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Conserved domains on  [gi|1491109465|gb|RLG02139|]
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CTP synthetase [Thermococci archaeon]

Protein Classification

CTP synthase( domain architecture ID 11423441)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-516 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: 945.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQL 158
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEEsgADVVIVEIGGTVGDIESLPFLEAIRQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 159 SWE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHD 235
Cdd:COG0504   161 RLElgrENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 236 VDDIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTG 312
Cdd:COG0504   241 VDSIYEVPLMLHEQGLDEIVLKKLGLEaREPDLSEWEELVERikNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 313 INVNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNA 387
Cdd:COG0504   321 VKVNIKWIDSEDLEEENaeelLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVlGLEDA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 388 NSTEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFT 466
Cdd:COG0504   401 NSTEFDpNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVFS 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491109465 467 GKSEDGR-MEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAMGRKK 516
Cdd:COG0504   481 GTSPDGRlVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYK 531
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-516 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: 945.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQL 158
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEEsgADVVIVEIGGTVGDIESLPFLEAIRQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 159 SWE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHD 235
Cdd:COG0504   161 RLElgrENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 236 VDDIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTG 312
Cdd:COG0504   241 VDSIYEVPLMLHEQGLDEIVLKKLGLEaREPDLSEWEELVERikNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 313 INVNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNA 387
Cdd:COG0504   321 VKVNIKWIDSEDLEEENaeelLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVlGLEDA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 388 NSTEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFT 466
Cdd:COG0504   401 NSTEFDpNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVFS 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491109465 467 GKSEDGR-MEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAMGRKK 516
Cdd:COG0504   481 GTSPDGRlVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYK 531
pyrG PRK05380
CTP synthetase; Validated
 1-516 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 935.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:PRK05380    2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGERYDFTVIEVGGTVGDIESMPFLEACRQLSW 160
Cdd:PRK05380   82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 161 E---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDVD 237
Cdd:PRK05380  162 ElgrENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 238 DIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTGIN 314
Cdd:PRK05380  242 SIYEVPLLLHEQGLDDIVLERLGLEaPEPDLSEWEELVERlkNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 315 VNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNANS 389
Cdd:PRK05380  322 VNIKWIDSEDLEEENvaelLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVlGLEDANS 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 390 TEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTGK 468
Cdd:PRK05380  402 TEFDpDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQLEKAGLVFSGT 481

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1491109465 469 SEDGR-MEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAMGRKK 516
Cdd:PRK05380  482 SPDGRlVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENK 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-511 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: 798.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQL 158
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKIsgPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 159 SWE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHD 235
Cdd:TIGR00337 161 RVEvgrENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 236 VDDIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTG 312
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNcDEADLSEWEQLVEKfaNPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 313 INVNLKWLESESIK---KEDLGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNAN 388
Cdd:TIGR00337 321 TKVNIKWIDSEDLEeegVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVaGLEGAN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 389 STEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTG 467
Cdd:TIGR00337 401 STEFDpDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQIENKGLIVSG 480

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1491109465 468 KSEDGRM-EVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKA 511
Cdd:TIGR00337 481 TSPDGRLvEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-261 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: 516.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   2 RYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNVD 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  82 LTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQLS 159
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEvgPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 160 WE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDV 236
Cdd:pfam06418 161 LEvgrENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....*
gi 1491109465 237 DDIYKVPLLLNEQKMGEKIVDKFGL 261
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-257 7.46e-173

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: 487.38  E-value: 7.46e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   2 RYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNVD 81
Cdd:cd03113     1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  82 LTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVG--ERYDFTVIEVGGTVGDIESMPFLEACRQLS 159
Cdd:cd03113    81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAkiPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 160 WE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDV 236
Cdd:cd03113   161 FEvgrENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                         250       260
                  ....*....|....*....|.
gi 1491109465 237 DDIYKVPLLLNEQKMGEKIVD 257
Cdd:cd03113   241 SSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-516 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: 945.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQL 158
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEEsgADVVIVEIGGTVGDIESLPFLEAIRQL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 159 SWE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHD 235
Cdd:COG0504   161 RLElgrENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 236 VDDIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTG 312
Cdd:COG0504   241 VDSIYEVPLMLHEQGLDEIVLKKLGLEaREPDLSEWEELVERikNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 313 INVNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNA 387
Cdd:COG0504   321 VKVNIKWIDSEDLEEENaeelLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVlGLEDA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 388 NSTEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFT 466
Cdd:COG0504   401 NSTEFDpNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVFS 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491109465 467 GKSEDGR-MEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAMGRKK 516
Cdd:COG0504   481 GTSPDGRlVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYK 531
pyrG PRK05380
CTP synthetase; Validated
 1-516 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 935.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:PRK05380    2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGERYDFTVIEVGGTVGDIESMPFLEACRQLSW 160
Cdd:PRK05380   82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 161 E---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDVD 237
Cdd:PRK05380  162 ElgrENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 238 DIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTGIN 314
Cdd:PRK05380  242 SIYEVPLLLHEQGLDDIVLERLGLEaPEPDLSEWEELVERlkNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 315 VNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNANS 389
Cdd:PRK05380  322 VNIKWIDSEDLEEENvaelLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVlGLEDANS 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 390 TEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTGK 468
Cdd:PRK05380  402 TEFDpDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQLEKAGLVFSGT 481

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1491109465 469 SEDGR-MEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAMGRKK 516
Cdd:PRK05380  482 SPDGRlVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENK 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-511 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: 798.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQL 158
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKIsgPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 159 SWE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHD 235
Cdd:TIGR00337 161 RVEvgrENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 236 VDDIYKVPLLLNEQKMGEKIVDKFGLR-RTPDLKKWRSIISR--KCDKDVTLALVGKYMDLHDSYISIREAVMHCSYYTG 312
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNcDEADLSEWEQLVEKfaNPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 313 INVNLKWLESESIK---KEDLGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICLGFQLATIEYARSI-GLKNAN 388
Cdd:TIGR00337 321 TKVNIKWIDSEDLEeegVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVaGLEGAN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 389 STEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTG 467
Cdd:TIGR00337 401 STEFDpDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQIENKGLIVSG 480

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1491109465 468 KSEDGRM-EVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKA 511
Cdd:TIGR00337 481 TSPDGRLvEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
PLN02327 PLN02327
CTP synthase
 1-511 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 743.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   1 MRYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNV 80
Cdd:PLN02327    1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  81 DLTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSV--------GERYDFTVIEVGGTVGDIESMPFL 152
Cdd:PLN02327   81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVakipvdgkEGPADVCVIELGGTVGDIESMPFI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 153 EACRQLSW---EEDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDH 229
Cdd:PLN02327  161 EALRQFSFrvgPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 230 VISNHDVDDIYKVPLLLNEQKMGEKIVDKFGLRRT---PDLKKWRSiISRKCDK---DVTLALVGKYMDLHDSYISIREA 303
Cdd:PLN02327  241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVarePDLEEWTA-RAESCDNltePVRIAMVGKYTGLSDSYLSVLKA 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 304 VMHCSYYTGINVNLKWLESESI----KKED----------LGDVDGILVPGGFGVRGTEEKIRAITYAREKKIPFLGICL 369
Cdd:PLN02327  320 LLHASVACSRKLVIDWVAASDLedetAKETpdayaaawklLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 370 GFQLATIEYARSI-GLKNANSTEFV-DTDEPVIDLLPEQKKiKNMGGTMRLGAYKIIL-DEKSMVYILYKSKS-IYERHR 445
Cdd:PLN02327  400 GMQIAVIEFARSVlGLKDANSTEFDpETPNPCVIFMPEGSK-THMGGTMRLGSRRTYFqTPDCKSAKLYGNVSfVDERHR 478

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491109465 446 HRYEVNPEYIDLLTKNGVKFTGKSEDG-RMEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKA 511
Cdd:PLN02327  479 HRYEVNPEMVPRLEKAGLSFVGKDETGrRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAA 545
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-261 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: 516.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   2 RYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNVD 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  82 LTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVGER--YDFTVIEVGGTVGDIESMPFLEACRQLS 159
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEvgPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 160 WE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDV 236
Cdd:pfam06418 161 LEvgrENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....*
gi 1491109465 237 DDIYKVPLLLNEQKMGEKIVDKFGL 261
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-257 7.46e-173

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: 487.38  E-value: 7.46e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   2 RYIIVTGGVLSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAGTMSPFEHGEVFVLHDGGEVDLDLGNYERFLNVD 81
Cdd:cd03113     1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465  82 LTRDHNITTGKIYKRVIEKERRGDYLGKTVQPIPHLTDEIKSEIRSVG--ERYDFTVIEVGGTVGDIESMPFLEACRQLS 159
Cdd:cd03113    81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAkiPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 160 WE---EDVVFVHVTLVPSLDVVGEQKTKPTQHSVKKLMETGISPHIIVCRSKSKLQEKTKRKIAQFCNVSEDHVISNHDV 236
Cdd:cd03113   161 FEvgrENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                         250       260
                  ....*....|....*....|.
gi 1491109465 237 DDIYKVPLLLNEQKMGEKIVD 257
Cdd:cd03113   241 SSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 282-509 1.25e-129

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: 376.51  E-value: 1.25e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 282 VTLALVGKYMDLHDSYISIREAVMHCSYYTGINVNLKWLESESIKKED----LGDVDGILVPGGFGVRGTEEKIRAITYA 357
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENaeeaLKGADGILVPGGFGIRGVEGKILAIKYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 358 REKKIPFLGICLGFQLATIEYARSI-GLKNANSTEFV-DTDEPVIDLLPEQKKIKNMGGTMRLGAYKIILDEKSMVYILY 435
Cdd:cd01746    81 RENNIPFLGICLGMQLAVIEFARNVlGLPDANSTEFDpDTPHPVVDLMPEQKGVKDLGGTMRLGAYPVILKPGTLAHKYY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491109465 436 KSKSIYERHRHRYEVNPEYIDLLTKNGVKFTGKSEDG-RMEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLV 509
Cdd:cd01746   161 GKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGgLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
295-511 2.69e-42

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 149.31  E-value: 2.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 295 DSYISIREAVMHCSYYTGINVNLKWLESeSIKKEDLGDVDGILVPGGFGVRGT-EEKIRAITYAREKKIPFLGICLGFQL 373
Cdd:pfam00117   4 DNGDSFTYNLARALRELGVEVTVVPNDT-PAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGHQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 374 ATIEYARSIGlknanstefvdtdepvidllpEQKKIKNMGGTMRLGaykiiLDEKSMVYILYksKSIYERHRHRYEVNPE 453
Cdd:pfam00117  83 LALAFGGKVV---------------------KAKKFGHHGKNSPVG-----DDGCGLFYGLP--NVFIVRRYHSYAVDPD 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 454 YIdlltKNGVKFTGKSEDG--RMEVLELEGhPFFiGTQYHPEFTSRVERPSPIFMGLVKA 511
Cdd:pfam00117 135 TL----PDGLEVTATSENDgtIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 284-512 1.88e-36

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 134.71  E-value: 1.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 284 LALVGKYMDLHDSYISIREAVMHCSYYTGINVNLKWLESESIKK-EDLGDVDGI-LVPGGfGVRGTEEKIRAITYAREKK 361
Cdd:PRK06186    4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDpEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARENG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 362 IPFLGICLGFQLATIEYARSI-GLKNANSTEfVDTD--EPVIDLLP----EQKKiknmggtmrlgayKIILDEKSMVYIL 434
Cdd:PRK06186   83 IPFLGTCGGFQHALLEYARNVlGWADAAHAE-TDPEgdRPVIAPLScslvEKTG-------------DIRLRPGSLIARA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491109465 435 YKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTGKSEDGRMEVLELEGHPFFIGTQYHPEFTSRVERPSPIFMGLVKAM 512
Cdd:PRK06186  149 YGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLVRAFLRAA 226
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 285-373 4.17e-10

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: 57.22  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 285 ALVGKYMDLHDSYISIREAVMHCsyytGINVNLKWLESESIK-KEDLGDVDGILVPGGFGVRGT----EEKIRAITYARE 359
Cdd:cd01653     2 AVLLFPGFEELELASPLDALREA----GAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTPDDlardEALLALLREAAA 77

                          90
                  ....*....|....
gi 1491109465 360 KKIPFLGICLGFQL 373
Cdd:cd01653    78 AGKPILGICLGAQL 91
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 285-373 2.23e-09

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: 54.51  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 285 ALVGKYMDLHDSYISIREAVMHCsyytGINVNLKWLESESIK-KEDLGDVDGILVPGGFGV----RGTEEKIRAITYARE 359
Cdd:cd03128     2 AVLLFGGSEELELASPLDALREA----GAEVDVVSPDGGPVEsDVDLDDYDGLILPGGPGTpddlAWDEALLALLREAAA 77

                          90
                  ....*....|....
gi 1491109465 360 KKIPFLGICLGFQL 373
Cdd:cd03128    78 AGKPVLGICLGAQL 91
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 281-511 1.04e-08

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: 55.95  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 281 DVTLALVGKYMDLHDSYIsirEAVMHCSyytGINVNLKWLESESIKKEDLGDVDGILVPGG-------FGVRGTEEK--- 350
Cdd:COG2071     4 DLRTAGGYPAHYLPEDYV---RAVRAAG---GLPVLLPPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpi 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 351 --------IRAITYAREKKIPFLGICLGFQLatieyarsiglknanstefvdtdepvidL-----------LPEQ--KKI 409
Cdd:COG2071    78 dperdafeLALIRAALERGKPVLGICRGMQL----------------------------LnvalggtlyqdLPDQvpGAL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 410 KNMGGTMRLGAYK-IILDEKSMVYilykskSIYERHRHRyeVN-----------PeyidlltknGVKFTGKSEDGRMEVL 477
Cdd:COG2071   130 DHRQPAPRYAPRHtVEIEPGSRLA------RILGEEEIR--VNslhhqavkrlgP---------GLRVSARAPDGVIEAI 192

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1491109465 478 ELEGHPFFIGTQYHPEFTSRVERPS-PIFMGLVKA 511
Cdd:COG2071   193 ESPGAPFVLGVQWHPEWLAASDPLSrRLFEAFVEA 227
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 333-493 1.43e-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: 55.34  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 333 VDGILVPGGFGV---RGTEEKIRAITY---------------AREKKIPFLGICLGFQLATIEYARSIGLKNANSTEFVD 394
Cdd:pfam07722  59 LDGLLLTGGPNVdphFYGEEPSESGGPydpardayelaliraALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGFTD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 395 TDEPvidllpEQKKIKNMGGTMRLgaykiilDEKSMVYILYKSKSIYERHRHRyevnpEYIDLLTKnGVKFTGKSEDGRM 474
Cdd:pfam07722 139 HREH------CQVAPYAPSHAVNV-------EPGSLLASLLGSEEFRVNSLHH-----QAIDRLAP-GLRVEAVAPDGTI 199

                         170       180
                  ....*....|....*....|
gi 1491109465 475 EVLELEGHP-FFIGTQYHPE 493
Cdd:pfam07722 200 EAIESPNAKgFALGVQWHPE 219
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-48 4.35e-07

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: 48.20  E-value: 4.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1491109465   2 RYIIVTGGVlSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDAG 48
Cdd:cd01983     1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGG 46
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 329-495 4.81e-06

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: 47.63  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 329 DLGDVDGILVPGG-FGVRGTEEKI----RAITYAREKKIPFLGICLGFQL------ATIEYA--RSIGLKNANSTEfvdt 395
Cdd:COG0518    45 DLEDPDGLILSGGpMSVYDEDPWLedepALIREAFELGKPVLGICYGAQLlahalgGKVEPGpgREIGWAPVELTE---- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 396 DEPVIDLLPeqkkiknmggtmrlgaykiildEKSMVYilyksksiyerHRHRYEVnpeyiDLLTKNGVKfTGKSEDGRME 475
Cdd:COG0518   121 ADPLFAGLP----------------------DEFTVW-----------MSHGDTV-----TELPEGAEV-LASSDNCPNQ 161

                         170       180
                  ....*....|....*....|
gi 1491109465 476 VLELEGHpfFIGTQYHPEFT 495
Cdd:COG0518   162 AFRYGRR--VYGVQFHPEVT 179
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 328-493 4.91e-06

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: 47.32  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 328 EDLGDVDGILVPG----GFGVRGTEE-KIRAIT-YAREKKIPFLGICLGFQLAtieYARSIGLKNANSTEFVDTDepVID 401
Cdd:TIGR01855  32 KEAELADKLILPGvgafGAAMARLREnGLDLFVeLVVRLGKPVLGICLGMQLL---FERSEEGGGVPGLGLIKGN--VVK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 402 LlpEQKKIKNMGGTmrlgaYKIILDEKSMVYILYKSKSIYERHRHRYEVNPEYIDLLTKNGVKFTGKSEDGRmevleleg 481
Cdd:TIGR01855 107 L--EARKVPHMGWN-----EVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEAVLAYADYGEKFPAAVQKGN-------- 171

                         170
                  ....*....|..
gi 1491109465 482 hpfFIGTQYHPE 493
Cdd:TIGR01855 172 ---IFGTQFHPE 180
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 320-509 5.32e-06

