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Conserved domains on  [gi|1468295864|ref|WP_117247384|]
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biotin/lipoyl-containing protein, partial [Klebsiella variicola]

Protein Classification

acetyl-CoA carboxylase biotin carboxylase subunit family protein( domain architecture ID 1562446)

acetyl-CoA carboxylase biotin carboxylase subunit family protein similar to Bacillus subtilis alanine--anticapsin ligase that is part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, and to the biotin-containing subunit of transcarboxylase from Propionibacterium shermanii

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12999 super family cl39082
pyruvate carboxylase; Reviewed
 1-155 1.81e-75

pyruvate carboxylase; Reviewed


The actual alignment was detected with superfamily member PRK14040:

Pssm-ID: 476865 [Multi-domain]  Cd Length: 593  Bit Score: 235.60  E-value: 1.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864   1 VALFPQPGLKFLENRHNPAAFEPVPQAEAAQPlAKAEKPAASGIYTVEVEGKAFVVKVSDGGDVSQL---SAAPVAAAPA 77
Cdd:PRK14040  437 YALFPQIGLKFLENRHNPAAFEPVPQAEAAQP-AAKAEPAGSETYTVEVEGKAYVVKVSEGGDISQItpaAPAAAPAAAA 515

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468295864  78 AAPAPAGAGTPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK14040  516 AAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
 
Name Accession Description Interval E-value
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
1-155 1.81e-75

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 235.60  E-value: 1.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864   1 VALFPQPGLKFLENRHNPAAFEPVPQAEAAQPlAKAEKPAASGIYTVEVEGKAFVVKVSDGGDVSQL---SAAPVAAAPA 77
Cdd:PRK14040  437 YALFPQIGLKFLENRHNPAAFEPVPQAEAAQP-AAKAEPAGSETYTVEVEGKAYVVKVSEGGDISQItpaAPAAAPAAAA 515

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468295864  78 AAPAPAGAGTPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK14040  516 AAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 89-154 3.90e-26

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: 93.63  E-value: 3.90e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:cd06850     2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 36-152 1.31e-23

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: 89.57  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  36 AEKPAASGIYTVEVEGKAFVVKVSDGGDVSQL--------SAAPVAAAPAAAPAPAGAGTPVTAPLAGTI-------WKV 100
Cdd:COG0511     2 IELLEESGLTELEVEEGEYKVRIKRGGAAAAApvaapaaaAPAAAAPAAAAAAAAASGGGAVKSPMVGTFyrapspgAKP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1468295864 101 LAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLL 152
Cdd:COG0511    82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLF 133
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 87-154 6.79e-15

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: 65.31  E-value: 6.79e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468295864  87 TPVTAPLAGT-----IWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:pfam00364   1 TEIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 95-154 3.28e-06

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


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 45.64  E-value: 3.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
 
Name Accession Description Interval E-value
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
1-155 1.81e-75

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 235.60  E-value: 1.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864   1 VALFPQPGLKFLENRHNPAAFEPVPQAEAAQPlAKAEKPAASGIYTVEVEGKAFVVKVSDGGDVSQL---SAAPVAAAPA 77
Cdd:PRK14040  437 YALFPQIGLKFLENRHNPAAFEPVPQAEAAQP-AAKAEPAGSETYTVEVEGKAYVVKVSEGGDISQItpaAPAAAPAAAA 515

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468295864  78 AAPAPAGAGTPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK14040  516 AAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 2-152 2.73e-32

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 119.95  E-value: 2.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864   2 ALFPQPGLKFLENRHNPAAFEPVPQAEAAQPlakaEKPAASGIYTVEVEGKAFVVKV-------------SDGGDVSQLS 68
Cdd:PRK09282  429 ALFPQIAKKFLEEREAGELKPEPEPKEAAAA----GAEGIPTEFKVEVDGEKYEVKIegvkaegkrpfylRVDGMPEEVV 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  69 AAPVAAAPAAAPAPAGAGTPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVG 148
Cdd:PRK09282  505 VEPLKEIVVGGRPRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPG 584


                  ....
gi 1468295864 149 DTLL 152
Cdd:PRK09282  585 DVLM 588
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 89-154 3.90e-26

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: 93.63  E-value: 3.90e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:cd06850     2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 36-152 1.31e-23

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: 89.57  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  36 AEKPAASGIYTVEVEGKAFVVKVSDGGDVSQL--------SAAPVAAAPAAAPAPAGAGTPVTAPLAGTI-------WKV 100
Cdd:COG0511     2 IELLEESGLTELEVEEGEYKVRIKRGGAAAAApvaapaaaAPAAAAPAAAAAAAAASGGGAVKSPMVGTFyrapspgAKP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1468295864 101 LAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLL 152
Cdd:COG0511    82 FVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLF 133
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 89-155 1.33e-22

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 92.89  E-value: 1.33e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1468295864   89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK12999  1079 VGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 89-154 3.01e-22

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: 91.68  E-value: 3.01e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468295864   89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:COG1038   1079 IGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 89-154 1.06e-16

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 69.82  E-value: 1.06e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PRK08225    4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 43-154 1.15e-16

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 72.20  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  43 GIYTVEVEGKAFVVKVSDGG-DVSQLSAAPVAAAPAAAPAPAGAGTP-----------------VTAPLAGTIWKVLAAE 104
Cdd:PRK05641   23 GKFRVSFEGKTYEVEAKGLGiDLSAVQEQVPTPAPAPAPAVPSAPTPvapaapapapasagenvVTAPMPGKILRILVRE 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1468295864 105 GQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PRK05641  103 GQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 23-155 1.11e-15

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 69.07  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  23 PVPQAEAAQPLAKAEKPAAsgiytvEVEGKAFVVKVSDGGDVsqlsaapvaaapaaapapagagtpVTAPLAGTIWKVLA 102
Cdd:PRK06549   28 AAPAQPASTPVPVPTEASP------QVEAQAPQPAAAAGADA------------------------MPSPMPGTILKVLV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1468295864 103 AEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK06549   78 AVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 87-154 6.79e-15

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: 65.31  E-value: 6.79e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468295864  87 TPVTAPLAGT-----IWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:pfam00364   1 TEIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 95-155 1.60e-10

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: 53.92  E-value: 1.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:COG0508    17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 95-151 2.51e-09

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: 50.87  E-value: 2.51e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTL 151
Cdd:cd06849    15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 2-154 1.98e-08

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 52.03  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864   2 ALFPQPGLKFLENRHNPaafEPVPQAEAAQplAKAEKPAASGIYTVEVEGKAFVVKVS----------------DGGDVS 65
Cdd:PRK14042  428 AMFPEIGRQFLEQRKNN---QLIPEPLLTQ--SSAPDNSVMSEFDIILHGESYHVKVAgygmiehgqqscflwvDGVPEE 502

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  66 QLSAAPVAAAPAAAPAPAGAGTP--VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGD 143
Cdd:PRK14042  503 VVVQHSELHDKIERSSVNNKIGPgdITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGD 582

                         170
                  ....*....|.
gi 1468295864 144 AVAVGDTLLQL 154
Cdd:PRK14042  583 KVTPGQVLIRV 593
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
89-155 2.18e-08

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 48.47  E-value: 2.18e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468295864  89 VTAPLAGTIWK-------VLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK07051    6 IVSPLPGTFYRrpspdapPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 95-155 7.94e-08

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


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 50.17  E-value: 7.94e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:PRK11856   17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE 77
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 94-145 1.23e-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: 46.28  E-value: 1.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1468295864  94 AGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAV 145
Cdd:cd06663    13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKV 64
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
89-149 2.71e-07

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 45.57  E-value: 2.71e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGD 149
Cdd:PRK05889    5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGD 65
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 95-154 3.28e-06

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


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 45.64  E-value: 3.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 95-154 4.94e-06

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


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 44.87  E-value: 4.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTL 189
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 19-154 6.76e-06

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 44.43  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  19 AAFEPVPQAEAAQPLAKAEKPAASGIYTVEVEGKAFVVKVSDGGDVSQlsaapvaaapaaapapagagtpvtaplaGTIW 98
Cdd:PRK11855   85 AAPAAAAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVEVKVPDIGEITE----------------------------VEVI 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1468295864  99 KVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PRK11855  137 EWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI 192
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 95-154 1.06e-05

