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Conserved domains on  [gi|489958225|ref|WP_003861532|]
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MULTISPECIES: aspartate 1-decarboxylase autocleavage activator PanM [Enterobacter]

Protein Classification

PanM family protein( domain architecture ID 14341006)

PanM family protein similar to aspartate 1-decarboxylase autocleavage activator PanM, an acetyl-coenzyme A sensor required for maturation of L-aspartate decarboxylase (PanD)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
matur_PanM NF033213
aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or ...
 1-126 9.23e-84

aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or PanZ), although related to the GNAT family N-acetyltransferases, have a different function. Then enzyme PanD, aspartate 1-decarboxylase, has an active site modified Ser residue, created by cleavage of a precursor form. PanM promotes the maturation of the CoA biosynthesis enzyme PanD, but also inhibits its activity in the presence of CoA. Figure 6 in PMID:26276430 identifies residues considered critical to interaction with PanD; seed alignment sequences and cutoff scores were chosen to separate proposed PanM from functionally distinct relatives.


:

Pssm-ID: 411104  Cd Length: 130  Bit Score: 240.55  E-value: 9.23e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958225   1 MKLTIVRLVTFSDQDHIDLGKIWPEYSPSSLA--VDENHRIYAARFNERLLAAVRVTLSGTEGALDSLRVRDVTRRRGVG 78
Cdd:NF033213   1 MKLTIIRLTTLSEQDRIDLAKIWPEQDPDQLQawLDEGHRLYAARFNDRLLGAVKVTIDGTQGELSDLCVREVTRRRGVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489958225  79 QYLIEEVIRENPSVTSWWMA--DVGVEDRGVMAAFMQALGFTAQANGWEK 126
Cdd:NF033213  81 LYLLEETLRQNPEIKHWWLAlaDVGVEDRAVMAAFMQACGFSAQSDGWEK 130
 
Name Accession Description Interval E-value
matur_PanM NF033213
aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or ...
 1-126 9.23e-84

aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or PanZ), although related to the GNAT family N-acetyltransferases, have a different function. Then enzyme PanD, aspartate 1-decarboxylase, has an active site modified Ser residue, created by cleavage of a precursor form. PanM promotes the maturation of the CoA biosynthesis enzyme PanD, but also inhibits its activity in the presence of CoA. Figure 6 in PMID:26276430 identifies residues considered critical to interaction with PanD; seed alignment sequences and cutoff scores were chosen to separate proposed PanM from functionally distinct relatives.


Pssm-ID: 411104  Cd Length: 130  Bit Score: 240.55  E-value: 9.23e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958225   1 MKLTIVRLVTFSDQDHIDLGKIWPEYSPSSLA--VDENHRIYAARFNERLLAAVRVTLSGTEGALDSLRVRDVTRRRGVG 78
Cdd:NF033213   1 MKLTIIRLTTLSEQDRIDLAKIWPEQDPDQLQawLDEGHRLYAARFNDRLLGAVKVTIDGTQGELSDLCVREVTRRRGVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489958225  79 QYLIEEVIRENPSVTSWWMA--DVGVEDRGVMAAFMQALGFTAQANGWEK 126
Cdd:NF033213  81 LYLLEETLRQNPEIKHWWLAlaDVGVEDRAVMAAFMQACGFSAQSDGWEK 130
PanZ pfam12568
Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is ...
 2-125 3.72e-66

Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is approximately 40 amino acids in length. The proteins in this family are members of the acetyltransferases of the GNAT family. Family members such as PanZ has been shown to be involved in the biosynthesis of Coenzyme A (CoA). CoA is a ubiquitous and essential cofactor, synthesized from the precursor pantothenate. In all organizms, the final step in pantothenate biosynthesis relies on the presence of beta-alanine, which comes from different sources in bacteria, yeast, and plants. In bacteria, beta-alanine is derived by the action of alpha-decarboxylase (ADC) enzyme. PanZ promotes the activation of the zymogen, PanD, to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Thereby, playing an essential role in the biosynthetic pathway to pantothenate and the regulation of CoA biosynthesis. Structure and function studies show that direct interaction of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to activation.


Pssm-ID: 432642  Cd Length: 128  Bit Score: 196.16  E-value: 3.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958225    2 KLTIVRLVTFSDQDHIDLGKIWPEYSPSSL--AVDENHRIYAARFNERLLAAVRVTLSGTEGALDSLRVRDVTRRRGVGQ 79
Cdd:pfam12568   1 KLTIERLTQFSPQDRIDLAKIWPYQSPDTLqaWLDEDHRLFAARFNDRLLGAVLVTLSDQEGELSDLCVREVTRRRGVGQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489958225   80 YLIEEVIRENPSVTSWWMADVGVE--DRGVMAAFMQALGFTAQANGWE 125
Cdd:pfam12568  81 YLIEETLRQNPEVKCWWLADEGVEpaDRGVMAGFMQACGFSAQQGGWE 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-88 7.09e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 34.20  E-value: 7.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489958225  34 DENHRIYAARFNERLLAAVRV-TLSGTEGALDSLRVRDVTRRRGVGQYLIEEVIRE 88
Cdd:COG1246   25 EEIGEFWVAEEDGEIVGCAALhPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAE 80
 
Name Accession Description Interval E-value
matur_PanM NF033213
aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or ...
 1-126 9.23e-84

aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or PanZ), although related to the GNAT family N-acetyltransferases, have a different function. Then enzyme PanD, aspartate 1-decarboxylase, has an active site modified Ser residue, created by cleavage of a precursor form. PanM promotes the maturation of the CoA biosynthesis enzyme PanD, but also inhibits its activity in the presence of CoA. Figure 6 in PMID:26276430 identifies residues considered critical to interaction with PanD; seed alignment sequences and cutoff scores were chosen to separate proposed PanM from functionally distinct relatives.


Pssm-ID: 411104  Cd Length: 130  Bit Score: 240.55  E-value: 9.23e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958225   1 MKLTIVRLVTFSDQDHIDLGKIWPEYSPSSLA--VDENHRIYAARFNERLLAAVRVTLSGTEGALDSLRVRDVTRRRGVG 78
Cdd:NF033213   1 MKLTIIRLTTLSEQDRIDLAKIWPEQDPDQLQawLDEGHRLYAARFNDRLLGAVKVTIDGTQGELSDLCVREVTRRRGVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489958225  79 QYLIEEVIRENPSVTSWWMA--DVGVEDRGVMAAFMQALGFTAQANGWEK 126
Cdd:NF033213  81 LYLLEETLRQNPEIKHWWLAlaDVGVEDRAVMAAFMQACGFSAQSDGWEK 130
PanZ pfam12568
Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is ...
 2-125 3.72e-66

Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is approximately 40 amino acids in length. The proteins in this family are members of the acetyltransferases of the GNAT family. Family members such as PanZ has been shown to be involved in the biosynthesis of Coenzyme A (CoA). CoA is a ubiquitous and essential cofactor, synthesized from the precursor pantothenate. In all organizms, the final step in pantothenate biosynthesis relies on the presence of beta-alanine, which comes from different sources in bacteria, yeast, and plants. In bacteria, beta-alanine is derived by the action of alpha-decarboxylase (ADC) enzyme. PanZ promotes the activation of the zymogen, PanD, to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Thereby, playing an essential role in the biosynthetic pathway to pantothenate and the regulation of CoA biosynthesis. Structure and function studies show that direct interaction of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to activation.


Pssm-ID: 432642  Cd Length: 128  Bit Score: 196.16  E-value: 3.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958225    2 KLTIVRLVTFSDQDHIDLGKIWPEYSPSSL--AVDENHRIYAARFNERLLAAVRVTLSGTEGALDSLRVRDVTRRRGVGQ 79
Cdd:pfam12568   1 KLTIERLTQFSPQDRIDLAKIWPYQSPDTLqaWLDEDHRLFAARFNDRLLGAVLVTLSDQEGELSDLCVREVTRRRGVGQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489958225   80 YLIEEVIRENPSVTSWWMADVGVE--DRGVMAAFMQALGFTAQANGWE 125
Cdd:pfam12568  81 YLIEETLRQNPEVKCWWLADEGVEpaDRGVMAGFMQACGFSAQQGGWE 128
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 34-88 7.09e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 34.20  E-value: 7.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489958225  34 DENHRIYAARFNERLLAAVRV-TLSGTEGALDSLRVRDVTRRRGVGQYLIEEVIRE 88
Cdd:COG1246   25 EEIGEFWVAEEDGEIVGCAALhPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAE 80
 
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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