NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501042077|ref|WP_012093981|]
View 

MULTISPECIES: 4'-phosphopantetheinyl transferase superfamily protein [Bacillus cereus group]

Protein Classification

4'-phosphopantetheinyl transferase family protein( domain architecture ID 11450000)

4-phosphopantetheinyl transferase family protein containing an ACPS (holo-[ACP] synthase) domain; ACPS transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of an acyl-carrier-protein (ACP)

CATH:  3.90.470.20
EC:  2.7.8.7
Gene Ontology:  GO:0008897
PubMed:  8939709

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
1-171 2.00e-53

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


:

Pssm-ID: 441694  Cd Length: 177  Bit Score: 170.14  E-value: 2.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077   1 MKVFALHIDrllqTSEFHTLMKHISPERITKINQLVFPKDKHRSLLSEIFVRFIIQEELHLPNHNITFQVGPYGKPFVEN 80
Cdd:COG2091   10 VHVWFIRLD----EEDLDELLALLSEDERARAARFRSEKRRRRFLAGRALLRELLARLLGLPPADLEFAYDPHGKPYLAD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  81 lPSFHFNISHSGNWIVCAI-DCHPIGIDIEKIAP-IDYSIAKHFFCYEEYEDLMAKIEPERMAYFYHLWTIKESFVKQSG 158
Cdd:COG2091   86 -PGLHFSLSHSGGLAAVAVsRGGPVGVDIERIRPrIDLALARRFFSPEERAWLAALPQDDRLEAFTRLWTLKEALLKATG 164

                        170
                 ....*....|...
gi 501042077 159 AGLTVPLHSFSIS 171
Cdd:COG2091  165 TGLSLPLRALAVE 177
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
1-171 2.00e-53

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 170.14  E-value: 2.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077   1 MKVFALHIDrllqTSEFHTLMKHISPERITKINQLVFPKDKHRSLLSEIFVRFIIQEELHLPNHNITFQVGPYGKPFVEN 80
Cdd:COG2091   10 VHVWFIRLD----EEDLDELLALLSEDERARAARFRSEKRRRRFLAGRALLRELLARLLGLPPADLEFAYDPHGKPYLAD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  81 lPSFHFNISHSGNWIVCAI-DCHPIGIDIEKIAP-IDYSIAKHFFCYEEYEDLMAKIEPERMAYFYHLWTIKESFVKQSG 158
Cdd:COG2091   86 -PGLHFSLSHSGGLAAVAVsRGGPVGVDIERIRPrIDLALARRFFSPEERAWLAALPQDDRLEAFTRLWTLKEALLKATG 164

                        170
                 ....*....|...
gi 501042077 159 AGLTVPLHSFSIS 171
Cdd:COG2091  165 TGLSLPLRALAVE 177
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 103-205 1.48e-18

4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.


Pssm-ID: 426364 [Multi-domain]  Cd Length: 111  Bit Score: 78.03  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  103 PIGIDIEKIAPIDY-------SIAKHFFCYEEYEDLmAKIEPERMAYFYHLWTIKESFVKQSGAGL--TVPLHSFSISID 173
Cdd:pfam01648   1 GVGIDIEEIARIRRpierlgeRLAERIFTPEERALL-ASLPAEARRAFARLWTAKEAVFKALGPGLskLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 501042077  174 SSQNVHIRTIEKTNPVCIEILHIGTGYKSAVC 205
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
69-158 5.35e-15

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 70.63  E-value: 5.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  69 QVGPYGKPFVENLPSFHFNISHSGNWIVCAI-DCHPIGIDIEKIAPIDY--SIAKHFFCYEEYEDLMAKIEPERMAYFYH 145
Cdd:PRK10351  44 IYGEQGKPAFAPETPLWFNLSHSGDDIALLLsDEGEVGCDIEVIRPRANwrSLANAVFSLGEHAEMDAVHPEQQLEAFWR 123

                         90
                 ....*....|...
gi 501042077 146 LWTIKESFVKQSG 158
Cdd:PRK10351 124 IWTRKEAIVKQRG 136
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 103-206 6.54e-13

phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]


