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Conserved domains on  [gi|492400708|ref|WP_005832361|]
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MULTISPECIES: bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC [Bacteroides]

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

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]; ...
5-408 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: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 165 KGRMEEPENIIRHLEMYFAAKdGDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQG 244
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 245 TyfPMH-QYHAVESAQEMFEAASAAFVHADAAILTAAVADYTPEQVADEKIKReKTGEMSLNLKPTRDIAAFLGNLKNDt 323
Cdd:COG0452  241 T--PAGvERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKK-TDDPLTLELVKNPDILAELGARKKP- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 324 ehqRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLNDKGAGFRCDTNKISIIDHQGK-TDYPLKSKAEVAADIVDRL 402
Cdd:COG0452  317 ---GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEI 393

                 ....*.
gi 492400708 403 VKDLNS 408
Cdd:COG0452  394 AELLAA 399
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
5-408 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: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 165 KGRMEEPENIIRHLEMYFAAKdGDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQG 244
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 245 TyfPMH-QYHAVESAQEMFEAASAAFVHADAAILTAAVADYTPEQVADEKIKReKTGEMSLNLKPTRDIAAFLGNLKNDt 323
Cdd:COG0452  241 T--PAGvERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKK-TDDPLTLELVKNPDILAELGARKKP- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 324 ehqRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLNDKGAGFRCDTNKISIIDHQGK-TDYPLKSKAEVAADIVDRL 402
Cdd:COG0452  317 ---GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEI 393

                 ....*.
gi 492400708 403 VKDLNS 408
Cdd:COG0452  394 AELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
5-408 1.40e-178

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 503.13  E-value: 1.40e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:PRK05579   4 LAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:PRK05579  84 DLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 165 KGRMEEPENIIRHLEMYFAAKdgDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQG 244
Cdd:PRK05579 164 PGRMAEPEEIVAAAERALSPK--DLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNLP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 245 TyFPMHQYHAVESAQEMFEAASAAFVHADAAILTAAVADYTPEQVADEKIKREKtGEMSLNLKPTRDIAAFLGNLKNdte 324
Cdd:PRK05579 242 T-PAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGE-GELTLELVPNPDILAEVAALKD--- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 325 hQRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLnDKGAGFRCDTNKISIIDHQG-KTDYPLKSKAEVAADIVDRLV 403
Cdd:PRK05579 317 -KRPFVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGgEVKLPLMSKLELARRLLDEIA 394

                 ....*
gi 492400708 404 KDLNS 408
Cdd:PRK05579 395 ERLLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
5-403 2.30e-138

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: 400.59  E-value: 2.30e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708    5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTwNSHVDLGLWA 84
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHN-ALHIDLAKWA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  165 KGRMEEPENIIRHLEMYFAAKDgDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVqQG 244
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKE-DLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPV-SL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  245 TYFPMHQYHAVESAQEMFEAASAAFVH-ADAAILTAAVADYTPEQVADEKIKReKTGEMSLNLKPTRDIAAFLGNLKNDt 323
Cdd:TIGR00521 238 LTPPGVKSIKVSTAEEMLEAALNELAKdFDIFISAAAVADFKPKTVFEGKIKK-QGEELSLKLVKNPDIIAEVRKIKKH- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  324 ehqrRLLVGFALETHNEQMN-AEDKLNRKNLDFIVLNSLnDKGAGFRCDTNKISIIDHQGKTDYPLKSKAEVAADIVDRL 402
Cdd:TIGR00521 316 ----QVIVGFKAETNDDLIKyAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEI 390

                  .
gi 492400708  403 V 403
Cdd:TIGR00521 391 K 391
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
189-375 2.18e-82

