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Conserved domains on  [gi|736683248|ref|WP_034689095|]
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MULTISPECIES: CTP synthase [Enterococcus]

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

CATH:  3.40.50.880|3.40.50.300
EC:  6.3.4.2
Gene Ontology:  GO:0042802|GO:0006241|GO:0046872|GO:0003883|GO:0006221|GO:0004359|GO:0005524
PubMed:  15296735
SCOP:  4003998|4003747

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 ...
 2-536 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: 1112.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQM 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 162 KADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 242 VDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAFD 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 322 ADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLEDA 401
Cdd:COG0504  321 VKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 402 ASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVF 481
Cdd:COG0504  401 NSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAY-GKEEISERHRHRYEFNNEYREQLEKAGLVF 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736683248 482 SGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGASLTERESK 536
Cdd:COG0504  480 SGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKK 534
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 2-536 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: 1112.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQM 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 162 KADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 242 VDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAFD 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 322 ADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLEDA 401
Cdd:COG0504  321 VKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 402 ASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVF 481
Cdd:COG0504  401 NSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAY-GKEEISERHRHRYEFNNEYREQLEKAGLVF 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736683248 482 SGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGASLTERESK 536
Cdd:COG0504  480 SGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKK 534
pyrG PRK05380
CTP synthetase; Validated
 1-536 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1110.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   1 MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  81 INLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAkmTDSDIIITEVGGTVGDIESLPFLEALRQ 160
Cdd:PRK05380  81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--TDADVVIVEIGGTVGDIESLPFLEAIRQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 161 MKADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESP 240
Cdd:PRK05380 159 LRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 241 DVDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAF 320
Cdd:PRK05380 239 DVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIAN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 321 DADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLED 400
Cdd:PRK05380 319 DVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLED 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 401 AASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLV 480
Cdd:PRK05380 399 ANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIY-GKEEIYERHRHRYEVNNKYREQLEKAGLV 477

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736683248 481 FSGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGASLTERESK 536
Cdd:PRK05380 478 FSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 2-528 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: 901.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248    2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQM 161
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISGPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  162 KADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPD 241
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  242 VDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAFD 321
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  322 ADIELDWVKAHELTSENVdERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLEDA 401
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGV-EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGA 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  402 ASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVF 481
Cdd:TIGR00337 400 NSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLY-GKEEVYERHRHRYEVNNEYREQIENKGLIV 478

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 736683248  482 SGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGA 528
Cdd:TIGR00337 479 SGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 3-267 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: 583.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248    3 KYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   83 LNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQMK 162
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEVGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  163 ADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPDV 242
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....*
gi 736683248  243 DTLYSIPLLLQSQGMDRIVCDHLKL 267
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 3-263 0e+00

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


Pssm-ID: 349767  Cd Length: 261  Bit Score: 515.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   3 KYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  83 LNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQMK 162
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 163 ADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPDV 242
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                        250       260
                 ....*....|....*....|.
gi 736683248 243 DTLYSIPLLLQSQGMDRIVCD 263
Cdd:cd03113  241 SSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 2-536 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: 1112.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQM 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 162 KADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 242 VDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAFD 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 322 ADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLEDA 401
Cdd:COG0504  321 VKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 402 ASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVF 481
Cdd:COG0504  401 NSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAY-GKEEISERHRHRYEFNNEYREQLEKAGLVF 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736683248 482 SGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGASLTERESK 536
Cdd:COG0504  480 SGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKK 534
pyrG PRK05380
CTP synthetase; Validated
 1-536 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1110.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   1 MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  81 INLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAkmTDSDIIITEVGGTVGDIESLPFLEALRQ 160
Cdd:PRK05380  81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--TDADVVIVEIGGTVGDIESLPFLEAIRQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 161 MKADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESP 240
Cdd:PRK05380 159 LRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 241 DVDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAF 320
Cdd:PRK05380 239 DVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIAN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 321 DADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLED 400
Cdd:PRK05380 319 DVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLED 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 401 AASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLV 480
Cdd:PRK05380 399 ANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIY-GKEEIYERHRHRYEVNNKYREQLEKAGLV 477

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736683248 481 FSGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGASLTERESK 536
Cdd:PRK05380 478 FSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 2-528 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: 901.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248    2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQM 161
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISGPDVVIVEIGGTVGDIESLPFLEAIRQF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  162 KADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPD 241
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  242 VDTLYSIPLLLQSQGMDRIVCDHLKLSTPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEALKHSGFAFD 321
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  322 ADIELDWVKAHELTSENVdERLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQMACVEFARNVVGLEDA 401
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGV-EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGA 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  402 ASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGTTTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVF 481
Cdd:TIGR00337 400 NSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLY-GKEEVYERHRHRYEVNNEYREQIENKGLIV 478

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 736683248  482 SGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGA 528
Cdd:TIGR00337 479 SGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
PLN02327 PLN02327
CTP synthase
 2-529 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 671.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   2 TKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  82 NLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMT------DSDIIITEVGGTVGDIESLPFL 155
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPvdgkegPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 156 EALRQMKADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEA 235
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 236 VIESPDVDTLYSIPLLLQSQGMDRIVCDHLKLS--TPEADMTEWKALENRVLNLKKKVRIALVGKYVELPDAYISVVEAL 313
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsvAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 314 KHSGFAFDADIELDWVKAHELTSENVDE----------RLKEADGILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLG 383
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAKEtpdayaaawkLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 384 MQMACVEFARNVVGLEDAASAETIPETTNNIIDLMADQENvENLGGTLRLG-------LYPCKvkkgttTATAYDGAEVV 456
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSK-THMGGTMRLGsrrtyfqTPDCK------SAKLYGNVSFV 473

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736683248 457 QERHRHRYEFNNKYRQQFEAHGLVFSGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFVGAS 529
Cdd:PLN02327 474 DERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 546
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 3-267 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: 583.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248    3 KYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   83 LNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQMK 162
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEVGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  163 ADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPDV 242
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....*
gi 736683248  243 DTLYSIPLLLQSQGMDRIVCDHLKL 267
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 3-263 0e+00

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


Pssm-ID: 349767  Cd Length: 261  Bit Score: 515.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   3 KYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  83 LNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITNEIKEKIMRAAKMTDSDIIITEVGGTVGDIESLPFLEALRQMK 162
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 163 ADVGSDNVMYIHTTLIPYLKAAGEMKTKPTQHSVKELRGLGIQPNILVVRTEQPVSQDVKNKLAQFCDVEPEAVIESPDV 242
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                        250       260
                 ....*....|....*....|.
gi 736683248 243 DTLYSIPLLLQSQGMDRIVCD 263
Cdd:cd03113  241 SSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 291-526 6.24e-139

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


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 400.78  E-value: 6.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 291 VRIALVGKYVELPDAYISVVEALKHSGFAFDADIELDWVKAHELTSENVDERLKEADGILVPGGFGDRGIEGKIEAIRYA 370
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEALKGADGILVPGGFGIRGVEGKILAIKYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 371 RENDVPFLGICLGMQMACVEFARNVVGLEDAASAETIPETTNNIIDLMADQENVENLGGTLRLGLYPCKVKKGtTTATAY 450
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKGVKDLGGTMRLGAYPVILKPG-TLAHKY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736683248 451 DGAEVVQERHRHRYEFNNKYRQQFEAHGLVFSGVSPDNRLVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKAFV 526
Cdd:cd01746  160 YGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
301-528 7.87e-46

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 158.94  E-value: 7.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  301 ELPDAYISVVEALKHSGFAFDADIELDWVkahelTSENVDERLKEADGILVPGGFGDRGI-EGKIEAIRYARENDVPFLG 379
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPN-----DTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  380 ICLGMQMACVEFARNVVGLEDaasaetipettnniidlmadqenVENLGGTLRLGLYPCKVKKGTttataydgAEVVQER 459
Cdd:pfam00117  76 ICLGHQLLALAFGGKVVKAKK-----------------------FGHHGKNSPVGDDGCGLFYGL--------PNVFIVR 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  460 HRHRYEFNNKyrqqFEAHGLVFSGVSPDN-RLVEIVEITEKkfFVGCQFHPELISRPNRPQKLIKAFVGA 528
Cdd:pfam00117 125 RYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 291-528 1.04e-42

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 152.04  E-value: 1.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 291 VRIALVGKYVELPDAYISVVEALKHSGFAFDADIELDWVKAHELTSEnvdERLKEADGI-LVPGGfGDRGIEGKIEAIRY 369
Cdd:PRK06186   2 LRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDP---EDLAGFDGIwCVPGS-PYRNDDGALTAIRF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 370 ARENDVPFLGICLGMQMACVEFARNVVGLEDAASAETIPETTNNII-----DLMADQENVENLGGTLrlglypckvkkgt 444
Cdd:PRK06186  78 ARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIaplscSLVEKTGDIRLRPGSL------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 445 tTATAYdGAEVVQERHRHRYEFNNKYRQQFEAHGLVFSGVSPDNRlVEIVEITEKKFFVGCQFHPELISRPNRPQKLIKA 524
Cdd:PRK06186 145 -IARAY-GTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALAGRPPPLVRA 221


