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Conserved domains on  [gi|489145697|ref|WP_003055447|]
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MULTISPECIES: phosphate propanoyltransferase [Streptococcus]

Protein Classification

phosphate propanoyltransferase( domain architecture ID 11487610)

phosphate propanoyltransferase is involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15070 PRK15070
phosphate propanoyltransferase;
29-231 4.77e-121

phosphate propanoyltransferase;


:

Pssm-ID: 237899 [Multi-domain]  Cd Length: 211  Bit Score: 342.57  E-value: 4.77e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  29 NIARESNKKVSASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKVRILGPV 108
Cdd:PRK15070   8 KIVREVVKEMLSAREREIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQYAAEETVTLVGPKGVIENVRILGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 109 RKQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPG 188
Cdd:PRK15070  88 RKKTQVEISRTDAFKLGIKAPVRMSGDLEGTPGITLVGPKGEVELEEGVIVAKRHIHMSPEDAEKFGVKDGDIVSVKVEG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489145697 189 ERGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:PRK15070 168 ERGLIFDNVLVRVSPDFALEMHIDTDEANAAGLKNGDKVKIIK 210
 
Name Accession Description Interval E-value
PRK15070 PRK15070
phosphate propanoyltransferase;
29-231 4.77e-121

phosphate propanoyltransferase;


Pssm-ID: 237899 [Multi-domain]  Cd Length: 211  Bit Score: 342.57  E-value: 4.77e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  29 NIARESNKKVSASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKVRILGPV 108
Cdd:PRK15070   8 KIVREVVKEMLSAREREIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQYAAEETVTLVGPKGVIENVRILGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 109 RKQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPG 188
Cdd:PRK15070  88 RKKTQVEISRTDAFKLGIKAPVRMSGDLEGTPGITLVGPKGEVELEEGVIVAKRHIHMSPEDAEKFGVKDGDIVSVKVEG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489145697 189 ERGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:PRK15070 168 ERGLIFDNVLVRVSPDFALEMHIDTDEANAAGLKNGDKVKIIK 210
PduL COG4869
Propanediol utilization protein [Secondary metabolites biosynthesis, transport and catabolism]; ...
23-231 7.18e-118

Propanediol utilization protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443897  Cd Length: 210  Bit Score: 334.45  E-value: 7.18e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  23 NSSQKTNIARESNKKVsASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKV 102
Cdd:COG4869    2 DEELIEQIVREVLERL-ASKPLTIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQFAAEETVTLVGPKGVIENV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 103 RILGPVRKQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSV 182
Cdd:COG4869   81 RVLGPVRKETQVEISRTDAFKLGIKAPVRESGDLEGTPGITLVGPKGSVELEEGVIVAKRHIHMSPEDAEKLGVKDGDRV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489145697 183 SLELPGERGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:COG4869  161 SVKVEGERGLIFDDVLVRVSPDFALEMHIDTDEANAAGLKNGDKVEIIK 209
BMC_EutD_Gpos NF040837
ethanolamine utilization phosphate acetyltransferase EutD, CD1920-type; Members of this family ...
30-231 1.71e-81

ethanolamine utilization phosphate acetyltransferase EutD, CD1920-type; Members of this family of bacterial microcompartment (BMC) enzymes for ethanolamine utilization are thought to have the same phosphate acetyltransferase activity (EC 2.3.1.8) as EutD of Salmonella and E. coli, but lacking sequence similarity and instead being related to PduL, phosphate propanoyltransferase (EC 2.3.1.222) of propanediol utilization BMC enzymes. Examples discussed in the literature, such as Lmo1182 from Listeria monocytogenes and CD1920 from Clostridium difficile, are called EutD despite the lack of homology.


Pssm-ID: 468776  Cd Length: 205  Bit Score: 242.16  E-value: 1.71e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  30 IARESNKKVSASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKVRILGPVR 109
Cdd:NF040837   4 IVDEVVKRIKERLFEGIEVEASGRHVHLSREDVDALFGEGYQLTKVKDLSQPGQFACKERVTLIGPKGTIHNVVVLGPER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 110 KQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPGE 189
Cdd:NF040837  84 KETQVEVSLTDAVALGIKAPVRESGDIEGTPGITLSNGDKSVQLDKGLIVAKRHIHMTPEDAKKFGVSDGEIVKVKVNGE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489145697 190 RGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:NF040837 164 RPLIFDDVVVRVSPKFRTYMHIDYDEANACGFTKGTRGRIVK 205
PTAC pfam06130
Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for ...
155-221 8.43e-30

Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for the degradation of 1,2-propanediol (1,2-PD).


