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Conserved domains on  [gi|2017294875|emb|CAF9985108|]
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unnamed protein product, partial [Emiliania huxleyi]

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. ...
 72-144 1.15e-30

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: 110.19  E-value: 1.15e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
aceF super family cl36067
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 73-233 4.87e-23

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


The actual alignment was detected with superfamily member PRK11854:

Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 99.31  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTmtEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIvENEADIA 152
Cdd:PRK11854    5 IKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF-ESADGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 153 SVSAGSGAPAATAAPAAAAPAAapasdvDAIPVMMPALSSTmkEGKISSWLVGVGDKVDAGDMLLVVESDKASLSqtLPA 232
Cdd:PRK11854   82 DAAPAQAEEKKEAAPAAAPAAA------AAKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASME--VPA 151


                  .
gi 2017294875 233 P 233
Cdd:PRK11854  152 P 152
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 72-144 1.15e-30

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: 110.19  E-value: 1.15e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 72-145 3.90e-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: 103.99  E-value: 3.90e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIV 145
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 72-156 1.93e-27

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 110.27  E-value: 1.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADI 151
Cdd:PRK11856    4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83


                  ....*
gi 2017294875 152 ASVSA 156
Cdd:PRK11856   84 AAAAA 88
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 73-157 1.31e-24

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: 102.95  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEG-ETADVGAPVAIIVENEADI 151
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81


                  ....*.
gi 2017294875 152 ASVSAG 157
Cdd:TIGR01349  82 ADAFKN 87
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 73-233 4.87e-23

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 99.31  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTmtEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIvENEADIA 152
Cdd:PRK11854    5 IKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF-ESADGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 153 SVSAGSGAPAATAAPAAAAPAAapasdvDAIPVMMPALSSTmkEGKISSWLVGVGDKVDAGDMLLVVESDKASLSqtLPA 232
Cdd:PRK11854   82 DAAPAQAEEKKEAAPAAAPAAA------AAKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASME--VPA 151


                  .
gi 2017294875 233 P 233
Cdd:PRK11854  152 P 152
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 72-276 9.33e-22

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 95.46  E-value: 9.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVE-NEAD 150
Cdd:TIGR02927   4 SVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEpGEAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 151 IASVSAGSGAPAA-----------TAAPAAAAPAAAPASDVDAIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVV 219
Cdd:TIGR02927  84 SEPAPAAPEPEAApepeapapaptPAAEAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEV 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017294875 220 ESDKasLSQTLPAP--------------------RLSPLPDSPLSQPLPSPRLAPLPASPRSQPLPSPRLPAPRLCP 276
Cdd:TIGR02927 164 STDK--VDTEIPSPvagtlleirapeddtvevgtVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAP 238
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 72-144 9.18e-18

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: 76.10  E-value: 9.18e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGkISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 183-233 3.69e-15

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: 68.97  E-value: 3.69e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017294875 183 IPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATV--EVEAP 49
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 182-233 1.48e-13

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: 64.70  E-value: 1.48e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATM--EVPAP 51
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 184-233 4.52e-07

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: 46.44  E-value: 4.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017294875 184 PVMMPALSSTMKEGkISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEM--EIPAP 48
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 72-144 1.15e-30

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: 110.19  E-value: 1.15e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:cd06849     2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 72-145 3.90e-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: 103.99  E-value: 3.90e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIV 145
Cdd:COG0508     4 EIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 72-156 1.93e-27

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 110.27  E-value: 1.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADI 151
Cdd:PRK11856    4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83


                  ....*
gi 2017294875 152 ASVSA 156
Cdd:PRK11856   84 AAAAA 88
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 73-157 1.31e-24

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: 102.95  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEG-ETADVGAPVAIIVENEADI 151
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtKDVPVNKPIAVLVEEKEDV 81


                  ....*.
gi 2017294875 152 ASVSAG 157
Cdd:TIGR01349  82 ADAFKN 87
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 73-233 4.87e-23

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 99.31  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTmtEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIvENEADIA 152
Cdd:PRK11854    5 IKVPDIGAD--EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF-ESADGAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 153 SVSAGSGAPAATAAPAAAAPAAapasdvDAIPVMMPALSSTmkEGKISSWLVGVGDKVDAGDMLLVVESDKASLSqtLPA 232
Cdd:PRK11854   82 DAAPAQAEEKKEAAPAAAPAAA------AAKDVHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASME--VPA 151


                  .
gi 2017294875 233 P 233
Cdd:PRK11854  152 P 152
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 72-276 9.33e-22

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 95.46  E-value: 9.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVE-NEAD 150
Cdd:TIGR02927   4 SVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDKVDTEIPSPAAGVLLEIRAPEDDTVEVGGVLAIIGEpGEAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 151 IASVSAGSGAPAA-----------TAAPAAAAPAAAPASDVDAIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVV 219
Cdd:TIGR02927  84 SEPAPAAPEPEAApepeapapaptPAAEAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEV 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017294875 220 ESDKasLSQTLPAP--------------------RLSPLPDSPLSQPLPSPRLAPLPASPRSQPLPSPRLPAPRLCP 276
Cdd:TIGR02927 164 STDK--VDTEIPSPvagtlleirapeddtvevgtVLAIIGDANAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAP 238
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 48-153 1.19e-21

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 94.92  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  48 GFArSSADLvvrrapPPGMEvkqstITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKI 127
Cdd:PLN02744  102 GFS-SSSDL------PPHQE-----IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKI 169

                          90       100
                  ....*....|....*....|....*..
gi 2017294875 128 LVGEG-ETADVGAPVAIIVENEADIAS 153
Cdd:PLN02744  170 VKGDGaKEIKVGEVIAITVEEEEDIGK 196
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 73-184 1.27e-21

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 94.60  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEG-ETADVGAPVAIIV---ENE 148
Cdd:PRK11892    5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLLeegESA 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2017294875 149 ADIASVSAGSGAPAATAAPAAAAPAAAPASDVDAIP 184
Cdd:PRK11892   85 SDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAP 120
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 61-233 1.73e-21

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 94.68  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  61 APPPGMEVKQstITMPALSSTmtEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAP 140
Cdd:PRK11854   98 AAPAAAAAKD--VHVPDIGSD--EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 141 VAIIVEneadiasvsAGSGAPAATAAPAAAAPAAAPASDVDAIPVMMPALSSTmkEGKISSWLVGVGDKVDAGDMLLVVE 220
Cdd:PRK11854  174 IMVFEV---------AGEAPAAAPAAAEAAAPAAAPAAAAGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVE 242

                         170
                  ....*....|...
gi 2017294875 221 SDKASLSqtLPAP 233
Cdd:PRK11854  243 GDKASME--VPAP 253
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 73-272 1.13e-20

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 92.19  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSStMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII-VENEADI 151
Cdd:PRK11855    5 FKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIeAAGAAAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 152 ASVSAG-----SGAPAATAAPAAAAPAAAPASDVDAIPVMMPALSStMKEGKISSWLVGVGDKVDAGDMLLVVESDKASL 226
Cdd:PRK11855   84 AAAPAAaaapaAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATM 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017294875 227 SqtLPAP-----------------------RLSPLPDSPLSQPLPSPRLAPLPASPRSQPLPSPRLPAP 272
Cdd:PRK11855  163 E--IPSPvagvvkeikvkvgdkvsvgsllvVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPA 229
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 72-144 9.18e-18

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: 76.10  E-value: 9.18e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGkISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 72-149 8.50e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 79.99  E-value: 8.50e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEA 149
Cdd:PRK14875    4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEV 81
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 183-233 3.69e-15

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: 68.97  E-value: 3.69e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017294875 183 IPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:cd06849     1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATV--EVEAP 49
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 72-144 4.36e-15

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: 69.01  E-value: 4.36e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:cd06663     1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
73-242 1.30e-14

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 73.72  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  73 ITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADIA 152
Cdd:PRK05704    5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 153 SVSAGSGAPAATAAPAAAAPAAAPASDVDAipvMMPALSSTMKEGKISSWLV---GVGDKVDAGDMLLVVESDKASLSQT 229
Cdd:PRK05704   85 AAAAAAAAAAAAAAPAQAQAAAAAEQSNDA---LSPAARKLAAENGLDASAVkgtGKGGRVTKEDVLAALAAAAAAPAAP 161

