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Conserved domains on  [gi|446082109|ref|WP_000159964|]
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MULTISPECIES: CTP synthase [Staphylococcus]

Protein Classification

CTP synthase( domain architecture ID 11423441)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
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: 1133.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQI 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 162 RSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 242 ADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYPF 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAR-EPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIAN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 322 AKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLEG 401
Cdd:COG0504  320 GVKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLED 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 402 AHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMVI 481
Cdd:COG0504  400 ANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVF 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446082109 482 SGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEASLKYQQNK 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: 1133.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQI 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 162 RSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 242 ADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYPF 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAR-EPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIAN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 322 AKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLEG 401
Cdd:COG0504  320 GVKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLED 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 402 AHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMVI 481
Cdd:COG0504  400 ANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVF 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446082109 482 SGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEASLKYQQNK 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: 1127.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   1 MTKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  81 INLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGEstNADVVITEIGGTTGDIESLPFIEAIRQ 160
Cdd:PRK05380  81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGT--DADVVIVEIGGTVGDIESLPFLEAIRQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 161 IRSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECR 240
Cdd:PRK05380 159 LRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 241 DADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYP 320
Cdd:PRK05380 239 DVDSIYEVPLLLHEQGLDDIVLERLGLEAP-EPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 321 FAKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLE 400
Cdd:PRK05380 318 NDVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 401 GAHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMV 480
Cdd:PRK05380 398 DANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQLEKAGLV 477
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446082109 481 ISGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEASLKYQQNK 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: 930.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109    2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQI 161
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  162 RSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRD 241
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  242 ADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYPF 321
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCD-EADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  322 AKDIDIRWIDSSEVTDENaAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLEG 401
Cdd:TIGR00337 320 DTKVNIKWIDSEDLEEEG-VEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  402 AHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMVI 481
Cdd:TIGR00337 399 ANSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQIENKGLIV 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446082109  482 SGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEA 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: 573.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109    3 KFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   83 LNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQIR 162
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEVGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  163 SDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRDA 242
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240
                         250       260
                  ....*....|....*....|....*
gi 446082109  243 DSLYEIPLQLSQQNMDDIVIKRLQL 267
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
3-263 4.53e-179

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: 503.94  E-value: 4.53e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   3 KFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  83 LNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQIR 162
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 163 SDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRDA 242
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240
                        250       260
                 ....*....|....*....|.
gi 446082109 243 DSLYEIPLQLSQQNMDDIVIK 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: 1133.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:COG0504    1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQI 161
Cdd:COG0504   81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEESGADVVIVEIGGTVGDIESLPFLEAIRQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 162 RSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRD 241
Cdd:COG0504  161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 242 ADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYPF 321
Cdd:COG0504  241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAR-EPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIAN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 322 AKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLEG 401
Cdd:COG0504  320 GVKVNIKWIDSEDLEEENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLED 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 402 AHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMVI 481
Cdd:COG0504  400 ANSTEFDPNTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQLEKAGLVF 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446082109 482 SGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEASLKYQQNK 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: 1127.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   1 MTKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
Cdd:PRK05380   1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  81 INLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGEstNADVVITEIGGTTGDIESLPFIEAIRQ 160
Cdd:PRK05380  81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGT--DADVVIVEIGGTVGDIESLPFLEAIRQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 161 IRSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECR 240
Cdd:PRK05380 159 LRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 241 DADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYP 320
Cdd:PRK05380 239 DVDSIYEVPLLLHEQGLDDIVLERLGLEAP-EPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 321 FAKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLE 400
Cdd:PRK05380 318 NDVKVNIKWIDSEDLEEENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 401 GAHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMV 480
Cdd:PRK05380 398 DANSTEFDPDTPHPVIDLMPEQKDVSDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQLEKAGLV 477
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446082109 481 ISGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEASLKYQQNK 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: 930.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109    2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQI 161
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  162 RSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRD 241
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  242 ADSLYEIPLQLSQQNMDDIVIKRLQLNAKyETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESLKHAGYPF 321
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCD-EADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  322 AKDIDIRWIDSSEVTDENaAEYLADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQLATVEFSRNVLGLEG 401
Cdd:TIGR00337 320 DTKVNIKWIDSEDLEEEG-VEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  402 AHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVYGKAEIEERHRHRYEFNNDYREQLEANGMVI 481
Cdd:TIGR00337 399 ANSTEFDPDTKYPVVDLLPEQKDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQIENKGLIV 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 446082109  482 SGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEA 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: 666.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   2 TKFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDI 81
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  82 NLNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLL------LAGESTNADVVITEIGGTTGDIESLPFI 155
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIErvakipVDGKEGPADVCVIELGGTVGDIESMPFI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 156 EAIRQIRSDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKES 235
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 236 VIECRDADSLYEIPLQLSQQNMDDIVIKRLQLNAK-YETQLDEWKQLLDIVNNLDGKITIGLVGKYVSLQDAYLSVVESL 314
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVaREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 315 KHAGYPFAKDIDIRWIDSSEVTDENAAEY----------LADVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLG 384
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAKETpdayaaawklLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 385 MQLATVEFSRNVLGLEGAHSAELDPATSYPIIDLLPEqKDIEDLGGTLRLGLYPCSIK-EGTLAQDVYGKAE-IEERHRH 462
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPE-GSKTHMGGTMRLGSRRTYFQtPDCKSAKLYGNVSfVDERHRH 479
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446082109 463 RYEFNNDYREQLEANGMVISGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEAS 529
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 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: 573.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109    3 KFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   83 LNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQIR 162
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKEVGPDVVIVEIGGTVGDIESLPFLEAIRQLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  163 SDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRDA 242
Cdd:pfam06418 161 LEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDV 240
                         250       260
                  ....*....|....*....|....*
gi 446082109  243 DSLYEIPLQLSQQNMDDIVIKRLQL 267
Cdd:pfam06418 241 SSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
3-263 4.53e-179

