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Conserved domains on  [gi|1963620336|emb|CAD8968562|]
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unnamed protein product, partial [Hemiselmis andersenii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 104-176 2.33e-31

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


:

Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 109.80  E-value: 2.33e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PLN02226 super family cl31848
2-oxoglutarate dehydrogenase E2 component
 26-186 7.32e-07

2-oxoglutarate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02226:

Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 49.37  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  26 SSAAATNRIASMRVILLATLAVAASAFNGPLSLGNP----RNIALRSAAVSSPSPALLASPLATRRRsaaspPLSGVRMQ 101
Cdd:PLN02226   16 SPSLFGKSLQSSRVAASSPSLLSGSETGALLHRGNHahsfHNLALPGNSGISRSASLVSSTLQRWVR-----PFSSESGD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PLN02226   91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170


                  ....*
gi 1963620336 182 EIDSV 186
Cdd:PLN02226  171 AASQV 175
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 104-176 2.33e-31

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 109.80  E-value: 2.33e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 102-182 4.92e-29

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 112.58  E-value: 4.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81


                  .
gi 1963620336 182 E 182
Cdd:PRK11856   82 A 82
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 102-177 8.00e-28

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 100.91  E-value: 8.00e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIA 177
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 104-185 2.28e-25

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 102.56  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGS-SAPVGSTVALIAETEGE 182
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkDVPVNKPIAVLVEEKED 80


                  ...
gi 1963620336 183 IDS 185
Cdd:TIGR01349  81 VAD 83
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 104-176 3.16e-17

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 73.40  E-value: 3.16e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1963620336 104 EITMPALSSTMKEGkIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 26-186 7.32e-07

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 49.37  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  26 SSAAATNRIASMRVILLATLAVAASAFNGPLSLGNP----RNIALRSAAVSSPSPALLASPLATRRRsaaspPLSGVRMQ 101
Cdd:PLN02226   16 SPSLFGKSLQSSRVAASSPSLLSGSETGALLHRGNHahsfHNLALPGNSGISRSASLVSSTLQRWVR-----PFSSESGD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PLN02226   91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170


                  ....*
gi 1963620336 182 EIDSV 186
Cdd:PLN02226  171 AASQV 175
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 104-176 2.33e-31

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 109.80  E-value: 2.33e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 102-182 4.92e-29

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 112.58  E-value: 4.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGE 81


                  .
gi 1963620336 182 E 182
Cdd:PRK11856   82 A 82
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 102-177 8.00e-28

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 100.91  E-value: 8.00e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIA 177
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 104-185 2.28e-25

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 102.56  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGS-SAPVGSTVALIAETEGE 182
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkDVPVNKPIAVLVEEKED 80


                  ...
gi 1963620336 183 IDS 185
Cdd:TIGR01349  81 VAD 83
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 102-182 1.70e-23

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 97.68  E-value: 1.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSS-APVGSTVALIAEtE 180
Cdd:PRK11892    2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLLE-E 80


                  ..
gi 1963620336 181 GE 182
Cdd:PRK11892   81 GE 82
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 59-185 6.08e-23

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 96.46  E-value: 6.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  59 GNPRNIALRSAAVSSPSPA-----LLASPLATRRRSAAS----PPlsgvrmqASEITMPALSSTMKEGKIVQWTKDVGDK 129
Cdd:PLN02744   67 LFGSNISRTARKNGSPMTGsglfkSLSSSQMQSARGFSSssdlPP-------HQEIGMPSLSPTMTEGNIARWLKKEGDK 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1963620336 130 VSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSA-PVGSTVALIAETEGEIDS 185
Cdd:PLN02744  140 VSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEiKVGEVIAITVEEEEDIGK 196
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 101-184 5.42e-19

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 84.23  E-value: 5.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 101 QASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETE 180
Cdd:PRK14875    1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80


                  ....*..
gi 1963620336 181 G---EID 184
Cdd:PRK14875   81 VsdaEID 87
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 104-176 3.16e-17

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 73.40  E-value: 3.16e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1963620336 104 EITMPALSSTMKEGkIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 104-170 1.79e-14

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 65.93  E-value: 1.79e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVG 170
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGD 67
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 104-178 1.78e-13

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 68.61  E-value: 1.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1963620336 104 EITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAE 178
Cdd:TIGR01347   2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE 76
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 69-181 7.55e-13

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 67.16  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  69 AAVSSPSPALLASPLATRRRSAASPPLSGVrmQASEITMPALSStMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDV 148
Cdd:PRK11855   88 AAAAAPAAAAAAAPAPAAAAPAAAAAAAGG--GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEI 164

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1963620336 149 EAFEDGFLAKILVPEGSSAPVGSTVALIaETEG 181
Cdd:PRK11855  165 PSPVAGVVKEIKVKVGDKVSVGSLLVVI-EVAA 196
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 105-180 3.35e-12

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 65.09  E-value: 3.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1963620336 105 ITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETE 180
Cdd:PTZ00144   47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG 122
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 101-182 3.51e-11

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 62.15  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 101 QASEITMPALSStMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIaETE 180
Cdd:PRK11855    1 MAIEFKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI-EAA 78


                  ..
gi 1963620336 181 GE 182
Cdd:PRK11855   79 GA 80
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 68-182 9.27e-11

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 61.17  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  68 SAAVSSPSPALLASPLAtrrrsAASPPLSGvrmQASEITMPALSSTmkEGKIVQWTKDVGDKVSAGDVIMVVESDKADMD 147
Cdd:PRK11854   79 GAADAAPAQAEEKKEAA-----PAAAPAAA---AAKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASME 148

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1963620336 148 VEAFEDGFLAKILVPEGSSAPVGSTVALIaETEGE 182
Cdd:PRK11854  149 VPAPFAGTVKEIKVNVGDKVSTGSLIMVF-EVAGE 182
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 68-181 2.92e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 59.63  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  68 SAAVSSPSPALLASPlatrrrsAASPPLSGvrmQASEITMPALSSTmkEGKIVQWTKDVGDKVSAGDVIMVVESDKADMD 147
Cdd:PRK11854  182 EAPAAAPAAAEAAAP-------AAAPAAAA---GVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASME 249

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1963620336 148 VEAFEDGFLAKILVPEGSSAPVGSTVALIaETEG 181
Cdd:PRK11854  250 VPAPFAGTVKEIKVNVGDKVKTGSLIMRF-EVEG 282
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 102-185 3.94e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 59.25  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTmkEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PRK11854    2 AIEIKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79


                  ....
gi 1963620336 182 EIDS 185
Cdd:PRK11854   80 AADA 83
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
102-178 4.00e-10

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 58.69  E-value: 4.00e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAE 178
Cdd:PRK05704    2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDE 78
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 117-176 7.28e-09

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 50.88  E-value: 7.28e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 117 GKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALI 176
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 90-176 3.43e-07

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 50.23  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  90 AASPPLSGVRMQASEITmpALSSTMKeGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPV 169
Cdd:PRK09282  507 PLKEIVVGGRPRASAPG--AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNP 583


                  ....*..
gi 1963620336 170 GSTVALI 176
Cdd:PRK09282  584 GDVLMEI 590
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 26-186 7.32e-07

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 49.37  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  26 SSAAATNRIASMRVILLATLAVAASAFNGPLSLGNP----RNIALRSAAVSSPSPALLASPLATRRRsaaspPLSGVRMQ 101
Cdd:PLN02226   16 SPSLFGKSLQSSRVAASSPSLLSGSETGALLHRGNHahsfHNLALPGNSGISRSASLVSSTLQRWVR-----PFSSESGD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336 102 ASEITMPALSSTMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEG 181
Cdd:PLN02226   91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170


                  ....*
gi 1963620336 182 EIDSV 186
Cdd:PLN02226  171 AASQV 175
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 80-181 1.59e-06

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 48.33  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  80 ASPLATRRRSAASPPLSGVRMQASEITMPALSStMKEGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKI 159
Cdd:TIGR01348  94 TAGAPAPAAQAQAAPAAGQSSGVQEVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSV 172

                          90       100
                  ....*....|....*....|..
gi 1963620336 160 LVPEGSSAPVGSTVaLIAETEG 181
Cdd:TIGR01348 173 KVKVGDSVPTGDLI-LTLSVAG 193
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
82-177 3.07e-06

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 47.62  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  82 PLATRRRSAASPPLSGVRMQASEITMPaLSstmkeGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILV 161
Cdd:PRK14040  504 PAAPAAAPAAAAAAAPAAAAGEPVTAP-LA-----GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAV 577

                          90
                  ....*....|....*.
gi 1963620336 162 PEGSSAPVGSTVALIA 177
Cdd:PRK14040  578 KEGDAVAVGDTLLTLA 593
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 116-182 3.39e-05

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 44.10  E-value: 3.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1963620336 116 EGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAETEGE 182
Cdd:TIGR01348  13 EGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGA 79
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 126-166 1.83e-04

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 40.26  E-value: 1.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1963620336 126 VGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSS 166
Cdd:COG0511    85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQP 125
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 68-170 6.16e-04

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 39.08  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1963620336  68 SAAVSSPSPALLASPLATRRRSAASPPlsgvrMQASE--ITMPAlsstmkEGKIVQWTKDVGDKVSAGDVIMVVESDKAD 145
Cdd:PRK05641   53 PTPAPAPAPAVPSAPTPVAPAAPAPAP-----ASAGEnvVTAPM------PGKILRILVREGQQVKVGQGLLILEAMKME 121

                          90       100
                  ....*....|....*....|....*
gi 1963620336 146 MDVEAFEDGFLAKILVPEGSSAPVG 170
Cdd:PRK05641  122 NEIPAPKDGVVKKILVKEGDTVDTG 146
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 117-148 1.22e-03

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 37.13  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1963620336 117 GKIVQ-WTKDVGDKVSAGDVIMVVESDKADMDV 148
Cdd:cd06848    29 GDIVFvELPEVGTEVKKGDPFGSVESVKAASDL 61
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
124-178 2.69e-03

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 35.76  E-value: 2.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1963620336 124 KDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTVALIAE 178
Cdd:PRK07051   26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 117-150 4.52e-03

Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440275  Cd Length: 128  Bit Score: 36.25  E-value: 4.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1963620336 117 GKIVQWT-KDVGDKVSAGDVIMVVESDKADMDVEA 150
Cdd:COG0509    37 GDIVFVElPEVGTEVEAGEPFGVVESVKAVSDLYA 71
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 117-164 5.29e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 37.81  E-value: 5.29e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1963620336  117 GKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEG 164
Cdd:PRK12999  1085 GSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAG 1132
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 106-166 5.51e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 37.75  E-value: 5.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1963620336  106 TMPalsstmkeGKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSS 166
Cdd:COG1038   1082 PMP--------GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQ 1134
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 117-173 5.61e-03

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 37.39  E-value: 5.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1963620336 117 GKIVQWTKDVGDKVSAGDVIMVVESDKADMDVEAFEDGFLAKILVPEGSSAPVGSTV 173
Cdd:PRK14042  534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVL 590
 
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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