                         170
                  ....*....|....*.
gi 2017294875 230 ---LPAPRLSPLPDSP 242
Cdd:PRK05704  162 aaaAPAAAPAPLGARP 177
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 84-272 4.12e-14

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: 72.60  E-value: 4.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  84 EGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADIASVSAGSGAPAA 163
Cdd:TIGR01348  13 EGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQAEAKKEAAPA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 164 TAAPAAAAPAAAPASDVDA-----IPVMMPALSStMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLSqtLPAP----- 233
Cdd:TIGR01348  93 PTAGAPAPAAQAQAAPAAGqssgvQEVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASME--VPAPasgvv 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017294875 234 ------------------RLSPLPDSPLSQPLPSPRLAPLPASPRSQPlPSPRLPAP 272
Cdd:TIGR01348 170 ksvkvkvgdsvptgdlilTLSVAGSTPATAPAPASAQPAAQSPAATQP-EPAAAPAA 225
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 182-233 1.48e-13

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: 64.70  E-value: 1.48e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:COG0508     2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATM--EVPAP 51
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 72-149 3.45e-13

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 69.33  E-value: 3.45e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEA 149
Cdd:PTZ00144   46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGA 123
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 72-239 4.16e-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: 69.38  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  72 TITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADI 151
Cdd:TIGR01347   2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 152 ASVSAGSGapaATAAPAAAAPAAAPASDVDAIPVMMPALSSTMKEGKISSWLV---GVGDKVDAGDmlLVVESDKASLSQ 228
Cdd:TIGR01347  82 AAPPAKSG---EEKEETPAASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVpgtGVTGRVTKED--IIKKTEAPASAQ 156

                         170
                  ....*....|.
gi 2017294875 229 TLPAPRLSPLP 239
Cdd:TIGR01347 157 PPAAAAAAAAP 167
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 61-144 2.50e-12

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 67.34  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  61 APPPGMEVKQSTITMPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAP 140
Cdd:TIGR02927 117 APQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTV 196


                  ....
gi 2017294875 141 VAII 144
Cdd:TIGR02927 197 LAII 200
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 182-233 7.65e-12

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 65.58  E-value: 7.65e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATV--EIPSP 51
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 61-156 3.28e-11

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 63.69  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  61 APPPGMEVKQstITMPALSStMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAP 140
Cdd:PRK11855  112 AAAAGGGVVE--VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188

                          90
                  ....*....|....*..
gi 2017294875 141 VAII-VENEADIASVSA 156
Cdd:PRK11855  189 LVVIeVAAAAPAAAAAP 205
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 182-224 8.93e-11

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 62.24  E-value: 8.93e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKA 224
Cdd:PRK11892    2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKA 44
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 61-153 3.44e-10

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 60.79  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  61 APPPGMEVKQstITMPALSSTmtEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAP 140
Cdd:PRK11854  199 APAAAAGVKD--VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSL 274

                          90
                  ....*....|....
gi 2017294875 141 VAII-VENEADIAS 153
Cdd:PRK11854  275 IMRFeVEGAAPAAA 288
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 77-144 1.96e-08

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: 50.11  E-value: 1.96e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017294875  77 ALSSTMTeGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:cd06850     1 EVTAPMP-GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 185-226 2.57e-08

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: 54.80  E-value: 2.57e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2017294875 185 VMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASL 226
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATM 43
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 36-144 2.82e-08

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 54.85  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  36 PGARSVAGLPFGGFARSSADLVVRRAPPPGMEVkqstitmpALSSTMTeGKISSWLMGVGDKVDAGDMVLVVESDKADMD 115
Cdd:PRK09282  491 PFYLRVDGMPEEVVVEPLKEIVVGGRPRASAPG--------AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMKMENE 561

                          90       100
                  ....*....|....*....|....*....
gi 2017294875 116 VESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:PRK09282  562 IQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 181-225 3.16e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 54.18  E-value: 3.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2017294875 181 DAIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKAS 225
Cdd:PRK14875    1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKIT 45
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 184-226 1.18e-07

