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Conserved domains on  [gi|16130687|ref|NP_417260|]
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CTP synthetase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

CTP synthase( domain architecture ID 11480813)

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

EC:  6.3.4.2
PubMed:  15296735

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
3-543 0e+00

CTP synthetase; Validated


:

Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1080.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVS 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  323 VNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  402 TEFVPDCKYPVVALITEWRDEngnvevrsekSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130687  482 EDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
3-543 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1080.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVS 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  323 VNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  402 TEFVPDCKYPVVALITEWRDEngnvevrsekSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130687  482 EDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
3-544 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: 1064.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 161 AVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504 161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504 241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 321 VSVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENA 399
Cdd:COG0504 321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 400 NSTEFVPDCKYPVVALITEwrdengnvevRSEKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLK 479
Cdd:COG0504 401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130687 480 QIEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQA 544
Cdd:COG0504 471 QLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
3-535 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: 974.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687     3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   161 AVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   321 VSVNIKLIDSQDVETRGVEILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   401 STEFVPDCKYPVVALITEWRDengnvevrseKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQ 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16130687   481 IEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
5-266 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: 524.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687     5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241
                         250       260
                  ....*....|....*....|....
gi 16130687   243 SIYKIPGLLKSQGLDDYICKRFSL 266
Cdd:pfam06418 242 SIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
5-262 1.36e-166

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: 472.74  E-value: 1.36e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113   2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGH--DVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113  82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPepDVCIVEIGGTVGDIESLPFLEALRQFQF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113 162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241
                       250       260
                ....*....|....*....|
gi 16130687 243 SIYKIPGLLKSQGLDDYICK 262
Cdd:cd03113 242 SIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
3-543 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1080.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:PRK05380 162 ELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  243 SIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVS 322
Cdd:PRK05380 242 SIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  323 VNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENANS 401
Cdd:PRK05380 322 VNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANS 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  402 TEFVPDCKYPVVALITEWRDEngnvevrsekSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQI 481
Cdd:PRK05380 402 TEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQL 471
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130687  482 EDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQ 543
Cdd:PRK05380 472 EKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
3-544 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: 1064.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 161 AVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504 161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:COG0504 241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 321 VSVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENA 399
Cdd:COG0504 321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 400 NSTEFVPDCKYPVVALITEwrdengnvevRSEKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLK 479
Cdd:COG0504 401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130687 480 QIEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQA 544
Cdd:COG0504 471 QLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
3-535 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: 974.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687     3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   161 AVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   241 VDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   321 VSVNIKLIDSQDVETRGVEILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   401 STEFVPDCKYPVVALITEWRDengnvevrseKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQ 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16130687   481 IEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
PLN02327 PLN02327
CTP synthase
3-537 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 639.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRT 82
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   83 KMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIK---ERV----LEGGEGH-DVVLVEIGGTVGDIESLPFL 154
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQewiERVakipVDGKEGPaDVCVIELGGTVGDIESMPFI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  155 EAIRQMAVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKA 234
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  235 VISLKDVDSIYKIPGLLKSQGLDDYICKRFSL--NCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEAL 312
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlsVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  313 KHGGLKNRVSVNIKLIDSQDVETRGV-----------EILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLG 381
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAketpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  382 MQVALIDYARHVANMENANSTEFVPDCKYPVVALITEwrdengnvevrSEKSDLGGTMRLGAQQCQL-VDDSLVRQLY-N 459
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPE-----------GSKTHMGGTMRLGSRRTYFqTPDCKSAKLYgN 469
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130687  460 APTIVERHRHRYEVNNMLLKQIEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAS 537
Cdd:PLN02327 470 VSFVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAAS 547
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
5-266 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: 524.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687     5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687    85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGE--GHDVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:pfam06418  82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241
                         250       260
                  ....*....|....*....|....
gi 16130687   243 SIYKIPGLLKSQGLDDYICKRFSL 266
Cdd:pfam06418 242 SIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
5-262 1.36e-166

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: 472.74  E-value: 1.36e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113   2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  85 SRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGH--DVVLVEIGGTVGDIESLPFLEAIRQMAV 162
Cdd:cd03113  82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPepDVCIVEIGGTVGDIESLPFLEALRQFQF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 163 EIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113 162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241
                       250       260
                ....*....|....*....|
gi 16130687 243 SIYKIPGLLKSQGLDDYICK 262
Cdd:cd03113 242 SIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
290-533 2.60e-136

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: 394.61  E-value: 2.60e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 290 VTIGMVGKYIELPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGYRGVEGMITTARFA 368
Cdd:cd01746   1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAeEALKGADGILVPGGFGIRGVEGKILAIKYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 369 RENNIPYLGICLGMQVALIDYARHVANMENANSTEFVPDCKYPVVALITEWRDengnvevrseKSDLGGTMRLGAQQCQL 448
Cdd:cd01746  81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKG----------VKDLGGTMRLGAYPVIL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 449 VDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQIEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPL 528
Cdd:cd01746 151 KPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230