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: 503.94  E-value: 4.53e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109   3 KFIFVTGGVVSSLGKGITASSLGRLLKDRGLNVTIQKFDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDIN 82
Cdd:cd03113    1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  83 LNKFSNVTAGKVYSHVLKKERRGDYLGGTVQVIPHITNEIKERLLLAGESTNADVVITEIGGTTGDIESLPFIEAIRQIR 162
Cdd:cd03113   81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPEPDVCIVEIGGTVGDIESLPFLEALRQFQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 163 SDLGRENVMYVHCTLLPYIKAAGEMKTKPTQHSVKELRGLGIQPDLIVVRTEYEMTQDLKDKIALFCDINKESVIECRDA 242
Cdd:cd03113  161 FEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDV 240
                        250       260
                 ....*....|....*....|.
gi 446082109 243 DSLYEIPLQLSQQNMDDIVIK 263
Cdd:cd03113  241 SSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
292-526 6.06e-146

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: 418.88  E-value: 6.06e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 292 ITIGLVGKYVSLQDAYLSVVESLKHAGYPFAKDIDIRWIDSSEVTDENAAEYLADVDGILVPGGFGFRASEGKISAIKYA 371
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEALKGADGILVPGGFGIRGVEGKILAIKYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 372 RENNVPFFGICLGMQLATVEFSRNVLGLEGAHSAELDPATSYPIIDLLPEQKDIEDLGGTLRLGLYPCSIKEGTLAQDVY 451
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKGVKDLGGTMRLGAYPVILKPGTLAHKYY 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446082109 452 GKAEIEERHRHRYEFNNDYREQLEANGMVISGTSPDGRLVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFI 526
Cdd:cd01746  161 GKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
303-528 2.26e-46

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 160.48  E-value: 2.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  303 LQDAYLSVVESLKHAGYPFAKDIDIRWIDSSEVTDENAAeyladVDGILVPGGFG-FRASEGKISAIKYARENNVPFFGI 381
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN-----PDGIILSGGPGsPGAAGGAIEAIREARELKIPILGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  382 CLGMQLATVEFSRNVLglegahsaeldpatsypiidllpEQKDIEDLGGTLRLGLYPCSIKEGTlaqdvygKAEIEERHR 461
Cdd:pfam00117  77 CLGHQLLALAFGGKVV-----------------------KAKKFGHHGKNSPVGDDGCGLFYGL-------PNVFIVRRY 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446082109  462 HRYEFNNDyreqLEANGMVISGTSPDG-RLVEMVEIPtnDFFIACQFHPEFLSRPNRPHPIFKSFIEA 528
Cdd:pfam00117 127 HSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKK--LPIFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
294-528 3.43e-45

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 158.59  E-value: 3.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 294 IGLVGKYVSLQDAYLSVVESLKHAGYPFAKDIDIRWIDSSEVTDEnaaEYLADVDGI-LVPGGfGFRASEGKISAIKYAR 372
Cdd:PRK06186   4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDP---EDLAGFDGIwCVPGS-PYRNDDGALTAIRFAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 373 ENNVPFFGICLGMQLATVEFSRNVLGLEGAHSAELDPATSYPIIDLLP----EQKdiedlgGTLRLGlypcsikEGTLAQ 448
Cdd:PRK06186  80 ENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLScslvEKT------GDIRLR-------PGSLIA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 449 DVYGKAEIEERHRHRYEFNNDYREQLEANGMVISGTSPDGRlVEMVEIPTNDFFIACQFHPEFLSRPNRPHPIFKSFIEA 528
Cdd:PRK06186 147 RAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALAGRPPPLVRAFLRA 225
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
337-532 1.42e-21

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: 93.31  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 337 DENAAEYLADVDGILVPGG-------FGFRASEGK-----------ISAIKYARENNVPFFGICLGMQLAtvefsrNVLg 398
Cdd:COG2071   40 EEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafeLALIRAALERGKPVLGICRGMQLL------NVA- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 399 legahsaeldpatsypiidllpeqkdiedLGGTLRlglypcsikegtlaQDVYgkAEIEERHRHRYEFNNDY-------- 470
Cdd:COG2071  113 -----------------------------LGGTLY--------------QDLP--DQVPGALDHRQPAPRYAprhtveie 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 471 ----------REQLEAN------------GMVISGTSPDGrLVEMVEIPTNDFFIACQFHPEFLSRPNRPH-PIFKSFIE 527
Cdd:COG2071  148 pgsrlarilgEEEIRVNslhhqavkrlgpGLRVSARAPDG-VIEAIESPGAPFVLGVQWHPEWLAASDPLSrRLFEAFVE 226

                 ....*
gi 446082109 528 ASLKY 532
Cdd:COG2071  227 AARAR 231
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
294-392 5.94e-15

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: 71.09  E-value: 5.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 294 IGLVGKYVSLQDAYLSVVESLKHAGYpfakDIDIRWIDSSEVTDEnaaEYLADVDGILVPGGFG----FRASEGKISAIK 369
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAGA----EVDVVSPDGGPVESD---VDLDDYDGLILPGGPGtpddLARDEALLALLR 73
                         90       100
                 ....*....|....*....|....*
gi 446082109 370 YARENNVPFFGICLGMQLA--TVEF 392
Cdd:cd01653   74 EAAAAGKPILGICLGAQLLvlGVQF 98
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
337-510 4.29e-14

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: 71.52  E-value: 4.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  337 DENAAEYLADVDGILVPGG-------FGFRASE--GKISA---------IKYARENNVPFFGICLGMQLATVefsrnVLG 398
Cdd:pfam07722  49 PEDAAAILDRLDGLLLTGGpnvdphfYGEEPSEsgGPYDPardayelalIRAALARGKPILGICRGFQLLNV-----ALG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  399 legahsaeldpATSYPIIdllPEQKDIEDLGGTLRLGLY----PCSIKEGTLAQDVYGKAEIEERHRHRyeFNNDyreQL 474
Cdd:pfam07722 124 -----------GTLYQDI---QEQPGFTDHREHCQVAPYapshAVNVEPGSLLASLLGSEEFRVNSLHH--QAID---RL 184
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446082109  475 eANGMVISGTSPDGrLVEMVEIPTND-FFIACQFHPE 510
Cdd:pfam07722 185 -APGLRVEAVAPDG-TIEAIESPNAKgFALGVQWHPE 219
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
294-387 8.30e-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: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 294 IGLVGKYVSLQDAYLSVVESLKHAGYpfakDIDIRWIDSSEVTDEnaaEYLADVDGILVPGGFG----FRASEGKISAIK 369
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAGA----EVDVVSPDGGPVESD---VDLDDYDGLILPGGPGtpddLAWDEALLALLR 73
                         90
                 ....*....|....*...
gi 446082109 370 YARENNVPFFGICLGMQL 387
Cdd:cd03128   74 EAAAAGKPVLGICLGAQL 91
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
337-526 6.03e-13