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: 250.02  E-value: 2.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  189 LVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQGTyfPMH-QYHAVESAQEMFEAASA 267
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPP--PPGvEVVDVESAEEMLEAVLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  268 AFVHADAAILTAAVADYTPEQVADEKIKREKTGE-MSLNLKPTRDIAAFLGNLKNdtehqRRLLVGFALETHNEQMNAED 346
Cdd:pfam04127  79 AFPEADIVIMAAAVADYRPAEVADGKIKKSSGGEeLTLELVKNPDILAELGKRKP-----GQLLVGFAAETEDLLENARA 153
                         170       180
                  ....*....|....*....|....*....
gi 492400708  347 KLNRKNLDFIVLNSLNDKGAGFRCDTNKI 375
Cdd:pfam04127 154 KLERKNLDLIVANDVSRPGAGFGSDTNEV 182
 
Name Accession Description Interval E-value
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
5-408 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: 603.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:COG0452    2 LAGKRILLGVTGGIAAYKAAELVRLLRKAGAEVRVVMTEAATEFVTPLTFQALSGNPVYTDLFDEEAEAEMGHIELARWA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:COG0452   82 DLIVIAPATANTIAKLAHGIADDLLTTTLLATTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 165 KGRMEEPENIIRHLEMYFAAKdGDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQG 244
Cdd:COG0452  162 KGRMAEPEEIVEAIEALLAPK-KDLAGKKVLITAGPTREPIDPVRFISNRSSGKMGYALAEAAAARGAEVTLVSGPVALP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 245 TyfPMH-QYHAVESAQEMFEAASAAFVHADAAILTAAVADYTPEQVADEKIKReKTGEMSLNLKPTRDIAAFLGNLKNDt 323
Cdd:COG0452  241 T--PAGvERIDVESAEEMLEAVLAAFPDADIVIMAAAVADYRPAEVADQKIKK-TDDPLTLELVKNPDILAELGARKKP- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 324 ehqRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLNDKGAGFRCDTNKISIIDHQGK-TDYPLKSKAEVAADIVDRL 402
Cdd:COG0452  317 ---GQFLVGFAAETENLLENARAKLARKNLDLIVANDVSDAGAGFGSDTNAVTLLDKDGReEELPLMSKLEVARRILDEI 393

                 ....*.
gi 492400708 403 VKDLNS 408
Cdd:COG0452  394 AELLAA 399
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
5-408 1.40e-178

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 503.13  E-value: 1.40e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:PRK05579   4 LAGKRIVLGVSGGIAAYKALELVRRLRKAGADVRVVMTEAAKKFVTPLTFQALSGNPVSTDLWDPAAEAAMGHIELAKWA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:PRK05579  84 DLVLIAPATADLIAKLAHGIADDLLTTTLLATTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 165 KGRMEEPENIIRHLEMYFAAKdgDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQG 244
Cdd:PRK05579 164 PGRMAEPEEIVAAAERALSPK--DLAGKRVLITAGPTREPIDPVRYITNRSSGKMGYALARAAARRGADVTLVSGPVNLP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 245 TyFPMHQYHAVESAQEMFEAASAAFVHADAAILTAAVADYTPEQVADEKIKREKtGEMSLNLKPTRDIAAFLGNLKNdte 324
Cdd:PRK05579 242 T-PAGVKRIDVESAQEMLDAVLAALPQADIFIMAAAVADYRPATVAEGKIKKGE-GELTLELVPNPDILAEVAALKD--- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 325 hQRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLnDKGAGFRCDTNKISIIDHQG-KTDYPLKSKAEVAADIVDRLV 403
Cdd:PRK05579 317 -KRPFVVGFAAETGDVLEYARAKLKRKGLDLIVANDV-SAGGGFGSDDNEVTLIWSDGgEVKLPLMSKLELARRLLDEIA 394

                 ....*
gi 492400708 404 KDLNS 408
Cdd:PRK05579 395 ERLLE 399
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
5-403 2.30e-138

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: 400.59  E-value: 2.30e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708    5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTwNSHVDLGLWA 84
Cdd:TIGR00521   1 LENKKILLGVTGGIAAYKTVELVRELVRQGAEVKVIMTEAAKKFITPLTLEALSGHKVVTELWGPIEHN-ALHIDLAKWA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:TIGR00521  80 DLILIAPATANTISKIAHGIADDLVSTTALAASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  165 KGRMEEPENIIRHLEMYFAAKDgDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVqQG 244
Cdd:TIGR00521 160 KGRLAEPETIVKAAEREFSPKE-DLEGKRVLITAGPTREPIDPVRFISNLSSGKMGLALAEAAYKRGADVTLITGPV-SL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  245 TYFPMHQYHAVESAQEMFEAASAAFVH-ADAAILTAAVADYTPEQVADEKIKReKTGEMSLNLKPTRDIAAFLGNLKNDt 323
Cdd:TIGR00521 238 LTPPGVKSIKVSTAEEMLEAALNELAKdFDIFISAAAVADFKPKTVFEGKIKK-QGEELSLKLVKNPDIIAEVRKIKKH- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  324 ehqrRLLVGFALETHNEQMN-AEDKLNRKNLDFIVLNSLnDKGAGFRCDTNKISIIDHQGKTDYPLKSKAEVAADIVDRL 402
Cdd:TIGR00521 316 ----QVIVGFKAETNDDLIKyAKEKLKKKNLDMIVANDV-SQGRGFGSDENEVYIFSKHGHKELPLMSKLEVAERILDEI 390

                  .
gi 492400708  403 V 403
Cdd:TIGR00521 391 K 391
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
5-409 1.91e-97

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 298.98  E-value: 1.91e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWA 84
Cdd:PRK13982  68 LASKRVTLIIGGGIAAYKALDLIRRLKERGAHVRCVLTKAAQQFVTPLTASALSGQRVYTDLFDPESEFDAGHIRLARDC 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  85 DAMLIAPATASTIGKMANGVADNMLITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELA-SHLV 163
Cdd:PRK13982 148 DLIVVAPATADLMAKMANGLADDLASAILLAANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIGPNAGEMAeRGEA 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 164 GKGRMEEPENIIRHLE-MYFAAKDGDLVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQ 242
Cdd:PRK13982 228 GVGRMAEPLEIAAAAEaLLRPPQPKPLAGRRVLITAGPTHEPIDPVRYIANRSSGKQGFAIAAAAAAAGAEVTLISGPVD 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 243 QGTYFPMHQYHaVESAQEMFEAASAAfVHADAAILTAAVADYTPEQVADEKIKREKTGEMSLNLKPTRDIAAFLGNLknd 322
Cdd:PRK13982 308 LADPQGVKVIH-VESARQMLAAVEAA-LPADIAIFAAAVADWRVATEGGQKLKKGAAGPPPLQLVENPDILATISKL--- 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 323 TEHQRRLLVGFALETHNEQMNAEDKLNRKNLDFIVLNSLNDKGAGFRCDTNKISII----DHQGKTDYPLKSKAEVAADI 398
Cdd:PRK13982 383 AENRPPLVIGFAAETEHLIDNARAKLARKGCDWIVANDVSPATGVMGGDRNTVHLLsrdgDAEKVESWPVMTKDEVATAL 462
                        410
                 ....*....|.
gi 492400708 399 VDRLVKDLNSK 409
Cdd:PRK13982 463 VARIASTFTTP 473
DFP pfam04127
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
189-375 2.18e-82

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: 250.02  E-value: 2.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  189 LVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAGPVQQGTyfPMH-QYHAVESAQEMFEAASA 267
Cdd:pfam04127   1 LAGKRVLVTAGPTREPIDPVRFISNRSSGKMGYALARAAAARGAEVTLVSGPTSLPP--PPGvEVVDVESAEEMLEAVLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  268 AFVHADAAILTAAVADYTPEQVADEKIKREKTGE-MSLNLKPTRDIAAFLGNLKNdtehqRRLLVGFALETHNEQMNAED 346
Cdd:pfam04127  79 AFPEADIVIMAAAVADYRPAEVADGKIKKSSGGEeLTLELVKNPDILAELGKRKP-----GQLLVGFAAETEDLLENARA 153
                         170       180
                  ....*....|....*....|....*....
gi 492400708  347 KLNRKNLDFIVLNSLNDKGAGFRCDTNKI 375
Cdd:pfam04127 154 KLERKNLDLIVANDVSRPGAGFGSDTNEV 182
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
7-185 7.32e-65

