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Conserved domains on  [gi|738093228|ref|WP_036051879|]
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beta-propeller fold lactonase family protein [Burkholderia gladioli]

Protein Classification

lactonase family protein( domain architecture ID 11457674)

lactonase family protein similar to 6-phosphogluconolactonase which\ncatalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway

CATH:  2.130.10.10
Gene Ontology:  GO:0052689
SCOP:  4002745|4000933

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
10-355 4.03e-69

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 220.55  E-value: 4.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  10 SNSISadlrVYRLDPDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALRSTPPAIARCRLDPGTGQLATDYRLDV-GAGH 88
Cdd:COG2706   20 SEGIY----VFRLDTATGELTLLGLVAALGNPSFLALSPDGRFLYAVNEVDDGGVSAFRIDPADGTLTLLNTVSSgGASP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  89 VSLAIDRAGRFLFGASYGSHQLVVHAIA---RLdeGDASPLQTLEGIR---------NAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:COG2706   96 CHLSVDPDGRFLFVANYGGGSVSVFPIDadgSL--GEPVQVIQHEGSGpnperqegpHAHSVVFDPDGRFLYVPDLGTDR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 157 LLCCSLDAErEAPLEIVDTLAFDKGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLS-RHHVTTrppelaamrd 235
Cdd:COG2706  174 IYVYRLDPA-TGKLPEPPEVSLPPGSGPRHLAFHPNGRFAYVINELDSTVSVYAYDAATGTLTlIQTVST---------- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 236 gqarppatepqpDPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEAD-GTLAHAGAVSTE-TQPRGFAIDPGGR 313
Cdd:COG2706  243 ------------LPEDFTGENWAADIHISPDGRFLYVSNRGHNSIAVFAIDADgGKLTLVGHVPTGgKWPRDFAIDPDGR 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 738093228 314 CLVACGEHSPQVSLYLIDDASGLPALHSRHPGGQGANWVEIV 355
Cdd:COG2706  311 FLLVANQKSDNITVFRIDADTGKLTPTGRSVPVPSPVCVAFL 352
 
Name Accession Description Interval E-value
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
10-355 4.03e-69

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 220.55  E-value: 4.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  10 SNSISadlrVYRLDPDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALRSTPPAIARCRLDPGTGQLATDYRLDV-GAGH 88
Cdd:COG2706   20 SEGIY----VFRLDTATGELTLLGLVAALGNPSFLALSPDGRFLYAVNEVDDGGVSAFRIDPADGTLTLLNTVSSgGASP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  89 VSLAIDRAGRFLFGASYGSHQLVVHAIA---RLdeGDASPLQTLEGIR---------NAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:COG2706   96 CHLSVDPDGRFLFVANYGGGSVSVFPIDadgSL--GEPVQVIQHEGSGpnperqegpHAHSVVFDPDGRFLYVPDLGTDR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 157 LLCCSLDAErEAPLEIVDTLAFDKGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLS-RHHVTTrppelaamrd 235
Cdd:COG2706  174 IYVYRLDPA-TGKLPEPPEVSLPPGSGPRHLAFHPNGRFAYVINELDSTVSVYAYDAATGTLTlIQTVST---------- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 236 gqarppatepqpDPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEAD-GTLAHAGAVSTE-TQPRGFAIDPGGR 313
Cdd:COG2706  243 ------------LPEDFTGENWAADIHISPDGRFLYVSNRGHNSIAVFAIDADgGKLTLVGHVPTGgKWPRDFAIDPDGR 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 738093228 314 CLVACGEHSPQVSLYLIDDASGLPALHSRHPGGQGANWVEIV 355
Cdd:COG2706  311 FLLVANQKSDNITVFRIDADTGKLTPTGRSVPVPSPVCVAFL 352
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
10-339 3.78e-57

