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Conserved domains on  [gi|148491070|ref|NP_001896|]
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CTP synthase 1 isoform a [Homo sapiens]

Protein Classification

CTP synthase( domain architecture ID 11476640)

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 PLN02327
CTP synthase
 1-556 0e+00

CTP synthase


:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 953.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 320 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 399
Cdd:PLN02327 319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 400 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 479
Cdd:PLN02327 399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070 480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 556
Cdd:PLN02327 479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-556 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 953.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 320 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 399
Cdd:PLN02327 319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 400 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 479
Cdd:PLN02327 399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070 480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 556
Cdd:PLN02327 479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-550 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: 853.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvDEDGLEpqVCVIELGGTVGDIESMPFI 160
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA----EESGAD--VVIVEIGGTVGDIESLPFL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:COG0504  155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 320
Cdd:COG0504  235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 321 LEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 400
Cdd:COG0504  312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 401 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYLEERH 478
Cdd:COG0504  382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEISERH 458

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148491070 479 RHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 550
Cdd:COG0504  459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 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: 803.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070    1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdeDGLEPQVCVIELGGTVGDIESMPFI 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  321 LEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  401 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070  480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070    2 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   82 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIpvdedgLEPQVCVIELGGTVGDIESMPFIE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  162 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 148491070  242 ICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

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: 543.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   2 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 81
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  82 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPvdedglEPQVCVIELGGTVGDIESMPFIE 161
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 162 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 241
Cdd:cd03113  155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                        250       260
                 ....*....|....*....|....*..
gi 148491070 242 ICVHDVSSIYRVPLLLEEQGVVDYFLR 268
Cdd:cd03113  235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-556 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 953.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 320 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 399
Cdd:PLN02327 319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 400 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 479
Cdd:PLN02327 399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070 480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 556
Cdd:PLN02327 479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
pyrG PRK05380
CTP synthetase; Validated
 1-550 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 855.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdedgLEPQVCVIELGGTVGDIESMPFI 160
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIeRQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPD--LSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEA 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 321 LEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 400
Cdd:PRK05380 311 LKHAGIANDVKVNIKWIDSEDLEE----------ENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICL 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 401 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLFQtKNSVMRKLYGdADYLEERHR 479
Cdd:PRK05380 381 GMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEIYG-KEEIYERHR 458

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148491070 480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 550
Cdd:PRK05380 459 HRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-550 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: 853.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvDEDGLEpqVCVIELGGTVGDIESMPFI 160
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA----EESGAD--VVIVEIGGTVGDIESLPFL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:COG0504  155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 320
Cdd:COG0504  235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 321 LEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 400
Cdd:COG0504  312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 401 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYLEERH 478
Cdd:COG0504  382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEISERH 458

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148491070 479 RHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 550
Cdd:COG0504  459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 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: 803.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070    1 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   81 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdeDGLEPQVCVIELGGTVGDIESMPFI 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  161 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  241 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  321 LEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  401 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070  480 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070    2 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   82 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIpvdedgLEPQVCVIELGGTVGDIESMPFIE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  162 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 148491070  242 ICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

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: 543.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070   2 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 81
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  82 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPvdedglEPQVCVIELGGTVGDIESMPFIE 161
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 162 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 241
Cdd:cd03113  155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                        250       260
                 ....*....|....*....|....*..
gi 148491070 242 ICVHDVSSIYRVPLLLEEQGVVDYFLR 268
Cdd:cd03113  235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 299-544 5.16e-139

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: 403.09  E-value: 5.16e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 299 CSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITsqeepvryheAWQKLCSAHGVLVPGGFGVRGT 378
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 379 EGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLF 457
Cdd:cd01746   71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 458 QtKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPS 537
Cdd:cd01746  151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                 ....*..
gi 148491070 538 PPYFGLL 544
Cdd:cd01746  229 PLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
312-546 2.71e-37

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 136.60  E-value: 2.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  312 DSYASVIKALEHSALAINHKLEIKYIDSADLEPItsQEEPvryheawqklcsaHGVLVPGGFGVRGT-EGKIQAIAWARN 390
Cdd:pfam00117   4 DNGDSFTYNLARALRELGVEVTVVPNDTPAEEIL--EENP-------------DGIILSGGPGSPGAaGGAIEAIREARE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  391 QKKPFLGVCLGMQLAVVEFSRNVLgwqdanstefdpttshpvvvdmPEHNPGQMGGTMRLGKRRTlfqtknsvmRKLYGD 470
Cdd:pfam00117  69 LKIPILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVGDDGC---------GLFYGL 117

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070  471 ADYLEERHRHRFEVNPVwkkcLEEQGLKFVGQDVEGE-RMEIVELEDhPFFvGVQYHPEFLSRPIKPSPPYFGLLLA 546
Cdd:pfam00117 118 PNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDGtIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 298-550 6.71e-37

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 137.02  E-value: 6.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 298 TCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADlepITSQEEPVRYHEAWqklcsahgvLVPGGfGVRG 377
Cdd:PRK06186   1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPE---ITDPEDLAGFDGIW---------CVPGS-PYRN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 378 TEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMP----EHNpgqmgGTMRLgkr 453
Cdd:PRK06186  68 DDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLScslvEKT-----GDIRL--- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 454 rtlfqTKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGErMEIVELEDHPFFVGVQYHPEFLSRP 533
Cdd:PRK06186 140 -----RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALA 212

                        250
                 ....*....|....*..
gi 148491070 534 IKPSPPYFGLLLASVGR 550
Cdd:PRK06186 213 GRPPPLVRAFLRAARAA 229
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 382-550 1.15e-12

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: 67.89  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 382 IQAIAWARNQKKPFLGVCLGMQLAVVefsrnVLG---WQDaNSTEFDPTTSH--PVVVDMPEHnpgqmggTMRLgkrrtl 456
Cdd:COG2071   86 LALIRAALERGKPVLGICRGMQLLNV-----ALGgtlYQD-LPDQVPGALDHrqPAPRYAPRH-------TVEI------ 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 457 fqTKNSVMRKLYGdadyleerhRHRFEVNpvwkkCLEEQGLKFVGQD-----------VEGermeiVELEDHPFFVGVQY 525
Cdd:COG2071  147 --EPGSRLARILG---------EEEIRVN-----SLHHQAVKRLGPGlrvsarapdgvIEA-----IESPGAPFVLGVQW 205

                        170       180
                 ....*....|....*....|....*
gi 148491070 526 HPEFLSRPIKPSPPYFGLLLASVGR 550
Cdd:COG2071  206 HPEWLAASDPLSRRLFEAFVEAARA 230
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-407 1.93e-11

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: 61.08  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 301 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGVRGT-- 378
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTPDDla 63

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148491070 379 --EGKIQAIAWARNQKKPFLGVCLGMQLAVV 407
Cdd:cd01653   64 rdEALLALLREAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-404 5.84e-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: 56.44  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 301 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGV----R 376
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTpddlA 63

                         90       100
                 ....*....|....*....|....*...
gi 148491070 377 GTEGKIQAIAWARNQKKPFLGVCLGMQL 404
Cdd:cd03128   64 WDEALLALLREAAAAGKPVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 391-528 2.13e-08

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: 54.96  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070  391 QKKPFLGVCLGMQLAVVefsrnVLG---WQDANSTefdpttshPVVVDMPEHNPGQMGGTmrlgkRRTLFQTKNSVMRKL 467
Cdd:pfam07722 104 RGKPILGICRGFQLLNV-----ALGgtlYQDIQEQ--------PGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148491070  468 YGDADyleerhrhrFEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHP-FFVGVQYHPE 528
Cdd:pfam07722 166 LGSEE---------FRVN-----SLHHQAIDRLAPGLRVEAvapdgtIEAIESPNAKgFALGVQWHPE 219
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 316-445 3.98e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 47.85  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 316 SVIKALEHSAlainhkleikyidsADLEP-ITSQEEPVRyheawqklcSAHGVLVPG---------GFGVRGTEGKIQAI 385
Cdd:PRK13146  16 SAAKALERAG--------------AGADVvVTADPDAVA---------AADRVVLPGvgafadcmrGLRAVGLGEAVIEA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148491070 386 AWARNqkKPFLGVCLGMQLAvveFSRNV-------LGWQDANSTEFDPTTSHPVVvdmPehnpgQMG 445
Cdd:PRK13146  73 VLAAG--RPFLGICVGMQLL---FERGLehgdtpgLGLIPGEVVRFQPDGPALKV---P-----HMG 126
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 316-439 2.03e-05

