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Conserved domains on  [gi|517168337|ref|WP_018357155|]
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bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC [Rodentibacter pneumotropicus]

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]; ...
 3-398 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: 666.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWA 82
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 163 AGRMSEPTEIFAALSDFFIQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSA 242
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 243 PNNVTRIDVVSAKEMWQAALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTECRPFTV 322
Cdd:COG0452  242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFLV 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517168337 323 GFAAETQNLAKYAKEKLKRKSLDMICANDVS-GGQVFNADDNALQLFWKEGS-KTLPLKSKTELAADLVNEIVEQYQK 398
Cdd:COG0452  322 GFAAETENLLENARAKLARKNLDLIVANDVSdAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEIAELLAA 399
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 3-398 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: 666.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWA 82
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 163 AGRMSEPTEIFAALSDFFIQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSA 242
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 243 PNNVTRIDVVSAKEMWQAALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTECRPFTV 322
Cdd:COG0452  242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFLV 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517168337 323 GFAAETQNLAKYAKEKLKRKSLDMICANDVS-GGQVFNADDNALQLFWKEGS-KTLPLKSKTELAADLVNEIVEQYQK 398
Cdd:COG0452  322 GFAAETENLLENARAKLARKNLDLIVANDVSdAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-398 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 647.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   1 MKLSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAK 80
Cdd:PRK05579   2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  81 WADAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGD 160
Cdd:PRK05579  82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 161 VGAGRMSEPTEIFAALSDFFiQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSL 240
Cdd:PRK05579 162 VGPGRMAEPEEIVAAAERAL-SPKDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 241 SAPNNVTRIDVVSAKEMWQAALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTECRPF 320
Cdd:PRK05579 241 PTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRPF 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517168337 321 TVGFAAETQNLAKYAKEKLKRKSLDMICANDVSGGQVFNADDNALQLFWKEGSKT-LPLKSKTELAADLVNEIVEQYQK 398
Cdd:PRK05579 321 VVGFAAETGDVLEYARAKLKRKGLDLIVANDVSAGGGFGSDDNEVTLIWSDGGEVkLPLMSKLELARRLLDEIAERLLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-393 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: 545.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337    3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMgHIELAKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  163 AGRMSEPTEIFAALSDFFIQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSA 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  243 PNNVTRIDVVSAKEMWQAALENAVKNQ-IFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTEcRPFT 321
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLEAALNELAKDFdIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKK-HQVI 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517168337  322 VGFAAETQN-LAKYAKEKLKRKSLDMICANDVSGGQVFNADDNALQLFWKEGSKTLPLKSKTELAADLVNEIV 393
Cdd:TIGR00521 319 VGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEIK 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-365 9.43e-99

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: 291.62  E-value: 9.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  186 LQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSAPNNVTRIDVVSAKEMWQAALENA 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  266 VKNQIFIGCAAVADYRVADISDQKIKKSA--DEMVLKLVKNPDIIADVGHLTEcRPFTVGFAAETQNLAKYAKEKLKRKS 343
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSggEELTLELVKNPDILAELGKRKP-GQLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|...
gi 517168337  344 LDMICANDVS-GGQVFNADDNAL 365
Cdd:pfam04127 160 LDLIVANDVSrPGAGFGSDTNEV 182
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 3-398 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: 666.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWA 82
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 163 AGRMSEPTEIFAALSDFFIQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSA 242
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 243 PNNVTRIDVVSAKEMWQAALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTECRPFTV 322
Cdd:COG0452  242 PAGVERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKKTDDPLTLELVKNPDILAELGARKKPGQFLV 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517168337 323 GFAAETQNLAKYAKEKLKRKSLDMICANDVS-GGQVFNADDNALQLFWKEGS-KTLPLKSKTELAADLVNEIVEQYQK 398
Cdd:COG0452  322 GFAAETENLLENARAKLARKNLDLIVANDVSdAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEIAELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 1-398 0e+00

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 647.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   1 MKLSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAK 80
Cdd:PRK05579   2 RMLAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  81 WADAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGD 160
Cdd:PRK05579  82 WADLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 161 VGAGRMSEPTEIFAALSDFFiQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSL 240
Cdd:PRK05579 162 VGPGRMAEPEEIVAAAERAL-SPKDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 241 SAPNNVTRIDVVSAKEMWQAALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTECRPF 320
Cdd:PRK05579 241 PTPAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGEGELTLELVPNPDILAEVAALKDKRPF 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517168337 321 TVGFAAETQNLAKYAKEKLKRKSLDMICANDVSGGQVFNADDNALQLFWKEGSKT-LPLKSKTELAADLVNEIVEQYQK 398
Cdd:PRK05579 321 VVGFAAETGDVLEYARAKLKRKGLDLIVANDVSAGGGFGSDDNEVTLIWSDGGEVkLPLMSKLELARRLLDEIAERLLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 3-393 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: 545.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337    3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMgHIELAKWA 82
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHNAL-HIDLAKWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  163 AGRMSEPTEIFAALSDFFIQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSA 242
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVSLLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  243 PNNVTRIDVVSAKEMWQAALENAVKNQ-IFIGCAAVADYRVADISDQKIKKSADEMVLKLVKNPDIIADVGHLTEcRPFT 321
Cdd:TIGR00521 240 PPGVKSIKVSTAEEMLEAALNELAKDFdIFISAAAVADFKPKTVFEGKIKKQGEELSLKLVKNPDIIAEVRKIKK-HQVI 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517168337  322 VGFAAETQN-LAKYAKEKLKRKSLDMICANDVSGGQVFNADDNALQLFWKEGSKTLPLKSKTELAADLVNEIV 393
Cdd:TIGR00521 319 VGFKAETNDdLIKYAKEKLKKKNLDMIVANDVSQGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEIK 391
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 3-394 2.91e-139