Pssm-ID: 273136 [Multi-domain]  Cd Length: 128  Bit Score: 63.61  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  103 PIGIDIEKIAPIDYSI------AKHFFCYEEYEDLMAKIEPERMAYFYHLWTIKESFVKQSGAGLtvplhsfSISIDSSQ 176
Cdd:TIGR00556   4 GIGIDIVEIKRIAEQIersgtfAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGI-------SLGELLFT 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 501042077  177 NVHIRTIEKTNP-VCIEILHIGTGYKSAVCS 206
Cdd:TIGR00556  77 DIEIVKDLKGAPrVCLIGEAAKDAEKLGVCS 107
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
1-171 2.00e-53

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 170.14  E-value: 2.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077   1 MKVFALHIDrllqTSEFHTLMKHISPERITKINQLVFPKDKHRSLLSEIFVRFIIQEELHLPNHNITFQVGPYGKPFVEN 80
Cdd:COG2091   10 VHVWFIRLD----EEDLDELLALLSEDERARAARFRSEKRRRRFLAGRALLRELLARLLGLPPADLEFAYDPHGKPYLAD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  81 lPSFHFNISHSGNWIVCAI-DCHPIGIDIEKIAP-IDYSIAKHFFCYEEYEDLMAKIEPERMAYFYHLWTIKESFVKQSG 158
Cdd:COG2091   86 -PGLHFSLSHSGGLAAVAVsRGGPVGVDIERIRPrIDLALARRFFSPEERAWLAALPQDDRLEAFTRLWTLKEALLKATG 164

                        170
                 ....*....|...
gi 501042077 159 AGLTVPLHSFSIS 171
Cdd:COG2091  165 TGLSLPLRALAVE 177
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 103-205 1.48e-18

4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.


Pssm-ID: 426364 [Multi-domain]  Cd Length: 111  Bit Score: 78.03  E-value: 1.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  103 PIGIDIEKIAPIDY-------SIAKHFFCYEEYEDLmAKIEPERMAYFYHLWTIKESFVKQSGAGL--TVPLHSFSISID 173
Cdd:pfam01648   1 GVGIDIEEIARIRRpierlgeRLAERIFTPEERALL-ASLPAEARRAFARLWTAKEAVFKALGPGLskLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 501042077  174 SSQNVHIRTIEKTNPVCIEILHIGTGYKSAVC 205
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
69-158 5.35e-15

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 70.63  E-value: 5.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  69 QVGPYGKPFVENLPSFHFNISHSGNWIVCAI-DCHPIGIDIEKIAPIDY--SIAKHFFCYEEYEDLMAKIEPERMAYFYH 145
Cdd:PRK10351  44 IYGEQGKPAFAPETPLWFNLSHSGDDIALLLsDEGEVGCDIEVIRPRANwrSLANAVFSLGEHAEMDAVHPEQQLEAFWR 123

                         90
                 ....*....|...
gi 501042077 146 LWTIKESFVKQSG 158
Cdd:PRK10351 124 IWTRKEAIVKQRG 136
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 103-206 6.54e-13

phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]


Pssm-ID: 273136 [Multi-domain]  Cd Length: 128  Bit Score: 63.61  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501042077  103 PIGIDIEKIAPIDYSI------AKHFFCYEEYEDLMAKIEPERMAYFYHLWTIKESFVKQSGAGLtvplhsfSISIDSSQ 176
Cdd:TIGR00556   4 GIGIDIVEIKRIAEQIersgtfAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGI-------SLGELLFT 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 501042077  177 NVHIRTIEKTNP-VCIEILHIGTGYKSAVCS 206
Cdd:TIGR00556  77 DIEIVKDLKGAPrVCLIGEAAKDAEKLGVCS 107
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 88-155 3.06e-05

4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 43.37  E-value: 3.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501042077  88 ISHSGNWIVCAI----DCHPIGIDIEKI--APIDYSIAKHFFCYEEYEdLMAKIEPERMAYFYHL-WTIKESFVK 155
Cdd:COG2977   70 ISHSDGYAAAVVapasDVRGLGIDIEPLldEPLAEELLPSILTPAERA-LLAALSPLPFAHALTLlFSAKESLYK 143
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH