NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568961898|ref|XP_006511430|]
View 

phosphopantothenoylcysteine decarboxylase isoform X4 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Flavoprotein super family cl19190
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 2-118 2.10e-52

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: 163.99  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   2 WKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLKA 81
Cdd:PLN02496  81 WNKIGDSVLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDE 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568961898  82 FGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:PLN02496 161 LGISLIPPVTKRLACGDYGNGAMAEPSLIYSTVRLFL 197
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 2-118 2.10e-52

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 163.99  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   2 WKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLKA 81
Cdd:PLN02496  81 WNKIGDSVLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDE 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568961898  82 FGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:PLN02496 161 LGISLIPPVTKRLACGDYGNGAMAEPSLIYSTVRLFL 197
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 1-122 4.70e-45

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: 150.56  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   1 MWKRRS-DPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAwdLNKPLLFCPAMNTAMWEHPLTAQQVAQL 79
Cdd:COG0452   63 LFDEEAeAEMGHIELARWADLIVIAPATANTIAKLAHGIADDLLTTTLLA--TTCPVLVAPAMNTNMWEHPATQRNLATL 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568961898  80 KAFGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVLSQHG 122
Cdd:COG0452  141 RERGVHIIGPASGELACGDVGKGRMAEPEEIVEAIEALLAPKK 183
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 1-118 1.34e-34

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: 117.61  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898    1 MWKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLK 80
Cdd:TIGR02113  60 MDEHDPKVINHIELAKKADLFLVAPASANTIAHLAHGFADNIVTSVALALPPETPKLIAPAMNTKMYQNPITQRNIKILK 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568961898   81 AFGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:TIGR02113 140 KIGYQEIQPKESLLACGDYGRGALADLDDILQTIKEIL 177
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 1-118 2.70e-31

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: 109.39  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898    1 MWKRRSDPVLHIDL---RRWADLMLVAPLDANTLGKVASGICDNLLTcviRAWDL-----------------NKPLLFCP 60
Cdd:pfam02441  59 TWRELDDDILHIELasgARWADAMVIAPASANTLAKIANGIADNLLT---RAADValkerrphlenmltltaKKPIIIAP 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961898   61 AMNTAMWEHPLTAQQVAQLKAFGyveipcvskklvcgdqGLGAMAEVETIVAKVQAVL 118
Cdd:pfam02441 136 AMNTAMYENPATLENLEDLKADG----------------GKGRMPEPEAIVGKVLDAL 177
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
 2-118 2.10e-52

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 163.99  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   2 WKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLKA 81
Cdd:PLN02496  81 WNKIGDSVLHIELRRWADVMVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDE 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568961898  82 FGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:PLN02496 161 LGISLIPPVTKRLACGDYGNGAMAEPSLIYSTVRLFL 197
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
 1-122 4.70e-45

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: 150.56  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   1 MWKRRS-DPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAwdLNKPLLFCPAMNTAMWEHPLTAQQVAQL 79
Cdd:COG0452   63 LFDEEAeAEMGHIELARWADLIVIAPATANTIAKLAHGIADDLLTTTLLA--TTCPVLVAPAMNTNMWEHPATQRNLATL 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568961898  80 KAFGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVLSQHG 122
Cdd:COG0452  141 RERGVHIIGPASGELACGDVGKGRMAEPEEIVEAIEALLAPKK 183
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
 8-119 1.75e-44

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 149.13  E-value: 1.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898   8 PVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDlnKPLLFCPAMNTAMWEHPLTAQQVAQLKAFGYVEI 87
Cdd:PRK05579  73 AMGHIELAKWADLVLIAPATADLIAKLAHGIADDLLTTTLLATT--APVLVAPAMNTQMWENPATQRNLATLRSRGVEII 150

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568961898  88 PCVSKKLVCGDQGLGAMAEVETIVAKVQAVLS 119
Cdd:PRK05579 151 GPASGRLACGDVGPGRMAEPEEIVAAAERALS 182
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
 11-118 5.00e-43

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 139.31  E-value: 5.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898  11 HIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLKAFGYVEIPCV 90
Cdd:PRK07313  71 HIELAKRADLFLVAPATANTIAKLAHGIADDLVTSVALALPATTPKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPK 150

                         90       100
                 ....*....|....*....|....*...
gi 568961898  91 SKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:PRK07313 151 EGLLACGDEGYGALADIETILETIENTL 178
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
 1-118 1.34e-34

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: 117.61  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898    1 MWKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDLNKPLLFCPAMNTAMWEHPLTAQQVAQLK 80
Cdd:TIGR02113  60 MDEHDPKVINHIELAKKADLFLVAPASANTIAHLAHGFADNIVTSVALALPPETPKLIAPAMNTKMYQNPITQRNIKILK 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568961898   81 AFGYVEIPCVSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:TIGR02113 140 KIGYQEIQPKESLLACGDYGRGALADLDDILQTIKEIL 177
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
 9-120 8.33e-32

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: 115.55  E-value: 8.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898    9 VLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAwdLNKPLLFCPAMNTAMWEHPLTAQQVAQLKAFGYVEIP 88
Cdd:TIGR00521  70 ALHIDLAKWADLILIAPATANTISKIAHGIADDLVSTTALA--ASAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIE 147

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568961898   89 CVSKKLVCGDQGLGAMAEVETIVAKVQAVLSQ 120
Cdd:TIGR00521 148 PRSGLLACGDEGKGRLAEPETIVKAAEREFSP 179
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 1-118 2.70e-31

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: 109.39  E-value: 2.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898    1 MWKRRSDPVLHIDL---RRWADLMLVAPLDANTLGKVASGICDNLLTcviRAWDL-----------------NKPLLFCP 60
Cdd:pfam02441  59 TWRELDDDILHIELasgARWADAMVIAPASANTLAKIANGIADNLLT---RAADValkerrphlenmltltaKKPIIIAP 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961898   61 AMNTAMWEHPLTAQQVAQLKAFGyveipcvskklvcgdqGLGAMAEVETIVAKVQAVL 118
Cdd:pfam02441 136 AMNTAMYENPATLENLEDLKADG----------------GKGRMPEPEAIVGKVLDAL 177
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
 11-118 2.78e-24

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 95.98  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961898  11 HIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAwdLNKPLLFCPAMNTAMWEHPLTAQQVAQLKAFGYVEI-PC 89
Cdd:PRK13982 140 HIRLARDCDLIVVAPATADLMAKMANGLADDLASAILLA--ANRPILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIgPN 217

                         90       100
                 ....*....|....*....|....*....
gi 568961898  90 VSKKLVCGDQGLGAMAEVETIVAKVQAVL 118
Cdd:PRK13982 218 AGEMAERGEAGVGRMAEPLEIAAAAEALL 246
PRK06029 PRK06029
UbiX family flavin prenyltransferase;
19-60 1.43e-04

UbiX family flavin prenyltransferase;


Pssm-ID: 235677  Cd Length: 185  Bit Score: 39.50  E-value: 1.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568961898  19 DLMLVAPLDANTLGKVASGICDNLLTcviRAWDL----NKPLLFCP 60
Cdd:PRK06029  80 DGMVIAPCSMKTLAKIAHGYSDNLIT---RAADVmlkeRRRLVLCV 122
PRK05920 PRK05920
aromatic acid decarboxylase; Validated
 19-51 1.77e-03

aromatic acid decarboxylase; Validated


Pssm-ID: 180312  Cd Length: 204  Bit Score: 36.37  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 568961898  19 DLMLVAPLDANTLGKVASGICDNLLTcviRAWD 51
Cdd:PRK05920  95 DGMVIAPCSMGTLAAIAHGLSDNLIE---RAAD 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH