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Conserved domains on  [gi|1975911705|emb|CAE3840263|]
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unnamed protein product, partial [Hemiselmis rufescens]

Protein Classification

lipoyl domain-containing protein( domain architecture ID 10160164)

lipoyl domain-containing protein similar to dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenase that 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

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. ...
 93-164 3.52e-32

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: 110.57  E-value: 3.52e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:cd06849     3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 93-164 3.52e-32

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: 110.57  E-value: 3.52e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:cd06849     3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 92-163 3.70e-31

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 116.71  E-value: 3.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  92 VIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:PTZ00144   46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSE 117
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 83-164 1.19e-30

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: 106.69  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:COG0508     1 MAIE------IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIA 74


                  ..
gi 1975911705 163 KF 164
Cdd:COG0508    75 VI 76
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 93-169 9.59e-25

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: 99.04  E-value: 9.59e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKFLKGAT 169
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND 79
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 92-164 7.55e-19

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: 7.55e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1975911705  92 VIPVPAMGDSITEGtVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
Name Accession Description Interval E-value
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 93-164 3.52e-32

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: 110.57  E-value: 3.52e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:cd06849     3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 92-163 3.70e-31

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 116.71  E-value: 3.70e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  92 VIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:PTZ00144   46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSE 117
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 83-164 1.19e-30

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: 106.69  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:COG0508     1 MAIE------IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIA 74


                  ..
gi 1975911705 163 KF 164
Cdd:COG0508    75 VI 76
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
83-169 1.52e-25

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 101.06  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:PRK05704    1 MMVE------IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLG 74


                  ....*..
gi 1975911705 163 KFLKGAT 169
Cdd:PRK05704   75 RIDEGAA 81
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 93-169 9.59e-25

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: 99.04  E-value: 9.59e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKFLKGAT 169
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND 79
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 90-158 3.77e-24

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 97.55  E-value: 3.77e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1975911705  90 ASVIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVG 158
Cdd:PRK11856    2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVG 70
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 83-164 5.85e-22

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 91.81  E-value: 5.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGDsITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:PRK11855    1 MAIE------FKVPDIGE-VVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLA 73


                  ..
gi 1975911705 163 KF 164
Cdd:PRK11855   74 VI 75
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 59-164 9.50e-22

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 91.42  E-value: 9.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  59 APASNPSFPALAHASFNAPRHSRGMAVEGGEASVIPVPAMGDsITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRA 138
Cdd:PRK11855   88 AAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPS 166

                          90       100
                  ....*....|....*....|....*.
gi 1975911705 139 PDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:PRK11855  167 PVAGVVKEIKVKVGDKVSVGSLLVVI 192
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 59-163 1.79e-20

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: 87.76  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  59 APASNPSFPALAHASfNAPRHSRGMAVEGGEASVIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRA 138
Cdd:TIGR02927  96 APEPEAPAPAPTPAA-EAPAPAAPQAGGSGEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPS 174

                          90       100
                  ....*....|....*....|....*
gi 1975911705 139 PDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:TIGR02927 175 PVAGTLLEIRAPEDDTVEVGTVLAI 199
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 92-164 7.55e-19

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: 7.55e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1975911705  92 VIPVPAMGDSITEGtVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:pfam00364   2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 36-168 2.59e-16

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 75.56  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  36 PALAAGSVS-CLRPRGLRTISFSK--APASNPSFPALAHASFNAPRHSRGMAVEGGEASVIPVPAMGDSITEGTVVKWHK 112
Cdd:PLN02226   34 PSLLSGSETgALLHRGNHAHSFHNlaLPGNSGISRSASLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLK 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1975911705 113 AVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKFLKGA 168
Cdd:PLN02226  114 KPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSE 169
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 93-164 1.39e-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: 67.85  E-value: 1.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:cd06663     2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 93-159 6.65e-14

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 68.43  E-value: 6.65e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGG 159
Cdd:PRK14875    5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGA 71
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 83-164 3.13e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 66.95  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGdsITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:PRK11854    1 MAIE------IKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIM 72


                  ..
gi 1975911705 163 KF 164
Cdd:PRK11854   73 IF 74
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 59-164 5.30e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 66.18  E-value: 5.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  59 APASNPSFPALAHASfnaprhsrgmAVEGGEASVIPVPAMGDsiTEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRA 138
Cdd:PRK11854   84 APAQAEEKKEAAPAA----------APAAAAAKDVHVPDIGS--DEVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPA 151

                          90       100
                  ....*....|....*....|....*.
gi 1975911705 139 PDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:PRK11854  152 PFAGTVKEIKVNVGDKVSTGSLIMVF 177
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 57-164 8.23e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 65.79  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  57 SKAPASNPSfPALAHASFNAPrhsrgmaVEGGEASVIPVPAMGDsiTEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEI 136
Cdd:PRK11854  181 GEAPAAAPA-AAEAAAPAAAP-------AAAAGVKDVNVPDIGG--DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEV 250

                          90       100
                  ....*....|....*....|....*...
gi 1975911705 137 RAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:PRK11854  251 PAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 92-152 8.50e-12

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: 62.50  E-value: 8.50e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1975911705  92 VIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEG 152
Cdd:TIGR01349   1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEG 61
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 83-152 6.33e-11

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 59.93  E-value: 6.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  83 MAVEggeasvIPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEG 152
Cdd:PRK11892    1 MAIE------ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEG 64
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 76-164 3.71e-10

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: 57.96  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  76 APRHSRGMAVEGGEASV---IPVPAMGDsITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEG 152
Cdd:TIGR01348  99 APAAQAQAAPAAGQSSGvqeVTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVG 177

                          90
                  ....*....|..
gi 1975911705 153 DTCTVGGDLVKF 164
Cdd:TIGR01348 178 DSVPTGDLILTL 189
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 105-164 5.97e-10

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: 52.80  E-value: 5.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705 105 GTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:cd06850     8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 93-152 1.22e-09

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 56.40  E-value: 1.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEG 152
Cdd:PLN02744  115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDG 174
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 93-163 1.87e-09

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 55.88  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1975911705  93 IPVPAMGDSITEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:PLN02528    1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLK 71
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 93-164 2.32e-08

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: 52.57  E-value: 2.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1975911705  93 IPVPAMGDSiTEGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVKF 164
Cdd:TIGR01348   3 IKVPDIGDN-EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
90-162 2.93e-07

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 49.54  E-value: 2.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1975911705  90 ASVIPVPAMGDSIT---EGTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLV 162
Cdd:PRK14040  515 AAAAPAAAAGEPVTaplAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 105-163 1.67e-06

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 47.41  E-value: 1.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1975911705 105 GTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:PRK14042  534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIR 592
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 114-153 1.04e-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: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1975911705 114 VGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGD 153
Cdd:COG0511    85 VGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ 124
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 105-158 1.38e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 41.37  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1975911705 105 GTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGDTCTVG 158
Cdd:PRK09282  531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPG 584
GcvH COG0509
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ...
 112-146 6.49e-04

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: 37.80  E-value: 6.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1975911705 112 KAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITE 146
Cdd:COG0509    45 PEVGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVE 79
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 61-162 1.81e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 36.71  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  61 ASNPSFPALAHASFNAPRHSRGMAVEGGEASVIPVPAMGDSITE---GTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIR 137
Cdd:PRK06549   23 APAQAAAPAQPASTPVPVPTEASPQVEAQAPQPAAAAGADAMPSpmpGTILKVLVAVGDQVTENQPLLILEAMKMENEIV 102

                          90       100
                  ....*....|....*....|....*
gi 1975911705 138 APDSGVITELCYQEGDTCTVGGDLV 162
Cdd:PRK06549  103 ASSAGTVTAIHVTPGQVVNPGDGLI 127
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 59-163 6.32e-03

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 35.61  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1975911705  59 APASNPSfPALAHASFNAPrhsrgMAVEGGEASVIPVPAMGDSITE---GTVVKWHKAVGDQVEMDEIMCEVETDKVTVE 135
Cdd:PRK05641   50 EQVPTPA-PAPAPAVPSAP-----TPVAPAAPAPAPASAGENVVTApmpGKILRILVREGQQVKVGQGLLILEAMKMENE 123

                          90       100
                  ....*....|....*....|....*...
gi 1975911705 136 IRAPDSGVITELCYQEGDTCTVGGDLVK 163
Cdd:PRK05641  124 IPAPKDGVVKKILVKEGDTVDTGQPLIE 151
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 105-153 7.71e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 33.99  E-value: 7.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1975911705 105 GTVVKWHKAVGDQVEMDEIMCEVETDKVTVEIRAPDSGVITELCYQEGD 153
Cdd:PRK08225   10 GNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGD 58
 
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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