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Conserved domains on  [gi|15600513|ref|NP_254007|]
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bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase [Pseudomonas aeruginosa PAO1]

Protein Classification

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase( domain architecture ID 11418829)

bifunctional phosphopantothenoylcysteine decarboxylase (CoaC)/phosphopantothenate synthase (CoaB) catalyzes two steps in the biosynthesis of coenzyme A, the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, followed by its decarboxylation to form 4'-phosphopantotheine

EC:  4.1.1.36|6.3.2.5
Gene Ontology:  GO:0071513|GO:0010181|GO:0046872|GO:0004632|GO:0004633|GO:0015937|GO:0015941

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 4-401 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 652.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   4 LYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWA 83
Cdd:COG0452   2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  84 DLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:COG0452  82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 164 LGRMLEAEELAQRAADCFQRQA-LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPT 242
Cdd:COG0452 162 KGRMAEPEEIVEAIEALLAPKKdLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 243 PDRVQRVDVVSARDMLAACEAAMP-CDLLIASAAVADYRPEVVAAHKLKKDptsGEGLLLQLVRNPDILATLAQREDR-P 320
Cdd:COG0452 242 PAGVERIDVESAEEMLEAVLAAFPdADIVIMAAAVADYRPAEVADQKIKKT---DDPLTLELVKNPDILAELGARKKPgQ 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 321 FSVGFAAETENLLDYAARKLKDKNLDLIVANDVANPSIGFNSDENAITVIDRDLHPSTFAQTSKGKIARQLVAFIADRLN 400
Cdd:COG0452 319 FLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398


                .
gi 15600513 401 Q 401
Cdd:COG0452 399 A 399
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 4-401 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 652.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   4 LYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWA 83
Cdd:COG0452   2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  84 DLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:COG0452  82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 164 LGRMLEAEELAQRAADCFQRQA-LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPT 242
Cdd:COG0452 162 KGRMAEPEEIVEAIEALLAPKKdLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 243 PDRVQRVDVVSARDMLAACEAAMP-CDLLIASAAVADYRPEVVAAHKLKKDptsGEGLLLQLVRNPDILATLAQREDR-P 320
Cdd:COG0452 242 PAGVERIDVESAEEMLEAVLAAFPdADIVIMAAAVADYRPAEVADQKIKKT---DDPLTLELVKNPDILAELGARKKPgQ 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 321 FSVGFAAETENLLDYAARKLKDKNLDLIVANDVANPSIGFNSDENAITVIDRDLHPSTFAQTSKGKIARQLVAFIADRLN 400
Cdd:COG0452 319 FLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398


                .
gi 15600513 401 Q 401
Cdd:COG0452 399 A 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-401 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 639.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    1 MQRLYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELA 80
Cdd:PRK05579   1 MRMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   81 RWADLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACG 160
Cdd:PRK05579  81 KWADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  161 DVGLGRMLEAEELAQRAADCFQRQALTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHL 240
Cdd:PRK05579 161 DVGPGRMAEPEEIVAAAERALSPKDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  241 PTPDRVQRVDVVSARDMLAACEAAMP-CDLLIASAAVADYRPEVVAAHKLKKDPtsgEGLLLQLVRNPDILATLAQR-ED 318
Cdd:PRK05579 241 PTPAGVKRIDVESAQEMLDAVLAALPqADIFIMAAAVADYRPATVAEGKIKKGE---GELTLELVPNPDILAEVAALkDK 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  319 RPFSVGFAAETENLLDYAARKLKDKNLDLIVANDVAnPSIGFNSDENAITVIDRDLHPSTFAQTSKGKIARQLVAFIADR 398
Cdd:PRK05579 318 RPFVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAER 396


                 ...
gi 15600513  399 LNQ 401
Cdd:PRK05579 397 LLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 4-396 1.43e-163

phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273116 [Multi-domain]  Cd Length: 391  Bit Score: 464.54  E-value: 1.43e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513     4 LYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMgHIELARWA 83
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    84 DLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   164 LGRMLEAEELAQRAADCF-QRQALTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPT 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFsPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   243 PDRVQRVDVVSARDML--AACEAAMPCDLLIASAAVADYRPEVVAAHKLKKdptSGEGLLLQLVRNPDILATLAQREDRP 320
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLeaALNELAKDFDIFISAAAVADFKPKTVFEGKIKK---QGEELSLKLVKNPDIIAEVRKIKKHQ 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600513   321 FSVGFAAETEN-LLDYAARKLKDKNLDLIVANDVANPSiGFNSDENAITVIDRDLHpSTFAQTSKGKIARQLVAFIA 396
Cdd:TIGR00521 317 VIVGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQGR-GFGSDENEVYIFSKHGH-KELPLMSKLEVAERILDEIK 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-368 1.10e-103

DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.


Pssm-ID: 461186 [Multi-domain]  Cd Length: 183  Bit Score: 304.33  E-value: 1.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   186 LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPTPDRVQRVDVVSARDMLAACEAAM 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   266 P-CDLLIASAAVADYRPEVVAAHKLKKDpTSGEGLLLQLVRNPDILATLAQREDRPFSVGFAAETENLLDYAARKLKDKN 344
Cdd:pfam04127  81 PeADIVIMAAAVADYRPAEVADGKIKKS-SGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|....
gi 15600513   345 LDLIVANDVANPSIGFNSDENAIT 368
Cdd:pfam04127 160 LDLIVANDVSRPGAGFGSDTNEVT 183
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 4-401 0e+00

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 652.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   4 LYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWA 83
Cdd:COG0452   2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  84 DLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:COG0452  82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 164 LGRMLEAEELAQRAADCFQRQA-LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPT 242
Cdd:COG0452 162 KGRMAEPEEIVEAIEALLAPKKdLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 243 PDRVQRVDVVSARDMLAACEAAMP-CDLLIASAAVADYRPEVVAAHKLKKDptsGEGLLLQLVRNPDILATLAQREDR-P 320
Cdd:COG0452 242 PAGVERIDVESAEEMLEAVLAAFPdADIVIMAAAVADYRPAEVADQKIKKT---DDPLTLELVKNPDILAELGARKKPgQ 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513 321 FSVGFAAETENLLDYAARKLKDKNLDLIVANDVANPSIGFNSDENAITVIDRDLHPSTFAQTSKGKIARQLVAFIADRLN 400
Cdd:COG0452 319 FLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGREEELPLMSKLEVARRILDEIAELLA 398


                .
gi 15600513 401 Q 401
Cdd:COG0452 399 A 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-401 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 639.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    1 MQRLYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELA 80
Cdd:PRK05579   1 MRMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   81 RWADLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACG 160
Cdd:PRK05579  81 KWADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  161 DVGLGRMLEAEELAQRAADCFQRQALTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHL 240
Cdd:PRK05579 161 DVGPGRMAEPEEIVAAAERALSPKDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  241 PTPDRVQRVDVVSARDMLAACEAAMP-CDLLIASAAVADYRPEVVAAHKLKKDPtsgEGLLLQLVRNPDILATLAQR-ED 318
Cdd:PRK05579 241 PTPAGVKRIDVESAQEMLDAVLAALPqADIFIMAAAVADYRPATVAEGKIKKGE---GELTLELVPNPDILAEVAALkDK 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  319 RPFSVGFAAETENLLDYAARKLKDKNLDLIVANDVAnPSIGFNSDENAITVIDRDLHPSTFAQTSKGKIARQLVAFIADR 398
Cdd:PRK05579 318 RPFVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDGGEVKLPLMSKLELARRLLDEIAER 396


                 ...
gi 15600513  399 LNQ 401
Cdd:PRK05579 397 LLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 4-396 1.43e-163

phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273116 [Multi-domain]  Cd Length: 391  Bit Score: 464.54  E-value: 1.43e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513     4 LYRKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMgHIELARWA 83
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    84 DLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   164 LGRMLEAEELAQRAADCF-QRQALTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPT 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFsPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   243 PDRVQRVDVVSARDML--AACEAAMPCDLLIASAAVADYRPEVVAAHKLKKdptSGEGLLLQLVRNPDILATLAQREDRP 320
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLeaALNELAKDFDIFISAAAVADFKPKTVFEGKIKK---QGEELSLKLVKNPDIIAEVRKIKKHQ 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600513   321 FSVGFAAETEN-LLDYAARKLKDKNLDLIVANDVANPSiGFNSDENAITVIDRDLHpSTFAQTSKGKIARQLVAFIA 396
Cdd:TIGR00521 317 VIVGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQGR-GFGSDENEVYIFSKHGH-KELPLMSKLEVAERILDEIK 391
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 6-399 9.36e-141

bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Provisional


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 409.53  E-value: 9.36e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    6 RKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWADL 85
Cdd:PRK13982  70 SKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDCDL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   86 VLIAPATADLMARLVQGVANDLLTTLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQA-CGDVGL 164
Cdd:PRK13982 150 IVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEAGV 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  165 GRMLEAEELAQRAA---DCFQRQALTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLP 241
Cdd:PRK13982 230 GRMAEPLEIAAAAEallRPPQPKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISGPVDLA 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  242 TPDRVQRVDVVSARDMLAACEAAMPCDLLIASAAVADYRPEVVAAHKLKKdpTSGEGLLLQLVRNPDILATLAQREDR-- 319
Cdd:PRK13982 310 DPQGVKVIHVESARQMLAAVEAALPADIAIFAAAVADWRVATEGGQKLKK--GAAGPPPLQLVENPDILATISKLAENrp 387

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  320 PFSVGFAAETENLLDYAARKLKDKNLDLIVANDVANPSIGFNSDENAITVIDRD---LHPSTFAQTSKGKIARQLVAFIA 396
Cdd:PRK13982 388 PLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRNTVHLLSRDgdaEKVESWPVMTKDEVATALVARIA 467


                 ...
gi 15600513  397 DRL 399
Cdd:PRK13982 468 STF 470
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-368 1.10e-103

DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.


Pssm-ID: 461186 [Multi-domain]  Cd Length: 183  Bit Score: 304.33  E-value: 1.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   186 LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHLPTPDRVQRVDVVSARDMLAACEAAM 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   266 P-CDLLIASAAVADYRPEVVAAHKLKKDpTSGEGLLLQLVRNPDILATLAQREDRPFSVGFAAETENLLDYAARKLKDKN 344
Cdd:pfam04127  81 PeADIVIMAAAVADYRPAEVADGKIKKS-SGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|....
gi 15600513   345 LDLIVANDVANPSIGFNSDENAIT 368
Cdd:pfam04127 160 LDLIVANDVSRPGAGFGSDTNEVT 183
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 6-185 4.70e-65

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 205.57  E-value: 4.70e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    6 RKRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWADL 85
Cdd:PRK07313   1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   86 VLIAPATADLMARLVQGVANDLLTTLVLATDAQIA--LAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVG 163
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALALPATTPklIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160

                        170       180
                 ....*....|....*....|..
gi 15600513  164 LGRMLEAEELAQRAADCFQRQA 185
Cdd:PRK07313 161 YGALADIETILETIENTLKEKT 182
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 7-176 5.52e-48

phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis (see TIGR00521). These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This model describes proteins from the genera Streptococcus and Enterococcus homologous to the N-terminal region of TIGR00521, corresponding to phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 131168  Cd Length: 177  Bit Score: 161.52  E-value: 5.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513     7 KRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHPVHTDLLDPAAEAAMGHIELARWADLV 86
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    87 LIAPATADLMARLVQGVANDLLTTLVLATDAQIA--LAPAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQACGDVGL 164
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALALPPETPklIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160

                         170
                  ....*....|..
gi 15600513   165 GRMLEAEELAQR 176
Cdd:TIGR02113 161 GALADLDDILQT 172
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 7-179 1.10e-40

Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).


Pssm-ID: 426775 [Multi-domain]  Cd Length: 177  Bit Score: 142.13  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513     7 KRIVLGVGGGIAAYKSAELVRRLRDQGAEVRVVMTQGGREFITPLTLQALSGHpVHTDLLDPAAEAAMGHIEL---ARWA 83
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSEN-VDEDLTWRELDDDILHIELasgARWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    84 DLVLIAPATADLMARLVQGVANDLLT----------------TLVLATDAQIALAPAMNQAMWRDTATQANAELLRQRGf 147
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 15600513   148 hlfgpaagsqacgdvGLGRMLEAEELAQRAAD 179
Cdd:pfam02441 159 ---------------GKGRMPEPEAIVGKVLD 175
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 6-169 4.69e-23

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 96.19  E-value: 4.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513    6 RKRIVLGVGGGIAAYKSAELVRRLrDQGAEVRVVMTQGGREFITPLTL-QALSghpVHTDLLDPAAEAAMG----HIELA 80
Cdd:PLN02496  19 KPRILLAASGSVAAIKFGNLCHCF-SEWAEVRAVVTKASLHFIDRASLpKDVT---LYTDEDEWSSWNKIGdsvlHIELR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513   81 RWADLVLIAPATADLMARLVQGVANDLLTTLVLATDAQIAL--APAMNQAMWRDTATQANAELLRQRGFHLFGPAAGSQA 158
Cdd:PLN02496  95 RWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPLfvAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLA 174

                        170
                 ....*....|.
gi 15600513  159 CGDVGLGRMLE 169
Cdd:PLN02496 175 CGDYGNGAMAE 185
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 191-355 1.35e-22

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 95.05  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  191 VLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTGPVHL-PTP-DRVQRVDVVSARDMLAACEAAMP-C 267
Cdd:PRK06732   3 ILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVkPEPhPNLSIIEIENVDDLLETLEPLVKdH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  268 DLLIASAAVADYRP-------EVVAAHK----LKKDPTSG------EGLLLQLVRNPDILATLAQREDRPFSVGFA---- 326
Cdd:PRK06732  83 DVLIHSMAVSDYTPvymtdleEVSASDNlnefLTKQNTEAkissasDYQVLFLKKTPKVISYVKKWNPNITLVGFKllvn 162

                        170       180
                 ....*....|....*....|....*....
gi 15600513  327 AETENLLDYAARKLKDKNLDLIVANDVAN 355
Cdd:PRK06732 163 VSKEELIKVARASLIKNQADYILANDLTD 191
PRK09620 PRK09620
hypothetical protein; Provisional
 186-351 1.89e-07

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 51.43  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  186 LTGVHVLITAGPTQENIDPVRYITNHSSGKMGFALAEAAVEAGARVTLVTG-----PVHLPTPDRVQRVD-VVSARDMLA 259
Cdd:PRK09620   1 MKGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGyfaekPNDINNQLELHPFEgIIDLQDKMK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600513  260 ACEAAMPCDLLIASAAVADYRPEVVAAH-----KLKKDPTSGEGLLLQLVRNPDILATLAQREDRPFSVGFAAET----E 330
Cdd:PRK09620  81 SIITHEKVDAVIMAAAGSDWVVDKICDQegnvlDMNGKISSDIAPIIHFQKAPKVLKQIKQWDPETVLVGFKLESdvneE 160

                        170       180
                 ....*....|....*....|.
gi 15600513  331 NLLDYAARKLKDKNLDLIVAN 351
Cdd:PRK09620 161 ELFERAKNRMEEAKASVMIAN 181
 
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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