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Conserved domains on  [gi|1373380331|gb|AVT42468|]
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diaminopimelate decarboxylase [Actinobacillus pleuropneumoniae serovar 17]

Protein Classification

LysA family protein( domain architecture ID 11414319)

LysA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 1-107 1.02e-56

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 181.50  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:COG0019    70 LAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRV 149

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVTN 107
Cdd:COG0019   150 NPGVDAGTHEYISTGGKDSKFGIPLED 176
 
Name Accession Description Interval E-value
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 1-107 1.02e-56

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 181.50  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:COG0019    70 LAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRV 149

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVTN 107
Cdd:COG0019   150 NPGVDAGTHEYISTGGKDSKFGIPLED 176
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 1-105 1.52e-55

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143501 [Multi-domain]  Cd Length: 373  Bit Score: 177.29  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06828    47 LAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRV 126

                          90       100
                  ....*....|....*....|....*
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSV 105
Cdd:cd06828   127 NPGVDAGTHPYISTGGKDSKFGIPL 151
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 1-106 2.65e-54

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 175.17  E-value: 2.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIrCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:TIGR01048  68 LAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRV 146

                          90       100
                  ....*....|....*....|....*.
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVT 106
Cdd:TIGR01048 147 NPGVDAKTHPYISTGLKDSKFGIDVE 172
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-107 8.50e-51

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 164.20  E-value: 8.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGqlGKIAPISLRV 80
Cdd:pfam00278  42 LAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDSEIRYALEAGVLCFNVDSEDELEKIAKLAP--ELVARVALRI 119

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHpYISTGLKENKFGVSVTN 107
Cdd:pfam00278 120 NPDVDAGTH-KISTGGLSSKFGIDLED 145
PLN02537 PLN02537
diaminopimelate decarboxylase
 1-103 5.76e-21

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 86.77  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIrCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:PLN02537   62 LRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKVNVLLRI 140

                          90       100
                  ....*....|....*....|...
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGV 103
Cdd:PLN02537  141 NPDVDPQVHPYVATGNKNSKFGI 163
 
Name Accession Description Interval E-value
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 1-107 1.02e-56

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 181.50  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:COG0019    70 LAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRV 149

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVTN 107
Cdd:COG0019   150 NPGVDAGTHEYISTGGKDSKFGIPLED 176
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 1-105 1.52e-55

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143501 [Multi-domain]  Cd Length: 373  Bit Score: 177.29  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06828    47 LAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRV 126

                          90       100
                  ....*....|....*....|....*
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSV 105
Cdd:cd06828   127 NPGVDAGTHPYISTGGKDSKFGIPL 151
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 1-106 2.65e-54

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 175.17  E-value: 2.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIrCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:TIGR01048  68 LAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRV 146

                          90       100
                  ....*....|....*....|....*.
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVT 106
Cdd:TIGR01048 147 NPGVDAKTHPYISTGLKDSKFGIDVE 172
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-107 8.50e-51

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 164.20  E-value: 8.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGqlGKIAPISLRV 80
Cdd:pfam00278  42 LAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDSEIRYALEAGVLCFNVDSEDELEKIAKLAP--ELVARVALRI 119

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHpYISTGLKENKFGVSVTN 107
Cdd:pfam00278 120 NPDVDAGTH-KISTGGLSSKFGIDLED 145
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 1-107 3.42e-35

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.


Pssm-ID: 143485 [Multi-domain]  Cd Length: 368  Bit Score: 124.34  E-value: 3.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06810    44 LAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRV 123

                          90       100
                  ....*....|....*....|....*..
gi 1373380331  81 NPDVDAHTHpYISTGLKENKFGVSVTN 107
Cdd:cd06810   124 NPDVSAGTH-KISTGGLKSKFGLSLSE 149
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 1-105 1.81e-34

Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.


Pssm-ID: 397077 [Multi-domain]  Cd Length: 241  Bit Score: 119.31  E-value: 1.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQlgkiAPISLRV 80
Cdd:pfam02784  36 LAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGVGCVTVDNVDELEKLARLAPE----ARVLLRI 111

                          90       100
                  ....*....|....*....|....*
gi 1373380331  81 NPDVDAHTHPYistglkENKFGVSV 105
Cdd:pfam02784 112 KPDDSAATCPL------SSKFGADL 130
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 1-105 2.70e-27

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143506 [Multi-domain]  Cd Length: 382  Bit Score: 103.44  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06839    50 LRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRI 129

                          90       100
                  ....*....|....*....|....*
gi 1373380331  81 NPDVDAhTHPYISTGLKENKFGVSV 105
Cdd:cd06839   130 NPDFEL-KGSGMKMGGGPSQFGIDV 153
PLN02537 PLN02537
diaminopimelate decarboxylase
 1-103 5.76e-21

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 86.77  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIrCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:PLN02537   62 LRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKVNVLLRI 140

                          90       100
                  ....*....|....*....|...
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGV 103
Cdd:PLN02537  141 NPDVDPQVHPYVATGNKNSKFGI 163
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 7-85 1.22e-20

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.


Pssm-ID: 143510 [Multi-domain]  Cd Length: 377  Bit Score: 85.41  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   7 GFDIVSQGELERVLAAGgePSK-VVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRVNPDVD 85
Cdd:cd06843    51 GFEVASGGEIAHVRAAV--PDApLIFGGPGKTDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALP 128
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 5-113 6.29e-20

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases; This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143505 [Multi-domain]  Cd Length: 379  Bit Score: 83.60  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   5 GSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRcFNIESIAELHRINEVAGQLGKIA-PISLRVNPD 83
Cdd:cd06836    50 GAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIDALVAEFKEASsRIGLRVNPQ 128

                          90       100       110
                  ....*....|....*....|....*....|
gi 1373380331  84 VDAHTHPYISTGLKENKFGVSVTnEGNKYW 113
Cdd:cd06836   129 VGAGKIGALSTATATSKFGVALE-DGARDE 157
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-105 2.99e-18

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.


Pssm-ID: 143484 [Multi-domain]  Cd Length: 211  Bit Score: 76.59  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06808    34 LAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRI 113

                          90       100
                  ....*....|....*....|....*
gi 1373380331  81 NPDVdahthpyistglKENKFGVSV 105
Cdd:cd06808   114 DTGD------------ENGKFGVRP 126
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 2-107 5.91e-16

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 72.53  E-value: 5.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   2 ARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRINevagqlgKIAP---ISL 78
Cdd:cd00622    45 AALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSISDIRYAAELGVRLFTFDSEDELEKIA-------KHAPgakLLL 117

                          90       100
                  ....*....|....*....|....*....
gi 1373380331  79 RVNPDVDAHTHPyISTglkenKFGVSVTN 107
Cdd:cd00622   118 RIATDDSGALCP-LSR-----KFGADPEE 140
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 1-85 1.75e-12

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.


Pssm-ID: 143508 [Multi-domain]  Cd Length: 379  Bit Score: 62.66  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRcFNIESIAELHRINEVAGQLGKIAPISLRV 80
Cdd:cd06841    53 LHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYKSKEELEKALEEGAL-INIDSFDELERILEIAKELGRVAKVGIRL 131


                  ....*
gi 1373380331  81 NPDVD 85
Cdd:cd06841   132 NMNYG 136
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 5-106 6.24e-11

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 58.22  E-value: 6.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   5 GSGFDIVSQGELERVLAA--GGEPSKVVFSGVAKSHSEIQRALEVGIRCF--NIESIAELHrinevagQLGKIAPISLRV 80
Cdd:cd06840    58 GLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNVTvdNLHPLREWP-------ELFRGREVILRI 130

                          90       100
                  ....*....|....*....|....*.
gi 1373380331  81 NPDVDAHTHPYISTGLKENKFGVSVT 106
Cdd:cd06840   131 DPGQGEGHHKHVRTGGPESKFGLDVD 156
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 5-90 1.42e-10

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.


Pssm-ID: 143509 [Multi-domain]  Cd Length: 423  Bit Score: 57.27  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   5 GSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIrCFNIESIAELHRINE-VAGQLGKIAPISLRVNPd 83
Cdd:cd06842    60 GIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLAlARGYTTGPARVLLRLSP- 137


                  ....*..
gi 1373380331  84 vDAHTHP 90
Cdd:cd06842   138 -FPASLP 143
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
5-106 2.36e-10

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 56.63  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373380331   5 GSGFDIVSQGELERVLAAGGE--PSKVVFSGVAKSHSEIQRALEVGIRcFNIESIAELHRINEV-AGQlgkiaPISLRVN 81
Cdd:PRK08961  549 GFGFECVSIGELRRVFELFPElsPERVLFTPNFAPRAEYEAAFALGVT-VTLDNVEPLRNWPELfRGR-----EVWLRID 622

                          90       100
                  ....*....|....*....|....*
gi 1373380331  82 PDVDAHTHPYISTGLKENKFGVSVT 106
Cdd:PRK08961  623 PGHGDGHHEKVRTGGKESKFGLSQT 647
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 1-63 1.66e-05

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.


Pssm-ID: 143504  Cd Length: 394  Bit Score: 42.53  E-value: 1.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373380331   1 MARLGSGFDIVSQGELERVLAAGGEPSKVVFSGVAKSHSEIQRALEVGIRCFNIESIAELHRI 63
Cdd:cd06831    55 LAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKI 117
 
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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