:TIGR01855  67 VVRLGKPVLGICLGMQL 83
 
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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