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Conserved domains on  [gi|2593808860|ref|WP_316454865|]
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4'-phosphopantetheinyl transferase superfamily protein [Hafnia alvei]

Protein Classification

4'-phosphopantetheinyl transferase family protein( domain architecture ID 11459479)

4'-phosphopantetheinyl transferase family protein catalyzes the post-translational modification of target proteins by phosphopantetheine

CATH:  3.90.470.20
EC:  2.7.8.7
Gene Ontology:  GO:0000287|GO:0008897
PubMed:  8939709

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
40-237 7.40e-73

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


:

Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 220.56  E-value: 7.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  40 YQDALFNQFAIPFPEFLNKAPIKRRAEYVAARYAAKLLLEDEGCYD-NVGSNLSRAPIWPTGFCGSISHSGNFAIASISP 118
Cdd:COG2977     4 FDDALFAQLGPPEPAALARAVPKRRAEFLAGRLCARRALAELGVPPaPILIGEDRAPLWPAGVVGSISHSDGYAAAVVAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 119 RTTTLTLGIDIEMLGS-KSIVRAADIFCTPIEQ-YLLSSCHIDYETALLIAFTAKESLFKALFPKVNHSFGFNASRIRQL 196
Cdd:COG2977    84 ASDVRGLGIDIEPLLDePLAEELLPSILTPAERaLLAALSPLPFAHALTLLFSAKESLYKALYPLVGRYFGFDDAELVAL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2593808860 197 DISACRITLELIQTLTPTQTNGSLFYGYFSLQDNKVITLIT 237
Cdd:COG2977   164 DPEAGTFTLRLLQDLSPGFPAGRRFEGRFALRDGLVLTLVA 204
 
Name Accession Description Interval E-value
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
40-237 7.40e-73

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


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 220.56  E-value: 7.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  40 YQDALFNQFAIPFPEFLNKAPIKRRAEYVAARYAAKLLLEDEGCYD-NVGSNLSRAPIWPTGFCGSISHSGNFAIASISP 118
Cdd:COG2977     4 FDDALFAQLGPPEPAALARAVPKRRAEFLAGRLCARRALAELGVPPaPILIGEDRAPLWPAGVVGSISHSDGYAAAVVAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 119 RTTTLTLGIDIEMLGS-KSIVRAADIFCTPIEQ-YLLSSCHIDYETALLIAFTAKESLFKALFPKVNHSFGFNASRIRQL 196
Cdd:COG2977    84 ASDVRGLGIDIEPLLDePLAEELLPSILTPAERaLLAALSPLPFAHALTLLFSAKESLYKALYPLVGRYFGFDDAELVAL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2593808860 197 DISACRITLELIQTLTPTQTNGSLFYGYFSLQDNKVITLIT 237
Cdd:COG2977   164 DPEAGTFTLRLLQDLSPGFPAGRRFEGRFALRDGLVLTLVA 204
PRK10251 PRK10251
enterobactin synthase subunit EntD;
36-235 2.86e-20

enterobactin synthase subunit EntD;


Pssm-ID: 182334 [Multi-domain]  Cd Length: 207  Bit Score: 85.30  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  36 DSHFYQDALFnqfaIPFPEFLNKAPIKRRAEYVAARYAAKLLLEDEG--CYDNVGSnlSRAPIWPTGFCGSISHSGNFAI 113
Cdd:PRK10251   26 ASFHEQDLLW----LPHYAQLQHAGRKRKAEHLAGRIAAVYALREYGykCVPAIGE--LRQPVWPAGVYGSISHCGTTAL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 114 ASISPRtttlTLGIDIEMLGSKSIVRA-ADIFCTPIEQYLLSSCHIDYETALLIAFTAKESLFKALfpKVNHSFGFNASR 192
Cdd:PRK10251  100 AVVSRQ----PIGIDIEEIFSAQTATElTDNIITPAEHERLADCGLAFPLALTLAFSAKESAFKAS--EIQTLAGFLDYQ 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2593808860 193 IrqLDISACRITLELIQTLTPTQtngslfygyFSLQDNKVITL 235
Cdd:PRK10251  174 I--ISWNKQQIIIHRENEFFAVH---------WQIKEKIVITL 205
4PPT_N pfam17837
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal ...
54-117 2.56e-17

4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the pfam01648 domain with which it forms a pseudodimeric arrangement.


Pssm-ID: 465526 [Multi-domain]  Cd Length: 68  Bit Score: 73.43  E-value: 2.56e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2593808860  54 EFLNKAPIKRRAEYVAARYAAKLLLEDEGCYDN-VGSNLSRAPIWPTGFCGSISHSGNFAIASIS 117
Cdd:pfam17837   4 ALIAQAVPKRRAEFLAGRICARRALAALGIPPVpLLSGEDRAPVWPAGVVGSISHTDGLAAAAVA 68
 
Name Accession Description Interval E-value
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
40-237 7.40e-73

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


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 220.56  E-value: 7.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  40 YQDALFNQFAIPFPEFLNKAPIKRRAEYVAARYAAKLLLEDEGCYD-NVGSNLSRAPIWPTGFCGSISHSGNFAIASISP 118
Cdd:COG2977     4 FDDALFAQLGPPEPAALARAVPKRRAEFLAGRLCARRALAELGVPPaPILIGEDRAPLWPAGVVGSISHSDGYAAAVVAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 119 RTTTLTLGIDIEMLGS-KSIVRAADIFCTPIEQ-YLLSSCHIDYETALLIAFTAKESLFKALFPKVNHSFGFNASRIRQL 196
Cdd:COG2977    84 ASDVRGLGIDIEPLLDePLAEELLPSILTPAERaLLAALSPLPFAHALTLLFSAKESLYKALYPLVGRYFGFDDAELVAL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2593808860 197 DISACRITLELIQTLTPTQTNGSLFYGYFSLQDNKVITLIT 237
Cdd:COG2977   164 DPEAGTFTLRLLQDLSPGFPAGRRFEGRFALRDGLVLTLVA 204
PRK10251 PRK10251
enterobactin synthase subunit EntD;
36-235 2.86e-20

enterobactin synthase subunit EntD;


Pssm-ID: 182334 [Multi-domain]  Cd Length: 207  Bit Score: 85.30  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  36 DSHFYQDALFnqfaIPFPEFLNKAPIKRRAEYVAARYAAKLLLEDEG--CYDNVGSnlSRAPIWPTGFCGSISHSGNFAI 113
Cdd:PRK10251   26 ASFHEQDLLW----LPHYAQLQHAGRKRKAEHLAGRIAAVYALREYGykCVPAIGE--LRQPVWPAGVYGSISHCGTTAL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 114 ASISPRtttlTLGIDIEMLGSKSIVRA-ADIFCTPIEQYLLSSCHIDYETALLIAFTAKESLFKALfpKVNHSFGFNASR 192
Cdd:PRK10251  100 AVVSRQ----PIGIDIEEIFSAQTATElTDNIITPAEHERLADCGLAFPLALTLAFSAKESAFKAS--EIQTLAGFLDYQ 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2593808860 193 IrqLDISACRITLELIQTLTPTQtngslfygyFSLQDNKVITL 235
Cdd:PRK10251  174 I--ISWNKQQIIIHRENEFFAVH---------WQIKEKIVITL 205
4PPT_N pfam17837
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal ...
54-117 2.56e-17

4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the pfam01648 domain with which it forms a pseudodimeric arrangement.


Pssm-ID: 465526 [Multi-domain]  Cd Length: 68  Bit Score: 73.43  E-value: 2.56e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2593808860  54 EFLNKAPIKRRAEYVAARYAAKLLLEDEGCYDN-VGSNLSRAPIWPTGFCGSISHSGNFAIASIS 117
Cdd:pfam17837   4 ALIAQAVPKRRAEFLAGRICARRALAALGIPPVpLLSGEDRAPVWPAGVVGSISHTDGLAAAAVA 68
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
62-178 2.24e-16

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 74.23  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860  62 KRRAEYVAARYAAKLLLEDEGCYDNVGSNLSRAP-----IWPTGFCGSISHSGNFAIASISPRTTtltLGIDIEMLGSKS 136
Cdd:COG2091    44 KRRRRFLAGRALLRELLARLLGLPPADLEFAYDPhgkpyLADPGLHFSLSHSGGLAAVAVSRGGP---VGVDIERIRPRI 120
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2593808860 137 IVRAADIFCTPIEQYLLSSC-HIDYETALLIAFTAKESLFKAL 178
Cdd:COG2091   121 DLALARRFFSPEERAWLAALpQDDRLEAFTRLWTLKEALLKAT 163
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
125-223 1.20e-12

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: 62.63  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2593808860 125 LGIDIEMLG------SKSIVRAADIFCTPIEQYLLSSCHIDYETALLIAFTAKESLFKALFPKVNHSFGFNasRIRQLDI 198
Cdd:pfam01648   2 VGIDIEEIArirrpiERLGERLAERIFTPEERALLASLPAEARRAFARLWTAKEAVFKALGPGLSKLLDFD--DIEVLLD 79
                          90       100
                  ....*....|....*....|....*
gi 2593808860 199 SACRITLELIQTLTPTQTNGSLFYG 223
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAG 104
 
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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