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Conserved domains on  [gi|1125799677|ref|WP_075114303|]
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MULTISPECIES: bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC [Aeromonas]

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: 658.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 163 PGRMLDPLELVDRCCQQLAAEPLLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLAT 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 243 PAGVTRVDVESAEQMHQAVMSRVGECDLFIGCAAVADYRPEQVASQKIKKTGDNdqMVVKLVKNPDIIAAVGAL-SDKPF 321
Cdd:COG0452   242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDP--LTLELVKNPDILAELGARkKPGQF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 322 TVGFAAETVDVEQYALDKLQRKRLDMIAANDVSREGQGFNADDNALTVFW-QGGQAPLPLADKLTLARHLIALIARHYRR 400
Cdd:COG0452   320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDkDGREEELPLMSKLEVARRILDEIAELLAA 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: 658.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 163 PGRMLDPLELVDRCCQQLAAEPLLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLAT 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 243 PAGVTRVDVESAEQMHQAVMSRVGECDLFIGCAAVADYRPEQVASQKIKKTGDNdqMVVKLVKNPDIIAAVGAL-SDKPF 321
Cdd:COG0452   242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDP--LTLELVKNPDILAELGARkKPGQF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 322 TVGFAAETVDVEQYALDKLQRKRLDMIAANDVSREGQGFNADDNALTVFW-QGGQAPLPLADKLTLARHLIALIARHYRR 400
Cdd:COG0452   320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDkDGREEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-399 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 621.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   1 MRLADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAK 80
Cdd:PRK05579    2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  81 WADLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGD 160
Cdd:PRK05579   82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 161 VGPGRMLDPLELVDRCCQQLAAEPlLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTL 240
Cdd:PRK05579  162 VGPGRMAEPEEIVAAAERALSPKD-LAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 241 ATPAGVTRVDVESAEQMHQAVMSRVGECDLFIGCAAVADYRPEQVASQKIKKTGdnDQMVVKLVKNPDIIAAVGALSDK- 319
Cdd:PRK05579  241 PTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGE--GELTLELVPNPDILAEVAALKDKr 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 320 PFTVGFAAETVDVEQYALDKLQRKRLDMIAANDVSrEGQGFNADDNALTVFWQ-GGQAPLPLADKLTLARHLIALIARHY 398
Cdd:PRK05579  319 PFVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSdGGEVKLPLMSKLELARRLLDEIAERL 397


                  .
gi 1125799677 399 R 399
Cdd:PRK05579  398 L 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-391 9.87e-174

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: 489.96  E-value: 9.87e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMgHIELAKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 163 PGRMLDPLELVDRCCQQLAAEPLLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLAT 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 243 PAGVTRVDVESAEQMHQAVM-SRVGECDLFIGCAAVADYRPEQVASQKIKKTGdnDQMVVKLVKNPDIIAAVGALSDKPF 321
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLEAALnELAKDFDIFISAAAVADFKPKTVFEGKIKKQG--EELSLKLVKNPDIIAEVRKIKKHQV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125799677 322 TVGFAAET-VDVEQYALDKLQRKRLDMIAANDVSrEGQGFNADDNALTVFWQGGQAPLPLADKLTLARHLI 391
Cdd:TIGR00521 318 IVGFKAETnDDLIKYAKEKLKKKNLDMIVANDVS-QGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERIL 387
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-368 2.95e-100

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: 295.47  E-value: 2.95e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 186 LAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLATPAGVTRVDVESAEQMHQAVMSRV 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 266 GECDLFIGCAAVADYRPEQVASQKIKKTGDNDQMVVKLVKNPDIIAAVGALSDKPFTVGFAAETVDVEQYALDKLQRKRL 345
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 1125799677 346 DMIAANDVSREGQGFNADDNALT 368
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 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: 658.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWA 82
Cdd:COG0452     2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVG 162
Cdd:COG0452    82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 163 PGRMLDPLELVDRCCQQLAAEPLLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLAT 242
Cdd:COG0452   162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 243 PAGVTRVDVESAEQMHQAVMSRVGECDLFIGCAAVADYRPEQVASQKIKKTGDNdqMVVKLVKNPDIIAAVGAL-SDKPF 321
Cdd:COG0452   242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDP--LTLELVKNPDILAELGARkKPGQF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 322 TVGFAAETVDVEQYALDKLQRKRLDMIAANDVSREGQGFNADDNALTVFW-QGGQAPLPLADKLTLARHLIALIARHYRR 400
Cdd:COG0452   320 LVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDkDGREEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-399 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 621.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   1 MRLADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAK 80
Cdd:PRK05579    2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  81 WADLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGD 160
Cdd:PRK05579   82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 161 VGPGRMLDPLELVDRCCQQLAAEPlLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTL 240
Cdd:PRK05579  162 VGPGRMAEPEEIVAAAERALSPKD-LAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 241 ATPAGVTRVDVESAEQMHQAVMSRVGECDLFIGCAAVADYRPEQVASQKIKKTGdnDQMVVKLVKNPDIIAAVGALSDK- 319
Cdd:PRK05579  241 PTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGE--GELTLELVPNPDILAEVAALKDKr 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 320 PFTVGFAAETVDVEQYALDKLQRKRLDMIAANDVSrEGQGFNADDNALTVFWQ-GGQAPLPLADKLTLARHLIALIARHY 398
Cdd:PRK05579  319 PFVVGFAAETGDVLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSdGGEVKLPLMSKLELARRLLDEIAERL 397


                  .
gi 1125799677 399 R 399
Cdd:PRK05579  398 L 398
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-391 9.87e-174

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: 489.96  E-value: 9.87e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMgHIELAKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 163 PGRMLDPLELVDRCCQQLAAEPLLAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLAT 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 243 PAGVTRVDVESAEQMHQAVM-SRVGECDLFIGCAAVADYRPEQVASQKIKKTGdnDQMVVKLVKNPDIIAAVGALSDKPF 321
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLEAALnELAKDFDIFISAAAVADFKPKTVFEGKIKKQG--EELSLKLVKNPDIIAEVRKIKKHQV 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125799677 322 TVGFAAET-VDVEQYALDKLQRKRLDMIAANDVSrEGQGFNADDNALTVFWQGGQAPLPLADKLTLARHLI 391
Cdd:TIGR00521 318 IVGFKAETnDDLIKYAKEKLKKKNLDMIVANDVS-QGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERIL 387
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 3-396 1.47e-120

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 357.91  E-value: 1.47e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   3 LADKRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWA 82
Cdd:PRK13982   68 LASKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDC 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLTTLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQA-CGDV 161
Cdd:PRK13982  148 DLIVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 162 GPGRMLDPLELVDrccqqlAAEPL--------LAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTL 233
Cdd:PRK13982  228 GVGRMAEPLEIAA------AAEALlrppqpkpLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTL 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 234 VSGPVTLATPAGVTRVDVESAEQMHQAVMSRVgECDLFIGCAAVADYRPEQVASQKIKKtGDNDQMVVKLVKNPDIIAAV 313
Cdd:PRK13982  302 ISGPVDLADPQGVKVIHVESARQMLAAVEAAL-PADIAIFAAAVADWRVATEGGQKLKK-GAAGPPPLQLVENPDILATI 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 314 GALSDK--PFTVGFAAETVDVEQYALDKLQRKRLDMIAANDVSREGQGFNADDNALTVFWQGGQA----PLPLADKLTLA 387
Cdd:PRK13982  380 SKLAENrpPLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRNTVHLLSRDGDAekveSWPVMTKDEVA 459


                  ....*....
gi 1125799677 388 RHLIALIAR 396
Cdd:PRK13982  460 TALVARIAS 468
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-368 2.95e-100

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: 295.47  E-value: 2.95e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 186 LAGVKLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGPVTLATPAGVTRVDVESAEQMHQAVMSRV 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 266 GECDLFIGCAAVADYRPEQVASQKIKKTGDNDQMVVKLVKNPDIIAAVGALSDKPFTVGFAAETVDVEQYALDKLQRKRL 345
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETEDLLENARAKLERKNL 160

                         170       180
                  ....*....|....*....|...
gi 1125799677 346 DMIAANDVSREGQGFNADDNALT 368
Cdd:pfam04127 161 DLIVANDVSRPGAGFGSDTNEVT 183
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 6-174 3.29e-68

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 213.66  E-value: 3.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   6 KRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWADLV 85
Cdd:PRK07313    2 KNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  86 LIAPASANLMARMAAGMADELLTTLCLATPA--PIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVGP 163
Cdd:PRK07313   82 LVAPATANTIAKLAHGIADDLVTSVALALPAttPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEGY 161

                         170
                  ....*....|.
gi 1125799677 164 GRMLDPLELVD 174
Cdd:PRK07313  162 GALADIETILE 172
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 6-168 3.25e-50

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: 166.91  E-value: 3.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   6 KRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVAYSLLDPSAEAGMGHIELAKWADLV 85
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  86 LIAPASANLMARMAAGMADELLTTLCLATPA--PIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQACGDVGP 163
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALALPPetPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160


                  ....*
gi 1125799677 164 GRMLD 168
Cdd:TIGR02113 161 GALAD 165
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 6-180 2.48e-47