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 188.97  E-value: 3.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228   10 SNSISADLRVYRLDPDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALRSTPP-AIARCRLDPGTGQL-ATDYRLDVGAG 87
Cdd:pfam10282   8 TKGDSKGIYVLTLDTETGALTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDQgGVAAFRIDPDSGALtLLNQVPTGGAS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228   88 HVSLAIDRAGRFLFGASYGSHQLVVHAIaRLD--EGDASPLQTLEGIR---------NAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:pfam10282  88 PCHLSVDPDGRFLFVANYHGGSVSVFPL-DADgsLGELSQVVQHEGSGppperqespHPHSVDLTPDGKFLVVPDLGTDR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  157 LLCCSLDAErEAPLEIVDTLAFDKGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLSRHHVTTrppelaamrdg 236
Cdd:pfam10282 167 VRVYKLDAG-GGKLTPPASVQTPPGSGPRHLAFHPNGKYAYVVNELSSTVTVFEYDPATGTFEELQTVS----------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  237 qarppatepqPDPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRV-EADGTLAHAGAVSTETQ-PRGFAIDPGGRC 314
Cdd:pfam10282 235 ----------TLPEGFTGTNGAAAIRVSPDGKFLYVSNRGHDSIAVFAVdEAGGTLTLVERVSTEGDfPRDFNIDPDGKF 304
                         330       340
                  ....*....|....*....|....*
gi 738093228  315 LVACGEHSPQVSLYLIDDASGLPAL 339
Cdd:pfam10282 305 LVVANQDSDNVTVFRRDPETGKLTL 329
PRK11028 PRK11028
6-phosphogluconolactonase; Provisional
91-356 5.23e-47

6-phosphogluconolactonase; Provisional


Pssm-ID: 182912 [Multi-domain]  Cd Length: 330  Bit Score: 162.44  E-value: 5.23e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  91 LAIDRAGRFLFGASYGSHQLVVHaiaRLDEGD--ASPLQTLEGIRNAHAVLVSPDDRHVYVTSLGSDALLCCSLDAE--- 165
Cdd:PRK11028  85 ISTDHQGRFLFSASYNANCVSVS---PLDKDGipVAPIQIIEGLEGCHSANIDPDNRTLWVPCLKEDRIRLFTLSDDghl 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 166 REAPLEIVDTLAfdkGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLSRhhVTTrppeLAAMrdgqarppatep 245
Cdd:PRK11028 162 VAQEPAEVTTVE---GAGPRHMVFHPNQQYAYCVNELNSSVDVWQLKDPHGEIEC--VQT----LDMM------------ 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 246 qpdPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEADG-TLAHAGAVSTETQPRGFAIDPGGRCLVACGEHSPQ 324
Cdd:PRK11028 221 ---PADFSDTRWAADIHITPDGRHLYACDRTASLISVFSVSEDGsVLSFEGHQPTETQPRGFNIDHSGKYLIAAGQKSHH 297
                        250       260       270
                 ....*....|....*....|....*....|..
gi 738093228 325 VSLYLIDDASGLPALHSRHPGGQGANWVEIVA 356
Cdd:PRK11028 298 ISVYEIDGETGLLTELGRYAVGQGPMWVSVLA 329
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
96-198 5.27e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 41.50  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  96 AGRFLFGASYGSHQLVVhaiarLDEGDASPLQTLEGIRNAHAVLVSPDDRHVYVTSLGSDALLCCSLDAEReapLEIVDT 175
Cdd:cd20778  249 AGDKAFVPAVGEHRVLV-----YDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVNFSGPDNDTVQVIDTKT---LKVVKT 320
                         90       100
                 ....*....|....*....|....*
gi 738093228 176 LAFDKGFgpRHMRFSPDG--AWLHV 198
Cdd:cd20778  321 LEPGKRV--LHMEFTPRGeaVYISV 343
 
Name Accession Description Interval E-value
Pgl COG2706
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
10-355 4.03e-69

6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];


