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Conserved domains on  [gi|2129719424|gb|UEG63669|]
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aspartate 1-decarboxylase autocleavage activator PanM [Stutzerimonas chloritidismutans]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 2-129 2.58e-48

N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase which catalyze the transfer of an acetyl group to a substrate. The mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and then CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam12568:

Pssm-ID: 473072  Cd Length: 128  Bit Score: 151.09  E-value: 2.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424   2 PVYVESVTQPSPQDLTDLAKIYadapewlltPYASAEALIEAALADGSLIAGRFNDRLLGAALLRRGDEAWRLSHLCVRK 81
Cdd:pfam12568   1 KLTIERLTQFSPQDRIDLAKIW---------PYQSPDTLQAWLDEDHRLFAARFNDRLLGAVLVTLSDQEGELSDLCVRE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2129719424  82 VTRKRGVGRRLLEETQR---------LASEAGKPLRLAAPAGHLEASALAARTHLPL 129
Cdd:pfam12568  72 VTRRRGVGQYLIEETLRqnpevkcwwLADEGVEPADRGVMAGFMQACGFSAQQGGWE 128
 
Name Accession Description Interval E-value
PanZ pfam12568
Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is ...
 2-129 2.58e-48

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: 151.09  E-value: 2.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424   2 PVYVESVTQPSPQDLTDLAKIYadapewlltPYASAEALIEAALADGSLIAGRFNDRLLGAALLRRGDEAWRLSHLCVRK 81
Cdd:pfam12568   1 KLTIERLTQFSPQDRIDLAKIW---------PYQSPDTLQAWLDEDHRLFAARFNDRLLGAVLVTLSDQEGELSDLCVRE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2129719424  82 VTRKRGVGRRLLEETQR---------LASEAGKPLRLAAPAGHLEASALAARTHLPL 129
Cdd:pfam12568  72 VTRRRGVGQYLIEETLRqnpevkcwwLADEGVEPADRGVMAGFMQACGFSAQQGGWE 128
matur_PanM NF033213
aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or ...
 1-98 4.88e-22

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: 84.54  E-value: 4.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424   1 MPVYVESVTQPSPQDLTDLAKIyadapeWlltPYASAEALIEAALADGSLIAGRFNDRLLGAALL-RRGDEAwRLSHLCV 79
Cdd:NF033213    1 MKLTIIRLTTLSEQDRIDLAKI------W---PEQDPDQLQAWLDEGHRLYAARFNDRLLGAVKVtIDGTQG-ELSDLCV 70

                          90
                  ....*....|....*....
gi 2129719424  80 RKVTRKRGVGRRLLEETQR 98
Cdd:NF033213   71 REVTRRRGVGLYLLEETLR 89
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
56-111 3.62e-06

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.25  E-value: 3.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2129719424  56 NDRLLGAA-LLRRGDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG-KPLRLAA 111
Cdd:COG2153    42 DGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGaRRIVLSA 99
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-104 8.16e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 35.71  E-value: 8.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129719424  56 NDRLLGAALLRR---GDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:cd04301     7 DGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
 
Name Accession Description Interval E-value
PanZ pfam12568
Acetyltransferase (GNAT) domain, PanZ; This domain family is found in bacteria, and is ...
 2-129 2.58e-48

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: 151.09  E-value: 2.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424   2 PVYVESVTQPSPQDLTDLAKIYadapewlltPYASAEALIEAALADGSLIAGRFNDRLLGAALLRRGDEAWRLSHLCVRK 81
Cdd:pfam12568   1 KLTIERLTQFSPQDRIDLAKIW---------PYQSPDTLQAWLDEDHRLFAARFNDRLLGAVLVTLSDQEGELSDLCVRE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2129719424  82 VTRKRGVGRRLLEETQR---------LASEAGKPLRLAAPAGHLEASALAARTHLPL 129
Cdd:pfam12568  72 VTRRRGVGQYLIEETLRqnpevkcwwLADEGVEPADRGVMAGFMQACGFSAQQGGWE 128
matur_PanM NF033213
aspartate 1-decarboxylase autocleavage activator PanM; Members of this family, called PanM (or ...
 1-98 4.88e-22

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: 84.54  E-value: 4.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424   1 MPVYVESVTQPSPQDLTDLAKIyadapeWlltPYASAEALIEAALADGSLIAGRFNDRLLGAALL-RRGDEAwRLSHLCV 79
Cdd:NF033213    1 MKLTIIRLTTLSEQDRIDLAKI------W---PEQDPDQLQAWLDEGHRLYAARFNDRLLGAVKVtIDGTQG-ELSDLCV 70

                          90
                  ....*....|....*....
gi 2129719424  80 RKVTRKRGVGRRLLEETQR 98
Cdd:NF033213   71 REVTRRRGVGLYLLEETLR 89
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 56-104 2.58e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 43.41  E-value: 2.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2129719424  56 NDRLLGAALLRRGdeaWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:pfam13673  39 GGQIVGVIALRDR---GHISLLFVDPDYQGQGIGKALLEAVEDYAEKDG 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
56-111 3.62e-06

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.25  E-value: 3.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2129719424  56 NDRLLGAA-LLRRGDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG-KPLRLAA 111
Cdd:COG2153    42 DGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGaRRIVLSA 99
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 16-104 3.89e-04

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 37.50  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424  16 LTDLAKIYADAPEWLLTPYASAEALIEAALADGSLIAGRFNDRLLGAALLRRGDEAWRLSHLC---VRKVTRKRGVGRRL 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTAL 80

                          90
                  ....*....|..
gi 2129719424  93 LEETQRLASEAG 104
Cdd:pfam00583  81 LQALLEWARERG 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-104 5.88e-04

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 37.37  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129719424  12 SPQDLTDLAKIYADApeWLLTPYASAEALIEAALADGSLIAGRFNDRLLGAALLRR-----GDEAWRLSHLCVRKVTRKR 86
Cdd:COG3153     5 TPEDAEAIAALLRAA--FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPvdidgEGPALLLGPLAVDPEYRGQ 82

                          90
                  ....*....|....*...
gi 2129719424  87 GVGRRLLEETQRLASEAG 104
Cdd:COG3153    83 GIGRALMRAALEAARERG 100
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-104 8.16e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 35.71  E-value: 8.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129719424  56 NDRLLGAALLRR---GDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:cd04301     7 DGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-104 1.76e-03

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 36.18  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2129719424  50 LIAGRFNDRLLGAALLRR-GDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:COG0454    36 FIAVDDKGEPIGFAGLRRlDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG 91
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-104 4.84e-03

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 34.25  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2129719424  62 AALLRRGDEAWRLSHLCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERG 46
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-104 6.15e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 33.58  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2129719424  56 NDRLLGAALLRRGDEAWRLSH--LCVRKVTRKRGVGRRLLEETQRLASEAG 104
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAElrLAVHPEYRGQGIGRALLEAAEAAAKEGG 61
 
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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