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Conserved domains on  [gi|1474167553|ref|WP_118578464|]
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MULTISPECIES: 3-isopropylmalate dehydratase small subunit [Clostridia]

Protein Classification

3-isopropylmalate dehydratase small subunit( domain architecture ID 10011439)

3-isopropylmalate dehydratase small subunit catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate

CATH:  3.20.19.10
EC:  4.2.1.33
Gene Ontology:  GO:0003861|GO:0009098
SCOP:  4003492

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-161 3.58e-108

3-isopropylmalate dehydratase small subunit; Reviewed


:

Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 305.21  E-value: 3.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:PRK00439    1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  84 AETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVNYINAQ 161
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKK 158
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-161 3.58e-108

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 305.21  E-value: 3.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:PRK00439    1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  84 AETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVNYINAQ 161
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKK 158
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-158 2.37e-96

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 131139 [Multi-domain]  Cd Length: 156  Bit Score: 275.13  E-value: 2.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   5 GRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474167553  85 ETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVNYI 158
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYV 154
HacB2_Meth NF040625
homoaconitase small subunit;
4-159 7.11e-70

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 208.41  E-value: 7.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:NF040625    5 KGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAII 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474167553  84 AETFARIFYRNAINIGLPIIecpEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVN-YIN 159
Cdd:NF040625   85 AKSFARIFYRNAINIGLPVI---VADIEADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNhYLK 158
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 4-157 1.36e-68

3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439836 [Multi-domain]  Cd Length: 195  Bit Score: 206.18  E-value: 1.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKY-GDNVDTDVIIPARYLNSSDPAELATHCMEDI------DNTFV---KRVQKGDIIVATKNFGCGSSREHAPIA 73
Cdd:COG0066     7 TGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFVlnqPRYQGADILVAGRNFGCGSSREHAPWA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  74 IKAAGVSCVIAETFARIFYRNAINIGLPIIECPEA-----SKGI--DEGDEVEVDFDSGMIYNRTKGT-EFKgqaFPEFM 145
Cdd:COG0066    87 LKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEavdalFAAIeaNPGDELTVDLEAGTVTNGTGETyPFE---IDPFR 163

                         170
                  ....*....|..
gi 1474167553 146 QKIIkAEGLVNY 157
Cdd:COG0066   164 RECL-LNGLDDI 174
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-158 4.41e-58

homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 178.39  E-value: 4.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   1 MQAKGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVS 80
Cdd:NF040604    1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  81 CVIAETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKgTEFKGQAFPEFMQKIIKAEGLVNYI 158
Cdd:NF040604   81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKIIINDK-KTLNCEVPKGIEKEILDAGGLINYA 157
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.73e-42

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 136.56  E-value: 1.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   9 KYGDNVDTDVIIPARYLnssdpaelathcmedidntfvkrvqkGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFA 88
Cdd:cd01577     1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474167553  89 RIFYRNAINIG-LPIIECPEASKGI--DEGDEVEVDF 122
Cdd:cd01577    55 RIFFRNAINNGlLPVTLADEDVEEVeaKPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 12-108 2.73e-19

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 78.56  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  12 DNVDTDVIIPARYLNSSDPAELATHC-----------------MEDIDNTFVKRVQKGDIIVAT-KNFGCGSSREHAPIA 73
Cdd:pfam00694  17 SNVDTDLIIPKQFLGTIANIGIGNINfegwrygkvrylpdgenPDFYDAAMRYKQHGAPIVVIGgKNFGCGSSREHAAWA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474167553  74 IKAAGVSCVIAETFARIFYRNAINIGLPIIECPEA 108
Cdd:pfam00694  97 LRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-161 3.58e-108

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 305.21  E-value: 3.58e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:PRK00439    1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  84 AETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVNYINAQ 161
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKK 158
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-158 2.37e-96

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 131139 [Multi-domain]  Cd Length: 156  Bit Score: 275.13  E-value: 2.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   5 GRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474167553  85 ETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVNYI 158
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYV 154
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 5-158 9.72e-73

3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.