Pssm-ID: 442025 [Multi-domain]  Cd Length: 352  Bit Score: 220.55  E-value: 4.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  10 SNSISadlrVYRLDPDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALRSTPPAIARCRLDPGTGQLATDYRLDV-GAGH 88
Cdd:COG2706   20 SEGIY----VFRLDTATGELTLLGLVAALGNPSFLALSPDGRFLYAVNEVDDGGVSAFRIDPADGTLTLLNTVSSgGASP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  89 VSLAIDRAGRFLFGASYGSHQLVVHAIA---RLdeGDASPLQTLEGIR---------NAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:COG2706   96 CHLSVDPDGRFLFVANYGGGSVSVFPIDadgSL--GEPVQVIQHEGSGpnperqegpHAHSVVFDPDGRFLYVPDLGTDR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 157 LLCCSLDAErEAPLEIVDTLAFDKGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLS-RHHVTTrppelaamrd 235
Cdd:COG2706  174 IYVYRLDPA-TGKLPEPPEVSLPPGSGPRHLAFHPNGRFAYVINELDSTVSVYAYDAATGTLTlIQTVST---------- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 236 gqarppatepqpDPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEAD-GTLAHAGAVSTE-TQPRGFAIDPGGR 313
Cdd:COG2706  243 ------------LPEDFTGENWAADIHISPDGRFLYVSNRGHNSIAVFAIDADgGKLTLVGHVPTGgKWPRDFAIDPDGR 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 738093228 314 CLVACGEHSPQVSLYLIDDASGLPALHSRHPGGQGANWVEIV 355
Cdd:COG2706  311 FLLVANQKSDNITVFRIDADTGKLTPTGRSVPVPSPVCVAFL 352
Lactonase pfam10282
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ...
10-339 3.78e-57

Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.


Pssm-ID: 431196 [Multi-domain]  Cd Length: 340  Bit Score: 188.97  E-value: 3.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228   10 SNSISADLRVYRLDPDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALRSTPP-AIARCRLDPGTGQL-ATDYRLDVGAG 87
Cdd:pfam10282   8 TKGDSKGIYVLTLDTETGALTLLGLVAEVGNPSYLALSPDGRTLYAVNEEGDQgGVAAFRIDPDSGALtLLNQVPTGGAS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228   88 HVSLAIDRAGRFLFGASYGSHQLVVHAIaRLD--EGDASPLQTLEGIR---------NAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:pfam10282  88 PCHLSVDPDGRFLFVANYHGGSVSVFPL-DADgsLGELSQVVQHEGSGppperqespHPHSVDLTPDGKFLVVPDLGTDR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  157 LLCCSLDAErEAPLEIVDTLAFDKGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLSRHHVTTrppelaamrdg 236
Cdd:pfam10282 167 VRVYKLDAG-GGKLTPPASVQTPPGSGPRHLAFHPNGKYAYVVNELSSTVTVFEYDPATGTFEELQTVS----------- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  237 qarppatepqPDPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRV-EADGTLAHAGAVSTETQ-PRGFAIDPGGRC 314
Cdd:pfam10282 235 ----------TLPEGFTGTNGAAAIRVSPDGKFLYVSNRGHDSIAVFAVdEAGGTLTLVERVSTEGDfPRDFNIDPDGKF 304
                         330       340
                  ....*....|....*....|....*
gi 738093228  315 LVACGEHSPQVSLYLIDDASGLPAL 339
Cdd:pfam10282 305 LVVANQDSDNVTVFRRDPETGKLTL 329
PRK11028 PRK11028
6-phosphogluconolactonase; Provisional
91-356 5.23e-47

6-phosphogluconolactonase; Provisional


Pssm-ID: 182912 [Multi-domain]  Cd Length: 330  Bit Score: 162.44  E-value: 5.23e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  91 LAIDRAGRFLFGASYGSHQLVVHaiaRLDEGD--ASPLQTLEGIRNAHAVLVSPDDRHVYVTSLGSDALLCCSLDAE--- 165
Cdd:PRK11028  85 ISTDHQGRFLFSASYNANCVSVS---PLDKDGipVAPIQIIEGLEGCHSANIDPDNRTLWVPCLKEDRIRLFTLSDDghl 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 166 REAPLEIVDTLAfdkGFGPRHMRFSPDGAWLHVLSEFRATVAVFRRDPLTGRLSRhhVTTrppeLAAMrdgqarppatep 245
Cdd:PRK11028 162 VAQEPAEVTTVE---GAGPRHMVFHPNQQYAYCVNELNSSVDVWQLKDPHGEIEC--VQT----LDMM------------ 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 246 qpdPATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEADG-TLAHAGAVSTETQPRGFAIDPGGRCLVACGEHSPQ 324
Cdd:PRK11028 221 ---PADFSDTRWAADIHITPDGRHLYACDRTASLISVFSVSEDGsVLSFEGHQPTETQPRGFNIDHSGKYLIAAGQKSHH 297
                        250       260       270
                 ....*....|....*....|....*....|..
gi 738093228 325 VSLYLIDDASGLPALHSRHPGGQGANWVEIVA 356
Cdd:PRK11028 298 ISVYEIDGETGLLTELGRYAVGQGPMWVSVLA 329
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
6-156 2.59e-12