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: 67.60  E-value: 6.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 337 DENAAEYLADVDGILVPGG-------FGFRASEG-----------KISAIKYARENNVPFFGICLGMQLATVEFsrnvlg 398
Cdd:cd01745   44 EEDLEQYLELLDGLLLTGGgdvdpplYGEEPHPElgpidperdafELALLRAALERGKPILGICRGMQLLNVAL------ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 399 legahsaeldpatsypiidllpeqkdiedlGGTLRlglypcsikegtlaQDvygkaeIEERHRHRYEFNndyreQLeANG 478
Cdd:cd01745  118 ------------------------------GGTLY--------------QD------IRVNSLHHQAIK-----RL-ADG 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446082109 479 MVISGTSPDGrLVEMVEIPTNDFFIACQFHPEFLSRPNRPH-PIFKSFI 526
Cdd:cd01745  142 LRVEARAPDG-VIEAIESPDRPFVLGVQWHPEWLADTDPDSlKLFEAFV 189
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
309-387 1.34e-07

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: 51.96  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGYPFakdidirwidssEVTDEnaAEYLADVDGILVPG-G-FG-----FRASEGkISAIKYARENNVPFFGI 381
Cdd:COG0118   15 SVAKALERLGAEV------------VVTSD--PDEIRAADRLVLPGvGaFGdamenLRERGL-DEAIREAVAGGKPVLGI 79

                 ....*.
gi 446082109 382 CLGMQL 387
Cdd:COG0118   80 CLGMQL 85
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
309-387 3.39e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 51.02  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGypfakdidirwidsSEVTDENAAEYLADVDGILVPGGFGFRASEGKIS----AIKYARENNVPFFGICLG 384
Cdd:PRK13143  15 SVSKALERAG--------------AEVVITSDPEEILDADGIVLPGVGAFGAAMENLSplrdVILEAARSGKPFLGICLG 80

                 ...
gi 446082109 385 MQL 387
Cdd:PRK13143  81 MQL 83
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
309-401 1.25e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 49.40  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGypfaKDIDIrwidssEVTDEnaAEYLADVDGILVPG--GF-----GFRASEGKISAIKYARENNVPFFGI 381
Cdd:PRK13146  16 SAAKALERAG----AGADV------VVTAD--PDAVAAADRVVLPGvgAFadcmrGLRAVGLGEAVIEAVLAAGRPFLGI 83
                         90       100
                 ....*....|....*....|
gi 446082109 382 CLGMQLAtveFSRnvlGLEG 401
Cdd:PRK13146  84 CVGMQLL---FER---GLEH 97
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
309-387 6.58e-06

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: 47.11  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGYpfakdiDIRWIDSSEVtdenaaeyLADVDGILVPG-G-FG-----FRASeGKISAIKYARENNVPFFGI 381
Cdd:cd01748   13 SVANALERLGA------EVIITSDPEE--------ILSADKLILPGvGaFGdamanLRER-GLIEALKEAIASGKPFLGI 77

                 ....*.
gi 446082109 382 CLGMQL 387
Cdd:cd01748   78 CLGMQL 83
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
309-387 9.67e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 46.66  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGYPfakdidirwidsSEVTDEnaAEYLADVDGILVPGGFGFRA------SEGKISAIKYARENNVPFFGIC 382
Cdd:PRK13141  14 SVEKALERLGAE------------AVITSD--PEEILAADGVILPGVGAFPDamanlrERGLDEVIKEAVASGKPLLGIC 79

                 ....*
gi 446082109 383 LGMQL 387
Cdd:PRK13141  80 LGMQL 84
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
330-510 1.26e-05

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 46.08  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 330 IDSSEVTDENAAEYLADVDGILVPGGFgFRASEGK-------ISAIKYARENNVPFFGICLGMQL------ATVEfsRNV 396
Cdd:cd01741   30 IDVVDVYAGELLPDLDDYDGLVILGGP-MSVDEDDypwlkklKELIRQALAAGKPVLGICLGHQLlaralgGKVG--RNP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 397 LGLE-GAHSAELDPAtsypiidllpEQKDIEDLGGTLRLGLYpcsikegtlaqdvygkaeieerHRHRYEFnndyrEQLe 475
Cdd:cd01741  107 KGWEiGWFPVTLTEA----------GKADPLFAGLPDEFPVF----------------------HWHGDTV-----VEL- 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446082109 476 ANGMVISGTSPDGRlVEMVEIPTNdfFIACQFHPE 510
Cdd:cd01741  149 PPGAVLLASSEACP-NQAFRYGDR--ALGLQFHPE 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
344-511 2.28e-05

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: 45.71  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 344 LADVDGILVPGGF-----GFRASEGKISAIKYARENNVPFFGICLGMQL------ATVEFSRnvlGLE-GAHSAELDPAT 411
Cdd:COG0518   46 LEDPDGLILSGGPmsvydEDPWLEDEPALIREAFELGKPVLGICYGAQLlahalgGKVEPGP---GREiGWAPVELTEAD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 412 syPIIDLLPEQkdiedlggtlrlglypcsikegtlaQDVYgkaeieerHRHRYEFnndyrEQLeANGMVISGTSPDGRlV 491
Cdd:COG0518  123 --PLFAGLPDE-------------------------FTVW--------MSHGDTV-----TEL-PEGAEVLASSDNCP-N 160
                        170       180
                 ....*....|....*....|
gi 446082109 492 EMVEIptNDFFIACQFHPEF 511
Cdd:COG0518  161 QAFRY--GRRVYGVQFHPEV 178
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
309-387 1.18e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 43.32  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 309 SVVESLKHAGYPFakdidirwidssEVTDeNAAEyLADVDGILVPG--GFG-----FRASeGKISAIKYARENNVPFFGI 381
Cdd:PRK13181  14 SVANALKRLGVEA------------VVSS-DPEE-IAGADKVILPGvgAFGqamrsLRES-GLDEALKEHVEKKQPVLGI 78

                 ....*.
gi 446082109 382 CLGMQL 387
Cdd:PRK13181  79 CLGMQL 84
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
344-387 1.66e-03

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: 40.29  E-value: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446082109 344 LADVDGILVPGGF----------GFRASEGKISAIKYARENNVPFFGICLGMQL 387
Cdd:cd01740   41 LDDYDGVVLPGGFsygdylragaIAAASPLLMEEVKEFAERGGLVLGICNGFQI 94
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
305-392 1.67e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 40.03  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 305 DAYLSVVESLKHAGYPFAKDIDIRWIDSSEVTDENAAEylADVDGILVPGGFGFRASEG-KISAIKYARENNVPFFGICL 383
Cdd:PRK07765   7 DNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVA--AQFDGVLLSPGPGTPERAGaSIDMVRACAAAGTPLLGVCL 84

                 ....*....
gi 446082109 384 GMQLATVEF 392
Cdd:PRK07765  85 GHQAIGVAF 93
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
309-387 1.99e-03

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: 39.62  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109  309 SVVESLKHAGYPfakdidirwidsSEVTDENaaEYLADVDGILVPGGFGF-----RASEGKISAIK-YARENNVPFFGIC 382
Cdd:TIGR01855  13 SVKRALKRVGAE------------PVVVKDS--KEAELADKLILPGVGAFgaamaRLRENGLDLFVeLVVRLGKPVLGIC 78

                  ....*
gi 446082109  383 LGMQL 387
Cdd:TIGR01855  79 LGMQL 83
PRK00758 PRK00758
GMP synthase subunit A; Validated
341-392 3.87e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 38.68  E-value: 3.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446082109 341 AEYLADVDGILVPGGfgfrASEGKI-SAIKYARENNVPFFGICLGMQLATVEF 392
Cdd:PRK00758  36 EEIKAFEDGLILSGG----PDIERAgNCPEYLKELDVPILGICLGHQLIAKAF 84
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
346-387 5.69e-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: 38.06  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446082109  346 DVDGILVPGGFGFRASEGKISAIKYARENNVPFFGICLGMQL 387
Cdd:TIGR00888  41 NPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGMQL 82
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
318-431 6.57e-03

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 37.78  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082109 318 GYPFAKDIDIrwidsSEVtdeNAAEYladvDGILVPGGFG----FRASEGKISAIKYARENNVPFFGICLGMQ-LATVEF 392
Cdd:COG0693   48 GITVTADKTL-----DDV---DPDDY----DALVLPGGHGapddLREDPDVVALVREFYEAGKPVAAICHGPAvLAAAGL 115
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446082109 393 srnvlgLEGAHsaeldpATSYPIIdllpeQKDIEDLGGT 431
Cdd:COG0693  116 ------LKGRK------VTSFPNI-----EDDLKNAGAT 137
 
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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