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 405.68  E-value: 2.91e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   3 LSGKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWA 82
Cdd:PRK13982  68 LASKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDC 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  83 DAIVIAPASADFIARFTVGMANDLLSTICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQA-CGDV 161
Cdd:PRK13982 148 DLIVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEA 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 162 GAGRMSEPTEIFAALSDFF--IQDQDLQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVS 239
Cdd:PRK13982 228 GVGRMAEPLEIAAAAEALLrpPQPKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISGPVD 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 240 LSAPNNVTRIDVVSAKEMWQaALENAVKNQIFIGCAAVADYRVADISDQKIKKSADEM-VLKLVKNPDIIADVGHLTECR 318
Cdd:PRK13982 308 LADPQGVKVIHVESARQMLA-AVEAALPADIAIFAAAVADWRVATEGGQKLKKGAAGPpPLQLVENPDILATISKLAENR 386

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 319 P-FTVGFAAETQNLAKYAKEKLKRKSLDMICANDVS-GGQVFNADDNALQLFWKEGSKT----LPLKSKTELAADLVNEI 392
Cdd:PRK13982 387 PpLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSpATGVMGGDRNTVHLLSRDGDAEkvesWPVMTKDEVATALVARI 466


                 ..
gi 517168337 393 VE 394
Cdd:PRK13982 467 AS 468
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 186-365 9.43e-99

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: 291.62  E-value: 9.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  186 LQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSLSAPNNVTRIDVVSAKEMWQAALENA 265
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  266 VKNQIFIGCAAVADYRVADISDQKIKKSA--DEMVLKLVKNPDIIADVGHLTEcRPFTVGFAAETQNLAKYAKEKLKRKS 343
Cdd:pfam04127  81 PEADIVIMAAAVADYRPAEVADGKIKKSSggEELTLELVKNPDILAELGKRKP-GQLLVGFAAETEDLLENARAKLERKN 159

                         170       180
                  ....*....|....*....|...
gi 517168337  344 LDMICANDVS-GGQVFNADDNAL 365
Cdd:pfam04127 160 LDLIVANDVSrPGAGFGSDTNEV 182
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 5-180 1.40e-62

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 199.02  E-value: 1.40e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   5 GKRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWADA 84
Cdd:PRK07313   1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  85 IVIAPASADFIARFTVGMANDLLSTICLA--THAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVG 162
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALAlpATTPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160

                        170
                 ....*....|....*...
gi 517168337 163 AGRMSEPTEIFAALSDFF 180
Cdd:PRK07313 161 YGALADIETILETIENTL 178
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 6-176 1.17e-42

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: 147.27  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337    6 KRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNAVAQSLLDPQAELAMGHIELAKWADAI 85
Cdd:TIGR02113   1 KKILLAVTGSIAAYKAADLTSQLTKLGYDVTVLMTQAATQFITPLTLQVLSKNPVHLDVMDEHDPKVINHIELAKKADLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   86 VIAPASADFIARFTVGMANDLLSTICLA--THAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGPNNGFQACGDVGA 163
Cdd:TIGR02113  81 LVAPASANTIAHLAHGFADNIVTSVALAlpPETPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGR 160

                         170
                  ....*....|...
gi 517168337  164 GRMSEPTEIFAAL 176
Cdd:TIGR02113 161 GALADLDDILQTI 173
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 6-180 6.75e-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: 140.20  E-value: 6.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337    6 KRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFVTPLTLQAISGNaVAQSLLDPQAELAMGHIEL---AKWA 82
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSEN-VDEDLTWRELDDDILHIELasgARWA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   83 DAIVIAPASADFIARFTVGMANDLLS----------------TICLATHAPIFLAPAMNQQMFRQQITQQNLTALQARGi 146
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 517168337  147 qligpnngfqacgdvGAGRMSEPTEIFAALSDFF 180
Cdd:pfam02441 159 ---------------GKGRMPEPEAIVGKVLDAL 177
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 7-180 2.10e-25