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: 45.80  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 316 SVIKALEHsalainhkLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG-G-FG-----VRGTEGkIQAIAWA 388
Cdd:COG0118   15 SVAKALER--------LGAEVVVTSDPD----------------EIRAADRLVLPGvGaFGdamenLRERGL-DEAIREA 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148491070 389 RNQKKPFLGVCLGMQL-------------------AVVEFSRNVL-----GWqdaNSTEFdpTTSHPVVVDMPEH 439
Cdd:COG0118   70 VAGGKPVLGICLGMQLlferseengdteglglipgEVVRFPASDLkvphmGW---NTVEI--AKDHPLFAGIPDG 139
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 315-404 6.26e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 44.35  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 315 ASVIKALEhsalainhKLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG--GFGV-------RGTEGKIQAI 385
Cdd:PRK13141  13 RSVEKALE--------RLGAEAVITSDPE----------------EILAADGVILPGvgAFPDamanlreRGLDEVIKEA 68

                         90
                 ....*....|....*....
gi 148491070 386 AwarNQKKPFLGVCLGMQL 404
Cdd:PRK13141  69 V---ASGKPLLGICLGMQL 84
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 382-530 8.39e-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: 43.72  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 382 IQAIAWARNQKKPFLGVCLGMQLAVVEFsrnvlgwqdanstefdpttshpvvvdmpehnpgqmGGTmrlgkrrtlfqtkn 461
Cdd:cd01745   90 LALLRAALERGKPILGICRGMQLLNVAL-----------------------------------GGT-------------- 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148491070 462 svmrkLYGDAdyleerhrhrfEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHPFFVGVQYHPEFL 530
Cdd:cd01745  121 -----LYQDI-----------RVN-----SLHHQAIKRLADGLRVEArapdgvIEAIESPDRPFVLGVQWHPEWL 174
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 451-531 3.94e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 42.58  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 451 GKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEV-------------------------NPVWKKCLEEQGLKFVGQDVE 505
Cdd:PRK11366 116 GLQELVVATGGSLHRKLCEQPELLEHREDPELPVeqqyapshevqveeggllsallpecSNFWVNSLHGQGAKVVSPRLR 195

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148491070 506 GER------MEIVELEDHPFFVGVQYHPEFLS 531
Cdd:PRK11366 196 VEArspdglVEAVSVINHPFALGVQWHPEWNS 227
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 382-444 5.56e-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: 5.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 382 IQAIAWARNQKKPFLGVCLGMQL------AVVEFSRNV-LGWqdansTEFDPTTSHPVVVDMPEHNPGQM 444
Cdd:COG0518   72 PALIREAFELGKPVLGICYGAQLlahalgGKVEPGPGReIGW-----APVELTEADPLFAGLPDEFTVWM 136
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 359-428 6.97e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 41.00  E-value: 6.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148491070 359 QKLCSAHGVLVPG----GFGVRGTE--GKIQAIAWARNQKKPFLGVCLGMQL---AVVEFSRNVLGWQDANSTEFDPTT 428
Cdd:PRK13181  33 EEIAGADKVILPGvgafGQAMRSLResGLDEALKEHVEKKQPVLGICLGMQLlfeSSEEGNVKGLGLIPGDVKRFRSEP 111
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 315-404 1.08e-03

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: 40.56  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 315 ASVIKALEHsalainhkLEIKYIDSADLEPITSqeepvryheawqklcsAHGVLVPG----GFGVRGTE--GKIQAIAWA 388
Cdd:cd01748   12 RSVANALER--------LGAEVIITSDPEEILS----------------ADKLILPGvgafGDAMANLRerGLIEALKEA 67

                         90
                 ....*....|....*.
gi 148491070 389 RNQKKPFLGVCLGMQL 404
Cdd:cd01748   68 IASGKPFLGICLGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 316-404 1.35e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 40.24  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148491070 316 SVIKALEHsalainhkleikyidsADLEP-ITSQEEpvryheawqKLCSAHGVLVPG----GFGVRGTEGKIQAIAWARN 390
Cdd:PRK13143  15 SVSKALER----------------AGAEVvITSDPE---------EILDADGIVLPGvgafGAAMENLSPLRDVILEAAR 69

                         90
                 ....*....|....
gi 148491070 391 QKKPFLGVCLGMQL 404
Cdd:PRK13143  70 SGKPFLGICLGMQL 83
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-48 4.49e-03

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 37.03  E-value: 4.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 148491070   2 KYILVTGGViSGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAG 48
Cdd:cd01983    1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGG 46
 
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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