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Conserved domains on  [gi|1907199558|ref|XP_036011082|]
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phosphopantothenoylcysteine decarboxylase isoform X2 [Mus musculus]

Protein Classification

HFCD family protein( domain architecture ID 139779)

HFCD (homooligomeric flavin containing Cys decarboxylase) family protein similar to Archaeoglobus fulgidus flavin prenyltransferase UbiX, Homo sapiens phosphopantothenoylcysteine decarboxylase and Bacillus sp. mersacidin decarboxylase

CATH:  3.40.50.1950
Gene Ontology:  GO:0000166|GO:0003824
SCOP:  4003907

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Flavoprotein super family cl19190
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
8-120 3.40e-34

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.-).


The actual alignment was detected with superfamily member PLN02496:

Pssm-ID: 450266  Cd Length: 209  Bit Score: 118.54  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558   8 PAAVPSEERKFRVLVGVTGSVAALKLPLLVSKLLDVPglEVTVVTTERAKHFYSPQDVP--VTLYSDADEWEMWKRRSDP 85
Cdd:PLN02496   10 AMEVNTAPRKPRILLAASGSVAAIKFGNLCHCFSEWA--EVRAVVTKASLHFIDRASLPkdVTLYTDEDEWSSWNKIGDS 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907199558  86 VLHIDLRRWADLMLVAPLDANTLGKVASGICDNLL 120
Cdd:PLN02496   88 VLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLL 122
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
8-120 3.40e-34

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 118.54  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558   8 PAAVPSEERKFRVLVGVTGSVAALKLPLLVSKLLDVPglEVTVVTTERAKHFYSPQDVP--VTLYSDADEWEMWKRRSDP 85
Cdd:PLN02496   10 AMEVNTAPRKPRILLAASGSVAAIKFGNLCHCFSEWA--EVRAVVTKASLHFIDRASLPkdVTLYTDEDEWSSWNKIGDS 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907199558  86 VLHIDLRRWADLMLVAPLDANTLGKVASGICDNLL 120
Cdd:PLN02496   88 VLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLL 122
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
19-120 1.78e-33

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: 115.55  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTGSVAALKLPLLVSKLLDvPGLEVTVVTTERAKHFYSPQDVPVTLYsDADEWEMWKRRSDPVLHIDL---RRWA 95
Cdd:pfam02441   2 RILVGITGSSAAIKALRLLEELKK-EGAEVRVIMTKAAKKVITPETLAALSE-NVDEDLTWRELDDDILHIELasgARWA 79
                          90       100
                  ....*....|....*....|....*
gi 1907199558  96 DLMLVAPLDANTLGKVASGICDNLL 120
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLL 104
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
19-142 6.27e-31

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: 113.97  E-value: 6.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSP--------QDVPVTLYSDADEWEMwkrrsdpvLHID 90
Cdd:COG0452     6 RILLGVTGGIAAYKAAELVRLLRKA-GAEVRVVMTEAATEFVTPltfqalsgNPVYTDLFDEEAEAEM--------GHIE 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907199558  91 LRRWADLMLVAPLDANTLGKVASGICDNLLdqgvalsgsSSTCLCT----AVLPTM 142
Cdd:COG0452    77 LARWADLIVIAPATANTIAKLAHGIADDLL---------TTTLLATtcpvLVAPAM 123
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
15-142 5.61e-24

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: 95.13  E-value: 5.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  15 ERKfRVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSPQDVPVTLYSDADEwEMWKRRSDPVLHIDLRRW 94
Cdd:TIGR00521   2 ENK-KILLGVTGGIAAYKTVELVRELVRQ-GAEVKVIMTEAAKKFITPLTLEALSGHKVVT-ELWGPIEHNALHIDLAKW 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907199558  95 ADLMLVAPLDANTLGKVASGICDNLLdqgvalsgsSSTCLCTA----VLPTM 142
Cdd:TIGR00521  79 ADLILIAPATANTISKIAHGIADDLV---------STTALAASapiiLAPAM 121
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
8-120 3.40e-34

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 118.54  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558   8 PAAVPSEERKFRVLVGVTGSVAALKLPLLVSKLLDVPglEVTVVTTERAKHFYSPQDVP--VTLYSDADEWEMWKRRSDP 85
Cdd:PLN02496   10 AMEVNTAPRKPRILLAASGSVAAIKFGNLCHCFSEWA--EVRAVVTKASLHFIDRASLPkdVTLYTDEDEWSSWNKIGDS 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907199558  86 VLHIDLRRWADLMLVAPLDANTLGKVASGICDNLL 120
Cdd:PLN02496   88 VLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLL 122
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
19-120 1.78e-33

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: 115.55  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTGSVAALKLPLLVSKLLDvPGLEVTVVTTERAKHFYSPQDVPVTLYsDADEWEMWKRRSDPVLHIDL---RRWA 95
Cdd:pfam02441   2 RILVGITGSSAAIKALRLLEELKK-EGAEVRVIMTKAAKKVITPETLAALSE-NVDEDLTWRELDDDILHIELasgARWA 79
                          90       100
                  ....*....|....*....|....*
gi 1907199558  96 DLMLVAPLDANTLGKVASGICDNLL 120
Cdd:pfam02441  80 DAMVIAPASANTLAKIANGIADNLL 104
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
19-142 6.27e-31

