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Conserved domains on  [gi|2508938833|ref|WP_283240972|]
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biotin/lipoyl-containing protein, partial [Pseudoalteromonas sp. S327]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
aceF super family cl36067
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-109 5.04e-41

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


The actual alignment was detected with superfamily member PRK11854:

Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 142.45  E-value: 5.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPE-APAKTEASAPAEASGSSTKEVTVPDIGDD 79
Cdd:PRK11854   37 VEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAADAAPAqAEEKKEAAPAAAPAAAAAKDVHVPDIGSD 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 2508938833  80 EVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11854  117 EVEVTEILVKVGDTVEAEQSLITVEGDKAS 146
 
Name Accession Description Interval E-value
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-109 5.04e-41

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 142.45  E-value: 5.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPE-APAKTEASAPAEASGSSTKEVTVPDIGDD 79
Cdd:PRK11854   37 VEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAADAAPAqAEEKKEAAPAAAPAAAAAKDVHVPDIGSD 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 2508938833  80 EVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11854  117 EVEVTEILVKVGDTVEAEQSLITVEGDKAS 146
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 1-109 5.62e-30

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: 111.51  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPE-------------APAKTEASAPAEASGSS 67
Cdd:TIGR01348  36 LESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQAEAkkeaapaptagapAPAAQAQAAPAAGQSSG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2508938833  68 TKEVTVPDIGDDE-VEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:TIGR01348 116 VQEVTVPDIGDIEkVTVIEVLVKVGDTVSADQSLITLESDKAS 158
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-38 8.38e-09

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: 48.14  E-value: 8.38e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:COG0508    39 VETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 1-38 3.98e-08

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: 46.24  E-value: 3.98e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:cd06849    37 VETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 1-38 2.65e-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: 44.13  E-value: 2.65e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:pfam00364  36 VEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
Name Accession Description Interval E-value
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-109 5.04e-41

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 142.45  E-value: 5.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPE-APAKTEASAPAEASGSSTKEVTVPDIGDD 79
Cdd:PRK11854   37 VEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAADAAPAqAEEKKEAAPAAAPAAAAAKDVHVPDIGSD 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 2508938833  80 EVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11854  117 EVEVTEILVKVGDTVEAEQSLITVEGDKAS 146
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-109 5.11e-39

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 137.06  E-value: 5.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSqsePEAPAKTEASAPAEAS--GSSTKEVTVPDIGD 78
Cdd:PRK11854  140 VEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAP---AAAPAAAEAAAPAAAPaaAAGVKDVNVPDIGG 216

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2508938833  79 DEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11854  217 DEVEVTEVMVKVGDKVEAEQSLITVEGDKAS 247
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-109 1.36e-34

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 124.16  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPEAPAKTEASAPAE--------------ASGS 66
Cdd:PRK11855   38 VETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAAAAAAAPAAAAAPAAAAAAapapaaaapaaaaaAAGG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2508938833  67 STKEVTVPDIGD-DEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11855  118 GVVEVKVPDIGEiTEVEVIEWLVKVGDTVEEDQSLITVETDKAT 161
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 1-109 5.62e-30

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: 111.51  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPE-------------APAKTEASAPAEASGSS 67
Cdd:TIGR01348  36 LESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQAEAkkeaapaptagapAPAAQAQAAPAAGQSSG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2508938833  68 TKEVTVPDIGDDE-VEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:TIGR01348 116 VQEVTVPDIGDIEkVTVIEVLVKVGDTVSADQSLITLESDKAS 158
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 1-74 1.16e-16

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 73.70  E-value: 1.16e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPEAPAKTEASAPAEASGSSTKEVTVP 74
Cdd:PRK11855  155 VETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAP 228
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 1-63 1.20e-16

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 73.88  E-value: 1.20e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFE--GEASGSQSEPEAPAKTEASAPAEA 63
Cdd:PRK11854  241 VEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEveGAAPAAAPAKQEAAAPAPAAAKAE 305
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 1-89 2.98e-14

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 66.74  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPEAPAKTEASAPAEASGSSTKEVTVPDIGDDE 80
Cdd:PRK11856   39 VETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPA 118


                  ....*....
gi 2508938833  81 VEVTEIMVA 89
Cdd:PRK11856  119 APAAAAAKA 127
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 1-64 6.09e-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: 66.05  E-value: 6.09e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASgSQSEPEAPAKTEASAPAEAS 64
Cdd:TIGR01348 152 LESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGS-TPATAPAPASAQPAAQSPAA 214
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 68-109 5.37e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 63.48  E-value: 5.37e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2508938833  68 TKEVTVPDIGDDEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11854    2 AIEIKVPDIGADEVEVTEILVKVGDKVEAEQSLITVEGDKAS 43
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-70 3.52e-12

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 61.00  E-value: 3.52e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   2 EGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLI-MIFEGEASGSQSEPEAPAKTEASAPAEASGSSTKE 70
Cdd:PRK05704   40 ETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLgRIDEGAAAGAAAAAAAAAAAAAAAPAQAQAAAAAE 109
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 69-109 9.57e-12

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 59.84  E-value: 9.57e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2508938833  69 KEVTVPDIGD-DEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:PRK11855    3 IEFKVPDIGEvVEVEVIEWLVKEGDTVEEDQPLVTVETDKAT 44
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 69-109 1.91e-09

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: 53.34  E-value: 1.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2508938833  69 KEVTVPDIGD-DEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:TIGR01348   1 TEIKVPDIGDnEEGEVIEVLVKPGDKVEAGQSLITLESDKAS 42
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 1-38 8.38e-09