Pssm-ID: 273961 [Multi-domain]  Cd Length: 154  Bit Score: 215.36  E-value: 9.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   5 GRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIA 84
Cdd:TIGR02087   1 GRVWKFGDDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1474167553  85 ETFARIFYRNAINIGLPIIECPeaSKGIDEGDEVEVDFDSGMIyNRTKGTEFKGQAFPEFMQKIIKAEGLVNYI 158
Cdd:TIGR02087  81 ESFARIFYRNAINIGLPLIEAK--TEGIKDGDEVTVDLETGEI-RVNGNEEYKGEPLPDFLLEILREGGLLEYL 151
HacB2_Meth NF040625
homoaconitase small subunit;
4-159 7.11e-70

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 208.41  E-value: 7.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:NF040625    5 KGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAII 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1474167553  84 AETFARIFYRNAINIGLPIIecpEASKGIDEGDEVEVDFDSGMIYNRTKGTEFKGQAFPEFMQKIIKAEGLVN-YIN 159
Cdd:NF040625   85 AKSFARIFYRNAINIGLPVI---VADIEADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNhYLK 158
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 4-157 1.36e-68

3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439836 [Multi-domain]  Cd Length: 195  Bit Score: 206.18  E-value: 1.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   4 KGRAFKY-GDNVDTDVIIPARYLNSSDPAELATHCMEDI------DNTFV---KRVQKGDIIVATKNFGCGSSREHAPIA 73
Cdd:COG0066     7 TGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFVlnqPRYQGADILVAGRNFGCGSSREHAPWA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  74 IKAAGVSCVIAETFARIFYRNAINIGLPIIECPEA-----SKGI--DEGDEVEVDFDSGMIYNRTKGT-EFKgqaFPEFM 145
Cdd:COG0066    87 LKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEavdalFAAIeaNPGDELTVDLEAGTVTNGTGETyPFE---IDPFR 163

                         170
                  ....*....|..
gi 1474167553 146 QKIIkAEGLVNY 157
Cdd:COG0066   164 RECL-LNGLDDI 174
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-158 4.41e-58

homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 178.39  E-value: 4.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   1 MQAKGRAFKYGDNVDTDVIIPARYLNSSDPAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVS 80
Cdd:NF040604    1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  81 CVIAETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIYNRTKgTEFKGQAFPEFMQKIIKAEGLVNYI 158
Cdd:NF040604   81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKIIINDK-KTLNCEVPKGIEKEILDAGGLINYA 157
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 6-157 6.01e-46

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 147.64  E-value: 6.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   6 RAFKYGDNVDTDVIIPARY---LNSSDpaELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCV 82
Cdd:PRK14023    3 RVWKFGDNINTDDILPGKYapfMVGED--RFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPEALKMLGIGAI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1474167553  83 IAETFARIFYRNAINIGLPIIECPEASKGIDEGDEVEVDFDSGMIynrTKGTE-FKGQAFPEFMQKIIKAEGLVNY 157
Cdd:PRK14023   81 IAKSYARIFYRNLVNLGIPPFESEEVVDALEDGDEVELDLETGVL---TRGGEtFQLRPPPEFLLEALKEGSILEY 153
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.73e-42

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 136.56  E-value: 1.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   9 KYGDNVDTDVIIPARYLnssdpaelathcmedidntfvkrvqkGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFA 88
Cdd:cd01577     1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1474167553  89 RIFYRNAINIG-LPIIECPEASKGI--DEGDEVEVDF 122
Cdd:cd01577    55 RIFFRNAINNGlLPVTLADEDVEEVeaKPGDEVEVDL 91
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 5-157 3.30e-34

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 120.35  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   5 GRAFKYGDNVDTDVIIPARYLN--SSDPAE---LATHCMEDIDNTFVKR-VQKGD------IIVATKNFGCGSSREHAPI 72
Cdd:PLN00072   71 GLCFVVGDNIDTDQIIPAEYLTlvPSKPDEyekLGSYALIGLPAFYKTRfVEPGEmktkysIIIGGENFGCGSSREHAPV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  73 AIKAAGVSCVIAETFARIFYRNAINIGlPIIECPEASKGIDE---GDEVEVDFDSGMIYNRTKGTEFK----GQAFPefm 145
Cdd:PLN00072  151 ALGAAGAKAVVAESYARIFFRNSVATG-EVYPLESEVRICEEcktGDVVTVELGNSVLINHTTGKEYKlkpiGDAGP--- 226