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 205.18  E-value: 7.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   7 GKKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWNSHVDLGLWADA 86
Cdd:PRK07313   1 MKNILLAVSGSIAAYKAADLTSQLTKRGYQVTVLMTKAATKFITPLTLQVLSKNPVHLDVMDEHDPKLMNHIELAKRADL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  87 MLIAPATASTIGKMANGVADNMLITTYLSAKA--PVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGELASHLVG 164
Cdd:PRK07313  81 FLVAPATANTIAKLAHGIADDLVTSVALALPAttPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEG 160
                        170       180
                 ....*....|....*....|.
gi 492400708 165 KGRMEEPENIIRHLEMYFAAK 185
Cdd:PRK07313 161 YGALADIETILETIENTLKEK 181
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
8-175 2.23e-44

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: 152.14  E-value: 2.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708    8 KKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFITPITLSALTSKPVISEFFAQRDGTWnSHVDLGL---WA 84
Cdd:pfam02441   1 KRILVGITGSSAAIKALRLLEELKKEGAEVRVIMTKAAKKVITPETLAALSENVDEDLTWRELDDDI-LHIELASgarWA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   85 DAMLIAPATASTIGKMANGVADNMLI----------------TTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGn 148
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLLTraadvalkerrphlenMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG- 158
                         170       180
                  ....*....|....*....|....*..
gi 492400708  149 hiiepatgelashlvGKGRMEEPENII 175
Cdd:pfam02441 159 ---------------GKGRMPEPEAIV 170
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
9-185 1.18e-23

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 97.74  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   9 KIVLGITGSIAAYKACYIIRGLiKRGAEVQVVITPAGKEFITPITLsaltskPVISEFFAQRD--GTWNS------HVDL 80
Cdd:PLN02496  21 RILLAASGSVAAIKFGNLCHCF-SEWAEVRAVVTKASLHFIDRASL------PKDVTLYTDEDewSSWNKigdsvlHIEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708  81 GLWADAMLIAPATASTIGKMANGVADNML--ITTYLSAKAPVFVAPAMDLDMYAHPSTQKNLDTLRSYGNHIIEPATGEL 158
Cdd:PLN02496  94 RRWADVMVIAPLSANTLGKIAGGLCDNLLtcIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRL 173
                        170       180
                 ....*....|....*....|....*..
gi 492400708 159 ASHLVGKGRMEEPENIIRHLEMYFAAK 185
Cdd:PLN02496 174 ACGDYGNGAMAEPSLIYSTVRLFLESR 200
PRK06732 PRK06732
phosphopantothenate--cysteine ligase; Validated
194-405 8.95e-13

phosphopantothenate--cysteine ligase; Validated


Pssm-ID: 235856 [Multi-domain]  Cd Length: 229  Bit Score: 67.32  E-value: 8.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 194 VMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAG-----PVQQgtyfPMHQYHAVESAQEMFEAASAA 268
Cdd:PRK06732   3 ILITSGGTTEPIDSVRGITNHSTGQLGKIIAETFLAAGHEVTLVTTktavkPEPH----PNLSIIEIENVDDLLETLEPL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 269 FVHADAAILTAAVADYTPEQVADEKikrektgemslNLKPTRDIAAFL------GNLKNDTEHQ---------------- 326
Cdd:PRK06732  79 VKDHDVLIHSMAVSDYTPVYMTDLE-----------EVSASDNLNEFLtkqnteAKISSASDYQvlflkktpkvisyvkk 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 327 ---RRLLVGFALETHNEQMN----AEDKLNRKNLDFIVLNSLNDkgagfrcdtnkISIIDHQG-----KTDYPLKSKAEV 394
Cdd:PRK06732 148 wnpNITLVGFKLLVNVSKEElikvARASLIKNQADYILANDLTD-----------ISADQHKAllvskNEVYTAQTKEEI 216
                        250
                 ....*....|.
gi 492400708 395 AADIVDRLVKD 405
Cdd:PRK06732 217 ADLLLERIEKY 227
PRK09620 PRK09620
hypothetical protein; Provisional
189-341 1.44e-11