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: 113.97  E-value: 6.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSP--------QDVPVTLYSDADEWEMwkrrsdpvLHID 90
Cdd:COG0452     6 RILLGVTGGIAAYKAAELVRLLRKA-GAEVRVVMTEAATEFVTPltfqalsgNPVYTDLFDEEAEAEM--------GHIE 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907199558  91 LRRWADLMLVAPLDANTLGKVASGICDNLLdqgvalsgsSSTCLCT----AVLPTM 142
Cdd:COG0452    77 LARWADLIVIAPATANTIAKLAHGIADDLL---------TTTLLATtcpvLVAPAM 123
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
19-143 2.49e-27

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 104.45  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSP--------QDVPVTLYSDADEWEMwkrrsdpvLHID 90
Cdd:PRK05579    8 RIVLGVSGGIAAYKALELVRRLRKA-GADVRVVMTEAAKKFVTPltfqalsgNPVSTDLWDPAAEAAM--------GHIE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907199558  91 LRRWADLMLVAPLDANTLGKVASGICDNLLdqgvalsgsSSTCLCTAVlPTMV 143
Cdd:PRK05579   79 LAKWADLVLIAPATADLIAKLAHGIADDLL---------TTTLLATTA-PVLV 121
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
15-142 5.61e-24

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: 95.13  E-value: 5.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  15 ERKfRVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSPQDVPVTLYSDADEwEMWKRRSDPVLHIDLRRW 94
Cdd:TIGR00521   2 ENK-KILLGVTGGIAAYKTVELVRELVRQ-GAEVKVIMTEAAKKFITPLTLEALSGHKVVT-ELWGPIEHNALHIDLAKW 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907199558  95 ADLMLVAPLDANTLGKVASGICDNLLdqgvalsgsSSTCLCTA----VLPTM 142
Cdd:TIGR00521  79 ADLILIAPATANTISKIAHGIADDLV---------STTALAASapiiLAPAM 121
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
18-120 8.42e-20

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 80.76  E-value: 8.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  18 FRVLVGVTGSVAALKLPLLVSKLLDVpGLEVTVVTTERAKHFYSPQDV------PVtlYSDADEWEMWKRrsdpVLHIDL 91
Cdd:PRK07313    2 KNILLAVSGSIAAYKAADLTSQLTKR-GYQVTVLMTKAATKFITPLTLqvlsknPV--HLDVMDEHDPKL----MNHIEL 74
                          90       100
                  ....*....|....*....|....*....
gi 1907199558  92 RRWADLMLVAPLDANTLGKVASGICDNLL 120
Cdd:PRK07313   75 AKRADLFLVAPATANTIAKLAHGIADDLV 103
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
3-142 1.36e-11

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 60.92  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558   3 PKAPCPAAVPSEERKfRVLVGVTGSVAALKLPLLVSKLLDvPGLEVTVVTTERAKHFYSP--------QDVPVTLYSDAD 74
Cdd:PRK13982   57 AAPPAAREQASLASK-RVTLIIGGGIAAYKALDLIRRLKE-RGAHVRCVLTKAAQQFVTPltasalsgQRVYTDLFDPES 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907199558  75 EWEmwkrrsdpVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLDqGVALSGSSSTCLCTAVLPTM 142
Cdd:PRK13982  135 EFD--------AGHIRLARDCDLIVVAPATADLMAKMANGLADDLAS-AILLAANRPILLAPAMNPLM 193
PRK06029 PRK06029
UbiX family flavin prenyltransferase;
19-120 2.01e-03

UbiX family flavin prenyltransferase;


Pssm-ID: 235677  Cd Length: 185  Bit Score: 36.80  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTG-SVAALKLPLLvSKLLDVPGLEVTVVTTERAKhfyspqdVPVTLYSDADEWEMwKRRSDpVLHIDLRRWA-- 95
Cdd:PRK06029    3 RLIVGISGaSGAIYGVRLL-QVLRDVGEIETHLVISQAAR-------QTLAHETDFSLRDV-QALAD-VVHDVRDIGAsi 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907199558  96 -------DLMLVAPLDANTLGKVASGICDNLL 120
Cdd:PRK06029   73 asgsfgtDGMVIAPCSMKTLAKIAHGYSDNLI 104
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
19-120 3.93e-03

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 35.98  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199558  19 RVLVGVTG-SVAALKLPLLvsKLLDVPGLEVTVVTTERA-KHFYSPQDVpvTLYSDADEWEMWKRRSDPVLHIDLR--RW 94
Cdd:PRK05920    5 RIVLAITGaSGAIYGVRLL--ECLLAADYEVHLVISKAAqKVLATETGL--KLPAVPDLAEAFLREQLGAAAGQLRvhGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907199558  95 ADL-------------MLVAPLDANTLGKVASGICDNLL 120
Cdd:PRK05920   81 DDWgapiasgsfrtdgMVIAPCSMGTLAAIAHGLSDNLI 119
 
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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