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: 47.19  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 320 LESESIKKEDLGDVDGILVPGG--------FGVRGTEEK----------IRAITYAREKKIPFLGICLGFQLatIEYArs 381
Cdd:cd01745    41 VDDEEDLEQYLELLDGLLLTGGgdvdpplyGEEPHPELGpidperdafeLALLRAALERGKPILGICRGMQL--LNVA-- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 382 iglknanstefvdtdepvidllpeqkkiknMGGTmrlgaykiildeksmvyiLYKSksIYERHRHRYEVNpeyiDLltKN 461
Cdd:cd01745   117 ------------------------------LGGT------------------LYQD--IRVNSLHHQAIK----RL--AD 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1491109465 462 GVKFTGKSEDGRMEVLELEGHPFFIGTQYHPEFTSRVERPS-PIFMGLV 509
Cdd:cd01745   141 GLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 328-373 3.94e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 44.47  E-value: 3.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1491109465 328 EDLGDVDGILVPG----GFGVRGTEEKIRAITYAREKKIPFLGICLGFQL 373
Cdd:PRK13143   34 EEILDADGIVLPGvgafGAAMENLSPLRDVILEAARSGKPFLGICLGMQL 83
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 328-373 5.26e-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: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 44.16  E-value: 5.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491109465 328 EDLGDVDGILVPGG-FGVRGTEEK-----IRAITYAREKKIPFLGICLGFQL 373
Cdd:cd01741    42 PDLDDYDGLVILGGpMSVDEDDYPwlkklKELIRQALAAGKPVLGICLGHQL 93
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 328-373 1.38e-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: 42.87  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491109465 328 EDLGDVDGILVPG----GFGVRGTEEK--IRAITYAREKKIPFLGICLGFQL 373
Cdd:cd01748    32 EEILSADKLILPGvgafGDAMANLRERglIEALKEAIASGKPFLGICLGMQL 83
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 328-373 1.78e-04

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: 42.72  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1491109465 328 EDLGDVDGILVPG----GFGVRGTEEK--IRAITYAREKKIPFLGICLGFQL 373
Cdd:COG0118    34 DEIRAADRLVLPGvgafGDAMENLRERglDEAIREAVAGGKPVLGICLGMQL 85
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 327-498 3.36e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 41.77  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 327 KEDLGDVDGILVPG----GFGVRGTEEK--IRAITYAREKKIPFLGICLGFQLAtieyarsiglknANSTE--------F 392
Cdd:PRK13181   32 PEEIAGADKVILPGvgafGQAMRSLRESglDEALKEHVEKKQPVLGICLGMQLL------------FESSEegnvkglgL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465 393 VDTDepVIDLLPEQKKIKNMG-----GTMRLGAYKIILDEkSMVYILyksksiyerhrHRYEV---NPEYIDLLTKNGVK 464
Cdd:PRK13181  100 IPGD--VKRFRSEPLKVPQMGwnsvkPLKESPLFKGIEEG-SYFYFV-----------HSYYVpceDPEDVLATTEYGVP 165

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1491109465 465 FTGKSEDGRmevleleghpfFIGTQYHPEFTSRV 498
Cdd:PRK13181  166 FCSAVAKDN-----------IYAVQFHPEKSGKA 188
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 312-373 6.90e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 41.45  E-value: 6.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491109465 312 GINVNLKWLESESIKKEDLGDVDGILVPGGF----------GVRGTEEKIRAITYAREKKIPFLGICLGFQL 373
Cdd:cd01740    23 GFEAEDVWHNDLLAGRKDLDDYDGVVLPGGFsygdylragaIAAASPLLMEEVKEFAERGGLVLGICNGFQI 94
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 327-373 1.05e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.50  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491109465 327 KEDLGDVDGILVPG--GFGV-------RGTEEKIRAityAREKKIPFLGICLGFQL 373
Cdd:PRK13141   32 PEEILAADGVILPGvgAFPDamanlreRGLDEVIKE---AVASGKPLLGICLGMQL 84
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 4-145 1.36e-03

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 40.41  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491109465   4 IIVTGGVlSGLGKGVTTASIAKILQSMGYKVTVIKIDPYLNVDA-GTMSPFEHGEVFVLHDG--GEVDLD---LGNYERF 77
Cdd:pfam01656   1 IAIAGTK-GGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSvEGLEGDIAPALQALAEGlkGRVNLDpilLKEKSDE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491109465  78 LNVDLtrdhniTTGKIYKRVIEKERRGDYLGKTVQPIphltdeikseIRSVGERYDFTVIEVGGTVGD 145
Cdd:pfam01656  80 GGLDL------IPGNIDLEKFEKELLGPRKEERLREA----------LEALKEDYDYVIIDGAPGLGE 131
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 315-373 2.03e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 39.54  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491109465 315 VNLKWLESesikKEDLGDVDGILVPGGfgvRGTEEKI---------RAITYAREKKIPFLGICLGFQL 373
Cdd:cd01750    24 VDVRYVEV----PEGLGDADLIILPGS---KDTIQDLawlrkrglaEAIKNYARAGGPVLGICGGYQM 84
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 334-373 3.11e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 39.00  E-value: 3.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1491109465 334 DGILVPG---------GFGVRGTEEKIRAITYAREKkiPFLGICLGFQL 373
Cdd:PRK13146   43 DRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLGICVGMQL 89
 
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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