NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491114886|ref|WP_004973343|]
View 

MULTISPECIES: CTP synthase [Acinetobacter]

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
Gene Ontology:  GO:0000166|GO:0006241|GO:0046872|GO:0003883
PubMed:  15296735

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-544 0e+00

CTP synthetase; Validated


:

Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1077.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   1 MTHFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLR 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  81 RaKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGEGYDVAIVEIGGTVGDIESLPFMESVRQL 160
Cdd:PRK05380  81 T-NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 161 MVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKD 240
Cdd:PRK05380 160 RLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 241 AKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQN 320
Cdd:PRK05380 240 VDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIAN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 321 RVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIAD 400
Cdd:PRK05380 319 DVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLED 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 401 ASSTEFNRSTKSPLIGLITEWLDErgevqqrsvdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRYI 480
Cdd:PRK05380 399 ANSTEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYR 468

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491114886 481 PVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQHQK 544
Cdd:PRK05380 469 EQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKR 532
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-544 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1077.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   1 MTHFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLR 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  81 RaKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGEGYDVAIVEIGGTVGDIESLPFMESVRQL 160
Cdd:PRK05380  81 T-NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 161 MVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKD 240
Cdd:PRK05380 160 RLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 241 AKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQN 320
Cdd:PRK05380 240 VDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIAN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 321 RVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIAD 400
Cdd:PRK05380 319 DVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLED 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 401 ASSTEFNRSTKSPLIGLITEWLDErgevqqrsvdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRYI 480
Cdd:PRK05380 399 ANSTEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYR 468

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491114886 481 PVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQHQK 544
Cdd:PRK05380 469 EQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKR 532
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 2-546 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: 1061.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   2 THFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRr 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  82 AKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQ 159
Cdd:COG0504   80 INLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 160 LMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCK 239
Cdd:COG0504  160 LRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 240 DAKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQ 319
Cdd:COG0504  240 DVDSIYEVPLMLHEQGLDEIVLKKLGLEA-REPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 320 NRVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIA 399
Cdd:COG0504  319 NGVKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 400 DASSTEFNRSTKSPLIGLITEwldergevqQRSVdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRY 479
Cdd:COG0504  399 DANSTEFDPNTPHPVIDLMPE---------QKDV-SDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEY 468

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491114886 480 IPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQHQKTK 546
Cdd:COG0504  469 REQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 2-537 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: 863.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886    2 THFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRR 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   82 aKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQ 159
Cdd:TIGR00337  81 -NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  160 LMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCK 239
Cdd:TIGR00337 160 FRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  240 DAKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQ 319
Cdd:TIGR00337 240 DVSSIYEVPLLLLKQGLDDYLCRRLNLNC-DEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  320 NRVKVEIDYVNAEDLESQDVnTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIA 399
Cdd:TIGR00337 319 LDTKVNIKWIDSEDLEEEGV-EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  400 DASSTEFNRSTKSPLIGLITEWLDErgevqqrsvdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRY 479
Cdd:TIGR00337 398 GANSTEFDPDTKYPVVDLLPEQKDI----------SDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEY 467

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 491114886  480 IPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGA 537
Cdd:TIGR00337 468 REQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 4-265 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: 522.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886    4 FIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRrAK 83
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLD-IN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   84 MTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQLM 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  162 VELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKDA 241
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....
gi 491114886  242 KTIYQIPRTFYEQDVDDLICERFG 265
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLN 264
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 4-262 3.19e-160

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: 456.56  E-value: 3.19e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   4 FIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRRaK 83
Cdd:cd03113    2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDV-N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  84 MTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAG--EGYDVAIVEIGGTVGDIESLPFMESVRQLM 161
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAkiPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 162 VELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKDA 241
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                        250       260
                 ....*....|....*....|.
gi 491114886 242 KTIYQIPRTFYEQDVDDLICE 262
Cdd:cd03113  241 SSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
pyrG PRK05380
CTP synthetase; Validated
 1-544 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 1077.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   1 MTHFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLR 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  81 RaKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGEGYDVAIVEIGGTVGDIESLPFMESVRQL 160
Cdd:PRK05380  81 T-NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 161 MVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKD 240
Cdd:PRK05380 160 RLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 241 AKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQN 320
Cdd:PRK05380 240 VDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIAN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 321 RVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIAD 400
Cdd:PRK05380 319 DVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLED 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 401 ASSTEFNRSTKSPLIGLITEWLDErgevqqrsvdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRYI 480
Cdd:PRK05380 399 ANSTEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYR 468

