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Conserved domains on  [gi|489552640|ref|WP_003457244|]
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MULTISPECIES: aspartate 1-decarboxylase [Pseudomonadaceae]

Protein Classification

aspartate 1-decarboxylase( domain architecture ID 10787124)

aspartate 1-decarboxylase catalyzes the formation of beta-alanine from L-aspartate

CATH:  2.40.40.20
EC:  4.1.1.11
Gene Ontology:  GO:0004068|GO:0006523|GO:0015940
PubMed:  9546220

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PanD COG0853
Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is ...
 1-119 1.09e-71

Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440614  Cd Length: 119  Bit Score: 209.51  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:COG0853    1 MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVICLNGAAARLVQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489552640  81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSN 119
Cdd:COG0853   81 PGDLVIIIAYAQMDEEEAKTHKPKVVFVDEDNRIVEIGN 119
 
Name Accession Description Interval E-value
PanD COG0853
Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is ...
 1-119 1.09e-71

Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440614  Cd Length: 119  Bit Score: 209.51  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:COG0853    1 MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVICLNGAAARLVQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489552640  81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSN 119
Cdd:COG0853   81 PGDLVIIIAYAQMDEEEAKTHKPKVVFVDEDNRIVEIGN 119
PRK05449 PRK05449
aspartate alpha-decarboxylase; Provisional
 1-126 4.55e-71

aspartate alpha-decarboxylase; Provisional


Pssm-ID: 180090  Cd Length: 126  Bit Score: 208.17  E-value: 4.55e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:PRK05449   1 MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILENEKVQIVNVNNGARFETYVIAGERGSGVICLNGAAARLVQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489552640  81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSNAIPVQVA 126
Cdd:PRK05449  81 VGDLVIIAAYAQMDEEEAKTHKPKVVFVDEDNRIKETAKYIPVQVA 126
Asp_decarbox pfam02261
Aspartate decarboxylase; Decarboxylation of aspartate is the major route of beta-alanine ...
 5-108 1.32e-63

Aspartate decarboxylase; Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme aspartate decarboxylase EC:4.1.1.11 which requires a pyruvoyl group for its activity. It is synthesized initially as a proenzyme which is then proteolytically cleaved to an alpha (C-terminal) and beta (N-terminal) subunit and a pyruvoyl group. This family contains both chains of aspartate decarboxylase.


Pssm-ID: 460515  Cd Length: 107  Bit Score: 188.72  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640    5 MLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAKVGDR 84
Cdd:pfam02261   3 MLKSKIHRATVTEANLNYVGSITIDEDLMEAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVICLNGAAARLVQPGDL 82

                          90       100
                  ....*....|....*....|....
gi 489552640   85 VIICAYAHYSEAELANFKPRMLYM 108
Cdd:pfam02261  83 VIIMAYAQMDEEEAKTHKPKVVFV 106
Asp_decarbox cd06919
Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent ...
 4-112 4.62e-57

Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production; Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme L-aspartate decarboxylase (ADC), EC:4.1.1.11 which requires a pyruvoyl group for its activity. The pyruvoyl cofactor is covalently bound to the enzyme. The protein is synthesized as a proenzyme and cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment), and the pyruvoyl group. Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The active site of the tetrameric enzyme is located at the interface of two subunits, with a Lysine and a Histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit. This alignment model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase.


Pssm-ID: 132994  Cd Length: 111  Bit Score: 172.31  E-value: 4.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   4 IMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAKVGD 83
Cdd:cd06919    3 TMLKSKIHRATVTEADLNYEGSITIDEDLLEAAGILPYEKVLVVNVNNGARFETYVIPGERGSGVICLNGAAARLGQPGD 82

                         90       100
                 ....*....|....*....|....*....
gi 489552640  84 RVIICAYAHYSEAELANFKPRMLYMAPGN 112
Cdd:cd06919   83 RVIIMAYALMDEEEAEGHKPKVVLVDEKN 111
panD TIGR00223
L-aspartate-alpha-decarboxylase; Members of this family are aspartate 1-decarboxylase, the ...
 1-126 7.76e-47

L-aspartate-alpha-decarboxylase; Members of this family are aspartate 1-decarboxylase, the enzyme that makes beta-alanine and C02 from aspartate. Beta-alanine is then used to make the vitamin pantothenate, from which coenzyme A is made. Aspartate 1-decarboxylase is synthesized as a proenzyme, then cleaved to an alpha (C-terminal) and beta (N-terminal) subunit with a pyruvoyl group. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 129327  Cd Length: 126  Bit Score: 147.37  E-value: 7.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640    1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:TIGR00223   1 MIRTMLQGKLHRATVTHANLNYEGSITIDEDLLDAAGILENEKVDIVNVNNGKRFSTYAIAGKRGSRIICVNGAAARCVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489552640   81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSNAIPVQVA 126
Cdd:TIGR00223  81 VGDIVIIASYVTMPDEEARTHRPNVAYFEGDNEIKRTAKAIPVQVA 126
 