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: 159.46  E-value: 2.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   6 KRILLGVSGGIAAYKSAELVRRLKDQGAEVRVVMTRSAKEFITPLTLQAVSGHPVaYSLLDPSAEAGMGHIEL---AKWA 82
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSENVD-EDLTWRELDDDILHIELasgARWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  83 DLVLIAPASANLMARMAAGMADELLT----------------TLCLATPAPIALAPAMNQQMYLNAATQANLKTLASRGi 146
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1125799677 147 llwgpdagsqacgdvGPGRMLDPLELVDRCCQQL 180
Cdd:pfam02441 159 ---------------GKGRMPEPEAIVGKVLDAL 177
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 7-169 5.38e-27

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 106.59  E-value: 5.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   7 RILLGVSGGIAAYKSAELVRRLKDQgAEVRVVMTRSAKEFITPLTL-QAVsghpVAYSLLDP-SAEAGMG----HIELAK 80
Cdd:PLN02496   21 RILLAASGSVAAIKFGNLCHCFSEW-AEVRAVVTKASLHFIDRASLpKDV----TLYTDEDEwSSWNKIGdsvlHIELRR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677  81 WADLVLIAPASANLMARMAAGMADELLTTLCLA--TPAPIALAPAMNQQMYLNAATQANLKTLASRGILLWGPDAGSQAC 158
Cdd:PLN02496   96 WADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAwdYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLAC 175

                         170
                  ....*....|.
gi 1125799677 159 GDVGPGRMLDP 169
Cdd:PLN02496  176 GDYGNGAMAEP 186
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 190-355 6.01e-18

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 82.34  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 190 KLLLTAGPTREALDPVRYISNHSSGKMGYAIARAAREAGAEVTLVSGP--VTLATPAGVTRVDVESAEQMHQAVMSRVGE 267
Cdd:PRK06732    2 KILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKtaVKPEPHPNLSIIEIENVDDLLETLEPLVKD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677 268 CDLFIGCAAVADYRP------EQVA-----SQKIKKT-------GDNDQMVVKLVKNPDIIAAVGALSDKPFTVGFAAeT 329
Cdd:PRK06732   82 HDVLIHSMAVSDYTPvymtdlEEVSasdnlNEFLTKQnteakisSASDYQVLFLKKTPKVISYVKKWNPNITLVGFKL-L 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1125799677 330 VDVEQ-----YALDKLQRKRLDMIAANDVSR 355
Cdd:PRK06732  161 VNVSKeelikVARASLIKNQADYILANDLTD 191
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
 1-141 3.12e-08

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 53.36  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   1 MRLADKRILLGVSGGIAAYKSA-ELVRRLKDQGAEVRVVMTRS----------AKEFITplTLQAVSGHPVAYSLldPSA 69
Cdd:PRK08305    1 MSLKGKRIGFGLTGSHCTYDEVmPEIEKLVDEGAEVTPIVSYTvqttdtrfgkAEEWIK--KIEEITGNKVINTI--VEA 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125799677  70 EAgmghIELAKWADLVLIAPASANLMARMAAGMADellTTLCLATPA------PIALAPAMNQQMYLNAatqANLKTL 141
Cdd:PRK08305   77 EP----LGPKKLLDCMVIAPCTGNTMAKLANAITD---SPVLMAAKAtlrnqrPVVLAISTNDALGLNA---KNLGRL 144
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
 5-108 9.79e-05

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 42.91  E-value: 9.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   5 DKRILLGV---SGGIAAYKSAELvrrLKDQGAEVRVVMTRSAKEFI---TPLTLQAVSGHpvAYSLLDPSAEAGMGHIEL 78
Cdd:PRK05920    3 MKRIVLAItgaSGAIYGVRLLEC---LLAADYEVHLVISKAAQKVLateTGLKLPAVPDL--AEAFLREQLGAAAGQLRV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1125799677  79 AKWADL-------------VLIAPASANLMARMAAGMADELLT 108
Cdd:PRK05920   78 HGKDDWgapiasgsfrtdgMVIAPCSMGTLAAIAHGLSDNLIE 120
PRK06029 PRK06029
UbiX family flavin prenyltransferase;
6-108 2.09e-03

UbiX family flavin prenyltransferase;


Pssm-ID: 235677  Cd Length: 185  Bit Score: 38.73  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799677   6 KRILLGVSGGIAAYKSAELVRRLKDQGA-EVRVVMTRSAKefitpLTLQavsgHPVAYSLLDPSAEAGMGHIELAKWA-- 82
Cdd:PRK06029    2 KRLIVGISGASGAIYGVRLLQVLRDVGEiETHLVISQAAR-----QTLA----HETDFSLRDVQALADVVHDVRDIGAsi 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125799677  83 -------DLVLIAPASANLMARMAAGMADELLT 108
Cdd:PRK06029   73 asgsfgtDGMVIAPCSMKTLAKIAHGYSDNLIT 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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