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491114886 481 PVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQHQK 544
Cdd:PRK05380 469 EQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKR 532
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 2-546 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: 1061.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   2 THFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRr 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  82 AKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQ 159
Cdd:COG0504   80 INLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 160 LMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCK 239
Cdd:COG0504  160 LRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 240 DAKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQ 319
Cdd:COG0504  240 DVDSIYEVPLMLHEQGLDEIVLKKLGLEA-REPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 320 NRVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIA 399
Cdd:COG0504  319 NGVKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 400 DASSTEFNRSTKSPLIGLITEwldergevqQRSVdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRY 479
Cdd:COG0504  399 DANSTEFDPNTPHPVIDLMPE---------QKDV-SDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEY 468

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491114886 480 IPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQHQKTK 546
Cdd:COG0504  469 REQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 2-537 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: 863.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886    2 THFIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRR 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   82 aKMTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQ 159
Cdd:TIGR00337  81 -NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  160 LMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCK 239
Cdd:TIGR00337 160 FRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAK 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  240 DAKTIYQIPRTFYEQDVDDLICERFGFNDlPEADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALLHAGIQ 319
Cdd:TIGR00337 240 DVSSIYEVPLLLLKQGLDDYLCRRLNLNC-DEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  320 NRVKVEIDYVNAEDLESQDVnTVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLAVIEYARNVAGIA 399
Cdd:TIGR00337 319 LDTKVNIKWIDSEDLEEEGV-EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  400 DASSTEFNRSTKSPLIGLITEWLDErgevqqrsvdSDLGGTMRLGAQKSELVEGTKTREVYGSAEIVERHRHRYEMNNRY 479
Cdd:TIGR00337 398 GANSTEFDPDTKYPVVDLLPEQKDI----------SDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEY 467

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 491114886  480 IPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGA 537
Cdd:TIGR00337 468 REQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
PLN02327 PLN02327
CTP synthase
 4-541 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 636.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   4 FIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRrAK 83
Cdd:PLN02327   3 YVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLD-VT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  84 MTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAG-------EG-YDVAIVEIGGTVGDIESLPFME 155
Cdd:PLN02327  82 LTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAkipvdgkEGpADVCVIELGGTVGDIESMPFIE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 156 SVRQLMVELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAV 235
Cdd:PLN02327 162 ALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAENI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 236 VVCKDAKTIYQIPRTFYEQDVDDLICERFGFNDLP-EADLSDWDNVVDALLNPEYSVRVAMVGKYVELPDAYKSVNEALL 314
Cdd:PLN02327 242 LNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVArEPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 315 HAGIQNRVKVEIDYVNAEDLESQDVN----------TVLKDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGM 384
Cdd:PLN02327 322 HASVACSRKLVIDWVAASDLEDETAKetpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLGM 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 385 QLAVIEYARNVAGIADASSTEFNRSTKSPLIGLITEWLDERgevqqrsvdsdLGGTMRLGAQKSEL-VEGTKTREVYGSA 463
Cdd:PLN02327 402 QIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTH-----------MGGTMRLGSRRTYFqTPDCKSAKLYGNV 470

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491114886 464 EIV-ERHRHRYEMNNRYIPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPLFAGFIGAAKQQ 541
Cdd:PLN02327 471 SFVdERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQ 549
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 4-265 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: 522.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886    4 FIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRrAK 83
Cdd:pfam06418   2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLD-IN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   84 MTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAGE--GYDVAIVEIGGTVGDIESLPFMESVRQLM 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  162 VELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKDA 241
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240

                         250       260
                  ....*....|....*....|....
gi 491114886  242 KTIYQIPRTFYEQDVDDLICERFG 265
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLN 264
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 4-262 3.19e-160

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: 456.56  E-value: 3.19e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886   4 FIFVTGGVVSSLGKGISAASVAALLEARGLKVTMVKMDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGYYERFLRRaK 83
Cdd:cd03113    2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDV-N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  84 MTKLNNFTSGRVYQDVLNKERRGDYLGGTVQVIPHITDNIKERVLRAG--EGYDVAIVEIGGTVGDIESLPFMESVRQLM 161
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAkiPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 162 VELGHKRTMLMHLTLLPYIKSAAELKTKPTQHSVKELLSIGIQPDILICRTEHDVDADTTRKIALFTNVEARAVVVCKDA 241
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240