Name Accession Description Interval E-value
PanD COG0853
Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is ...
 1-119 1.09e-71

Aspartate 1-decarboxylase [Coenzyme transport and metabolism]; Aspartate 1-decarboxylase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440614  Cd Length: 119  Bit Score: 209.51  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:COG0853    1 MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVICLNGAAARLVQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489552640  81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSN 119
Cdd:COG0853   81 PGDLVIIIAYAQMDEEEAKTHKPKVVFVDEDNRIVEIGN 119
PRK05449 PRK05449
aspartate alpha-decarboxylase; Provisional
 1-126 4.55e-71

aspartate alpha-decarboxylase; Provisional


Pssm-ID: 180090  Cd Length: 126  Bit Score: 208.17  E-value: 4.55e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:PRK05449   1 MLRTMLKSKIHRATVTEADLNYEGSITIDEDLLDAAGILENEKVQIVNVNNGARFETYVIAGERGSGVICLNGAAARLVQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489552640  81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSNAIPVQVA 126
Cdd:PRK05449  81 VGDLVIIAAYAQMDEEEAKTHKPKVVFVDEDNRIKETAKYIPVQVA 126
Asp_decarbox pfam02261
Aspartate decarboxylase; Decarboxylation of aspartate is the major route of beta-alanine ...
 5-108 1.32e-63

Aspartate decarboxylase; Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme aspartate decarboxylase EC:4.1.1.11 which requires a pyruvoyl group for its activity. It is synthesized initially as a proenzyme which is then proteolytically cleaved to an alpha (C-terminal) and beta (N-terminal) subunit and a pyruvoyl group. This family contains both chains of aspartate decarboxylase.


Pssm-ID: 460515  Cd Length: 107  Bit Score: 188.72  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640    5 MLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAKVGDR 84
Cdd:pfam02261   3 MLKSKIHRATVTEANLNYVGSITIDEDLMEAAGILPYEKVQIVNVNNGERFETYVIPGERGSGVICLNGAAARLVQPGDL 82

                          90       100
                  ....*....|....*....|....
gi 489552640   85 VIICAYAHYSEAELANFKPRMLYM 108
Cdd:pfam02261  83 VIIMAYAQMDEEEAKTHKPKVVFV 106
Asp_decarbox cd06919
Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent ...
 4-112 4.62e-57

Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production; Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme L-aspartate decarboxylase (ADC), EC:4.1.1.11 which requires a pyruvoyl group for its activity. The pyruvoyl cofactor is covalently bound to the enzyme. The protein is synthesized as a proenzyme and cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment), and the pyruvoyl group. Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The active site of the tetrameric enzyme is located at the interface of two subunits, with a Lysine and a Histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit. This alignment model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase.


Pssm-ID: 132994  Cd Length: 111  Bit Score: 172.31  E-value: 4.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640   4 IMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAKVGD 83
Cdd:cd06919    3 TMLKSKIHRATVTEADLNYEGSITIDEDLLEAAGILPYEKVLVVNVNNGARFETYVIPGERGSGVICLNGAAARLGQPGD 82

                         90       100
                 ....*....|....*....|....*....
gi 489552640  84 RVIICAYAHYSEAELANFKPRMLYMAPGN 112
Cdd:cd06919   83 RVIIMAYALMDEEEAEGHKPKVVLVDEKN 111
panD TIGR00223
L-aspartate-alpha-decarboxylase; Members of this family are aspartate 1-decarboxylase, the ...
 1-126 7.76e-47

L-aspartate-alpha-decarboxylase; Members of this family are aspartate 1-decarboxylase, the enzyme that makes beta-alanine and C02 from aspartate. Beta-alanine is then used to make the vitamin pantothenate, from which coenzyme A is made. Aspartate 1-decarboxylase is synthesized as a proenzyme, then cleaved to an alpha (C-terminal) and beta (N-terminal) subunit with a pyruvoyl group. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 129327  Cd Length: 126  Bit Score: 147.37  E-value: 7.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489552640    1 MHAIMLKAKLHRAEVTHAVLDYEGSCAIDGEWLDLAGIREYEQIQIYNVDNGERFTTYAIRGENGSRMISVNGAAAHKAK 80
Cdd:TIGR00223   1 MIRTMLQGKLHRATVTHANLNYEGSITIDEDLLDAAGILENEKVDIVNVNNGKRFSTYAIAGKRGSRIICVNGAAARCVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489552640   81 VGDRVIICAYAHYSEAELANFKPRMLYMAPGNELSHTSNAIPVQVA 126
Cdd:TIGR00223  81 VGDIVIIASYVTMPDEEARTHRPNVAYFEGDNEIKRTAKAIPVQVA 126
 
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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