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Conserved domains on  [gi|666875806|ref|NP_001288032|]
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phosphopantothenoylcysteine decarboxylase isoform d [Homo sapiens]

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 ...
34-129 8.95e-23

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: 88.49  E-value: 8.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666875806  34 PLLVSKLLDIPG-------TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAM 106
Cdd:PLN02496 104 PLSANTLGKIAGglcdnllTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLACGDYGNGAM 183
                         90       100
                 ....*....|....*....|...
gi 666875806 107 AEVGTIVDKVKevLFQHSGFQQS 129
Cdd:PLN02496 184 AEPSLIYSTVR--LFLESRAQSQ 204
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
34-129 8.95e-23

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 88.49  E-value: 8.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666875806  34 PLLVSKLLDIPG-------TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAM 106
Cdd:PLN02496 104 PLSANTLGKIAGglcdnllTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLACGDYGNGAM 183
                         90       100
                 ....*....|....*....|...
gi 666875806 107 AEVGTIVDKVKevLFQHSGFQQS 129
Cdd:PLN02496 184 AEPSLIYSTVR--LFLESRAQSQ 204
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
54-120 1.79e-19

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: 82.38  E-value: 1.79e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666875806  54 RSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:COG0452  113 TTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGRMAEPEEIVEAIEALL 179
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
46-120 4.91e-18

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: 75.23  E-value: 4.91e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 666875806   46 TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:TIGR02113 103 TSVALALPPETPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGRGALADLDDILQTIKEIL 177
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
44-120 9.27e-12

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: 58.92  E-value: 9.27e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666875806   44 PGTCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGyveipcvakklvcgdeGLGAMAEVGTIVDKVKEVL 120
Cdd:pfam02441 117 PHLENMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG----------------GKGRMPEPEAIVGKVLDAL 177
 
Name Accession Description Interval E-value
PLN02496 PLN02496
probable phosphopantothenoylcysteine decarboxylase
34-129 8.95e-23

probable phosphopantothenoylcysteine decarboxylase


Pssm-ID: 215274  Cd Length: 209  Bit Score: 88.49  E-value: 8.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666875806  34 PLLVSKLLDIPG-------TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAM 106
Cdd:PLN02496 104 PLSANTLGKIAGglcdnllTCIVRAWDYSKPLFVAPAMNTFMWNNPFTERHLMSIDELGISLIPPVTKRLACGDYGNGAM 183
                         90       100
                 ....*....|....*....|...
gi 666875806 107 AEVGTIVDKVKevLFQHSGFQQS 129
Cdd:PLN02496 184 AEPSLIYSTVR--LFLESRAQSQ 204
PRK07313 PRK07313
phosphopantothenoylcysteine decarboxylase; Validated
35-120 2.46e-22

phosphopantothenoylcysteine decarboxylase; Validated


Pssm-ID: 235986 [Multi-domain]  Cd Length: 182  Bit Score: 86.54  E-value: 2.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666875806  35 LLVSKLLDIPGTCvmrawdrskPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVD 114
Cdd:PRK07313 102 LVTSVALALPATT---------PKLIAPAMNTKMYENPATQRNLKTLKEDGVQEIEPKEGLLACGDEGYGALADIETILE 172

                 ....*.
gi 666875806 115 KVKEVL 120
Cdd:PRK07313 173 TIENTL 178
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
54-120 1.00e-21

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 88.65  E-value: 1.00e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666875806  54 RSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:PRK05579 115 TTAPVLVAPAMNTQMWENPATQRNLATLRSRGVEIIGPASGRLACGDVGPGRMAEPEEIVAAAERAL 181
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
54-120 1.79e-19

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: 82.38  E-value: 1.79e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666875806  54 RSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:COG0452  113 TTCPVLVAPAMNTNMWEHPATQRNLATLRERGVHIIGPASGELACGDVGKGRMAEPEEIVEAIEALL 179
coaC_strep TIGR02113
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
46-120 4.91e-18

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: 75.23  E-value: 4.91e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 666875806   46 TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:TIGR02113 103 TSVALALPPETPKLIAPAMNTKMYQNPITQRNIKILKKIGYQEIQPKESLLACGDYGRGALADLDDILQTIKEIL 177
coaBC_dfp TIGR00521
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
55-127 1.85e-14

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: 68.17  E-value: 1.85e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 666875806   55 SKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGAMAEVGTIVDKVKEVLFQHSGFQ 127
Cdd:TIGR00521 112 SAPIILAPAMNENMYNNPAVQENIKRLKDDGYIFIEPRSGLLACGDEGKGRLAEPETIVKAAEREFSPKEDLE 184
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
44-120 9.27e-12

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: 58.92  E-value: 9.27e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 666875806   44 PGTCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGyveipcvakklvcgdeGLGAMAEVGTIVDKVKEVL 120
Cdd:pfam02441 117 PHLENMLTLTAKKPIIIAPAMNTAMYENPATLENLEDLKADG----------------GKGRMPEPEAIVGKVLDAL 177
PRK13982 PRK13982
bifunctional SbtC-like/phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; ...
46-120 3.12e-10

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


Pssm-ID: 172484 [Multi-domain]  Cd Length: 475  Bit Score: 56.30  E-value: 3.12e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 666875806  46 TCVMRAWDRskPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEI-PCVAKKLVCGDEGLGAMAEVGTIVDKVKEVL 120
Cdd:PRK13982 173 SAILLAANR--PILLAPAMNPLMWNNPATRRNVAQLKRDGVHMIgPNAGEMAERGEAGVGRMAEPLEIAAAAEALL 246
 
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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