                        250       260
                 ....*....|....*....|.
gi 491114886 242 KTIYQIPRTFYEQDVDDLICE 262
Cdd:cd03113  241 SSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 291-535 1.14e-134

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: 390.38  E-value: 1.14e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 291 VRVAMVGKYVELPDAYKSVNEALLHAGIQNRVKVEIDYVNAEDLESQDVNTVLKDADAILVPGGFGERGTEGKMQAIKYA 370
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEALKGADGILVPGGFGIRGVEGKILAIKYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 371 RENGVPFLGICLGMQLAVIEYARNVAGIADASSTEFNRSTKSPLIGLITEWLDergevqqrsvDSDLGGTMRLGAQKSEL 450
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKG----------VKDLGGTMRLGAYPVIL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 451 VEGTKTREVYGSAEIVERHRHRYEMNNRYIPVLEEAGLKISGYSPIQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGHPL 530
Cdd:cd01746  151 KPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230


                 ....*
gi 491114886 531 FAGFI 535
Cdd:cd01746  231 FVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
301-537 5.10e-46

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 159.71  E-value: 5.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  301 ELPDAYKSVNEALLHAGIQNRVKVEIDYVNAEDLESQDVNtvlkdADAILVPGGFGERGT-EGKMQAIKYARENGVPFLG 379
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN-----PDGIILSGGPGSPGAaGGAIEAIREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  380 ICLGMQLAVIEYARNVAgiadasstefnrstKSPLIGlitewldergevqqrsvdsDLGGTMRLGAQKSELVEGTKTrev 459
Cdd:pfam00117  76 ICLGHQLLALAFGGKVV--------------KAKKFG-------------------HHGKNSPVGDDGCGLFYGLPN--- 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491114886  460 ygsaEIVERHRHRYEMNNRYIPvleeAGLKISGYSPIQHLVETVEIPQHPwFIAVQFHPEFTSSPRDGHPLFAGFIGA 537
Cdd:pfam00117 120 ----VFIVRRYHSYAVDPDTLP----DGLEVTATSENDGTIMGIRHKKLP-IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 291-541 3.30e-42

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 150.88  E-value: 3.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 291 VRVAMVGKYVELPDAYKSVNEALLHAGIQNRVKVEIDYVNAEDLESQDVntvLKDADAI-LVPGGfGERGTEGKMQAIKY 369
Cdd:PRK06186   2 LRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPED---LAGFDGIwCVPGS-PYRNDDGALTAIRF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 370 ARENGVPFLGICLGMQLAVIEYARNVAGIADASSTEFNRSTKSPLIG-LITEWLDERGEVqqrsvdsdlggtmrlgaqks 448
Cdd:PRK06186  78 ARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDI-------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 449 ELVEGTKTREVYGSAEIVERHRHRYEMNNRYIPVLEEAGLKISGYSPiQHLVETVEIPQHPWFIAVQFHPEFTSSPRDGH 528
Cdd:PRK06186 138 RLRPGSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDE-DGDVRAVELPGHPFFVATLFQPERAALAGRPP 216

                        250
                 ....*....|...
gi 491114886 529 PLFAGFIGAAKQQ 541
Cdd:PRK06186 217 PLVRAFLRAARAA 229
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 315-540 5.99e-15

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: 74.43  E-value: 5.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 315 HAGIQNRVKVEIDYVNA------------EDLESQDVNTVLKDADAILVPGG-------FGERGTEGK-----------M 364
Cdd:COG2071    7 TAGGYPAHYLPEDYVRAvraagglpvllpPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 365 QAIKYARENGVPFLGICLGMQLAvieyarNVA-GiadasstefnrstkspliG-LITEWLDERGEVQQRSVDSDlggtMR 442
Cdd:COG2071   87 ALIRAALERGKPVLGICRGMQLL------NVAlG------------------GtLYQDLPDQVPGALDHRQPAP----RY 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 443 LGAQKSELVEGTKTREVYGSAEIVERHRHRyemnnryipvleEA------GLKISGYSPiQHLVETVEIPQHPWFIAVQF 516
Cdd:COG2071  139 APRHTVEIEPGSRLARILGEEEIRVNSLHH------------QAvkrlgpGLRVSARAP-DGVIEAIESPGAPFVLGVQW 205