Pssm-ID: 461835 [Multi-domain]  Cd Length: 67  Bit Score: 105.56  E-value: 8.43e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489145697  155 KGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPGERGGIINHVIIRVHDSFSLECHLDTEEANALGV 221
Cdd:pfam06130   1 EGVIVAARHIHLSPEDAEKLGFGDGETVTVKGPGERGLIFENVRVRGPERFALQVHIDTDEANALGL 67
 
Name Accession Description Interval E-value
PRK15070 PRK15070
phosphate propanoyltransferase;
29-231 4.77e-121

phosphate propanoyltransferase;


Pssm-ID: 237899 [Multi-domain]  Cd Length: 211  Bit Score: 342.57  E-value: 4.77e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  29 NIARESNKKVSASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKVRILGPV 108
Cdd:PRK15070   8 KIVREVVKEMLSAREREIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQYAAEETVTLVGPKGVIENVRILGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 109 RKQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPG 188
Cdd:PRK15070  88 RKKTQVEISRTDAFKLGIKAPVRMSGDLEGTPGITLVGPKGEVELEEGVIVAKRHIHMSPEDAEKFGVKDGDIVSVKVEG 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489145697 189 ERGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:PRK15070 168 ERGLIFDNVLVRVSPDFALEMHIDTDEANAAGLKNGDKVKIIK 210
PduL COG4869
Propanediol utilization protein [Secondary metabolites biosynthesis, transport and catabolism]; ...
23-231 7.18e-118

Propanediol utilization protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443897  Cd Length: 210  Bit Score: 334.45  E-value: 7.18e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  23 NSSQKTNIARESNKKVsASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKV 102
Cdd:COG4869    2 DEELIEQIVREVLERL-ASKPLTIPVGVSNRHVHLSQEDLEILFGPGYELTPKKDLSQPGQFAAEETVTLVGPKGVIENV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 103 RILGPVRKQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSV 182
Cdd:COG4869   81 RVLGPVRKETQVEISRTDAFKLGIKAPVRESGDLEGTPGITLVGPKGSVELEEGVIVAKRHIHMSPEDAEKLGVKDGDRV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489145697 183 SLELPGERGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:COG4869  161 SVKVEGERGLIFDDVLVRVSPDFALEMHIDTDEANAAGLKNGDKVEIIK 209
BMC_EutD_Gpos NF040837
ethanolamine utilization phosphate acetyltransferase EutD, CD1920-type; Members of this family ...
30-231 1.71e-81

ethanolamine utilization phosphate acetyltransferase EutD, CD1920-type; Members of this family of bacterial microcompartment (BMC) enzymes for ethanolamine utilization are thought to have the same phosphate acetyltransferase activity (EC 2.3.1.8) as EutD of Salmonella and E. coli, but lacking sequence similarity and instead being related to PduL, phosphate propanoyltransferase (EC 2.3.1.222) of propanediol utilization BMC enzymes. Examples discussed in the literature, such as Lmo1182 from Listeria monocytogenes and CD1920 from Clostridium difficile, are called EutD despite the lack of homology.


Pssm-ID: 468776  Cd Length: 205  Bit Score: 242.16  E-value: 1.71e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697  30 IARESNKKVSASDGFTIPLGVSNHHVHLSQADADSLFGANYTFTKLKDLSQKGQYAMQECLMVAGPKGVIDKVRILGPVR 109
Cdd:NF040837   4 IVDEVVKRIKERLFEGIEVEASGRHVHLSREDVDALFGEGYQLTKVKDLSQPGQFACKERVTLIGPKGTIHNVVVLGPER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697 110 KQTQVEVTATDCFKLGIKAPLRLSGDLEGSPGCTLIGPDGSVQLEKGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPGE 189
Cdd:NF040837  84 KETQVEVSLTDAVALGIKAPVRESGDIEGTPGITLSNGDKSVQLDKGLIVAKRHIHMTPEDAKKFGVSDGEIVKVKVNGE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489145697 190 RGGIINHVIIRVHDSFSLECHLDTEEANALGVSGKDYLRLIK 231
Cdd:NF040837 164 RPLIFDDVVVRVSPKFRTYMHIDYDEANACGFTKGTRGRIVK 205
PTAC pfam06130
Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for ...
155-221 8.43e-30

Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for the degradation of 1,2-propanediol (1,2-PD).


Pssm-ID: 461835 [Multi-domain]  Cd Length: 67  Bit Score: 105.56  E-value: 8.43e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489145697  155 KGCVVAKRHIHMSPQDANHYGVSDGQSVSLELPGERGGIINHVIIRVHDSFSLECHLDTEEANALGV 221
Cdd:pfam06130   1 EGVIVAARHIHLSPEDAEKLGFGDGETVTVKGPGERGLIFENVRVRGPERFALQVHIDTDEANALGL 67
PTAC pfam06130
Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for ...
46-126 1.34e-16

Phosphate propanoyltransferase; This family includes phosphotransacylases (PTACs) required for the degradation of 1,2-propanediol (1,2-PD).


Pssm-ID: 461835 [Multi-domain]  Cd Length: 67  Bit Score: 71.27  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489145697   46 IPLGVSNHHVHLSQADADSL-FGANytftklkdlsqkgqyamqECLMVAGP---KGVIDKVRILGPVRKQTQVEVTATDC 121
Cdd:pfam06130   1 EGVIVAARHIHLSPEDAEKLgFGDG------------------ETVTVKGPgerGLIFENVRVRGPERFALQVHIDTDEA 62

                  ....*
gi 489145697  122 FKLGI 126
Cdd:pfam06130  63 NALGL 67
 
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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