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Conserved domains on  [gi|489179798|ref|WP_003089287|]
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MULTISPECIES: antibiotic biosynthesis monooxygenase [Pseudomonas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06186 PRK06186
hypothetical protein; Validated
 8-233 8.93e-122

hypothetical protein; Validated


:

Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 350.42  E-value: 8.93e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   8 PLRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRLPAEPALERYDGFWCVPGSPYRDADAVLRLIAHARG 87
Cdd:PRK06186   1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDLAGFDGIWCVPGSPYRNDDGALTAIRFARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  88 RRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPCALLEAREEVRLLRGSRLALAYAADWIEADYHC 167
Cdd:PRK06186  81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTGDIRLRPGSLIARAYGTLEIEEGYHC 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489179798 168 RYAIAPRFAAELTGGALRASAWSADGAIRAVELEQHPFFVATLFQPERAALAGVLPPLPKAFVEAC 233
Cdd:PRK06186 161 RYGVNPEFVAALESGDLRVTGWDEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLVRAFLRAA 226
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
 248-323 2.80e-17

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


:

Pssm-ID: 441901  Cd Length: 98  Bit Score: 76.19  E-value: 2.80e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489179798 248 YYAVIFSSHRSA-VDDGYAEAAERMLELASRQPGYLGVESVRGAD--GFGITVSYWDSEAAIRAWSRHAEHRDAQARGR 323
Cdd:COG2329    1 MIVVINRFRVKPgQEEEFEEAFAERRELLAEQPGFLGFELLRSLEdpGEYLVVSYWESEEAFRAWFRSSEHRAAHAKGR 79
 
Name Accession Description Interval E-value
PRK06186 PRK06186
hypothetical protein; Validated
 8-233 8.93e-122

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 350.42  E-value: 8.93e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   8 PLRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRLPAEPALERYDGFWCVPGSPYRDADAVLRLIAHARG 87
Cdd:PRK06186   1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDLAGFDGIWCVPGSPYRNDDGALTAIRFARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  88 RRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPCALLEAREEVRLLRGSRLALAYAADWIEADYHC 167
Cdd:PRK06186  81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTGDIRLRPGSLIARAYGTLEIEEGYHC 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489179798 168 RYAIAPRFAAELTGGALRASAWSADGAIRAVELEQHPFFVATLFQPERAALAGVLPPLPKAFVEAC 233
Cdd:PRK06186 161 RYGVNPEFVAALESGDLRVTGWDEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLVRAFLRAA 226
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 9-230 1.49e-77

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: 237.84  E-value: 1.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   9 LRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRL---PAEPALERYDGFWCVPGSPYRDADAVLRLIAHA 85
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLeeeNAEEALKGADGILVPGGFGIRGVEGKILAIKYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  86 RGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPCA----------LLEAReEVRLLRGSRLALA 155
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQkgvkdlggtmRLGAY-PVILKPGTLAHKY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489179798 156 YAADWIEADYHCRYAIAPRFAAELTGGALRASAWSADG-AIRAVELEQHPFFVATLFQPERAALAGVLPPLPKAFV 230
Cdd:cd01746  160 YGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGgLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLFVGFV 235
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 5-233 4.28e-24

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: 103.16  E-value: 4.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   5 PAAPLRIALVGD----HDphitAHRAIPLALRLAGEALGLEIAFDWLASDRL---PAEPALERYDGFwCVPGS-PYRDAD 76
Cdd:COG0504  286 PKKEVTIALVGKyvelPD----AYKSVVEALKHAGIANGVKVNIKWIDSEDLeeeNAEELLKGVDGI-LVPGGfGERGIE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  77 AVLRLIAHARGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIaalpcALLEAREEV------------ 144
Cdd:COG0504  361 GKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVI-----DLMPEQKDVsdlggtmrlgay 435

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 145 --RLLRGSRLALAYAADWI-EADYHcRYAIAPRFAAELTGGALRASAWSADGA-IRAVELEQHPFFVATLFQPE------ 214
Cdd:COG0504  436 pcKLKPGTLAAEAYGKEEIsERHRH-RYEFNNEYREQLEKAGLVFSGTSPDGRlVEIVELPDHPWFVGVQFHPEfksrpn 514

                        250
                 ....*....|....*....
gi 489179798 215 RAAlagvlpPLPKAFVEAC 233
Cdd:COG0504  515 RPH------PLFRGFVKAA 527
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
 248-323 2.80e-17

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


Pssm-ID: 441901  Cd Length: 98  Bit Score: 76.19  E-value: 2.80e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489179798 248 YYAVIFSSHRSA-VDDGYAEAAERMLELASRQPGYLGVESVRGAD--GFGITVSYWDSEAAIRAWSRHAEHRDAQARGR 323
Cdd:COG2329    1 MIVVINRFRVKPgQEEEFEEAFAERRELLAEQPGFLGFELLRSLEdpGEYLVVSYWESEEAFRAWFRSSEHRAAHAKGR 79
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 248-319 1.03e-08

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 51.50  E-value: 1.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489179798  248 YYAVIFSSHRSAVDDGYAEAAERMLELASRQPGYLGVESVRGADGFG--ITVSYWDSEAAIRAWSRHAEHRDAQ 319
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPDeyVVLEVWEDEAAFEAHLQSPHFKAAH 74
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 70-214 1.29e-07

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: 51.49  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   70 SPYRDADAvLRLIAHARGRRRPFLGTCAGFQhtileFARNALG---WQAA---THGEEHPHSDQAVIAAlpcalleAREE 143
Cdd:pfam07722  87 DPARDAYE-LALIRAALARGKPILGICRGFQ-----LLNVALGgtlYQDIqeqPGFTDHREHCQVAPYA-------PSHA 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489179798  144 VRLLRGSRLALAYAADWIE-ADYHcryaiapRFAAELTGGALRASAWSADGAIRAVELEQHP-FFVATLFQPE 214
Cdd:pfam07722 154 VNVEPGSLLASLLGSEEFRvNSLH-------HQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
 
Name Accession Description Interval E-value
PRK06186 PRK06186
hypothetical protein; Validated
 8-233 8.93e-122

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 350.42  E-value: 8.93e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   8 PLRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRLPAEPALERYDGFWCVPGSPYRDADAVLRLIAHARG 87
Cdd:PRK06186   1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDLAGFDGIWCVPGSPYRNDDGALTAIRFARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  88 RRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPCALLEAREEVRLLRGSRLALAYAADWIEADYHC 167
Cdd:PRK06186  81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTGDIRLRPGSLIARAYGTLEIEEGYHC 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489179798 168 RYAIAPRFAAELTGGALRASAWSADGAIRAVELEQHPFFVATLFQPERAALAGVLPPLPKAFVEAC 233
Cdd:PRK06186 161 RYGVNPEFVAALESGDLRVTGWDEDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLVRAFLRAA 226
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 9-230 1.49e-77

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: 237.84  E-value: 1.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   9 LRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRL---PAEPALERYDGFWCVPGSPYRDADAVLRLIAHA 85
Cdd:cd01746    1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLeeeNAEEALKGADGILVPGGFGIRGVEGKILAIKYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  86 RGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPCA----------LLEAReEVRLLRGSRLALA 155
Cdd:cd01746   81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQkgvkdlggtmRLGAY-PVILKPGTLAHKY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489179798 156 YAADWIEADYHCRYAIAPRFAAELTGGALRASAWSADG-AIRAVELEQHPFFVATLFQPERAALAGVLPPLPKAFV 230
Cdd:cd01746  160 YGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGgLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLFVGFV 235
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 5-233 4.28e-24

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: 103.16  E-value: 4.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   5 PAAPLRIALVGD----HDphitAHRAIPLALRLAGEALGLEIAFDWLASDRL---PAEPALERYDGFwCVPGS-PYRDAD 76
Cdd:COG0504  286 PKKEVTIALVGKyvelPD----AYKSVVEALKHAGIANGVKVNIKWIDSEDLeeeNAEELLKGVDGI-LVPGGfGERGIE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  77 AVLRLIAHARGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIaalpcALLEAREEV------------ 144
Cdd:COG0504  361 GKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHPVI-----DLMPEQKDVsdlggtmrlgay 435

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 145 --RLLRGSRLALAYAADWI-EADYHcRYAIAPRFAAELTGGALRASAWSADGA-IRAVELEQHPFFVATLFQPE------ 214
Cdd:COG0504  436 pcKLKPGTLAAEAYGKEEIsERHRH-RYEFNNEYREQLEKAGLVFSGTSPDGRlVEIVELPDHPWFVGVQFHPEfksrpn 514

                        250
                 ....*....|....*....
gi 489179798 215 RAAlagvlpPLPKAFVEAC 233
Cdd:COG0504  515 RPH------PLFRGFVKAA 527
pyrG PRK05380
CTP synthetase; Validated
 9-233 3.73e-22

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 97.40  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   9 LRIALVGD----HDphitAHRAIPLALRLAGEALGLEIAFDWLASDRL---PAEPALERYDGFwCVP-GSPYRDADAVLR 80
Cdd:PRK05380 289 VTIALVGKyvelPD----AYKSVIEALKHAGIANDVKVNIKWIDSEDLeeeNVAELLKGVDGI-LVPgGFGERGIEGKIL 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  81 LIAHARGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPcallEARE-------------EVRLL 147
Cdd:PRK05380 364 AIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMP----EQKDvsdlggtmrlgayPCKLK 439

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 148 RGSRLALAYAADWI-EADYHcRYAIAPRFAAELTGGALRASAWSADGA-IRAVELEQHPFFVATLFQPE------RAAla 219
Cdd:PRK05380 440 PGTLAAEIYGKEEIyERHRH-RYEVNNKYREQLEKAGLVFSGTSPDGRlVEIVELPDHPWFVGVQFHPEfksrprRPH-- 516

                        250
                 ....*....|....
gi 489179798 220 gvlpPLPKAFVEAC 233
Cdd:PRK05380 517 ----PLFAGFVKAA 526
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
 248-323 2.80e-17

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


Pssm-ID: 441901  Cd Length: 98  Bit Score: 76.19  E-value: 2.80e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489179798 248 YYAVIFSSHRSA-VDDGYAEAAERMLELASRQPGYLGVESVRGAD--GFGITVSYWDSEAAIRAWSRHAEHRDAQARGR 323
Cdd:COG2329    1 MIVVINRFRVKPgQEEEFEEAFAERRELLAEQPGFLGFELLRSLEdpGEYLVVSYWESEEAFRAWFRSSEHRAAHAKGR 79
PLN02327 PLN02327
CTP synthase
 7-214 3.96e-15

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 76.22  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   7 APLRIALVGDHDPHITAHRAIPLALRLAGEALGLEIAFDWLASDRLPAEPALER---YDGFWcvpgSPYRDADAVL---- 79
Cdd:PLN02327 296 EPVRIAMVGKYTGLSDSYLSVLKALLHASVACSRKLVIDWVAASDLEDETAKETpdaYAAAW----KLLKGADGILvpgg 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  80 --------RLIA--HARGRRRPFLGTCAGFQHTILEFARNALGWQAATHGEEHPHSDQAVIAALPcallEAREE-----V 144
Cdd:PLN02327 372 fgdrgvegKILAakYARENKVPYLGICLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMP----EGSKThmggtM 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 145 RLlrGSRLALAYAADWIEAD-YHC----------RYAIAPRFAAELTGGALRASAWSADGA-IRAVELEQHPFFVATLFQ 212
Cdd:PLN02327 448 RL--GSRRTYFQTPDCKSAKlYGNvsfvderhrhRYEVNPEMVPRLEKAGLSFVGKDETGRrMEIVELPSHPFFVGVQFH 525


                 ..
gi 489179798 213 PE 214
Cdd:PLN02327 526 PE 527
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 66-233 4.24e-11

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: 62.11  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  66 CVPGSPYRDAdAVLRLIAHARGRRRPFLGTCAGFQhtILefarN-ALG---WQ--AATHGEEHPHSDQAVIAALpcalle 139
Cdd:COG2071   74 LGPIDPERDA-FELALIRAALERGKPVLGICRGMQ--LL----NvALGgtlYQdlPDQVPGALDHRQPAPRYAP------ 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 140 aREEVRLLRGSRLALAYAADWIEAD-YHcryaiapRFAAELTGGALRASAWSADGAIRAVELEQHPFFVATLFQPER-AA 217
Cdd:COG2071  141 -RHTVEIEPGSRLARILGEEEIRVNsLH-------HQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWlAA 212

                        170
                 ....*....|....*.
gi 489179798 218 LAGVLPPLPKAFVEAC 233
Cdd:COG2071  213 SDPLSRRLFEAFVEAA 228
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
 248-319 1.03e-08

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 51.50  E-value: 1.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489179798  248 YYAVIFSSHRSAVDDGYAEAAERMLELASRQPGYLGVESVRGADGFG--ITVSYWDSEAAIRAWSRHAEHRDAQ 319
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELVEATRNEPGCLSYELLRSLEDPDeyVVLEVWEDEAAFEAHLQSPHFKAAH 74
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 70-214 1.29e-07

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: 51.49  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   70 SPYRDADAvLRLIAHARGRRRPFLGTCAGFQhtileFARNALG---WQAA---THGEEHPHSDQAVIAAlpcalleAREE 143
Cdd:pfam07722  87 DPARDAYE-LALIRAALARGKPILGICRGFQ-----LLNVALGgtlYQDIqeqPGFTDHREHCQVAPYA-------PSHA 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489179798  144 VRLLRGSRLALAYAADWIE-ADYHcryaiapRFAAELTGGALRASAWSADGAIRAVELEQHP-FFVATLFQPE 214
Cdd:pfam07722 154 VNVEPGSLLASLLGSEEFRvNSLH-------HQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 11-100 2.23e-05

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: 43.36  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  11 IALVGDHDPHITAHRAIPLALRlageALGLEIAFDWLASDRLPAEPALERYDGFWcVPGSP-----YRDADAVLRLIAHA 85
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALR----EAGAEVDVVSPDGGPVESDVDLDDYDGLI-LPGGPgtpddLARDEALLALLREA 75

                         90
                 ....*....|....*
gi 489179798  86 RGRRRPFLGTCAGFQ 100
Cdd:cd01653   76 AAAGKPILGICLGAQ 90
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 11-100 2.27e-05

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: 42.57  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  11 IALVGDHDPHITAHRAIPLALRlageALGLEIAFDWLASDRLPAEPALERYDGFwCVPGSP-----YRDADAVLRLIAHA 85
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALR----EAGAEVDVVSPDGGPVESDVDLDDYDGL-ILPGGPgtpddLAWDEALLALLREA 75

                         90
                 ....*....|....*
gi 489179798  86 RGRRRPFLGTCAGFQ 100
Cdd:cd03128   76 AAAGKPVLGICLGAQ 90
DUF4188 pfam13826
Domain of unknown function (DUF4188);
267-318 8.97e-05

Domain of unknown function (DUF4188);


Pssm-ID: 433506  Cd Length: 118  Bit Score: 41.46  E-value: 8.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489179798  267 AAERMLELASRQP--GYLGVESVRGADGFGITVSYWDSEAAIRAWSRHAEHRDA 318
Cdd:pfam13826  25 AMPRMLRELRADPelGLLGYESYIGAPREVMLVQYWRDFESLHAFAHSEPHREA 78
GATase pfam00117
Glutamine amidotransferase class-I;
68-214 1.64e-03

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 39.14  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798   68 PGSPYRDADAVlRLIAHARGRRRPFLGTCAGFQHTILEFARN--ALGWQaATHGEEHP--HSDQAVIAALPCALLEARee 143
Cdd:pfam00117  50 PGSPGAAGGAI-EAIREARELKIPILGICLGHQLLALAFGGKvvKAKKF-GHHGKNSPvgDDGCGLFYGLPNVFIVRR-- 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489179798  144 vrllrgsrlalayaadwieadYHcRYAIAPRFAAEltggALRASAWSADG----AIRAVELeqhPFFvATLFQPE 214
Cdd:pfam00117 126 ---------------------YH-SYAVDPDTLPD----GLEVTATSENDgtimGIRHKKL---PIF-GVQFHPE 170
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 181-217 2.79e-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: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 38.33  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489179798 181 GGALRASAWSADGAIRAVELEQHPFFVATLFQPERAA 217
Cdd:cd01745  139 ADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLA 175
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 37-214 3.17e-03

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 38.73  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  37 ALGLEIAFDWLASDRLPAEPALERYDGFWcVPGSPYR-------------DADA-----VLRLIAHARGRRRPFLGTCAG 98
Cdd:PRK11366  38 AGGLPIALPHALAEPSLLEQLLPKLDGIY-LPGSPSNvqphlygengdepDADPgrdllSMALINAALERRIPIFAICRG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798  99 FQHTILefarnalgwqaATHGEEHPHsdqavIAALPcALLEAREEVRLLRGSRLALAYAADWIEADYHCRyaIAP---RF 175
Cdd:PRK11366 117 LQELVV-----------ATGGSLHRK-----LCEQP-ELLEHREDPELPVEQQYAPSHEVQVEEGGLLSA--LLPecsNF 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489179798 176 --------AAELTGGALRASAWSADGAIRAVELEQHPFFVATLFQPE 214
Cdd:PRK11366 178 wvnslhgqGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPE 224
COG3224 COG3224
Antibiotic biosynthesis monooxygenase (ABM) superfamily enzyme [General function prediction ...
 262-353 8.63e-03

Antibiotic biosynthesis monooxygenase (ABM) superfamily enzyme [General function prediction only];


Pssm-ID: 442457  Cd Length: 183  Bit Score: 36.81  E-value: 8.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489179798 262 DGYAEAAERMLELASRQPGYLGVESVR---GADGFGITVSYwDSEAAIRAWSRHAEHRDAQARGRrdwyaGFSARIARVE 338
Cdd:COG3224   21 AEFEAWLREITALAARFPGFLGVGVIRpsgGSDEWVILLRF-DSEENLDAWLESPERRAWLEEGE-----PLLEGEERVE 94

                         90       100
                 ....*....|....*....|.
gi 489179798 339 REYAF------PAQPDTAQSP 353
Cdd:COG3224   95 RRTGLegwftpPGAPAAAPPP 115
 
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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