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Conserved domains on  [gi|375366772|gb|EHS70753|]
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putative acetyl-CoA carboxylase, biotin carboxyl carrier protein [Staphylococcus aureus subsp. aureus IS-125]

Protein Classification

acetyl-CoA carboxylase biotin carboxyl carrier protein( domain architecture ID 11423502)

acetyl-CoA carboxylase biotin carboxyl carrier protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA

CATH:  2.40.50.100
Gene Ontology:  GO:0003989|GO:0006633|GO:0009317
PubMed:  1370469
SCOP:  4002909
TCDB:  3.B.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-149 1.11e-32

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: 112.30  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772   9 IIKLVKENDVKKFKYKNFEDEIEIdftdSNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYHDIKSPMIGTFFLQDS 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRI----KRGGAAAAAPVAAPAAAAPAAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375366772  89 KELtEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:COG0511   77 PGA-KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-149 1.11e-32

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: 112.30  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772   9 IIKLVKENDVKKFKYKNFEDEIEIdftdSNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYHDIKSPMIGTFFLQDS 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRI----KRGGAAAAAPVAAPAAAAPAAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375366772  89 KELtEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:COG0511   77 PGA-KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-149 2.97e-29

acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273123 [Multi-domain]  Cd Length: 155  Bit Score: 104.53  E-value: 2.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772    1 MNIEKIEQIIKLVKENDVKKFKYKNFEDEIEID-------FTDSNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYH 73
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSVRLSkaaaaasFSVVQQAAAPVPAQVPAQSSAAVPAPAPAAPAPAADIKGH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772   74 DIKSPMIGTFFLQDSKElTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:TIGR00531  81 IVRSPMVGTFYRAPSPD-AKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 75-148 1.49e-19

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: 76.69  E-value: 1.49e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375366772  75 IKSPMIGTFflqdskelTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:cd06850    2 VTAPMPGTV--------VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
73-148 2.94e-19

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 76.59  E-value: 2.94e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772  73 HDIKSPMIGTFFLQDSKElTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK07051   4 HEIVSPLPGTFYRRPSPD-APPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 73-148 5.39e-16

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: 68.01  E-value: 5.39e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772   73 HDIKSPMIGTFflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:pfam00364   1 TEIKSPMIGES---VREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-149 1.11e-32

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: 112.30  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772   9 IIKLVKENDVKKFKYKNFEDEIEIdftdSNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYHDIKSPMIGTFFLQDS 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRI----KRGGAAAAAPVAAPAAAAPAAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375366772  89 KELtEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:COG0511   77 PGA-KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-149 2.97e-29

acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273123 [Multi-domain]  Cd Length: 155  Bit Score: 104.53  E-value: 2.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772    1 MNIEKIEQIIKLVKENDVKKFKYKNFEDEIEID-------FTDSNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYH 73
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSVRLSkaaaaasFSVVQQAAAPVPAQVPAQSSAAVPAPAPAAPAPAADIKGH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772   74 DIKSPMIGTFFLQDSKElTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:TIGR00531  81 IVRSPMVGTFYRAPSPD-AKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 75-148 1.49e-19

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: 76.69  E-value: 1.49e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375366772  75 IKSPMIGTFflqdskelTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:cd06850    2 VTAPMPGTV--------VKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
73-148 2.94e-19

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 76.59  E-value: 2.94e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772  73 HDIKSPMIGTFFLQDSKElTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK07051   4 HEIVSPLPGTFYRRPSPD-APPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 74-149 2.85e-18

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 79.89  E-value: 2.85e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772  74 DIKSPMIGTFflqdskelTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK09282 524 AVTSPMPGTV--------VKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 75-148 3.00e-17

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 75.65  E-value: 3.00e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366772  75 IKSPMIGTFFlqDSKELTEP-IVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PLN02983 200 LKSPMAGTFY--RSPAPGEPpFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVI 272
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 73-148 5.39e-16

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: 68.01  E-value: 5.39e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772   73 HDIKSPMIGTFflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:pfam00364   1 TEIKSPMIGES---VREGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 69-148 2.14e-08

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: 51.62  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772   69 TNDYHdIKSPMIGTfflqdskeLTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:COG1038  1074 GNPGH-IGAPMPGT--------VVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 69-149 2.33e-08

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 51.68  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366772   69 TNDYHdIKSPMIGTfflqdskeLTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK12999 1074 GNPGH-VGAPMPGS--------VVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144


                  .
gi 375366772  149 K 149
Cdd:PRK12999 1145 E 1145
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 96-148 2.63e-08

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: 48.21  E-value: 2.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375366772  96 VNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:cd06663   21 KKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 75-149 2.82e-07

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 46.73  E-value: 2.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366772  75 IKSPMIGTfflqdskeLTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK06549  64 MPSPMPGT--------ILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 90-148 1.90e-06

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: 43.13  E-value: 1.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 375366772  90 ELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:COG0508   18 TIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 75-149 6.87e-06

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 44.29  E-value: 6.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375366772  75 IKSPMIGtfflqDS---KELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PTZ00144  47 IKVPTMG-----DSiseGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 97-148 1.14e-05

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: 43.57  E-value: 1.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 375366772   97 NVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:TIGR01347  23 KVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL 74
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
96-149 1.34e-05

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 43.67  E-value: 1.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375366772  96 VNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK05704  24 KKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID 77
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
74-148 4.86e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 41.84  E-value: 4.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366772  74 DIKSPMIGTFFlqdskeltEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK14040 526 PVTAPLAGNIF--------KVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 73-149 7.79e-05

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 41.35  E-value: 7.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375366772  73 HDIKSPMIGTFflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK11855 120 VEVKVPDIGEI---TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 74-149 1.08e-04

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.96  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772  74 DIKSPMIGTFflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK11855   4 EFKVPDIGEV---VEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 74-149 1.20e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.76  E-value: 1.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366772  74 DIKSPMIGTfflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK11854 208 DVNVPDIGG----DEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 73-145 1.52e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.37  E-value: 1.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375366772  73 HDIKSPMIGTfflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVL 145
Cdd:PRK11854   3 IEIKVPDIGA----DEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALI 71
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 96-149 1.68e-04

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 40.47  E-value: 1.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375366772  96 VNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK 149
Cdd:PRK14042 541 VSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 93-134 2.20e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 40.15  E-value: 2.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 375366772  93 EPIVNVGDKVNKGDIIGYVEAM-----KVLneVTTDVAGEITEIVAD 134
Cdd:PRK04192 121 TPTVKVGDKVEAGDILGTVQETpsiehKIM--VPPGVSGTVKEIVSE 165
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 74-131 7.00e-04

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: 38.70  E-value: 7.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 375366772   74 DIKSPMIGTFflqDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEI 131
Cdd:TIGR01348   2 EIKVPDIGDN---EEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEI 56
ATP-synt_ab_Xtn pfam16886
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ...
 93-149 8.40e-04

ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.


Pssm-ID: 465299 [Multi-domain]  Cd Length: 120  Bit Score: 36.99  E-value: 8.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375366772   93 EPIVNVGDKVNKGDIIGYV---EAM--KVLneVTTDVAGEITEIVADhGtnvEY--DQVLVRIK 149
Cdd:pfam16886  37 TPTVKVGDKVSGGDILGTVqetSLIehKIM--VPPGVSGTVTEIAPE-G---EYtvEDTIAEVE 94
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 96-148 4.77e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 36.08  E-value: 4.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 375366772  96 VNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK14875  24 VQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVV 76
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 91-111 7.96e-03

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 33.72  E-value: 7.96e-03
                         10        20
                 ....*....|....*....|.
gi 375366772  91 LTEPIVNVGDKVNKGDIIGYV 111
Cdd:cd12797   50 LSSILVKVGQRVKKGQVIGTV 70
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 95-148 8.32e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 33.22  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375366772  95 IVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRI 148
Cdd:PRK08225  16 VVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
rpoB PRK00405
DNA-directed RNA polymerase subunit beta; Reviewed
 94-108 8.60e-03

DNA-directed RNA polymerase subunit beta; Reviewed


Pssm-ID: 234749 [Multi-domain]  Cd Length: 1112  Bit Score: 35.46  E-value: 8.60e-03
                          10
                  ....*....|....*
gi 375366772   94 PIVNVGDKVNKGDII 108
Cdd:PRK00405  688 PIVKVGDRVEKGDVL 702
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 86-149 9.67e-03

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 35.38  E-value: 9.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375366772   86 QDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNE---VTTDVAGEITEIvADHGtnvEY--DQVLVRIK 149
Cdd:PRK14698  114 RDKKWHFIPKVKVGDKVVGGDIIGEVPETSIITHkimVPPGIEGEIVEI-ADEG---EYtiEEVIAKVK 178
 
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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