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 65.87  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228   6 TVIVSNSISADLRVYrldpDAPSMQAAGHHPLGPQLMPLAIASDRSTLFAALrSTPPAIARcrLDPGTGQLATdyRLDVG 85
Cdd:COG3391   81 RLYVANSGSGRVSVI----DLATGKVVATIPVGGGPRGLAVDPDGGRLYVAD-SGNGRVSV--IDTATGKVVA--TIPVG 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093228  86 AGHVSLAIDRAGRFLFGASYGSHQLVVhAIARLDEGDASPLQTLEGIRNAHAVLVSPDDRHVYVTSLGSDA 156
Cdd:COG3391  152 AGPHGIAVDPDGKRLYVANSGSNTVSV-IVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLYVANRGSNT 221
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
68-198 6.48e-11

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 61.63  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  68 RLDPGTGQLATdyRLDVGAGHVSLAIDRAGRFLFGASYGSHQLVVhaiarLDEGDASPLQTLEGIRNAHAVLVSPDDRHV 147
Cdd:COG3391   94 VIDLATGKVVA--TIPVGGGPRGLAVDPDGGRLYVADSGNGRVSV-----IDTATGKVVATIPVGAGPHGIAVDPDGKRL 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738093228 148 YVTSLGSDALLC--CSLDAEReapLEIVDTLAFdkGFGPRHMRFSPDGAWLHV 198
Cdd:COG3391  167 YVANSGSNTVSVivSVIDTAT---GKVVATIPV--GGGPVGVAVSPDGRRLYV 214
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
70-237 5.38e-10

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 58.94  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  70 DPGTGQLATDYRLDVGAGHVSLAIDRAGRFLFGASYGSHQLVVhaiarLDEGDASPLQTLEGIRNAHAVLVSPDDRHVYV 149
Cdd:COG3391   52 GGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSV-----IDLATGKVVATIPVGGGPRGLAVDPDGGRLYV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 150 TSLGSDALLccSLDAereAPLEIVDTLAFdkGFGPRHMRFSPDGAWLHVLSEFRATVAVFRR--DPLTGR-LSRHHVTTR 226
Cdd:COG3391  127 ADSGNGRVS--VIDT---ATGKVVATIPV--GAGPHGIAVDPDGKRLYVANSGSNTVSVIVSviDTATGKvVATIPVGGG 199
                        170
                 ....*....|.
gi 738093228 227 PPELAAMRDGQ 237
Cdd:COG3391  200 PVGVAVSPDGR 210
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
31-336 3.16e-09

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 56.95  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  31 AAGHHPLGPqlmplAIASDRSTLFAALRStpPAIARcrLDPGTGQLaTDYRLDVGAGHVSLAIDRAGRFLFGASYGshql 110
Cdd:COG4257   14 APGSGPRDV-----AVDPDGAVWFTDQGG--GRIGR--LDPATGEF-TEYPLGGGSGPHGIAVDPDGNLWFTDNGN---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 111 vvHAIARLD--EGDASPLQTLEGIRNAHAVLVSPDDRhVYVTSLGSDALLccSLDAEREaplEIVDTLAFDKGFGPRHMR 188
Cdd:COG4257   80 --NRIGRIDpkTGEITTFALPGGGSNPHGIAFDPDGN-LWFTDQGGNRIG--RLDPATG---EVTEFPLPTGGAGPYGIA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 189 FSPDGAWLHVLSEFRAtvaVFRRDPLTGRLSRHhvttrppelaamrdgqarppatePQPDPATLAGAIWAAdlqvrPDGR 268
Cdd:COG4257  152 VDPDGNLWVTDFGANA---IGRIDPDTGTLTEY-----------------------ALPTPGAGPRGLAVD-----PDGN 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738093228 269 fVYLSERTTSRLFVLRvEADGTLAHAGAVSTETQPRGFAIDPGGRCLVAcgEHSPQvSLYLIDDASGL 336
Cdd:COG4257  201 -LWVADTGSGRIGRFD-PKTGTVTEYPLPGGGARPYGVAVDGDGRVWFA--ESGAN-RIVRFDPDTEL 263
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
18-199 1.06e-05

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 46.42  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  18 RVYRLDPDAPSMQaaghHPLGPQLMPLAIASDRS-TLFAAlrSTPPAIARcrLDPGTGQLATdYRLDVGAGHVS---LAI 93
Cdd:COG3386   30 RIHRYDPDGGAVE----VFAEPSGRPNGLAFDPDgRLLVA--DHGRGLVR--FDPADGEVTV-LADEYGKPLNRpndGVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  94 DRAGRFLFGASYGSHQlvVHAIARLD-EGDASPLqtLEGIRNAHAVLVSPDDRHVYVTSLGSDALLCCSLDAERE-APLE 171
Cdd:COG3386  101 DPDGRLYFTDMGEYLP--TGALYRVDpDGSLRVL--ADGLTFPNGIAFSPDGRTLYVADTGAGRIYRFDLDADGTlGNRR 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 738093228 172 IVDTLAFDKGF------------------GPRHMRFSPDGAWLHVL 199
Cdd:COG3386  177 VFADLPDGPGGpdglavdadgnlwvalwgGGGVVRFDPDGELLGRI 222
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
138-322 2.48e-05

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 45.27  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 138 VLVSPDDRhVYVTSLGSDALLCCSLDAEReapleiVDTLAFDKGFgPRHMRFSPDGAWLHVlsefRATVAVFRRDPLTGR 217
Cdd:COG3386   13 PVWDPDGR-LYWVDIPGGRIHRYDPDGGA------VEVFAEPSGR-PNGLAFDPDGRLLVA----DHGRGLVRFDPADGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 218 LSRHH-----VTTRPPELAAMRDGQArpPATEPQPDPATlaGAIW--AADLQVR---------------PDGRFVYLSER 275
Cdd:COG3386   81 VTVLAdeygkPLNRPNDGVVDPDGRL--YFTDMGEYLPT--GALYrvDPDGSLRvladgltfpngiafsPDGRTLYVADT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 738093228 276 TTSRLFVLRVEADGTLAHAGAVSTETQ----PRGFAIDPGGRCLVACGEHS 322
Cdd:COG3386  157 GAGRIYRFDLDADGTLGNRRVFADLPDgpggPDGLAVDADGNLWVALWGGG 207
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
250-358 1.29e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 42.76  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228 250 ATLAGAIWAADLQVRPDGRFVYLSERTTSRLFVLRVEadgTLAHAGAVSTETQPRGFAIDPGGRCLVACGEHSPQVSLYL 329
Cdd:COG3391  104 ATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTA---TGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSNTVSVIV 180
                         90       100       110
                 ....*....|....*....|....*....|.
gi 738093228 330 --IDDASGlpALHSRHPGGQGANWVEIVASG 358
Cdd:COG3391  181 svIDTATG--KVVATIPVGGGPVGVAVSPDG 209
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
96-198 5.27e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 41.50  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093228  96 AGRFLFGASYGSHQLVVhaiarLDEGDASPLQTLEGIRNAHAVLVSPDDRHVYVTSLGSDALLCCSLDAEReapLEIVDT 175
Cdd:cd20778  249 AGDKAFVPAVGEHRVLV-----YDTNDWKFIKSIPLAGQPVFAVARPDGRYVWVNFSGPDNDTVQVIDTKT---LKVVKT 320
                         90       100
                 ....*....|....*....|....*
gi 738093228 176 LAFDKGFgpRHMRFSPDG--AWLHV 198
Cdd:cd20778  321 LEPGKRV--LHMEFTPRGeaVYISV 343
 
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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