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Conserved domains on  [gi|512561403|ref|WP_016447783|]
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MULTISPECIES: holo-ACP synthase [Delftia]

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
PubMed:  9211277
SCOP:  4003652

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
1-130 6.84e-58

4'-phosphopantetheinyl transferase; Provisional


:

Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 175.32  E-value: 6.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELstwraRRARWPERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKER-----AKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARN-LQVHLSVTDESDYAASFCVVERR 130
Cdd:PRK00070  76 IEVLNDELGKPIVRLSGEAAERLEKLGgARIHLSISHDGDYAVAFVILESL 126
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
1-130 6.84e-58

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 175.32  E-value: 6.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELstwraRRARWPERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKER-----AKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARN-LQVHLSVTDESDYAASFCVVERR 130
Cdd:PRK00070  76 IEVLNDELGKPIVRLSGEAAERLEKLGgARIHLSISHDGDYAVAFVILESL 126
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-129 4.90e-51

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 157.60  E-value: 4.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   4 GIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRarwpeRGIRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEV 83
Cdd:COG0736    1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRK-----RPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEV 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 512561403  84 VKLPSGQPAIVLHGALKEWFEARN-LQVHLSVTDESDYAASFCVVER 129
Cdd:COG0736   76 LNDPSGKPTVRLSGRAAELAAELGiTRIHLSISHERDYAVAFVILEA 122
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
1-129 1.26e-24

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: 90.96  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403    1 MIYGIGTDICDVRRIRASLERHGdRFAEKVLAEGELSTWRARRarwPERGIRFVATRFSAKEAFSKAIGMGM-VMPMTWR 79
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLS---PKSQTESLAGRWAAKEAFIKALGKGIsLGELLFT 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 512561403   80 SCEVVKLPSGQPAIVLHG-ALKEWFEARNLQVHLSVTDESDYAASFCVVER 129
Cdd:TIGR00556  77 DIEIVKDLKGAPRVCLIGeAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
4-125 1.56e-16

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: 69.94  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403    4 GIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRARWPergiRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEV 83
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEAR----RAFARLWTAKEAVFKALGPGLSKLLDFDDIEV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 512561403   84 VKLPSGQPAIVLHGALKEWfearnlQVHLSVTDEsDYAASFC 125
Cdd:pfam01648  77 LLDPDGRPTLRLLGEAADL------AWRFEVLAG-DYALAVA 111
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
1-130 6.84e-58

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 175.32  E-value: 6.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELstwraRRARWPERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK00070   1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKER-----AKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARN-LQVHLSVTDESDYAASFCVVERR 130
Cdd:PRK00070  76 IEVLNDELGKPIVRLSGEAAERLEKLGgARIHLSISHDGDYAVAFVILESL 126
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-129 4.90e-51

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 157.60  E-value: 4.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   4 GIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRarwpeRGIRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEV 83
Cdd:COG0736    1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRK-----RPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEV 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 512561403  84 VKLPSGQPAIVLHGALKEWFEARN-LQVHLSVTDESDYAASFCVVER 129
Cdd:COG0736   76 LNDPSGKPTVRLSGRAAELAAELGiTRIHLSISHERDYAVAFVILEA 122
acpS PRK14657
holo-[acyl-carrier-protein] synthase;
1-129 3.47e-29

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173120 [Multi-domain]  Cd Length: 123  Bit Score: 102.54  E-value: 3.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELstwrarrARWPERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK14657   1 MIVGLGIDITELDRIAKALERFGDRFARRILHPAEL-------AAMPAAPVAFLAGRFAAKEAAVKALGTGFSQGIGPRD 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARNLQ-VHLSVTDESDYAASFCVVER 129
Cdd:PRK14657  74 IEVGVLPAGAPQLVLHGKALARAEALGATsTHVSLTHGRDTAAAVVVLEG 123
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
1-129 1.26e-24

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: 90.96  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403    1 MIYGIGTDICDVRRIRASLERHGdRFAEKVLAEGELSTWRARRarwPERGIRFVATRFSAKEAFSKAIGMGM-VMPMTWR 79
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLS---PKSQTESLAGRWAAKEAFIKALGKGIsLGELLFT 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 512561403   80 SCEVVKLPSGQPAIVLHG-ALKEWFEARNLQVHLSVTDESDYAASFCVVER 129
Cdd:TIGR00556  77 DIEIVKDLKGAPRVCLIGeAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
acpS PRK14660
holo-[acyl-carrier-protein] synthase;
1-128 1.79e-24

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173123  Cd Length: 125  Bit Score: 90.71  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELStWRARRARWPERgirfVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK14660   1 MILGTGVDIVEVERIARSIERHGDRFLRRIYTPGEIA-YCTSKANRAER----LAARFAAKEAVMKAIGTGLREGVRWTD 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARNL-QVHLSVTDESDYAASFCVVE 128
Cdd:PRK14660  76 FEVCRDERGRPTVRLHGRAAEIAAALGAtRIHLSLSHTQEYAVAQVILE 124
acpS PRK14659
holo-[acyl-carrier-protein] synthase;
1-127 6.80e-23

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237780  Cd Length: 122  Bit Score: 86.35  E-value: 6.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTwrARRARWPERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK14659   1 MIVGIGTDIVYIPRILNLLKKFGNKFLNRVFSEKEIED--SLKYTSQEARARHFAKRFAAKEAYVKALGTGFGRGIKMKD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWfearnlQVHLSVTDESDYAASFCVV 127
Cdd:PRK14659  79 ISVYNDLYGKPQITVSKSNIDH------KIELSLSDDGDYAIAFVVL 119
acpS PRK14656
holo-[acyl-carrier-protein] synthase;
1-129 2.79e-19

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237779 [Multi-domain]  Cd Length: 126  Bit Score: 77.11  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRarwpeRGIRFVATRFSAKEAFSKAIGMGMVMPMTWRS 80
Cdd:PRK14656   1 MIFGTGVDIVDISRFERFVDEGNVALLERIFTPHEQEYCAGKK-----HSAQHYALRFAAKEAFLKALGTGLRDGISWHD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 512561403  81 CEVVKLPSGQPAIVLHGALKEWFEARNLQ-VHLSVTDESDYAASFCVVER 129
Cdd:PRK14656  76 MEVVNDQLGKPELRLYGRALELFAQAGLSkTFLSLSHDGGCAVAMVVLER 125
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
4-129 1.80e-18

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: 75.11  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403    4 GIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRARwpeRGIRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEV 83
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKKKFAERFLSPSEIDLCKDKSEK---RKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 512561403   84 VKLPSGQPAIVLHGALKEWFEARNlqVHLSVTDESDYAASFCVVER 129
Cdd:TIGR00516  78 RKDPKGAPLITLSKEICDKFNIAA--LHASISHDAEFAAAQVVIER 121
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
4-125 1.56e-16

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: 69.94  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403    4 GIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRARWPergiRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEV 83
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEAR----RAFARLWTAKEAVFKALGPGLSKLLDFDDIEV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 512561403   84 VKLPSGQPAIVLHGALKEWfearnlQVHLSVTDEsDYAASFC 125
Cdd:pfam01648  77 LLDPDGRPTLRLLGEAADL------AWRFEVLAG-DYALAVA 111
acpS PRK14662
4'-phosphopantetheinyl transferase; Provisional
1-130 4.31e-15

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 184783  Cd Length: 120  Bit Score: 66.35  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRASLERHGDRFAEKVLAEGELSTWRARRARWPErgirfVATRFSAKEAFSKAigmgMVMPMTWRS 80
Cdd:PRK14662   1 MIVAIGHDLVEIARIRRVLERHGERALERLFHPEELAYCLAKADPAPS-----LAARFAAKEAFQKC----WPESHGWRE 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 512561403  81 CEVVKlPSGQPAIVLHGALKEWFEARNLQVHLSVTDESDYAASFCVVERR 130
Cdd:PRK14662  72 VWVER-EGARPVLGFAPKIAARMEEEGWVAHLSLSHEKEHALAVVVLEAR 120
acpS PRK14661
holo-[acyl-carrier-protein] synthase;
1-130 3.94e-11

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 184782  Cd Length: 169  Bit Score: 57.24  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   1 MIYGIGTDICDVRRIRaslerhgDRFAEKVLAEGELSTWRARRARwpergIRFVATRFSAKEAFSKAIGMGMvmpMTWRS 80
Cdd:PRK14661   1 MIVGVGIDVLEVERVP-------EKFAERILGESEKRLFLTRKRR-----REFIAGRFALKEAFFKALGTGL---NGHSF 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 512561403  81 CEVVKLPS-GQPAIVLHGAlkewFEARNLqVHLSVTDESdYAASFCVVERR 130
Cdd:PRK14661  66 TDVEFLESnGKPVLCVHKD----FGFFNY-AHVSLSHDR-FAVALVVLEKR 110
acpS PRK14663
holo-[acyl-carrier-protein] synthase;
8-93 3.21e-09

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237781 [Multi-domain]  Cd Length: 116  Bit Score: 50.99  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512561403   8 DICDVRRIRASLERHGDRFAEKVLAEGELSTWRARrarwpERGIRFVATRFSAKEAFSKAIGMGMVMPMTWRSCEVVKLP 87
Cdd:PRK14663   2 DIVDLERIEKAYNRYGVKFLEKILTPEEIELCLQK-----PQPVASIAGRFAAKEAVVKALGTGFSQGVHWKSFAILNDA 76

                 ....*.
gi 512561403  88 SGQPAI 93
Cdd:PRK14663  77 AGRPFV 82
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
10-77 6.44e-03

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 34.94  E-value: 6.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512561403  10 CDVRRIRASLErhgDRFAEKVLAEGELSTWRARRARWPERgiRFvaTRF-SAKEAFSKAIGMGMVMPMT 77
Cdd:COG2091  111 VDIERIRPRID---LALARRFFSPEERAWLAALPQDDRLE--AF--TRLwTLKEALLKATGTGLSLPLR 172
 
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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