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Conserved domains on  [gi|490261967|ref|WP_004159185|]
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holo-ACP synthase [Erwinia amylovora]

Protein Classification

holo-ACP synthase( domain architecture ID 10011191)

holo-[acyl-carrier-protein] synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of acyl-carrier-protein (ACP)

CATH:  3.90.470.20
EC:  2.7.8.7
Gene Ontology:  GO:0008897|GO:0006633|GO:0000287|GO:0016740
PubMed:  9211277
SCOP:  4003652

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 2-126 4.98e-62

4'-phosphopantetheinyl transferase; Provisional


:

Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 185.33  E-value: 4.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   2 AILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYN 81
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEVLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490261967  82 DELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:PRK00070  81 DELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILES 125
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 2-126 4.98e-62

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 185.33  E-value: 4.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   2 AILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYN 81
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEVLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490261967  82 DELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:PRK00070  81 DELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILES 125
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
5-126 1.09e-56

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 171.85  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   5 GLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYNDEL 84
Cdd:COG0736    1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLNDPS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490261967  85 GKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:COG0736   81 GKPTVRLSGRAAELAAELGITRIHLSISHERDYAVAFVILEA 122
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 2-126 6.49e-41

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: 132.18  E-value: 6.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967    2 AILGLGSDIVEIARISAVISRSGdRLAQRVLSENEWLQYQAHQQPVR--FLAKRFAVKEAAAKAFGTGIRGG-LAFNQFE 78
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLSPKSQteSLAGRWAAKEAFIKALGKGISLGeLLFTDIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 490261967   79 VYNDELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:TIGR00556  80 IVKDLKGAPRVCLIGEAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 5-92 3.91e-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: 73.80  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967    5 GLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVR-FLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYNDE 83
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEARrAFARLWTAKEAVFKALGPGLSKLLDFDDIEVLLDP 80


                  ....*....
gi 490261967   84 LGKPGLRFL 92
Cdd:pfam01648  81 DGRPTLRLL 89
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 2-126 4.98e-62

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 185.33  E-value: 4.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   2 AILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYN 81
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEVLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490261967  82 DELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:PRK00070  81 DELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILES 125
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
5-126 1.09e-56

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 171.85  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   5 GLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYNDEL 84
Cdd:COG0736    1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLNDPS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490261967  85 GKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:COG0736   81 GKPTVRLSGRAAELAAELGITRIHLSISHERDYAVAFVILEA 122
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 2-126 6.49e-41

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: 132.18  E-value: 6.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967    2 AILGLGSDIVEIARISAVISRSGdRLAQRVLSENEWLQYQAHQQPVR--FLAKRFAVKEAAAKAFGTGIRGG-LAFNQFE 78
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLSPKSQteSLAGRWAAKEAFIKALGKGISLGeLLFTDIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 490261967   79 VYNDELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:TIGR00556  80 IVKDLKGAPRVCLIGEAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
acpS PRK14657
holo-[acyl-carrier-protein] synthase;
3-126 5.92e-33

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173120 [Multi-domain]  Cd Length: 123  Bit Score: 111.79  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAhqQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYND 82
Cdd:PRK14657   2 IVGLGIDITELDRIAKALERFGDRFARRILHPAELAAMPA--APVAFLAGRFAAKEAAVKALGTGFSQGIGPRDIEVGVL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490261967  83 ELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:PRK14657  80 PAGAPQLVLHGKALARAEALGATSTHVSLTHGRDTAAAVVVLEG 123
acpS PRK14656
holo-[acyl-carrier-protein] synthase;
3-126 3.66e-27

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237779 [Multi-domain]  Cd Length: 126  Bit Score: 97.14  E-value: 3.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYND 82
Cdd:PRK14656   2 IFGTGVDIVDISRFERFVDEGNVALLERIFTPHEQEYCAGKKHSAQHYALRFAAKEAFLKALGTGLRDGISWHDMEVVND 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490261967  83 ELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:PRK14656  82 QLGKPELRLYGRALELFAQAGLSKTFLSLSHDGGCAVAMVVLER 125
acpS PRK14660
holo-[acyl-carrier-protein] synthase;
3-125 1.94e-26

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173123  Cd Length: 125  Bit Score: 95.33  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYND 82
Cdd:PRK14660   2 ILGTGVDIVEVERIARSIERHGDRFLRRIYTPGEIAYCTSKANRAERLAARFAAKEAVMKAIGTGLREGVRWTDFEVCRD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490261967  83 ELGKPGLRFLQHAQEMARQLGVAHVHVTLADERHYACATVIIE 125
Cdd:PRK14660  82 ERGRPTVRLHGRAAEIAAALGATRIHLSLSHTQEYAVAQVILE 124
acpS PRK14659
holo-[acyl-carrier-protein] synthase;
3-124 2.48e-24

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237780  Cd Length: 122  Bit Score: 89.82  E-value: 2.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISAVISRSGDRLAQRVLSENEW---LQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEV 79
Cdd:PRK14659   2 IVGIGTDIVYIPRILNLLKKFGNKFLNRVFSEKEIedsLKYTSQEARARHFAKRFAAKEAYVKALGTGFGRGIKMKDISV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490261967  80 YNDELGKPGLrflqhaqEMARQLGVAHVHVTLADERHYACATVII 124
Cdd:PRK14659  82 YNDLYGKPQI-------TVSKSNIDHKIELSLSDDGDYAIAFVVL 119
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 5-126 4.32e-21

holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273114 [Multi-domain]  Cd Length: 121  Bit Score: 81.66  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967    5 GLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQ--AHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYND 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKKKFAERFLSPSEIDLCKdkSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490261967   83 ELGKPglrFLQHAQEMARQLGVAHVHVTLADERHYACATVIIES 126
Cdd:TIGR00516  81 PKGAP---LITLSKEICDKFNIAALHASISHDAEFAAAQVVIER 121
acpS PRK14663
holo-[acyl-carrier-protein] synthase;
9-125 2.60e-18

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237781 [Multi-domain]  Cd Length: 116  Bit Score: 74.48  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   9 DIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYNDELGKPg 88
Cdd:PRK14663   2 DIVDLERIEKAYNRYGVKFLEKILTPEEIELCLQKPQPVASIAGRFAAKEAVVKALGTGFSQGVHWKSFAILNDAAGRP- 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490261967  89 lrFLQHAQEMARQLGVAhVHVTLADERHYACATVIIE 125
Cdd:PRK14663  81 --FVKVIDDGCLPPGCV-IKISISHDRHSAVATALIE 114
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 5-92 3.91e-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: 73.80  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967    5 GLGSDIVEIARISAVISRSGDRLAQRVLSENEWLQYQAHQQPVR-FLAKRFAVKEAAAKAFGTGIRGGLAFNQFEVYNDE 83
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEARrAFARLWTAKEAVFKALGPGLSKLLDFDDIEVLLDP 80


                  ....*....
gi 490261967   84 LGKPGLRFL 92
Cdd:pfam01648  81 DGRPTLRLL 89
acpS PRK14662
4'-phosphopantetheinyl transferase; Provisional
 3-125 6.81e-14

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 184783  Cd Length: 120  Bit Score: 63.27  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISAVISRSGDRLAQRVLSENEwLQYQAHQQ-PVRFLAKRFAVKEAAAKAFGTgirgglAFNQFEVYN 81
Cdd:PRK14662   2 IVAIGHDLVEIARIRRVLERHGERALERLFHPEE-LAYCLAKAdPAPSLAARFAAKEAFQKCWPE------SHGWREVWV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490261967  82 D-ELGKPGLRFLQH-AQEMARQLGVAhvHVTLADERHYACATVIIE 125
Cdd:PRK14662  75 ErEGARPVLGFAPKiAARMEEEGWVA--HLSLSHEKEHALAVVVLE 118
acpS PRK14661
holo-[acyl-carrier-protein] synthase;
3-125 2.55e-12

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 184782  Cd Length: 169  Bit Score: 60.32  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490261967   3 ILGLGSDIVEIARISavisrsgDRLAQRVLSENEWLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIrGGLAFNQFEvYND 82
Cdd:PRK14661   2 IVGVGIDVLEVERVP-------EKFAERILGESEKRLFLTRKRRREFIAGRFALKEAFFKALGTGL-NGHSFTDVE-FLE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490261967  83 ELGKPGLRflqhaqeMARQLGV-AHVHVTLADERhYACATVIIE 125
Cdd:PRK14661  73 SNGKPVLC-------VHKDFGFfNYAHVSLSHDR-FAVALVVLE 108
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
21-72 6.01e-05

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 40.33  E-value: 6.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490261967  21 SRSGDRLAQRVLSENE--WLQYQAHQQPVRFLAKRFAVKEAAAKAFGTGIRGGL 72
Cdd:COG2091  118 PRIDLALARRFFSPEEraWLAALPQDDRLEAFTRLWTLKEALLKATGTGLSLPL 171
 
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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