                        250       260
                 ....*....|....*....|....*.
gi 491114886 517 HPEFT--SSPRDgHPLFAGFIGAAKQ 540
Cdd:COG2071  206 HPEWLaaSDPLS-RRLFEAFVEAARA 230
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 293-389 5.83e-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: 68.39  E-value: 5.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 293 VAMVGKYVELPDAYKSVNEALLHAGiqnrvkVEIDYVNAEDLESQDvNTVLKDADAILVPGGFG----ERGTEGKMQAIK 368
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAG------AEVDVVSPDGGPVES-DVDLDDYDGLILPGGPGtpddLARDEALLALLR 73

                         90       100
                 ....*....|....*....|.
gi 491114886 369 YARENGVPFLGICLGMQLAVI 389
Cdd:cd01653   74 EAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 293-386 1.55e-12

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: 63.37  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 293 VAMVGKYVELPDAYKSVNEALLHAGiqnrvkVEIDYVNAEDLESQDvNTVLKDADAILVPGGFG----ERGTEGKMQAIK 368
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAG------AEVDVVSPDGGPVES-DVDLDDYDGLILPGGPGtpddLAWDEALLALLR 73

                         90
                 ....*....|....*...
gi 491114886 369 YARENGVPFLGICLGMQL 386
Cdd:cd03128   74 EAAAAGKPVLGICLGAQL 91
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 307-386 6.26e-09

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 55.91  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 307 KSVNEALLHAGIQNRVkveidyvnaedleSQDVNtVLKDADAILVPG--GFG-------ERGTEgkmQAIKYARENGVPF 377
Cdd:PRK13141  13 RSVEKALERLGAEAVI-------------TSDPE-EILAADGVILPGvgAFPdamanlrERGLD---EVIKEAVASGKPL 75


                 ....*....
gi 491114886 378 LGICLGMQL 386
Cdd:PRK13141  76 LGICLGMQL 84
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 333-519 1.49e-08

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 55.34  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  333 DLESQDVNTVLKDADAILVPGG-------FGERGTEG-----------KMQAIKYARENGVPFLGICLGMQLAvieyarN 394
Cdd:pfam07722  46 LGDPEDAAAILDRLDGLLLTGGpnvdphfYGEEPSESggpydpardayELALIRAALARGKPILGICRGFQLL------N 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  395 VAgiadasstefnrstkspLIGL----ITEWLDERGEVQQRSVDSDLGgtmrlgAQKSELVEGTKTREVYGSAEIVERHR 470
Cdd:pfam07722 120 VA-----------------LGGTlyqdIQEQPGFTDHREHCQVAPYAP------SHAVNVEPGSLLASLLGSEEFRVNSL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 491114886  471 HRyemnnRYIPVLEEaGLKISGYSPIQhLVETVEIPQHPWF-IAVQFHPE 519
Cdd:pfam07722 177 HH-----QAIDRLAP-GLRVEAVAPDG-TIEAIESPNAKGFaLGVQWHPE 219
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 307-386 2.95e-08

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: 53.89  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 307 KSVNEALLHAGIQNRVkveidyvnAEDLEsqdvntVLKDADAILVPG-G-FGE-----RGTEGKmQAIKYARENGVPFLG 379
Cdd:COG0118   14 RSVAKALERLGAEVVV--------TSDPD------EIRAADRLVLPGvGaFGDamenlRERGLD-EAIREAVAGGKPVLG 78


                 ....*..
gi 491114886 380 ICLGMQL 386
Cdd:COG0118   79 ICLGMQL 85
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 307-386 5.80e-07

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: 50.19  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 307 KSVNEALLHAGIQNRVkveidYVNAEDLESqdvntvlkdADAILVPG-G-FG---ERGTEGKM-QAIKYARENGVPFLGI 380
Cdd:cd01748   12 RSVANALERLGAEVII-----TSDPEEILS---------ADKLILPGvGaFGdamANLRERGLiEALKEAIASGKPFLGI 77


                 ....*.
gi 491114886 381 CLGMQL 386
Cdd:cd01748   78 CLGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-386 2.02e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 48.71  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 308 SVNEALLHAGiqnrVKVEIdyvnaedleSQDVNTVLkDADAILVPG--GFGE--RGTEGKMQAIKYARENGVPFLGICLG 383
Cdd:PRK13143  15 SVSKALERAG----AEVVI---------TSDPEEIL-DADGIVLPGvgAFGAamENLSPLRDVILEAARSGKPFLGICLG 80


                 ...
gi 491114886 384 MQL 386
Cdd:PRK13143  81 MQL 83
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 308-386 2.16e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 48.63  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 308 SVNEALLHAGIQNRVKVeidyvnaedleSQDVNTVLkDADAILVPG---------GFGERGTEGKMqaIKYARENGVPFL 378
Cdd:PRK13146  16 SAAKALERAGAGADVVV-----------TADPDAVA-AADRVVLPGvgafadcmrGLRAVGLGEAV--IEAVLAAGRPFL 81


                 ....*...
gi 491114886 379 GICLGMQL 386
Cdd:PRK13146  82 GICVGMQL 89
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 324-386 3.78e-06

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 48.02  E-value: 3.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491114886 324 VEIDYVNAEDLESQDVNTVLKDADAILVPGGF-----GERGTEGKMQAIKYARENGVPFLGICLGMQL 386
Cdd:COG0518   27 IELDVLRVYAGEILPYDPDLEDPDGLILSGGPmsvydEDPWLEDEPALIREAFELGKPVLGICYGAQL 94
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 343-386 3.91e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 47.55  E-value: 3.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491114886 343 LKDADAILVPG---------GFGERGTEgkmQAIKYARENGVPFLGICLGMQL 386
Cdd:PRK13181  35 IAGADKVILPGvgafgqamrSLRESGLD---EALKEHVEKKQPVLGICLGMQL 84
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 333-535 4.38e-06

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 47.57  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 333 DLESQDVNTVLKDADAILVPGG--------FGERGTEGK----------MQAIKYARENGVPFLGICLGMQLAvieyarN 394
Cdd:cd01745   41 VDDEEDLEQYLELLDGLLLTGGgdvdpplyGEEPHPELGpidperdafeLALLRAALERGKPILGICRGMQLL------N 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 395 VAgiadasstefnrstkspliglitewldergevqqrsvdsdLGGTMrlgaqkselvegtktrevygsaeiverhrHRYE 474
Cdd:cd01745  115 VA----------------------------------------LGGTL-----------------------------YQDI 125

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491114886 475 MNNRY----IPVLEEaGLKISGYSPIQhLVETVEIPQHPWFIAVQFHPEFTSSPRDGH-PLFAGFI 535
Cdd:cd01745  126 RVNSLhhqaIKRLAD-GLRVEARAPDG-VIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 335-546 1.32e-05

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 46.82  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 335 ESQDVNTVLKDADAILVPGG--------FGERGTE-----GK----MQAIKYARENGVPFLGICLGMQLAVIeyarnvag 397
Cdd:PRK11366  51 EPSLLEQLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALINAALERRIPIFAICRGLQELVV-------- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 398 iadASSTEFNRStkspliglitewLDERGEVQQRSVDSDLGGTMRLG-AQKSELVEGTKTREVYGsaeiverhrhryEMN 476
Cdd:PRK11366 123 ---ATGGSLHRK------------LCEQPELLEHREDPELPVEQQYApSHEVQVEEGGLLSALLP------------ECS 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491114886 477 NRYIPVLEEAG-------LKISGYSPiQHLVETVEIPQHPWFIAVQFHPEFTSSPRD-GHPLFAGFIGAAkQQHQKTK 546
Cdd:PRK11366 176 NFWVNSLHGQGakvvsprLRVEARSP-DGLVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITAC-QHHIAEK 251
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 320-386 1.79e-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: 45.78  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  320 NRVKVEIDYVNAEDLESQDvNTVLKDADAILVPG--GFGErgtegkmqAIKYARENGV------------PFLGICLGMQ 385
Cdd:TIGR01855  12 GSVKRALKRVGAEPVVVKD-SKEAELADKLILPGvgAFGA--------AMARLRENGLdlfvelvvrlgkPVLGICLGMQ 82


                  .
gi 491114886  386 L 386
Cdd:TIGR01855  83 L 83
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 324-386 2.06e-05

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: 46.07  E-value: 2.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491114886 324 VEIDYVNAEDLESQDVNtvLKDADAILVPGGF----------GERGTEGKMQAIKYARENGVPFLGICLGMQL 386
Cdd:cd01740   24 FEAEDVWHNDLLAGRKD--LDDYDGVVLPGGFsygdylragaIAAASPLLMEEVKEFAERGGLVLGICNGFQI 94
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
344-386 4.20e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 41.46  E-value: 4.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 491114886  344 KDADAILVPGGFGERG------TEGKMQAIKYARENGVPFLGICLGMQL 386
Cdd:pfam07685  41 PDADLIILPGGKPTIQdlallrNSGMDEAIKEAAEDGGPVLGICGGYQM 89
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
343-385 7.61e-04

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 41.25  E-value: 7.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491114886 343 LKDADAILVPGGF--GER---GTEGK----MQAIKYARENGVPFLGICLGMQ 385
Cdd:PRK03619  39 LDGVDAVVLPGGFsyGDYlrcGAIAAfspiMKAVKEFAEKGKPVLGICNGFQ 90
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 344-535 1.88e-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: 39.61  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  344 KDADAILVPGGFGERGTEGKMQAIKYARENGVPFLGICLGMQLavieyarnvagIADASSTEFNRSTKSpliglitewld 423
Cdd:TIGR00888  40 KNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGMQL-----------MAKQLGGEVGRAEKR----------- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886  424 ERGEVQQRSVDSDlggtmrlgaqksELVEGTKTR-EVYGSA--EIVErhrhryemnnryIPvleeAGLKISGYSPIQHlV 500
Cdd:TIGR00888  98 EYGKAELEILDED------------DLFRGLPDEsTVWMSHgdKVKE------------LP----EGFKVLATSDNCP-V 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 491114886  501 ETVEIPQHPWFiAVQFHPEFTSSpRDGHPLFAGFI 535
Cdd:TIGR00888 149 AAMAHEEKPIY-GVQFHPEVTHT-EYGNELLENFV 181
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 5-54 2.96e-03

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 37.41  E-value: 2.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491114886   5 IFVTGGVvSSLGKGISAASVAALLEARGLKVTMVKMDPYINVD-PGTMSPF 54
Cdd:cd01983    3 IAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDgGGGLETG 52
PLN02347 PLN02347
GMP synthetase
 345-388 3.95e-03

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 40.05  E-value: 3.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 491114886 345 DADAILVPGGFgergtegkmqaIKYARENGVPFLGICLGMQLAV 388
Cdd:PLN02347  68 VEGAPTVPEGF-----------FDYCRERGVPVLGICYGMQLIV 100
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 324-386 4.18e-03

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: 38.38  E-value: 4.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491114886 324 VEIDYVnaeDLESQDVNTVLKDADAILVPGGFGERGTEGK------MQAIKYARENGVPFLGICLGMQL 386
Cdd:cd01741   28 IEIDVV---DVYAGELLPDLDDYDGLVILGGPMSVDEDDYpwlkklKELIRQALAAGKPVLGICLGHQL 93
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 307-386 5.30e-03

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 39.69  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 307 KSVNEALLHAGIQNRvkveiDYVNAEDLESqdvntvlkdADAILVPG--GFGER----GTEGKMQAIKYARENGVPFLGI 380
Cdd:PLN02617  20 RSVRNAIRHLGFTIK-----DVQTPEDILN---------ADRLIFPGvgAFGSAmdvlNNRGMAEALREYIQNDRPFLGI 85


                 ....*.
gi 491114886 381 CLGMQL 386
Cdd:PLN02617  86 CLGLQL 91
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 324-386 5.61e-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: 38.38  E-value: 5.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491114886 324 VEIDYVN-AEDLEsqdvntvlkDADAILVPGGfgeRGTEGKM---------QAIKYARENGVPFLGICLGMQL 386
Cdd:cd01750   24 VDVRYVEvPEGLG---------DADLIILPGS---KDTIQDLawlrkrglaEAIKNYARAGGPVLGICGGYQM 84
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 322-386 5.66e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 38.30  E-value: 5.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491114886 322 VKVEIDYVNAEDLESQDVNTVLKdADAILVPGgfgeRGTEGkmQAIKYARENGV---------PFLGICLGMQL 386
Cdd:PRK13170  16 VKFAIERLGYEPVVSRDPDVILA-ADKLFLPG----VGTAQ--AAMDQLRERELidlikactqPVLGICLGMQL 82
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 342-418 6.65e-03

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 37.94  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491114886 342 VLKDADAILVPGGfgERGT-------EGKMQAIKYARENGVPFLGICLGMQLAvieyARNVagiADASSTEfnrsTKSPL 414
Cdd:PRK13527  40 DLPDCDALIIPGG--ESTTigrlmkrEGILDEIKEKIEEGLPILGTCAGLILL----AKEV---GDDRVTK----TEQPL 106


                 ....
gi 491114886 415 IGLI 418
Cdd:PRK13527 107 LGLM 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH