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Conserved domains on  [gi|1447253747|gb|REI87587|]
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bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC [Klebsiella variicola]

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]; ...
 3-400 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: 650.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFASPvKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLP 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 243 TPPFVQRIDVTTALEMEAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHRPYV 322
Cdd:COG0452   241 TPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFL 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447253747 323 VGFAAETNNVEEYARQKRARKNLDLICANDVSQPDQGFNSDNNALHLFWQDG-EKRLPLERKELLGQLLLDEIVTRYDE 400
Cdd:COG0452   321 VGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGrEEELPLMSKLEVARRILDEIAELLAA 399
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 3-400 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: 650.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFASPvKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLP 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 243 TPPFVQRIDVTTALEMEAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHRPYV 322
Cdd:COG0452   241 TPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFL 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447253747 323 VGFAAETNNVEEYARQKRARKNLDLICANDVSQPDQGFNSDNNALHLFWQDG-EKRLPLERKELLGQLLLDEIVTRYDE 400
Cdd:COG0452   321 VGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGrEEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-400 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 647.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   1 MTLAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGK 80
Cdd:PRK05579    2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  81 WADLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGD 160
Cdd:PRK05579   82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 161 VGPGRMLDPLTIVEMAAQHFASpvKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVS 240
Cdd:PRK05579  162 VGPGRMAEPEEIVAAAERALSP--KDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 241 LPTPPFVQRIDVTTALEMEAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHRP 320
Cdd:PRK05579  240 LPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 321 YVVGFAAETNNVEEYARQKRARKNLDLICANDVSqPDQGFNSDNNALHLFWQDG-EKRLPLERKELLGQLLLDEIVTRYD 399
Cdd:PRK05579  320 FVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDGgEVKLPLMSKLELARRLLDEIAERLL 398


                  .
gi 1447253747 400 E 400
Cdd:PRK05579  399 E 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-395 0e+00

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: 556.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMgHIELGKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFaSPVKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLP 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREF-SPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 243 TPPFVQRIDVTTALEM-EAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHrPY 321
Cdd:TIGR00521 239 TPPGVKSIKVSTAEEMlEAALNELAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKKH-QV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447253747 322 VVGFAAETNN-VEEYARQKRARKNLDLICANDVSQPdQGFNSDNNALHLFWQDGEKRLPLERKELLGQLLLDEIV 395
Cdd:TIGR00521 318 IVGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQG-RGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEIK 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 187-368 4.62e-93

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: 277.37  E-value: 4.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 187 LQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLPTPPFVQRIDVTTALEMEAAVQAGA 266
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 267 QQQHIFIGCAAVADYRAAVIAEDKIKKQ--GDELTIKMIKNPDIVAGVAALKAHrPYVVGFAAETNNVEEYARQKRARKN 344
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSsgGEELTLELVKNPDILAELGKRKPG-QLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|....
gi 1447253747 345 LDLICANDVSQPDQGFNSDNNALH 368
Cdd:pfam04127 160 LDLIVANDVSRPGAGFGSDTNEVT 183
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 3-400 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: 650.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFASPvKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLP 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 243 TPPFVQRIDVTTALEMEAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHRPYV 322
Cdd:COG0452   241 TPAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFL 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447253747 323 VGFAAETNNVEEYARQKRARKNLDLICANDVSQPDQGFNSDNNALHLFWQDG-EKRLPLERKELLGQLLLDEIVTRYDE 400
Cdd:COG0452   321 VGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGrEEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-400 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 647.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   1 MTLAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGK 80
Cdd:PRK05579    2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  81 WADLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGD 160
Cdd:PRK05579   82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 161 VGPGRMLDPLTIVEMAAQHFASpvKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVS 240
Cdd:PRK05579  162 VGPGRMAEPEEIVAAAERALSP--KDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 241 LPTPPFVQRIDVTTALEMEAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHRP 320
Cdd:PRK05579  240 LPTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 321 YVVGFAAETNNVEEYARQKRARKNLDLICANDVSqPDQGFNSDNNALHLFWQDG-EKRLPLERKELLGQLLLDEIVTRYD 399
Cdd:PRK05579  320 FVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDGgEVKLPLMSKLELARRLLDEIAERLL 398


                  .
gi 1447253747 400 E 400
Cdd:PRK05579  399 E 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-395 0e+00

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: 556.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMgHIELGKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFaSPVKDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLP 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREF-SPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 243 TPPFVQRIDVTTALEM-EAAVQAGAQQQHIFIGCAAVADYRAAVIAEDKIKKQGDELTIKMIKNPDIVAGVAALKAHrPY 321
Cdd:TIGR00521 239 TPPGVKSIKVSTAEEMlEAALNELAKDFDIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKKH-QV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447253747 322 VVGFAAETNN-VEEYARQKRARKNLDLICANDVSQPdQGFNSDNNALHLFWQDGEKRLPLERKELLGQLLLDEIV 395
Cdd:TIGR00521 318 IVGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQG-RGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEIK 391
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 3-401 1.07e-117

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 350.98  E-value: 1.07e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   3 LAGKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWA 82
Cdd:PRK13982   68 LASKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDC 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVSTICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQA-CGDV 161
Cdd:PRK13982  148 DLIVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 162 GPGRMLDPLTIVEmAAQHFASPV--KDLQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPV 239
Cdd:PRK13982  228 GVGRMAEPLEIAA-AAEALLRPPqpKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISGPV 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 240 SLPTPPFVQRIDVTTALEM-EAAVQAGAQQQHIFIgcAAVADYRAAVIAEDKIKKQGDEL-TIKMIKNPDIVAGVAALKA 317
Cdd:PRK13982  307 DLADPQGVKVIHVESARQMlAAVEAALPADIAIFA--AAVADWRVATEGGQKLKKGAAGPpPLQLVENPDILATISKLAE 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 318 HRP-YVVGFAAETNNVEEYARQKRARKNLDLICANDVSQPDQGFNSDNNALHLFWQDGE----KRLPLERKELLGQLLLD 392
Cdd:PRK13982  385 NRPpLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRNTVHLLSRDGDaekvESWPVMTKDEVATALVA 464