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: 48.14  E-value: 8.38e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:COG0508    39 VETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 1-76 1.01e-08

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: 51.27  E-value: 1.01e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASGSQSEPEAPAKTEASAPAEASGSSTKEVTVPDI 76
Cdd:TIGR01347  37 IETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPPAKSGEEKEETPAASAAAAPTAAANRPS 112
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 1-38 3.98e-08

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: 46.24  E-value: 3.98e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:cd06849    37 VETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 1-38 2.65e-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: 44.13  E-value: 2.65e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:pfam00364  36 VEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 67-109 4.06e-07

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: 43.90  E-value: 4.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2508938833  67 STKEVTVPDIGD--DEVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:COG0508     1 MAIEIKMPDLGEsmTEGTIVEWLVKEGDTVKEGDPLAEVETDKAT 45
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 68-108 6.55e-07

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 45.94  E-value: 6.55e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2508938833  68 TKEVTVPDIGDD--EVEVTEIMVAVGDSVDEEQSILSVEGDKA 108
Cdd:PRK11856    2 MFEFKMPDLGEGmtEGEIVEWLVKVGDTVKEGQPLAEVETDKA 44
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 69-109 3.18e-06

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: 41.62  E-value: 3.18e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2508938833  69 KEVTVPDIGDD--EVEVTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:cd06849     1 TEIKMPDLGESmtEGTIVEWLVKEGDSVEEGDVLAEVETDKAT 43
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 1-74 8.64e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.62  E-value: 8.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLI-MIFEGEASGSQ----SEPEAPAKTEASAPAEASGSSTKEVTVP 74
Cdd:PRK14875   39 VETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLaVVADAEVSDAEidafIAPFARRFAPEGIDEEDAGPAPRKARIG 117
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 1-74 1.16e-05

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 42.21  E-value: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEG-DTVTTGSLIMIF--EGE-ASGSQSEPEAPAKTEASAPAEASGSSTKEVTVP 74
Cdd:PRK11892   39 IETDKATMEVEAVDEGTLGKILVPEGtEGVKVNTPIAVLleEGEsASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPA 116
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 1-40 8.49e-05

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 39.83  E-value: 8.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEG 40
Cdd:PRK09282  553 LEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 10-105 2.22e-04

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.67  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833  10 VPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGeasgsqsepeapAKTEASAPAEASGsstkevtvpdigddevEVTEIMVA 89
Cdd:PRK09282  525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEA------------MKMENEIQAPVDG----------------TVKEILVK 576

                          90
                  ....*....|....*.
gi 2508938833  90 VGDSVDEEQSILSVEG 105
Cdd:PRK09282  577 EGDRVNPGDVLMEIEP 592
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 8-38 3.60e-04

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: 35.85  E-value: 3.60e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2508938833   8 MEVPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 1-68 4.20e-04

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 38.12  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTG-SLIMIFEGEASG------------SQSEPEAPAKTEASAPAEASGSS 67
Cdd:PTZ00144   81 IETDKVSVDIRAPASGVITKIFAEEGDTVEVGaPLSEIDTGGAPPaaapaaaaaakaEKTTPEKPKAAAPTPEPPAASKP 160


                  .
gi 2508938833  68 T 68
Cdd:PTZ00144  161 T 161
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
2-36 4.45e-04

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 37.99  E-value: 4.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2508938833   2 EGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIM 36
Cdd:PRK14040  556 EAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 69-109 4.57e-04

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: 36.04  E-value: 4.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2508938833  69 KEVTVPDIGDDEVE-VTEIMVAVGDSVDEEQSILSVEGDKAS 109
Cdd:pfam00364   1 TEIKSPMIGESVREgVVEWLVKVGDKVKAGQPLAEVEAMKME 42
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 1-72 9.08e-04

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 37.04  E-value: 9.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508938833   1 VEGDKASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGEASG------SQSEPEAPAkTEASAPAEASGSSTKEVT 72
Cdd:PLN02226  128 IETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAasqvtpSQKIPETTD-PKPSPPAEDKQKPKVESA 204
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 8-38 2.21e-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: 35.83  E-value: 2.21e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2508938833    8 ME--VPAAQAGTVKEIKVSEGDTVTTGSLIMIF 38
Cdd:COG1038   1112 MEttITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 8-40 2.71e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 35.50  E-value: 2.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2508938833    8 ME--VPAAQAGTVKEIKVSEGDTVTTGSLIMIFEG 40
Cdd:PRK12999  1112 MEttITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
6-103 5.47e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 34.91  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833   6 ASMEVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEGeasgsqsepeapAKTEASAPAEASGsstkevtvpdigddevEVTE 85
Cdd:PRK14040  523 AGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEA------------MKMETEIRAAQAG----------------TVRG 574

                          90
                  ....*....|....*...
gi 2508938833  86 IMVAVGDSVDEEQSILSV 103
Cdd:PRK14040  575 IAVKEGDAVAVGDTLLTL 592
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 9-95 7.42e-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: 34.28  E-value: 7.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508938833    9 EVPAAQAGTVKEIKVSEGDTVTTGSLIMIFEgeasgsqsepeapA-KTEASAPAEASGsstkevtvpdigddevEVTEIM 87
Cdd:COG1038   1078 HIGAPMPGTVVKVLVKEGDEVKKGDPLLTIE-------------AmKMETTITAPRDG----------------TVKEVL 1128


                   ....*...
gi 2508938833   88 VAVGDSVD 95
Cdd:COG1038   1129 VKEGDQVE 1136
 
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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