                         170
                  ....*....|..
gi 1474167553 146 qkIIKAEGLVNY 157
Cdd:PLN00072  227 --VIDAGGIFAY 236
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
11-121 8.58e-31

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 109.83  E-value: 8.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  11 GDNVDTDVIIPARYLNSSDPAELATHCMED--------IDNTFV---KRVQKGDIIVATKNFGCGSSREHAPIAIKAAGV 79
Cdd:PRK01641   16 RANVDTDQIIPKQFLKRITRTGFGKGLFDDwrylddgqPNPDFVlnqPRYQGASILLAGDNFGCGSSREHAPWALADYGF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1474167553  80 SCVIAETFARIFYRNAINIGLPIIECPEAS-------KGIDEGDEVEVD 121
Cdd:PRK01641   96 RAVIAPSFADIFYNNCFKNGLLPIVLPEEDvdelfklVEANPGAELTVD 144
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 12-114 1.01e-26

Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238837 [Multi-domain]  Cd Length: 129  Bit Score: 97.74  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  12 DNVDTDVIIPARYLNSSD--PAELATHCMEDIDNTFVKRVQKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFAR 89
Cdd:cd01674     4 DNLNTDGIYPGKYTYQDDitPEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGN 83

                          90       100
                  ....*....|....*....|....*
gi 1474167553  90 IFYRNAINIGLPIIECPEASKGIDE 114
Cdd:cd01674    84 IFSRNSINNALLSIELPFLVQKLRE 108
PRK07229 PRK07229
aconitate hydratase; Validated
 9-162 2.35e-26

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 103.69  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   9 KYGDNVDTDVIIPA--RYLN--SSDPAeLATHCMEDIDNTFVKRVQK--GDIIVATKNFGCGSSREHAPIAIKAAGVSCV 82
Cdd:PRK07229  476 KVGDNITTDHIMPAgaKWLPyrSNIPN-ISEFVFEGVDNTFPERAKEqgGGIVVGGENYGQGSSREHAALAPRYLGVKAV 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  83 IAETFARIFYRNAINIG-LP-IIECPEASKGIDEGDEVEVD-----FDSG--MIYNRTKGTEFKGQA-FPEFMQKIIKAE 152
Cdd:PRK07229  555 LAKSFARIHKANLINFGiLPlTFADPADYDKIEEGDVLEIEdlrefLPGGplTVVNVTKDEEIEVRHtLSERQIEILLAG 634

                         170
                  ....*....|
gi 1474167553 153 GLVNYINAQH 162
Cdd:PRK07229  635 GALNLIKKKL 644
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 9-121 3.11e-24

Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.


Pssm-ID: 238811 [Multi-domain]  Cd Length: 121  Bit Score: 90.96  E-value: 3.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   9 KYGDNVDTDVIIPA--RYLN-SSDPAELATHCMEDIDNTFVKRVQKGD--IIVATKNFGCGSSREHAPIAIKAAGVSCVI 83
Cdd:cd01579     1 KVGDNITTDHIMPAgaKVLPlRSNIPAISEFVFHRVDPTFAERAKAAGpgFIVGGENYGQGSSREHAALAPMYLGVRAVL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1474167553  84 AETFARIFYRNAINIG-LPI-IECPEASKGIDEGDEVEVD 121
Cdd:cd01579    81 AKSFARIHRANLINFGiLPLtFADEDDYDRFEQGDQLELP 120
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 9-121 2.05e-19

Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.


Pssm-ID: 238236 [Multi-domain]  Cd Length: 88  Bit Score: 77.51  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553   9 KYGDNVDTDVIIPArylnssdpaelathcmedidntfvkrvqKGDIIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFA 88
Cdd:cd00404     1 KVAGNITTDHISPA----------------------------GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFA 52

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474167553  89 RIFYRNAINIG-LPI-IECPEASKGIDEGDEVEVD 121
Cdd:cd00404    53 RIFFRNLVDQGlLPLeFADPEDYLKLHTGDELDIY 87
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 12-108 2.73e-19

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 78.56  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  12 DNVDTDVIIPARYLNSSDPAELATHC-----------------MEDIDNTFVKRVQKGDIIVAT-KNFGCGSSREHAPIA 73
Cdd:pfam00694  17 SNVDTDLIIPKQFLGTIANIGIGNINfegwrygkvrylpdgenPDFYDAAMRYKQHGAPIVVIGgKNFGCGSSREHAAWA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1474167553  74 IKAAGVSCVIAETFARIFYRNAINIGLPIIECPEA 108
Cdd:pfam00694  97 LRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 13-108 5.96e-19

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 129275 [Multi-domain]  Cd Length: 188  Bit Score: 79.09  E-value: 5.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  13 NVDTDVIIPARYLNSSDPAELATHCM----------EDIDNTFVKRV---QKGDIIVATKNFGCGSSREHAPIAIKAAGV 79
Cdd:TIGR00171  18 NVDTDAIIPKQFLKRITRTGFGKHLFfdwrfldangKEPNPDFVLNQpqyQGASILLARENFGCGSSREHAPWALDDYGF 97

                          90       100
                  ....*....|....*....|....*....
gi 1474167553  80 SCVIAETFARIFYRNAINIGLPIIECPEA 108
Cdd:TIGR00171  98 KVIIAPSFADIFYNNSFKNGLLPIRLSYD 126
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 54-90 1.39e-07

Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 49.72  E-value: 1.39e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARI 90
Cdd:COG1048   763 VVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERI 799
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 54-118 1.45e-06

Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238812 [Multi-domain]  Cd Length: 171  Bit Score: 45.73  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIGLPIIECPE----ASKGIDeGDEV 118
Cdd:cd01580    99 VILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPgenaDSLGLT-GEET 166
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 54-127 1.75e-06

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 46.54  E-value: 1.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIGLPIIECPE----ASKGIDEGDEVEVDFDSGMI 127
Cdd:PTZ00092  774 IVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgenaDSLGLTGKEQFSIDLNSGEL 851
acnA PRK12881
aconitate hydratase AcnA;
54-127 7.95e-06

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 44.54  E-value: 7.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIG-LPiIECPE----ASKGIDEGDEVEVDFDSGMI 127
Cdd:PRK12881  762 VVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGvLP-LQFKGgdsrQSLGLTGGETFDIEGLPGEI 839
PRK14812 PRK14812
hypothetical protein; Provisional
 64-151 1.09e-05

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 42.40  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  64 GSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIG-LPIIECPEASKGIDE---GDEVEVDFDSGMIYNRTKgtEFKGQ 139
Cdd:PRK14812    3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGmLPIVQPREVREKLAQlkpTDQVTVDLEQQKIISPVE--EFTFE 80

                          90
                  ....*....|..
gi 1474167553 140 AFPEFMQKIIKA 151
Cdd:PRK14812   81 IDSEWKHKLLNS 92
PRK09277 PRK09277
aconitate hydratase AcnA;
54-118 4.02e-05

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 42.80  E-value: 4.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIG-LPiIECPE----ASKGIDeGDEV 118
Cdd:PRK09277  761 VVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGvLP-LQFKPgesrKTLGLD-GTET 828
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 54-94 5.21e-05

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 40.91  E-value: 5.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRN 94
Cdd:cd01578    72 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 112
PLN00070 PLN00070
aconitate hydratase
 54-125 1.37e-03

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 38.25  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474167553  54 IIVATKNFGCGSSREHAPIAIKAAGVSCVIAETFARIFYRNAINIGL-PI--------------------IECPEASKGI 112
Cdd:PLN00070  810 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIiPLcfksgedadtlgltgherytIDLPSNISEI 889

                          90
                  ....*....|...
gi 1474167553 113 DEGDEVEVDFDSG 125
Cdd:PLN00070  890 KPGQDVTVTTDNG 902
 
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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