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Conserved domains on  [gi|126015091|gb|ABN70469|]
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Phosphopantothenoylcysteine decarboxylase / Phosphopantothenate-cysteine ligase [Staphylothermus marinus F1]

Protein Classification

phosphopantothenoylcysteine synthetase/decarboxylase family protein( domain architecture ID 1008203)

bifunctional phosphopantothenoylcysteine synthetase/decarboxylase (CoaBC) family protein similar to Staphylococcus epidermidis peptidyl-cysteine decarboxylase EpiD and Streptomyces olivoviridis FMN-dependent cysteine decarboxylase

CATH:  3.40.50.1950
Gene Ontology:  GO:0010181
PubMed:  10922366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaBC super family cl33883
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 13-406 2.12e-106

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


The actual alignment was detected with superfamily member COG0452:

Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 319.28  E-value: 2.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEwAIGSKPLI--EFTGRAE----HIELANW 86
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQ-ALSGNPVYtdLFDEEAEaemgHIELARW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  87 AEAFIIAPATLNTISRIAYGIADQLLhlTAiTMMGAGKKLAILPTMNMKLYNSPQYREAINKLASYNnVSIINPLI---- 162
Cdd:COG0452   81 ADLIVIAPATANTIAKLAHGIADDLL--TT-TLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERG-VHIIGPASgela 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 163 --EEGKAKFPPINDVVHCIDALVNRGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGP 240
Cdd:COG0452  157 cgDVGKGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 241 LRVEPPYNVNKYPVTTTAQMAKTIskLTNEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRS 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAV--LAAFPDADIVIMAAAVADYRPAEVADQKIKKTDD-PLTLELVKNPDILAELGAR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 321 KKPKLLII-FSAETvDNhleLVEKARNKLLEYNADLAIANNVSISGVGFSSNYIDACIVSSD-SHECMGVIRKEVLARKI 398
Cdd:COG0452  314 KKPGQFLVgFAAET-EN---LLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDgREEELPLMSKLEVARRI 389


                 ....*...
gi 126015091 399 IDIVKQNI 406
Cdd:COG0452  390 LDEIAELL 397
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 13-406 2.12e-106

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: 319.28  E-value: 2.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEwAIGSKPLI--EFTGRAE----HIELANW 86
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQ-ALSGNPVYtdLFDEEAEaemgHIELARW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  87 AEAFIIAPATLNTISRIAYGIADQLLhlTAiTMMGAGKKLAILPTMNMKLYNSPQYREAINKLASYNnVSIINPLI---- 162
Cdd:COG0452   81 ADLIVIAPATANTIAKLAHGIADDLL--TT-TLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERG-VHIIGPASgela 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 163 --EEGKAKFPPINDVVHCIDALVNRGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGP 240
Cdd:COG0452  157 cgDVGKGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 241 LRVEPPYNVNKYPVTTTAQMAKTIskLTNEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRS 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAV--LAAFPDADIVIMAAAVADYRPAEVADQKIKKTDD-PLTLELVKNPDILAELGAR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 321 KKPKLLII-FSAETvDNhleLVEKARNKLLEYNADLAIANNVSISGVGFSSNYIDACIVSSD-SHECMGVIRKEVLARKI 398
Cdd:COG0452  314 KKPGQFLVgFAAET-EN---LLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDgREEELPLMSKLEVARRI 389


                 ....*...
gi 126015091 399 IDIVKQNI 406
Cdd:COG0452  390 LDEIAELL 397
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 13-404 4.86e-105