                  ....*....
gi 1447253747 393 EIVTRYDEK 401
Cdd:PRK13982  465 RIASTFTTP 473
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 187-368 4.62e-93

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: 277.37  E-value: 4.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 187 LQHLNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSLPTPPFVQRIDVTTALEMEAAVQAGA 266
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 267 QQQHIFIGCAAVADYRAAVIAEDKIKKQ--GDELTIKMIKNPDIVAGVAALKAHrPYVVGFAAETNNVEEYARQKRARKN 344
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSsgGEELTLELVKNPDILAELGKRKPG-QLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|....
gi 1447253747 345 LDLICANDVSQPDQGFNSDNNALH 368
Cdd:pfam04127 160 LDLIVANDVSRPGAGFGSDTNEVT 183
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 5-182 1.90e-63

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 201.33  E-value: 1.90e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   5 GKKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWADL 84
Cdd:PRK07313    1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  85 VILAPATADLIARVAAGMANDLVSTICLATP--SPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVG 162
Cdd:PRK07313   81 FLVAPATANTIAKLAHGIADDLVTSVALALPatTPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160

                         170       180
                  ....*....|....*....|
gi 1447253747 163 PGRMLDPLTIVEMAAQHFAS 182
Cdd:PRK07313  161 YGALADIETILETIENTLKE 180
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 6-174 1.60e-45

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: 154.97  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   6 KKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGYPVSDSLLDPAAEAAMGHIELGKWADLV 85
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  86 ILAPATADLIARVAAGMANDLVSTICLATPS--PVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQACGDVGP 163
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALALPPetPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160

                         170
                  ....*....|.
gi 1447253747 164 GRMLDPLTIVE 174
Cdd:TIGR02113 161 GALADLDDILQ 171
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 6-180 1.43e-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: 1.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   6 KKIVLGVSGGIAAYKTPELVRRLRERGAEVRVAMTEAAKAFITPLSLQAVSGyPVSDSLLDPAAEAAMGHIELG---KWA 82
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSE-NVDEDLTWRELDDDILHIELAsgaRWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  83 DLVILAPATADLIARVAAGMANDLVS----------------TICLATPSPVAVVPAMNQQMYRAQATQQNLQTLASRGl 146
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447253747 147 llwgpdsgsqacgdvGPGRMLDPLTIVEMAAQHF 180
Cdd:pfam02441 159 ---------------GKGRMPEPEAIVGKVLDAL 177
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 7-172 8.93e-23

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 95.42  E-value: 8.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   7 KIVLGVSGGIAAYKTPELVRRLRErGAEVRVAMTEAAKAFITPLSL-QAVSGYPVSDS------LLDPAAeaamgHIELG 79
Cdd:PLN02496   21 RILLAASGSVAAIKFGNLCHCFSE-WAEVRAVVTKASLHFIDRASLpKDVTLYTDEDEwsswnkIGDSVL-----HIELR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747  80 KWADLVILAPATADLIARVAAGMANDLVSTICLA--TPSPVAVVPAMNQQMYRAQATQQNLQTLASRGLLLWGPDSGSQA 157
Cdd:PLN02496   95 RWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAwdYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLA 174

                         170
                  ....*....|....*
gi 1447253747 158 CGDVGPGRMLDPLTI 172
Cdd:PLN02496  175 CGDYGNGAMAEPSLI 189
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 190-399 1.25e-15

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 75.41  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 190 LNLMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAAQRGANVTLVSGPVSL-PTP-PFVQRIDVTTALEMEAAVQAGAQ 267
Cdd:PRK06732    1 MKILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVkPEPhPNLSIIEIENVDDLLETLEPLVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747 268 QQHIFIGCAAVADYR-------AAVIA-------------EDKIKKQGDELTIKMIKNPDIVAGVaalKAHRPYV--VGF 325
Cdd:PRK06732   81 DHDVLIHSMAVSDYTpvymtdlEEVSAsdnlnefltkqntEAKISSASDYQVLFLKKTPKVISYV---KKWNPNItlVGF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447253747 326 AAETNNVEEY----ARQKRARKNLDLICANDVSQpdqgFNSDNNALHLFWQDGEkrLPLERKELLGQLLLdEIVTRYD 399
Cdd:PRK06732  158 KLLVNVSKEElikvARASLIKNQADYILANDLTD----ISADQHKALLVSKNEV--YTAQTKEEIADLLL-ERIEKYD 228
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
 1-102 7.45e-04

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 40.26  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447253747   1 MTLAGKKIVLGVSGGIAAYK--TPELvRRLRERGAEVRVAMTEAAKAFITPL--------SLQAVSGYPVSDSLldPAAE 70
Cdd:PRK08305    1 MSLKGKRIGFGLTGSHCTYDevMPEI-EKLVDEGAEVTPIVSYTVQTTDTRFgkaeewikKIEEITGNKVINTI--VEAE 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1447253747  71 AamghIELGKWADLVILAPATADLIARVAAGM 102
Cdd:PRK08305   78 P----LGPKKLLDCMVIAPCTGNTMAKLANAI 105
 
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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