                ....*
gi 16130687 529 FAGFV 533
Cdd:cd01746 231 FVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
300-535 1.64e-45

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 158.17  E-value: 1.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   300 ELPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGVEIlkglDAILVPGGFGYRG-VEGMITTARFARENNIPYLGI 378
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENP----DGIILSGGPGSPGaAGGAIEAIREARELKIPILGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   379 CLGMQVALIDYArhvanmenanstefvpdckypvvalitewrdenGNVEVRSEKSDLGGTMRLGAQQCQLVDDSlvrqly 458
Cdd:pfam00117  77 CLGHQLLALAFG---------------------------------GKVVKAKKFGHHGKNSPVGDDGCGLFYGL------ 117
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130687   459 nAPTIVERHRHRYEVNNMLLKqiedAGLRVAGRSGDD-QLVEIIEVPNhPWFvACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:pfam00117 118 -PNVFIVRRYHSYAVDPDTLP----DGLEVTATSENDgTIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
292-538 1.19e-35

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 133.17  E-value: 1.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  292 IGMVGKYIELPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVetRGVEILKGLDAI-LVPGGfGYRGVEGMITTARFARE 370
Cdd:PRK06186   4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI--TDPEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  371 NNIPYLGICLGMQVALIDYARHVANMENANSTEFVPDCKYPVVA-LITEWRDENGNVEVRSeksdlggtmrlgaqqcqlv 449
Cdd:PRK06186  81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDIRLRP------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  450 dDSLVRQLYNAPTIVERHRHRYEVNNMLLKQIEDAGLRVAGRsGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLF 529
Cdd:PRK06186 142 -GSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGW-DEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLV 219

                 ....*....
gi 16130687  530 AGFVKAASE 538
Cdd:PRK06186 220 RAFLRAARA 228
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
327-539 1.60e-14

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: 72.89  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 327 LIDSQDVETRGVEILKGLDAILVPGG-------FGYRGVEGM-----------ITTARFARENNIPYLGICLGMQVAlid 388
Cdd:COG2071  33 LLPPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLL--- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 389 yarhvanmenaNstefvpdckypvVA----LITEWRDENGNVEVRSEKSDlggtMRLGAQQCQLVDDSLVRQLYNAPTIv 464
Cdd:COG2071 110 -----------N------------VAlggtLYQDLPDQVPGALDHRQPAP----RYAPRHTVEIEPGSRLARILGEEEI- 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130687 465 erhrhryEVN---NMLLKQIEDaGLRVAGRSgDDQLVEIIEVPNHPWFVACQFHPEF-TSTPRDGHPLFAGFVKAASEF 539
Cdd:COG2071 162 -------RVNslhHQAVKRLGP-GLRVSARA-PDGVIEAIESPGAPFVLGVQWHPEWlAASDPLSRRLFEAFVEAARAR 231
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
292-387 1.74e-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: 1.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvsVNIKLIDSQDVETRGVEILKGLDAILVPGGFGYRGV----EGMITTARF 367
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDlardEALLALLRE 74
                        90       100
                ....*....|....*....|
gi 16130687 368 ARENNIPYLGICLGMQVALI 387
Cdd:cd01653  75 AAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
292-384 3.07e-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: 56.83  E-value: 3.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 292 IGMVGKYIELPDAYKSVIEALKHGGlknrvsVNIKLIDSQDVETRGVEILKGLDAILVPGGFGY----RGVEGMITTARF 367
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTpddlAWDEALLALLRE 74
                        90
                ....*....|....*..
gi 16130687 368 ARENNIPYLGICLGMQV 384
Cdd:cd03128  75 AAAAGKPVLGICLGAQL 91
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
327-533 3.58e-07

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: 50.65  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 327 LIDSQDVETRGVEILKGLDAILVPGG-----FGYRGV-------------EGMITTARFARENNIPYLGICLGMQvalid 388
Cdd:cd01745  37 LLPPVDDEEDLEQYLELLDGLLLTGGgdvdpPLYGEEphpelgpidperdAFELALLRAALERGKPILGICRGMQ----- 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 389 yarhvanmenanstefvpdckypvvaLItewrdengNVEvrseksdLGGTMrlgaqqCQLVddslvrqlynaptiverhr 468
Cdd:cd01745 112 --------------------------LL--------NVA-------LGGTL------YQDI------------------- 125
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130687 469 hryEVN---NMLLKQIEDaGLRVAGRSGDdQLVEIIEVPNHPWFVACQFHPEFTSTPRDGH-PLFAGFV 533
Cdd:cd01745 126 ---RVNslhHQAIKRLAD-GLRVEARAPD-GVIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
135-210 4.44e-06

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: 45.50  E-value: 4.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130687 135 DVVLVEIGGTVGDIESLPFleairQMAVEIGREHTLFMHLTLVPYMAASGEVKTKptqhSVKELLSIGIQPDILIC 210
Cdd:cd01983  39 DYVLIDGGGGLETGLLLGT-----IVALLALKKADEVIVVVDPELGSLLEAVKLL----LALLLLGIGIRPDGIVL 105
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
366-517 9.34e-06

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: 46.87  E-value: 9.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   366 RFARENNIPYLGICLGMQ---VAL-------IDYARHVanmenansTEFVPDCKYPVVAlitewrdengnvevrseksdl 435
Cdd:pfam07722  99 RAALARGKPILGICRGFQllnVALggtlyqdIQEQPGF--------TDHREHCQVAPYA--------------------- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   436 ggtmrlGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMllkqieDAGLRVAGRSgDDQLVEIIEVPNHPWFV-ACQF 514
Cdd:pfam07722 150 ------PSHAVNVEPGSLLASLLGSEEFRVNSLHHQAIDRL------APGLRVEAVA-PDGTIEAIESPNAKGFAlGVQW 216

                  ...
gi 16130687   515 HPE 517
Cdd:pfam07722 217 HPE 219
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
306-383 1.44e-04

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: 43.08  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687   306 KSVIEALKHGGLKNRVSVNiklidsqdvetrgVEILKGLDAILVPG----GFGYRGVE--GMITTARFARENNIPYLGIC 379
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVVKD-------------SKEAELADKLILPGvgafGAAMARLRenGLDLFVELVVRLGKPVLGIC 78

                  ....
gi 16130687   380 LGMQ 383
Cdd:TIGR01855  79 LGMQ 82
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
484-543 1.74e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 43.35  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130687  484 AGLRVAGRSGDDqLVEIIEVPNHPWFVACQFHPEFTSTPRD-GHPLFAGFVKAASEFQKRQ 543
Cdd:PRK11366 192 PRLRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITACQHHIAEK 251
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
306-384 5.50e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 41.27  E-value: 5.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  306 KSVIEALKHGGLKNRVsvniklidsqdveTRGVEILKGLDAILVPG--GFG-------YRGvegMITTARFARENNIPYL 376
Cdd:PRK13141  13 RSVEKALERLGAEAVI-------------TSDPEEILAADGVILPGvgAFPdamanlrERG---LDEVIKEAVASGKPLL 76

                 ....*...
gi 16130687  377 GICLGMQV 384
Cdd:PRK13141  77 GICLGMQL 84
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
306-384 1.27e-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: 40.17  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 306 KSVIEALKHGGLKNRVsvniklidsqdveTRGVEILKGLDAILVPG----GFGYRGVE--GMITTARFARENNIPYLGIC 379
Cdd:cd01748  12 RSVANALERLGAEVII-------------TSDPEEILSADKLILPGvgafGDAMANLRerGLIEALKEAIASGKPFLGIC 78

                ....*
gi 16130687 380 LGMQV 384
Cdd:cd01748  79 LGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
307-384 1.27e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 40.24  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687  307 SVIEALKHGGLKNRVSVNIKLIDSQDvetrgveilkgldAILVPG--GFGyrgvEGMITTARF------ARENNIPYLGI 378
Cdd:PRK13143  15 SVSKALERAGAEVVITSDPEEILDAD-------------GIVLPGvgAFG----AAMENLSPLrdvileAARSGKPFLGI 77

                 ....*.
gi 16130687  379 CLGMQV 384
Cdd:PRK13143  78 CLGMQL 83
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
306-384 4.38e-03

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


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 38.48  E-value: 4.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130687 306 KSVIEALKhgglknRVSVNIKLIDSQDVetrgveiLKGLDAILVPG----GFGYRGVE--GMITTARFARENNIPYLGIC 379
Cdd:COG0118  14 RSVAKALE------RLGAEVVVTSDPDE-------IRAADRLVLPGvgafGDAMENLRerGLDEAIREAVAGGKPVLGIC 80

                ....*
gi 16130687 380 LGMQV 384
Cdd:COG0118  81 LGMQL 85
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
341-384 5.15e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 38.56  E-value: 5.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130687  341 LKGLDAILVPGGFGY----RGveGMIttARFAR---------ENNIPYLGICLGMQV 384
Cdd:PRK03619  39 LDGVDAVVLPGGFSYgdylRC--GAI--AAFSPimkavkefaEKGKPVLGICNGFQI 91
 
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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