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 52.93  E-value: 1.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2017294875 184 PVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASL 226
Cdd:PLN02744  114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATV 156
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 75-155 2.27e-07

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 52.06  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  75 MPALSSTMTEGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAIIVENEADIASV 154
Cdd:PLN02226   96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQV 175


                  .
gi 2017294875 155 S 155
Cdd:PLN02226  176 T 176
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 184-233 4.52e-07

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: 46.44  E-value: 4.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017294875 184 PVMMPALSSTMKEGkISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEM--EIPAP 48
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 182-276 6.77e-07

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 50.40  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKasLSQTLPAPRLSPLPD--------------------- 240
Cdd:TIGR02927   2 AESVKMPALGESVTEGTVTSWLKAVGDTVEADEPLLEVSTDK--VDTEIPSPAAGVLLEirapeddtvevggvlaiigep 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017294875 241 ----SPLSQPLPSPRLAPLPASPRSQPLPSPRLPAPRLCP 276
Cdd:TIGR02927  80 geagSEPAPAAPEPEAAPEPEAPAPAPTPAAEAPAPAAPQ 119
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 185-233 7.75e-07

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: 45.90  E-value: 7.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2017294875 185 VMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLsqTLPAP 233
Cdd:cd06663     2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATS--DVEAP 48
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 57-141 1.28e-05

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 44.47  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  57 VVRRAPPPGMEVKQSTITMPALSSTMTE---GKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGE 133
Cdd:PRK05641   62 AVPSAPTPVAPAAPAPAPASAGENVVTApmpGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGD 141


                  ....*...
gi 2017294875 134 TADVGAPV 141
Cdd:PRK05641  142 TVDTGQPL 149
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 94-144 3.39e-05

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: 42.96  E-value: 3.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017294875  94 VGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:COG0511    85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
61-141 7.66e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 44.15  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875  61 APPPGMEVKQSTITMPA-LSstmteGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGA 139
Cdd:PRK14040  513 AAAAAAPAAAAGEPVTApLA-----GNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGD 587


                  ..
gi 2017294875 140 PV 141
Cdd:PRK14040  588 TL 589
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 75-138 7.98e-05

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 40.16  E-value: 7.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017294875  75 MPALSSTMTeGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVG 138
Cdd:PRK08225    1 MTKVYASMA-GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEG 63
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
182-233 7.03e-04

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 40.97  E-value: 7.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017294875 182 AIPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLSqtLPAP 233
Cdd:PRK05704    2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLE--VPAP 51
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 179-225 2.39e-03

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 39.28  E-value: 2.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2017294875 179 DVDAIPVmmPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKAS 225
Cdd:PTZ00144   43 SIKVIKV--PTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVS 87
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 183-273 3.27e-03

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: 38.95  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017294875 183 IPVMMPALSSTMKEGKISSWLVGVGDKVDAGDMLLVVESDKASLS-----------------------QTLPAPRLSPLP 239
Cdd:TIGR01347   1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEvpspadgvlqeilfkegdtvesgQVLAILEEGNDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2017294875 240 DSPLSQPL----PSPRLAPLPASPRSQPLPSPRLPAPR 273
Cdd:TIGR01347  81 TAAPPAKSgeekEETPAASAAAAPTAAANRPSLSPAAR 118
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 74-138 3.35e-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: 39.29  E-value: 3.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017294875   74 TMPalsstmteGKISSWLMGVGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVG 138
Cdd:COG1038   1082 PMP--------GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAG 1138
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 189-223 3.91e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.67  E-value: 3.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2017294875 189 ALSSTMKeGKISSWLVGVGDKVDAGDMLLVVESDK 223
Cdd:PRK09282  524 AVTSPMP-GTVVKVKVKEGDKVKAGDTVLVLEAMK 557
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
94-144 4.07e-03

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 35.76  E-value: 4.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017294875  94 VGDKVDAGDMVLVVESDKADMDVESYEEGYIAKILVGEGETADVGAPVAII 144
Cdd:PRK07051   28 VGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 197-221 5.95e-03

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: 34.70  E-value: 5.95e-03
                          10        20
                  ....*....|....*....|....*
gi 2017294875 197 GKISSWLVGVGDKVDAGDMLLVVES 221
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEA 32
 
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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