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 315.92  E-value: 4.86e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSKPLIEF-----TGRAEHIELANWA 87
Cdd:PRK05579   4 LAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLwdpaaEAAMGHIELAKWA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  88 EAFIIAPATLNTISRIAYGIADQLLHLTAITmmgAGKKLAILPTMNMKLYNSPQYREAINKLASyNNVSIINPL------ 161
Cdd:PRK05579  84 DLVLIAPATADLIAKLAHGIADDLLTTTLLA---TTAPVLVAPAMNTQMWENPATQRNLATLRS-RGVEIIGPAsgrlac 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 162 IEEGKAKFPPINDVVHCIDALVNRgRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPL 241
Cdd:PRK05579 160 GDVGPGRMAEPEEIVAAAERALSP-KDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 242 RVEPPYNVNKYPVTTTAQMAKTISKltNEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRSK 321
Cdd:PRK05579 239 NLPTPAGVKRIDVESAQEMLDAVLA--ALPQADIFIMAAAVADYRPATVAEGKIKKGEG-ELTLELVPNPDILAEVAALK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 322 KPKLLII-FSAETVDnhleLVEKARNKLLEYNADLAIANNVSiSGVGFSSNYIDACIVSSD-SHECMGVIRKEVLARKII 399
Cdd:PRK05579 316 DKRPFVVgFAAETGD----VLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDgGEVKLPLMSKLELARRLL 390


                 ....*
gi 126015091 400 DIVKQ 404
Cdd:PRK05579 391 DEIAE 395
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 13-403 1.80e-97

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: 296.20  E-value: 1.80e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSKPLIEFTGRAEH----IELANWAE 88
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHnalhIDLAKWAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   89 AFIIAPATLNTISRIAYGIADQLLHLTAITmmgAGKKLAILPTMNMKLYNSPQYREAINKLASYNnVSIINP------LI 162
Cdd:TIGR00521  81 LILIAPATANTISKIAHGIADDLVSTTALA---ASAPIILAPAMNENMYNNPAVQENIKRLKDDG-YIFIEPrsgllaCG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  163 EEGKAKFPPINDVVHCIDALVNRGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPLR 242
Cdd:TIGR00521 157 DEGKGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  243 VEPPYNVNKYPVTTTAQMAKtisKLTNE--KQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRS 320
Cdd:TIGR00521 237 LLTPPGVKSIKVSTAEEMLE---AALNElaKDFDIFISAAAVADFKPKTVFEGKIKKQGE-ELSLKLVKNPDIIAEVRKI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  321 KKPKLLIIFSAETVDNhleLVEKARNKLLEYNADLAIANNVSiSGVGFSSNYIDACIVSSDSHECMGVIRKEVLARKIID 400
Cdd:TIGR00521 313 KKHQVIVGFKAETNDD---LIKYAKEKLKKKNLDMIVANDVS-QGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILD 388


                  ...
gi 126015091  401 IVK 403
Cdd:TIGR00521 389 EIK 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 189-372 5.03e-71

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: 221.13  E-value: 5.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  189 LEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPLRVEPPYNVNKYPVTTTAQMAKTISKLT 268
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  269 neKQYDAAIFAAAPSDYTVLSRSHKKIS-THEHVSLVVRLKQTPKTIKYVSRSKKPKLLIIFSAETVDnhleLVEKARNK 347
Cdd:pfam04127  81 --PEADIVIMAAAVADYRPAEVADGKIKkSSGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETED----LLENARAK 154

                         170       180
                  ....*....|....*....|....*
gi 126015091  348 LLEYNADLAIANNVSISGVGFSSNY 372
Cdd:pfam04127 155 LERKNLDLIVANDVSRPGAGFGSDT 179
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 13-406 2.12e-106

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: 319.28  E-value: 2.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEwAIGSKPLI--EFTGRAE----HIELANW 86
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQ-ALSGNPVYtdLFDEEAEaemgHIELARW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  87 AEAFIIAPATLNTISRIAYGIADQLLhlTAiTMMGAGKKLAILPTMNMKLYNSPQYREAINKLASYNnVSIINPLI---- 162
Cdd:COG0452   81 ADLIVIAPATANTIAKLAHGIADDLL--TT-TLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERG-VHIIGPASgela 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 163 --EEGKAKFPPINDVVHCIDALVNRGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGP 240
Cdd:COG0452  157 cgDVGKGRMAEPEEIVEAIEALLAPKKDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 241 LRVEPPYNVNKYPVTTTAQMAKTIskLTNEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRS 320
Cdd:COG0452  237 VALPTPAGVERIDVESAEEMLEAV--LAAFPDADIVIMAAAVADYRPAEVADQKIKKTDD-PLTLELVKNPDILAELGAR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 321 KKPKLLII-FSAETvDNhleLVEKARNKLLEYNADLAIANNVSISGVGFSSNYIDACIVSSD-SHECMGVIRKEVLARKI 398
Cdd:COG0452  314 KKPGQFLVgFAAET-EN---LLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDgREEELPLMSKLEVARRI 389


                 ....*...
gi 126015091 399 IDIVKQNI 406
Cdd:COG0452  390 LDEIAELL 397
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 13-404 4.86e-105

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 315.92  E-value: 4.86e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSKPLIEF-----TGRAEHIELANWA 87
Cdd:PRK05579   4 LAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLwdpaaEAAMGHIELAKWA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  88 EAFIIAPATLNTISRIAYGIADQLLHLTAITmmgAGKKLAILPTMNMKLYNSPQYREAINKLASyNNVSIINPL------ 161
Cdd:PRK05579  84 DLVLIAPATADLIAKLAHGIADDLLTTTLLA---TTAPVLVAPAMNTQMWENPATQRNLATLRS-RGVEIIGPAsgrlac 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 162 IEEGKAKFPPINDVVHCIDALVNRgRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPL 241
Cdd:PRK05579 160 GDVGPGRMAEPEEIVAAAERALSP-KDLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 242 RVEPPYNVNKYPVTTTAQMAKTISKltNEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRSK 321
Cdd:PRK05579 239 NLPTPAGVKRIDVESAQEMLDAVLA--ALPQADIFIMAAAVADYRPATVAEGKIKKGEG-ELTLELVPNPDILAEVAALK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 322 KPKLLII-FSAETVDnhleLVEKARNKLLEYNADLAIANNVSiSGVGFSSNYIDACIVSSD-SHECMGVIRKEVLARKII 399
Cdd:PRK05579 316 DKRPFVVgFAAETGD----VLEYARAKLKRKGLDLIVANDVS-AGGGFGSDDNEVTLIWSDgGEVKLPLMSKLELARRLL 390


                 ....*
gi 126015091 400 DIVKQ 404
Cdd:PRK05579 391 DEIAE 395
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 13-403 1.80e-97

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: 296.20  E-value: 1.80e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   13 LRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSKPLIEFTGRAEH----IELANWAE 88
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHnalhIDLAKWAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   89 AFIIAPATLNTISRIAYGIADQLLHLTAITmmgAGKKLAILPTMNMKLYNSPQYREAINKLASYNnVSIINP------LI 162
Cdd:TIGR00521  81 LILIAPATANTISKIAHGIADDLVSTTALA---ASAPIILAPAMNENMYNNPAVQENIKRLKDDG-YIFIEPrsgllaCG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  163 EEGKAKFPPINDVVHCIDALVNRGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPLR 242
Cdd:TIGR00521 157 DEGKGRLAEPETIVKAAEREFSPKEDLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPVS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  243 VEPPYNVNKYPVTTTAQMAKtisKLTNE--KQYDAAIFAAAPSDYTVLSRSHKKISTHEHvSLVVRLKQTPKTIKYVSRS 320
Cdd:TIGR00521 237 LLTPPGVKSIKVSTAEEMLE---AALNElaKDFDIFISAAAVADFKPKTVFEGKIKKQGE-ELSLKLVKNPDIIAEVRKI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  321 KKPKLLIIFSAETVDNhleLVEKARNKLLEYNADLAIANNVSiSGVGFSSNYIDACIVSSDSHECMGVIRKEVLARKIID 400
Cdd:TIGR00521 313 KKHQVIVGFKAETNDD---LIKYAKEKLKKKNLDMIVANDVS-QGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILD 388


                  ...
gi 126015091  401 IVK 403
Cdd:TIGR00521 389 EIK 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
 189-372 5.03e-71