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 44.04  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PRK11855   16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 95-152 3.39e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 42.68  E-value: 3.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLL 152
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIM 276
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 95-149 5.87e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.91  E-value: 5.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGD 149
Cdd:PRK11854  118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGS 172
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 95-154 5.99e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.91  E-value: 5.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PRK11854   15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 87-117 2.60e-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: 37.40  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1468295864  87 TPVTAPLAGTIWKVLAAEGQTVSEGEVLLIL 117
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 87-131 4.87e-04

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 39.16  E-value: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1468295864  87 TPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQA 131
Cdd:COG0845    24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQA 68
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 95-155 5.05e-04

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: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQLA 155
Cdd:TIGR01347  15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE 75
PRK06748 PRK06748
hypothetical protein; Validated
 89-151 5.20e-04

hypothetical protein; Validated


Pssm-ID: 180678 [Multi-domain]  Cd Length: 83  Bit Score: 37.15  E-value: 5.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAM-KMETEIRAAQAGTVRGIAVKAGDAVAVGDTL 151
Cdd:PRK06748    7 VYSPCYGKVEKLFVRESSYVYEWEKLALIETIdKQKVEIKVGISGYIESLEVVEGQAIADQKLL 70
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
95-151 1.03e-03

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 38.28  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTL 151
Cdd:PRK05704   17 ATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL 73
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
88-131 1.33e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 35.11  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1468295864  88 PVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQA 131
Cdd:pfam13533   4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
PYC_OADA pfam02436
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ...
 2-56 2.10e-03

Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.


Pssm-ID: 460557 [Multi-domain]  Cd Length: 201  Bit Score: 36.67  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468295864   2 ALFPQPGLKFLENRHNPAAFEPVPQAEAAQPLAKAEKpaasgiYTVEVEGKAFVV 56
Cdd:pfam02436 151 ALYPKVAEKFLKFREKYGDVSVLPTPVFFYGLEPGEE------YEVEIEGGKYLI 199
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 95-154 3.63e-03

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 36.58  E-value: 3.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTLLQL 154
Cdd:PTZ00144   59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 18-154 3.80e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 36.52  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  18 PAAFEPVPQAEAAQPLAKAEKPAASGIYTV--------EVEGKAFVVKVSDGGDVSQlsaapvaaaPAAAPAPAGAGTPV 89
Cdd:PRK11854   79 GAADAAPAQAEEKKEAAPAAAPAAAAAKDVhvpdigsdEVEVTEILVKVGDTVEAEQ---------SLITVEGDKASMEV 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468295864  90 TAPLAGTIWKVLAAEGQTVSEGEVLLILE------AMKMETEIRAAQA---------------------GTVRGIAVKAG 142
Cdd:PRK11854  150 PAPFAGTVKEIKVNVGDKVSTGSLIMVFEvageapAAAPAAAEAAAPAaapaaaagvkdvnvpdiggdeVEVTEVMVKVG 229

                         170
                  ....*....|..
gi 1468295864 143 DAVAVGDTLLQL 154
Cdd:PRK11854  230 DKVEAEQSLITV 241
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
87-131 4.33e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 36.18  E-value: 4.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1468295864  87 TPVTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQA 131
Cdd:COG1566    46 VTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEA 90
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 89-131 5.03e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 36.34  E-value: 5.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1468295864  89 VTAPLAGTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQA 131
Cdd:PRK11855  164 IPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPA 206
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 88-118 5.38e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 33.99  E-value: 5.38e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1468295864  88 PVTAPLAGTIWKVLAAEGQTVSEGEVLLILE 118
Cdd:PRK08225   40 PIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 87-118 6.36e-03

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: 34.87  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1468295864  87 TPVTAPLAGTIWKVLAAEGQTVSEGEVLLILE 118
Cdd:COG0511   105 NEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 95-151 7.28e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 35.69  E-value: 7.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468295864  95 GTIWKVLAAEGQTVSEGEVLLILEAMKMETEIRAAQAGTVRGIAVKAGDAVAVGDTL 151
Cdd:PRK14875   17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
 
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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