                 ....
gi 736683248 525 FVGA 528
Cdd:PRK06186 222 FLRA 225
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 293-389 1.13e-14

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: 70.32  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 293 IALVGKYVELPDAYISVVEALKHSGFafdadiELDWVKAHELTSENvDERLKEADGILVPGGFGD----RGIEGKIEAIR 368
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAGA------EVDVVSPDGGPVES-DVDLDDYDGLILPGGPGTpddlARDEALLALLR 73

                         90       100
                 ....*....|....*....|.
gi 736683248 369 YARENDVPFLGICLGMQMACV 389
Cdd:cd01653   74 EAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 293-386 8.63e-14

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: 67.23  E-value: 8.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 293 IALVGKYVELPDAYISVVEALKHSGFafdadiELDWVKAHELTSEnVDERLKEADGILVPGGFGD----RGIEGKIEAIR 368
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAGA------EVDVVSPDGGPVE-SDVDLDDYDGLILPGGPGTpddlAWDEALLALLR 73

                         90
                 ....*....|....*...
gi 736683248 369 YARENDVPFLGICLGMQM 386
Cdd:cd03128   74 EAAAAGKPVLGICLGAQL 91
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 337-528 9.77e-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: 70.58  E-value: 9.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 337 ENVDERLKEADGILVPGG-------FGDRGIEGK-----------IEAIRYARENDVPFLGICLGMQMAcvefarNVVgl 398
Cdd:COG2071   41 EDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLL------NVA-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 399 edaasaetipettnniidlmadqenvenLGGTlrlgLYPckvkkgtttatayDGAEVVQERHRHRyefnNKYRQQFEAH- 477
Cdd:COG2071  113 ----------------------------LGGT----LYQ-------------DLPDQVPGALDHR----QPAPRYAPRHt 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 478 ---------------------------------GLVFSGVSPDNrLVEIVEITEKKFFVGCQFHPELISRPNRPQ-KLIK 523
Cdd:COG2071  144 veiepgsrlarilgeeeirvnslhhqavkrlgpGLRVSARAPDG-VIEAIESPGAPFVLGVQWHPEWLAASDPLSrRLFE 222


                 ....*
gi 736683248 524 AFVGA 528
Cdd:COG2071  223 AFVEA 227
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 308-386 3.35e-10

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: 59.67  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGfafdADIELdwvkaheltSENVDErLKEADGILVPG-G-FGD--RGIE--GKIEAIRYARENDVPFLGIC 381
Cdd:COG0118   15 SVAKALERLG----AEVVV---------TSDPDE-IRAADRLVLPGvGaFGDamENLRerGLDEAIREAVAGGKPVLGIC 80


                 ....*
gi 736683248 382 LGMQM 386
Cdd:COG0118   81 LGMQL 85
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-408 5.02e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 59.41  E-value: 5.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGfafdADIELdwvkahELTSEnvDERLKEADGILVPG--GFGD--RGIE--GKIEAIRYARE-NDVPFLGI 380
Cdd:PRK13146  16 SAAKALERAG----AGADV------VVTAD--PDAVAAADRVVLPGvgAFADcmRGLRavGLGEAVIEAVLaAGRPFLGI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736683248 381 CLGMQM------------ACVEFARNVVGLEDAASAETIP 408
Cdd:PRK13146  84 CVGMQLlferglehgdtpGLGLIPGEVVRFQPDGPALKVP 123
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 336-526 6.56e-09

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: 55.66  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 336 SENVDERLKEADGILVPGG--------FGDRGIEGK----------IEAIRYARENDVPFLGICLGMQMAcvefarNVVg 397
Cdd:cd01745   44 EEDLEQYLELLDGLLLTGGgdvdpplyGEEPHPELGpidperdafeLALLRAALERGKPILGICRGMQLL------NVA- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 398 ledaasaetipettnniidlmadqenvenLGGTLRLGLYpckvkkgtttataydgaevVQERHRhryefnnkyrQQFE-- 475
Cdd:cd01745  117 -----------------------------LGGTLYQDIR-------------------VNSLHH----------QAIKrl 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 736683248 476 AHGLVFSGVSPDnRLVEIVEITEKKFFVGCQFHPELISRPNRPQ-KLIKAFV 526
Cdd:cd01745  139 ADGLRVEARAPD-GVIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 308-386 9.92e-09

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: 55.20  E-value: 9.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGFAFdadieldwvkahELTSEnvDERLKEADGILVPG-G-FGD-------RGIegkIEAIRYARENDVPFL 378
Cdd:cd01748   13 SVANALERLGAEV------------IITSD--PEEILSADKLILPGvGaFGDamanlreRGL---IEALKEAIASGKPFL 75


                 ....*...
gi 736683248 379 GICLGMQM 386
Cdd:cd01748   76 GICLGMQL 83
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 347-510 2.08e-08

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 54.96  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  347 DGILVPGG-------FGDRGIEG-----------KIEAIRYARENDVPFLGICLGMQMACVEFARNVvgledaasAETIP 408
Cdd:pfam07722  60 DGLLLTGGpnvdphfYGEEPSESggpydpardayELALIRAALARGKPILGICRGFQLLNVALGGTL--------YQDIQ 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  409 ETTNNIIDLMADQENVENLGGTLRlglypckVKKGTTTATAYDGAEVvqerhrhryEFNNKYRQQFE--AHGLVFSGVSP 486
Cdd:pfam07722 132 EQPGFTDHREHCQVAPYAPSHAVN-------VEPGSLLASLLGSEEF---------RVNSLHHQAIDrlAPGLRVEAVAP 195

                         170       180
                  ....*....|....*....|....*
gi 736683248  487 DNrLVEIVE-ITEKKFFVGCQFHPE 510
Cdd:pfam07722 196 DG-TIEAIEsPNAKGFALGVQWHPE 219
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-386 7.62e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 52.95  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGfafdADIELdwvkaheltSENVDErLKEADGILVPG--GFGD--RGIEGKIEAIRYARENDVPFLGICLG 383
Cdd:PRK13143  15 SVSKALERAG----AEVVI---------TSDPEE-ILDADGIVLPGvgAFGAamENLSPLRDVILEAARSGKPFLGICLG 80


                 ...
gi 736683248 384 MQM 386
Cdd:PRK13143  81 MQL 83
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-386 1.73e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 51.67  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGFafDADIeldwvkaheltSENVDErLKEADGILVPG--GFGD-------RGIegkIEAIRYARENDVPFL 378
Cdd:PRK13141  14 SVEKALERLGA--EAVI-----------TSDPEE-ILAADGVILPGvgAFPDamanlreRGL---DEVIKEAVASGKPLL 76


                 ....*...
gi 736683248 379 GICLGMQM 386
Cdd:PRK13141  77 GICLGMQL 84
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 321-388 3.55e-07

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: 51.10  E-value: 3.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736683248 321 DADIELDWVKAH--ELTSENVDerLKEADGILVPGGF-----GDRGIEGKIEAIRYARENDVPFLGICLGMQMAC 388
Cdd:COG0518   24 EAGIELDVLRVYagEILPYDPD--LEDPDGLILSGGPmsvydEDPWLEDEPALIREAFELGKPVLGICYGAQLLA 96
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-388 8.09e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 49.86  E-value: 8.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGFafDADIeldwvkaheltSENVDErLKEADGILVPG-GFGDRGIE-----GKIEAIRYARENDVPFLGIC 381
Cdd:PRK13181  14 SVANALKRLGV--EAVV-----------SSDPEE-IAGADKVILPGvGAFGQAMRslresGLDEALKEHVEKKQPVLGIC 79


                 ....*..
gi 736683248 382 LGMQMAC 388
Cdd:PRK13181  80 LGMQLLF 86
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 308-386 4.01e-05

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: 44.62  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248  308 SVVEALKHSGFAFdadieldwvkahELTSENvdERLKEADGILVPG--GFGD---RGIEGKIEAI-RYARENDVPFLGIC 381
Cdd:TIGR01855  13 SVKRALKRVGAEP------------VVVKDS--KEAELADKLILPGvgAFGAamaRLRENGLDLFvELVVRLGKPVLGIC 78


                  ....*
gi 736683248  382 LGMQM 386
Cdd:TIGR01855  79 LGMQL 83
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-109 4.45e-05

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: 42.80  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248   3 KYIFVTGGVvSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINVDPGtmspyQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:cd01983    1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGG-----GGLETGLLLGTIVALLALKKADEVIVVV 74

                         90       100
                 ....*....|....*....|....*..
gi 736683248  83 LNKYSNVTTGKIYSEVLRKERKGEYLG 109
Cdd:cd01983   75 DPELGSLLEAVKLLLALLLLGIGIRPD 101
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 313-399 1.96e-04

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: 42.62  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 313 LKHSGFAFDADIElDWVKAHELTSENVD----------ERLKEADGILVPGGF------GDRGIEGKIEAIRYARENDVP 376
Cdd:cd01741    5 LQHDTPEGPGLFE-DLLREAGAETIEIDvvdvyagellPDLDDYDGLVILGGPmsvdedDYPWLKKLKELIRQALAAGKP 83

                         90       100
                 ....*....|....*....|....*..
gi 736683248 377 FLGICLGMQMACV----EFARNVVGLE 399
Cdd:cd01741   84 VLGICLGHQLLARalggKVGRNPKGWE 110
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 312-386 4.16e-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: 42.22  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 312 ALKHSGFafdaDIELDWVKahELTSENVDerLKEADGILVPGGF--GD--RGieGKI--------EAIRYARENDVPFLG 379
Cdd:cd01740   18 AFELAGF----EAEDVWHN--DLLAGRKD--LDDYDGVVLPGGFsyGDylRA--GAIaaaspllmEEVKEFAERGGLVLG 87


                 ....*..
gi 736683248 380 ICLGMQM 386
Cdd:cd01740   88 ICNGFQI 94
PRK00758 PRK00758
GMP synthase subunit A; Validated
 339-391 8.99e-04

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 40.61  E-value: 8.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736683248 339 VDERLKEADGILVPGGfgdRGIEGKIEAIRYARENDVPFLGICLGMQMACVEF 391
Cdd:PRK00758  35 VEEIKAFEDGLILSGG---PDIERAGNCPEYLKELDVPILGICLGHQLIAKAF 84
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 302-386 1.35e-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: 39.92  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 302 LPDayISVVEALKHsgFAFDADIELDWVkaheltseNVDERLKEADGILVPGG---FGD------RGIEgkiEAIRYARE 372
Cdd:cd01750    6 YPD--ISNFTDLDP--LAREPGVDVRYV--------EVPEGLGDADLIILPGSkdtIQDlawlrkRGLA---EAIKNYAR 70

                         90
                 ....*....|....
gi 736683248 373 NDVPFLGICLGMQM 386
Cdd:cd01750   71 AGGPVLGICGGYQM 84
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
340-388 1.96e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 39.71  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736683248 340 DERLKEADGILVPGGF--GDRGIEGKI-------EAIRYARENDVPFLGICLGMQMAC 388
Cdd:PRK03619  36 ETDLDGVDAVVLPGGFsyGDYLRCGAIaafspimKAVKEFAEKGKPVLGICNGFQILT 93
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 329-391 2.00e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 39.44  E-value: 2.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736683248 329 VKAHELTSEnvDERLKEADGILV---PGGFGDRGIegKIEAIRYARENdVPFLGICLGMQMACVEF 391
Cdd:cd01743   28 VRNDEITLE--ELELLNPDAIVIspgPGHPEDAGI--SLEIIRALAGK-VPILGVCLGHQAIAEAF 88
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 308-386 3.82e-03

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 40.08  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736683248 308 SVVEALKHSGFafdadieldwvkahELTSENVDERLKEADGILVPG--GFGDR----GIEGKIEAIRYARENDVPFLGIC 381
Cdd:PLN02617  21 SVRNAIRHLGF--------------TIKDVQTPEDILNADRLIFPGvgAFGSAmdvlNNRGMAEALREYIQNDRPFLGIC 86


                 ....*
gi 736683248 382 LGMQM 386
Cdd:PLN02617  87 LGLQL 91
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 347-386 6.41e-03

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 38.85  E-value: 6.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 736683248 347 DGILVPGGFGD-RGIEGKIEAIRYARENDVPFLGICLGMQM 386
Cdd:COG0505  219 DGVFLSNGPGDpAALDYAIETIRELLGKGIPIFGICLGHQL 259
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 341-387 7.30e-03

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 37.68  E-value: 7.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 736683248  341 ERLKEAD--GILVPGGFGDRGIEGKIEAIRYARENDVPFLGICLGMQ-MA 387
Cdd:TIGR00888  35 EEIREKNpkGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGMQlMA 84
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
345-386 8.01e-03

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 38.52  E-value: 8.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 736683248 345 EADGILVPGGFGD-RGIEGKIEAIRYARENDVPFLGICLGMQM 386
Cdd:PRK12564 218 NPDGVFLSNGPGDpAALDYAIEMIRELLEKKIPIFGICLGHQL 260
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
344-386 8.91e-03

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 37.60  E-value: 8.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 736683248  344 KEADGILVPGGFGDRGI------EGKIEAIRYARENDVPFLGICLGMQM 386
Cdd:pfam07685  41 PDADLIILPGGKPTIQDlallrnSGMDEAIKEAAEDGGPVLGICGGYQM 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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