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 102.36  E-value: 2.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   7 RIVVGITGGIAAykaIEFIRLLR--KSDAEVRVVLTPSAAEFVTPLTL-----------QAISGNAVAQSLLdpqaelam 73
Cdd:PLN02496  21 RILLAASGSVAA---IKFGNLCHcfSEWAEVRAVVTKASLHFIDRASLpkdvtlytdedEWSSWNKIGDSVL-------- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337  74 gHIELAKWADAIVIAPASADFIARFTVGMANDLLSTICLA--THAPIFLAPAMNQQMFRQQITQQNLTALQARGIQLIGP 151
Cdd:PLN02496  90 -HIELRRWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAwdYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPP 168

                        170       180
                 ....*....|....*....|....*....
gi 517168337 152 NNGFQACGDVGAGRMSEPTEIFAALSDFF 180
Cdd:PLN02496 169 VTKRLACGDYGNGAMAEPSLIYSTVRLFL 197
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 190-398 4.55e-25

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 101.99  E-value: 4.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 190 KVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSL---SAPnNVTRIDVVSAKEMWQaALENAV 266
Cdd:PRK06732   2 KILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKTAVkpePHP-NLSIIEIENVDDLLE-TLEPLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 267 KN-QIFIGCAAVADYR---------VADISD-----------QKIKKSADEMVLKLVKNPDIIADVghlTECRPFT--VG 323
Cdd:PRK06732  80 KDhDVLIHSMAVSDYTpvymtdleeVSASDNlnefltkqnteAKISSASDYQVLFLKKTPKVISYV---KKWNPNItlVG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517168337 324 FA----AETQNLAKYAKEKLKRKSLDMICANDVSggQVFNADDNALQLFWKEgskTLPLKSKTELaADLVNEIVEQYQK 398
Cdd:PRK06732 157 FKllvnVSKEELIKVARASLIKNQADYILANDLT--DISADQHKALLVSKNE---VYTAQTKEEI-ADLLLERIEKYDS 229
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
 6-108 2.11e-07

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 51.00  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   6 KRIVVGITGGIAAYKAIEFIRLLRKSDAEVRVVLTPSAAEFV---TPLTLQAISgnAVAQSLLDPQAELAMGHIELAKW- 81
Cdd:PRK05920   4 KRIVLAITGASGAIYGVRLLECLLAADYEVHLVISKAAQKVLateTGLKLPAVP--DLAEAFLREQLGAAAGQLRVHGKd 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517168337  82 ------------ADAIVIAPASADFIARFTVGMANDLLS 108
Cdd:PRK05920  82 dwgapiasgsfrTDGMVIAPCSMGTLAAIAHGLSDNLIE 120
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
 1-102 4.98e-06

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 46.81  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   1 MKLSGKRIVVGITGGIAAY-KAIEFIRLLRKSDAEVRVVLTPS----------AAEFVTplTLQAISGNAVAQSLldPQA 69
Cdd:PRK08305   1 MSLKGKRIGFGLTGSHCTYdEVMPEIEKLVDEGAEVTPIVSYTvqttdtrfgkAEEWIK--KIEEITGNKVINTI--VEA 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 517168337  70 ElamgHIELAKWADAIVIAPASADFIARFTVGM 102
Cdd:PRK08305  77 E----PLGPKKLLDCMVIAPCTGNTMAKLANAI 105
PRK09620 PRK09620
hypothetical protein; Provisional
 186-350 9.70e-05

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 43.34  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 186 LQGVKVVITAGPTREAVDPVRYISNHSSGKMGFAIAENFAKRGASVTLIAGPVSlSAPNNVTRI-------DVVSAKEMW 258
Cdd:PRK09620   1 MKGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGYFA-EKPNDINNQlelhpfeGIIDLQDKM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337 259 QAALENAvKNQIFIGCAAVADYRVADISDQK-------IKKSADEM-VLKLVKNPDIIadvGHLTECRPFT--VGFAAET 328
Cdd:PRK09620  80 KSIITHE-KVDAVIMAAAGSDWVVDKICDQEgnvldmnGKISSDIApIIHFQKAPKVL---KQIKQWDPETvlVGFKLES 155

                        170       180
                 ....*....|....*....|....*.
gi 517168337 329 QN----LAKYAKEKLKRKSLDMICAN 350
Cdd:PRK09620 156 DVneeeLFERAKNRMEEAKASVMIAN 181
PRK06029 PRK06029
UbiX family flavin prenyltransferase;
6-108 1.56e-03

UbiX family flavin prenyltransferase;


Pssm-ID: 235677  Cd Length: 185  Bit Score: 39.11  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517168337   6 KRIVVGITGGIAAYKAIEFIRLLRK-SDAEVRVVLTPSA---AEFVTPLTLQAISGNA-VAQSLLDPQAELAMGHIElak 80
Cdd:PRK06029   2 KRLIVGISGASGAIYGVRLLQVLRDvGEIETHLVISQAArqtLAHETDFSLRDVQALAdVVHDVRDIGASIASGSFG--- 78

                         90       100
                 ....*....|....*....|....*...
gi 517168337  81 wADAIVIAPASADFIARFTVGMANDLLS 108
Cdd:PRK06029  79 -TDGMVIAPCSMKTLAKIAHGYSDNLIT 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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