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: 221.13  E-value: 5.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  189 LEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPLRVEPPYNVNKYPVTTTAQMAKTISKLT 268
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPPPPGVEVVDVESAEEMLEAVLAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  269 neKQYDAAIFAAAPSDYTVLSRSHKKIS-THEHVSLVVRLKQTPKTIKYVSRSKKPKLLIIFSAETVDnhleLVEKARNK 347
Cdd:pfam04127  81 --PEADIVIMAAAVADYRPAEVADGKIKkSSGGEELTLELVKNPDILAELGKRKPGQLLVGFAAETED----LLENARAK 154

                         170       180
                  ....*....|....*....|....*
gi 126015091  348 LLEYNADLAIANNVSISGVGFSSNY 372
Cdd:pfam04127 155 LERKNLDLIVANDVSRPGAGFGSDT 179
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 5-362 7.12e-51

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 177.64  E-value: 7.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   5 PLIEEYSPLRNRRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSK-------PLIEFTgr 77
Cdd:PRK13982  60 PAAREQASLASKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRvytdlfdPESEFD-- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  78 AEHIELANWAEAFIIAPATLNTISRIAYGIADQLLhlTAItMMGAGKKLAILPTMNMKLYNSPQYREAINKLASyNNVSI 157
Cdd:PRK13982 138 AGHIRLARDCDLIVVAPATADLMAKMANGLADDLA--SAI-LLAANRPILLAPAMNPLMWNNPATRRNVAQLKR-DGVHM 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 158 INPLI-------EEGKAKFPPINDVVHCIDALVN--RGRDLEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAV 228
Cdd:PRK13982 214 IGPNAgemaergEAGVGRMAEPLEIAAAAEALLRppQPKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAA 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 229 CRGAVVDLVHGPLRVEPPYNVNKYPVTTTAQMAKTISKltnEKQYDAAIFAAAPSDYTVLSRSHKKISTHEHVSLVVRLK 308
Cdd:PRK13982 294 AAGAEVTLISGPVDLADPQGVKVIHVESARQMLAAVEA---ALPADIAIFAAAVADWRVATEGGQKLKKGAAGPPPLQLV 370

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 126015091 309 QTPKTIKYVS--RSKKPKLLIIFSAETVDnhleLVEKARNKLLEYNADLAIANNVS 362
Cdd:PRK13982 371 ENPDILATISklAENRPPLVIGFAAETEH----LIDNARAKLARKGCDWIVANDVS 422
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 16-179 2.28e-38

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: 136.35  E-value: 2.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   16 RRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEWAIGSK----PLIEFTGRAEHIEL---ANWAE 88
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSENVdedlTWRELDDDILHIELasgARWAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091   89 AFIIAPATLNTISRIAYGIADQLL-------------HLTAITMMGAGKKLAILPTMNMKLYNSPQYREAINKLASYnnv 155
Cdd:pfam02441  81 AMVIAPASANTLAKIANGIADNLLtraadvalkerrpHLENMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKAD--- 157

                         170       180
                  ....*....|....*....|....
gi 126015091  156 siinplieEGKAKFPPINDVVHCI 179
Cdd:pfam02441 158 --------GGKGRMPEPEAIVGKV 173
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 16-185 1.60e-26

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 104.64  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  16 RRILFGLTASSSIYRSIDLIRKLIRLGAEIKVVMTRESLSLITPDLVEwAIGSKPLI------EFTGRAEHIELANWAEA 89
Cdd:PRK07313   2 KNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQ-VLSKNPVHldvmdeHDPKLMNHIELAKRADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  90 FIIAPATLNTISRIAYGIADQLLHLTAITMMGAGKKLaILPTMNMKLYNSPQYREAINKLASYnNVSIINPLI------E 163
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALALPATTPKL-IAPAMNTKMYENPATQRNLKTLKED-GVQEIEPKEgllacgD 158

                        170       180
                 ....*....|....*....|..
gi 126015091 164 EGKAKFPPINDVVHCIDALVNR 185
Cdd:PRK07313 159 EGYGALADIETILETIENTLKE 180
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
 195-359 8.31e-21

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 90.43  E-value: 8.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 195 LITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGP--LRVEPPYNVNKYPVTTTAQMAKTISKLTneKQ 272
Cdd:PRK06732   4 LITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTKtaVKPEPHPNLSIIEIENVDDLLETLEPLV--KD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 273 YDAAIFAAAPSDYTV------------------LSRSHK--KISTHEHVsLVVRLKQTPKTIKYVsRSKKP-------KL 325
Cdd:PRK06732  82 HDVLIHSMAVSDYTPvymtdleevsasdnlnefLTKQNTeaKISSASDY-QVLFLKKTPKVISYV-KKWNPnitlvgfKL 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126015091 326 LIIFSAEtvdnhlELVEKARNKLLEYNADLAIAN 359
Cdd:PRK06732 160 LVNVSKE------ELIKVARASLIKNQADYILAN 187
PRK09620 PRK09620
hypothetical protein; Provisional
 189-360 2.28e-17

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 80.71  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 189 LEGKYMLITAGPTIEYIDPVRIITNNSSGLMGVLLAREAVCRGAVVDLVHGPLrVEPPYNVNK----YPVTTTAQMAKTI 264
Cdd:PRK09620   1 MKGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGYF-AEKPNDINNqlelHPFEGIIDLQDKM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091 265 SKLTNEKQYDAAIFAAAPSDYTV---------LSRSHKKISTHEhvSLVVRLKQTPKTIKYVSRSKKPKLLIIFSAETVD 335
Cdd:PRK09620  80 KSIITHEKVDAVIMAAAGSDWVVdkicdqegnVLDMNGKISSDI--APIIHFQKAPKVLKQIKQWDPETVLVGFKLESDV 157

                        170       180
                 ....*....|....*....|....*
gi 126015091 336 NHLELVEKARNKLLEYNADLAIANN 360
Cdd:PRK09620 158 NEEELFERAKNRMEEAKASVMIANS 182
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 43-140 1.05e-09

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 58.06  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  43 AEIKVVMTRESLSLIT-----------PDLVEWA----IGSKPLieftgraeHIELANWAEAFIIAPATLNTISRIAYGI 107
Cdd:PLN02496  46 AEVRAVVTKASLHFIDraslpkdvtlyTDEDEWSswnkIGDSVL--------HIELRRWADVMVIAPLSANTLGKIAGGL 117

                         90       100       110
                 ....*....|....*....|....*....|...
gi 126015091 108 ADQLLhLTAITMMGAGKKLAILPTMNMKLYNSP 140
Cdd:PLN02496 118 CDNLL-TCIVRAWDYSKPLFVAPAMNTFMWNNP 149
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
 13-109 4.77e-06

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 46.81  E-value: 4.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126015091  13 LRNRRILFGLTASSSIY-RSIDLIRKLIRLGAEIKVVMTRESLSLITP--DLVEW-----AIGSKPLIEFTGRAEHIELA 84
Cdd:PRK08305   3 LKGKRIGFGLTGSHCTYdEVMPEIEKLVDEGAEVTPIVSYTVQTTDTRfgKAEEWikkieEITGNKVINTIVEAEPLGPK 82

                         90       100
                 ....*....|....*....|....*
gi 126015091  85 NWAEAFIIAPATLNTISRIAYGIAD 109
Cdd:PRK08305  83 KLLDCMVIAPCTGNTMAKLANAITD 107
AfpA COG1036
Archaeal flavoprotein [Energy production and conversion];
88-112 9.99e-05

Archaeal flavoprotein [Energy production and conversion];


Pssm-ID: 440659 [Multi-domain]  Cd Length: 174  Bit Score: 42.50  E-value: 9.99e-05
                         10        20
                 ....*....|....*....|....*
gi 126015091  88 EAFIIAPATLNTISRIAYGIADQLL 112
Cdd:COG1036   81 DTLVIAPATSNTVAKIVLGIADTLV 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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