hypothetical protein; Provisional


Pssm-ID: 181997  Cd Length: 229  Bit Score: 63.76  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 189 LVGKTVMITAGPTYEKIDPVRFIGNYSSGKMGLALADECTARGAKVILIAG-----PVQQGTYFPMHQYHAVESAQEMFE 263
Cdd:PRK09620   1 MKGKKVLITSGGCLEKWDQVRGHTNMAKGTIGRIIAEELISKGAHVIYLHGyfaekPNDINNQLELHPFEGIIDLQDKMK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708 264 AAsAAFVHADAAILTAAVADYTPEQVADEKIK-REKTGEMSLNLKPT---RDIAAFLGNLKN-DTEhqrRLLVGFALETH 338
Cdd:PRK09620  81 SI-ITHEKVDAVIMAAAGSDWVVDKICDQEGNvLDMNGKISSDIAPIihfQKAPKVLKQIKQwDPE---TVLVGFKLESD 156

                 ...
gi 492400708 339 NEQ 341
Cdd:PRK09620 157 VNE 159
spoVFB PRK08305
dipicolinate synthase subunit B; Reviewed
5-123 2.56e-09

dipicolinate synthase subunit B; Reviewed


Pssm-ID: 181370 [Multi-domain]  Cd Length: 196  Bit Score: 56.44  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   5 LKGKKIVLGITGSIAAYKACY-IIRGLIKRGAEVQVVITPA----------GKEFITPITlsALTSKPVIseffaqrdgt 73
Cdd:PRK08305   3 LKGKRIGFGLTGSHCTYDEVMpEIEKLVDEGAEVTPIVSYTvqttdtrfgkAEEWIKKIE--EITGNKVI---------- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492400708  74 wNSHVD---LG--LWADAMLIAPATASTIGKMANGVADNmliTTYLSAKA------PVFVA 123
Cdd:PRK08305  71 -NTIVEaepLGpkKLLDCMVIAPCTGNTMAKLANAITDS---PVLMAAKAtlrnqrPVVLA 127
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
8-111 1.10e-07

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 51.77  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   8 KKIVLGITGSIAAYKACYIIRGLIKRGAEVQVVITPAGKEFI---TPITLSALTSK--PVISEFFAQRDGTWNSHVDLGL 82
Cdd:PRK05920   4 KRIVLAITGASGAIYGVRLLECLLAADYEVHLVISKAAQKVLateTGLKLPAVPDLaeAFLREQLGAAAGQLRVHGKDDW 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492400708  83 WA---------DAMLIAPATASTIGKMANGVADNmLIT 111
Cdd:PRK05920  84 GApiasgsfrtDGMVIAPCSMGTLAAIAHGLSDN-LIE 120
PRK06029 PRK06029
UbiX family flavin prenyltransferase;
8-111 1.11e-03

UbiX family flavin prenyltransferase;


Pssm-ID: 235677  Cd Length: 185  Bit Score: 39.88  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492400708   8 KKIVLGITGsiaAYKACYIIRgLIKR-----GAEVQVVITPAGKEFItpitlsALTSKPVISEFFAQRDGTWNSHvDLGL 82
Cdd:PRK06029   2 KRLIVGISG---ASGAIYGVR-LLQVlrdvgEIETHLVISQAARQTL------AHETDFSLRDVQALADVVHDVR-DIGA 70
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 492400708  83 W-------ADAMLIAPATASTIGKMANGVADNmLIT 111
Cdd:PRK06029  71 SiasgsfgTDGMVIAPCSMKTLAKIAHGYSDN-LIT 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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