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Conserved domains on  [gi|2728022295|ref|WP_343237237|]
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4'-phosphopantetheinyl transferase superfamily protein [Xanthomonas sp.]

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

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List of domain hits

 Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
39-160 6.09e-34

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


:

Pssm-ID: 441694  Cd Length: 177  Bit Score: 119.30  E-value: 6.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  39 ARRLLAWELATPEAELPLRRDERGRPWLHEPLAHVGtgWSHSGDYLLVAIGAHARLGVDIEHQRPRPRLpEVAQRFFHAD 118
Cdd:COG2091    56 LRELLARLLGLPPADLEFAYDPHGKPYLADPGLHFS--LSHSGGLAAVAVSRGGPVGVDIERIRPRIDL-ALARRFFSPE 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2728022295 119 EAATLQALDEPAREALFFRLWCAKEALLKAHGHGLSFGLHRL 160
Cdd:COG2091   133 ERAWLAALPQDDRLEAFTRLWTLKEALLKATGTGLSLPLRAL 174
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
39-160 6.09e-34

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 119.30  E-value: 6.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  39 ARRLLAWELATPEAELPLRRDERGRPWLHEPLAHVGtgWSHSGDYLLVAIGAHARLGVDIEHQRPRPRLpEVAQRFFHAD 118
Cdd:COG2091    56 LRELLARLLGLPPADLEFAYDPHGKPYLADPGLHFS--LSHSGGLAAVAVSRGGPVGVDIERIRPRIDL-ALARRFFSPE 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2728022295 119 EAATLQALDEPAREALFFRLWCAKEALLKAHGHGLSFGLHRL 160
Cdd:COG2091   133 ERAWLAALPQDDRLEAFTRLWTLKEALLKATGTGLSLPLRAL 174
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 93-201 2.55e-19

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: 79.57  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  93 RLGVDIEH-----QRPRPRLPEVAQRFFHADEAATLQALDEPAReALFFRLWCAKEALLKAHGHGLS--FGLHRLRFAED 165
Cdd:pfam01648   1 GVGIDIEEiarirRPIERLGERLAERIFTPEERALLASLPAEAR-RAFARLWTAKEAVFKALGPGLSklLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2728022295 166 GGGVLRLAWCDPALGqverWRLHEWVAAPGYRAALA 201
Cdd:pfam01648  80 PDGRPTLRLLGEAAD----LAWRFEVLAGDYALAVA 111
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
20-150 1.46e-11

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 60.62  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  20 GPVAVWLRAHPPRTPGEAQ---ARRLLAWELAT-PEAELplrrDERGRPWLhEPLAHVGTGWSHSGDYLLVAIGAHARLG 95
Cdd:PRK10351    7 APLPPALREQAPQGPRRARwlaGRVLLSHALSPlPEIIY----GEQGKPAF-APETPLWFNLSHSGDDIALLLSDEGEVG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2728022295  96 VDIEHQRPRPRLPEVAQRFFHADEAATLQALDEPAREALFFRLWCAKEALLKAHG 150
Cdd:PRK10351   82 CDIEVIRPRANWRSLANAVFSLGEHAEMDAVHPEQQLEAFWRIWTRKEAIVKQRG 136
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 94-156 1.77e-08

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: 50.90  E-value: 1.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728022295  94 LGVDIEHQRP----RPRLPEVAQRFFHADEAATLQALDEPAREALFFRLWCAKEALLKAHGHGLSFG 156
Cdd:TIGR00556   5 IGIDIVEIKRiaeqIERSGTFAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGISLG 71
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
39-160 6.09e-34

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 119.30  E-value: 6.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  39 ARRLLAWELATPEAELPLRRDERGRPWLHEPLAHVGtgWSHSGDYLLVAIGAHARLGVDIEHQRPRPRLpEVAQRFFHAD 118
Cdd:COG2091    56 LRELLARLLGLPPADLEFAYDPHGKPYLADPGLHFS--LSHSGGLAAVAVSRGGPVGVDIERIRPRIDL-ALARRFFSPE 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2728022295 119 EAATLQALDEPAREALFFRLWCAKEALLKAHGHGLSFGLHRL 160
Cdd:COG2091   133 ERAWLAALPQDDRLEAFTRLWTLKEALLKATGTGLSLPLRAL 174
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 93-201 2.55e-19

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: 79.57  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  93 RLGVDIEH-----QRPRPRLPEVAQRFFHADEAATLQALDEPAReALFFRLWCAKEALLKAHGHGLS--FGLHRLRFAED 165
Cdd:pfam01648   1 GVGIDIEEiarirRPIERLGERLAERIFTPEERALLASLPAEAR-RAFARLWTAKEAVFKALGPGLSklLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2728022295 166 GGGVLRLAWCDPALGqverWRLHEWVAAPGYRAALA 201
Cdd:pfam01648  80 PDGRPTLRLLGEAAD----LAWRFEVLAGDYALAVA 111
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
20-150 1.46e-11

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 60.62  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  20 GPVAVWLRAHPPRTPGEAQ---ARRLLAWELAT-PEAELplrrDERGRPWLhEPLAHVGTGWSHSGDYLLVAIGAHARLG 95
Cdd:PRK10351    7 APLPPALREQAPQGPRRARwlaGRVLLSHALSPlPEIIY----GEQGKPAF-APETPLWFNLSHSGDDIALLLSDEGEVG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2728022295  96 VDIEHQRPRPRLPEVAQRFFHADEAATLQALDEPAREALFFRLWCAKEALLKAHG 150
Cdd:PRK10351   82 CDIEVIRPRANWRSLANAVFSLGEHAEMDAVHPEQQLEAFWRIWTRKEAIVKQRG 136
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 94-156 1.77e-08

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: 50.90  E-value: 1.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728022295  94 LGVDIEHQRP----RPRLPEVAQRFFHADEAATLQALDEPAREALFFRLWCAKEALLKAHGHGLSFG 156
Cdd:TIGR00556   5 IGIDIVEIKRiaeqIERSGTFAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGISLG 71
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 39-172 2.44e-08

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


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 51.84  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728022295  39 ARRLLAwELATPEAelPLRRDERGRP-WlheplahvGTGW----SHSGDYLLVAIGAHAR---LGVDIEHQRPRPRLPEV 110
Cdd:COG2977    38 ARRALA-ELGVPPA--PILIGEDRAPlW--------PAGVvgsiSHSDGYAAAVVAPASDvrgLGIDIEPLLDEPLAEEL 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2728022295 111 AQRFFHADEAATLQALDEPAREALFFRLWCAKEALLKA--HGHGLSFGLH--RLRFAEDGGGVLRL 172
Cdd:COG2977   107 LPSILTPAERALLAALSPLPFAHALTLLFSAKESLYKAlyPLVGRYFGFDdaELVALDPEAGTFTL 172
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
93-158 4.85e-05

Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 41.27  E-value: 4.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2728022295  93 RLGVDIEH--------QRPRPRLpevAQRFFHADEAATLQALDEPARealFF-RLWCAKEALLKAHGHGLSFGLH 158
Cdd:COG0736     1 GIGIDIVEiarieralERHGERF---LERVFTPAERAYCQSRKRPAE---FLaGRFAAKEAVSKALGTGIGKGVS 69
 
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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