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Conserved domains on  [gi|547883143|ref|WP_022288466|]
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MULTISPECIES: 3-isopropylmalate dehydratase small subunit [Oscillospiraceae]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 5-159 8.76e-103

3-isopropylmalate dehydratase small subunit; Reviewed


:

Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 291.35  E-value: 8.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:PRK00439   2 GRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVIA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143  85 KTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:PRK00439  82 KSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLK 156
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 5-159 8.76e-103

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 291.35  E-value: 8.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:PRK00439   2 GRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVIA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143  85 KTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:PRK00439  82 KSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLK 156
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-159 9.44e-94

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: 268.20  E-value: 9.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143    5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143   85 KTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVK 155
HacB2_Meth NF040625
homoaconitase small subunit;
5-156 3.58e-70

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 208.80  E-value: 3.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:NF040625   6 GKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAIIA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547883143  85 KTFARIFYRNAINIGLPIIECEEAAEKidnGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLN 156
Cdd:NF040625  86 KSFARIFYRNAINIGLPVIVADIEADD---GDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVN 154
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 5-156 8.20e-66

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: 198.86  E-value: 8.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKY-GDNVDTDVIIPARYLNTPDMQELAQHCMEDI------DVDFAKN---VQKGDIMVAKSNFGCGSSREHAPAAI 74
Cdd:COG0066    8 GRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFVLNqprYQGADILVAGRNFGCGSSREHAPWAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  75 KASGISCVIAKTFARIFYRNAINIGLPIIEC-EEAAEKI------DNGDEVEIDFDSGVITNKTKnETYQGQsFPEFLIN 147
Cdd:COG0066   88 KDYGFRAVIAPSFADIFYRNAINNGLLPIELpEEAVDALfaaieaNPGDELTVDLEAGTVTNGTG-ETYPFE-IDPFRRE 165


                 ....*....
gi 547883143 148 IINsNGLLN 156
Cdd:COG0066  166 CLL-NGLDD 173
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-159 5.44e-54

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 167.61  E-value: 5.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   1 MKACGKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGIS 80
Cdd:NF040604   1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  81 CVIAKTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVItnKTKNETYQGQSFPEFLI-NIINSNGLLNSLK 159
Cdd:NF040604  81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKI--IINDKKTLNCEVPKGIEkEILDAGGLINYAK 158
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.65e-40

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: 131.17  E-value: 1.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   9 KYGDNVDTDVIIPARYLntpdmqelaqhcmedidvdfaknvqkGDIMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFA 88
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 547883143  89 RIFYRNAINIG-LPIIECEEAAEKI--DNGDEVEIDF 122
Cdd:cd01577   55 RIFFRNAINNGlLPVTLADEDVEEVeaKPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 3-102 1.71e-17

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: 73.55  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143    3 ACGKVHKygDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIM------------------VAKSNFGCG 64
Cdd:pfam00694  10 KTTPDFN--SNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPdfydaamrykqhgapivvIGGKNFGCG 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 547883143   65 SSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPI 102
Cdd:pfam00694  88 SSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGlLPL 126
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 5-159 8.76e-103

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 291.35  E-value: 8.76e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:PRK00439   2 GRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVIA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143  85 KTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:PRK00439  82 KSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLK 156
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-159 9.44e-94

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: 268.20  E-value: 9.44e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143    5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143   85 KTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVK 155
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 5-159 4.45e-75

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: 221.14  E-value: 4.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143    5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:TIGR02087   1 GRVWKFGDDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547883143   85 KTFARIFYRNAINIGLPIIECEeaAEKIDNGDEVEIDFDSGVITnKTKNETYQGQSFPEFLINIINSNGLLNSLK 159
Cdd:TIGR02087  81 ESFARIFYRNAINIGLPLIEAK--TEGIKDGDEVTVDLETGEIR-VNGNEEYKGEPLPDFLLEILREGGLLEYLK 152
HacB2_Meth NF040625
homoaconitase small subunit;
5-156 3.58e-70

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 208.80  E-value: 3.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIA 84
Cdd:NF040625   6 GKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSAIIA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547883143  85 KTFARIFYRNAINIGLPIIECEEAAEKidnGDEVEIDFDSGVITNKTKNETYQGQSFPEFLINIINSNGLLN 156
Cdd:NF040625  86 KSFARIFYRNAINIGLPVIVADIEADD---GDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVN 154
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 5-156 8.20e-66

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: 198.86  E-value: 8.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKY-GDNVDTDVIIPARYLNTPDMQELAQHCMEDI------DVDFAKN---VQKGDIMVAKSNFGCGSSREHAPAAI 74
Cdd:COG0066    8 GRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFVLNqprYQGADILVAGRNFGCGSSREHAPWAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  75 KASGISCVIAKTFARIFYRNAINIGLPIIEC-EEAAEKI------DNGDEVEIDFDSGVITNKTKnETYQGQsFPEFLIN 147
Cdd:COG0066   88 KDYGFRAVIAPSFADIFYRNAINNGLLPIELpEEAVDALfaaieaNPGDELTVDLEAGTVTNGTG-ETYPFE-IDPFRRE 165


                 ....*....
gi 547883143 148 IINsNGLLN 156
Cdd:COG0066  166 CLL-NGLDD 173
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-159 5.44e-54

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 167.61  E-value: 5.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   1 MKACGKVHKYGDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGIS 80
Cdd:NF040604   1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  81 CVIAKTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVItnKTKNETYQGQSFPEFLI-NIINSNGLLNSLK 159
Cdd:NF040604  81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKI--IINDKKTLNCEVPKGIEkEILDAGGLINYAK 158
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 6-155 2.43e-47

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 151.11  E-value: 2.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   6 KVHKYGDNVDTDVIIPARYlnTPDM---QELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCV 82
Cdd:PRK14023   3 RVWKFGDNINTDDILPGKY--APFMvgeDRFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPEALKMLGIGAI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547883143  83 IAKTFARIFYRNAINIGLPIIECEEAAEKIDNGDEVEIDFDSGVITNKTknETYQGQSFPEFLINIINSNGLL 155
Cdd:PRK14023  81 IAKSYARIFYRNLVNLGIPPFESEEVVDALEDGDEVELDLETGVLTRGG--ETFQLRPPPEFLLEALKEGSIL 151
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.65e-40

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: 131.17  E-value: 1.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   9 KYGDNVDTDVIIPARYLntpdmqelaqhcmedidvdfaknvqkGDIMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFA 88
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 547883143  89 RIFYRNAINIG-LPIIECEEAAEKI--DNGDEVEIDF 122
Cdd:cd01577   55 RIFFRNAINNGlLPVTLADEDVEEVeaKPGDEVEVDL 91
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
11-136 5.76e-32

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 112.91  E-value: 5.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  11 GDNVDTDVIIPARYLNTPDMQELAQHCMED--------IDVDFAKNV---QKGDIMVAKSNFGCGSSREHAPAAIKASGI 79
Cdd:PRK01641  16 RANVDTDQIIPKQFLKRITRTGFGKGLFDDwrylddgqPNPDFVLNQpryQGASILLAGDNFGCGSSREHAPWALADYGF 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547883143  80 SCVIAKTFARIFYRNAINIG-LPIIECEEAAEKI------DNGDEVEIDFDSGVITnkTKNETY 136
Cdd:PRK01641  96 RAVIAPSFADIFYNNCFKNGlLPIVLPEEDVDELfklveaNPGAELTVDLEAQTVT--APDKTF 157
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 5-137 3.77e-31

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 112.26  E-value: 3.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   5 GKVHKYGDNVDTDVIIPARYL-----NTPDMQELAQHCMEDID-------VDFAKNVQKGDIMVAKSNFGCGSSREHAPA 72
Cdd:PLN00072  71 GLCFVVGDNIDTDQIIPAEYLtlvpsKPDEYEKLGSYALIGLPafyktrfVEPGEMKTKYSIIIGGENFGCGSSREHAPV 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547883143  73 AIKASGISCVIAKTFARIFYRNAINIG-LPIIECEE-AAEKIDNGDEVEIDFDSGVITNKTKNETYQ 137
Cdd:PLN00072 151 ALGAAGAKAVVAESYARIFFRNSVATGeVYPLESEVrICEECKTGDVVTVELGNSVLINHTTGKEYK 217
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 12-104 1.79e-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: 96.97  E-value: 1.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  12 DNVDTDVIIPARYLNTPDM--QELAQHCMEDIDVDFAKNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFAR 89
Cdd:cd01674    4 DNLNTDGIYPGKYTYQDDItpEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGN 83

                         90
                 ....*....|....*
gi 547883143  90 IFYRNAINIGLPIIE 104
Cdd:cd01674   84 IFSRNSINNALLSIE 98
PRK07229 PRK07229
aconitate hydratase; Validated
 9-159 4.44e-26

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 102.92  E-value: 4.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   9 KYGDNVDTDVIIPA--RYL----NTPdmqELAQHCMEDIDVDFAKNVQK--GDIMVAKSNFGCGSSREHAPAAIKASGIS 80
Cdd:PRK07229 476 KVGDNITTDHIMPAgaKWLpyrsNIP---NISEFVFEGVDNTFPERAKEqgGGIVVGGENYGQGSSREHAALAPRYLGVK 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  81 CVIAKTFARIFYRNAINIG-LPIIECEEAA-EKIDNGDEVEID-----FDSGVIT--NKTKNETYQGQ-SFPEFLINIIN 150
Cdd:PRK07229 553 AVLAKSFARIHKANLINFGiLPLTFADPADyDKIEEGDVLEIEdlrefLPGGPLTvvNVTKDEEIEVRhTLSERQIEILL 632


                 ....*....
gi 547883143 151 SNGLLNSLK 159
Cdd:PRK07229 633 AGGALNLIK 641
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 9-121 4.71e-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: 90.19  E-value: 4.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   9 KYGDNVDTDVIIPA--RYL----NTPdmqELAQHCMEDIDVDFAKNVQKGD--IMVAKSNFGCGSSREHAPAAIKASGIS 80
Cdd:cd01579    1 KVGDNITTDHIMPAgaKVLplrsNIP---AISEFVFHRVDPTFAERAKAAGpgFIVGGENYGQGSSREHAALAPMYLGVR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 547883143  81 CVIAKTFARIFYRNAINIG-LPI-IECEEAAEKIDNGDEVEID 121
Cdd:cd01579   78 AVLAKSFARIHRANLINFGiLPLtFADEDDYDRFEQGDQLELP 120
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 13-102 2.79e-20

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: 82.56  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   13 NVDTDVIIPARYLNTPDMQELAQHCMED---IDV-------DFAKNV---QKGDIMVAKSNFGCGSSREHAPAAIKASGI 79
Cdd:TIGR00171  18 NVDTDAIIPKQFLKRITRTGFGKHLFFDwrfLDAngkepnpDFVLNQpqyQGASILLARENFGCGSSREHAPWALDDYGF 97

                          90       100
                  ....*....|....*....|....
gi 547883143   80 SCVIAKTFARIFYRNAINIG-LPI 102
Cdd:TIGR00171  98 KVIIAPSFADIFYNNSFKNGlLPI 121
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 9-121 5.99e-18

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: 73.66  E-value: 5.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143   9 KYGDNVDTDVIIPArylntpdmqelaqhcmedidvdfaknvqKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFA 88
Cdd:cd00404    1 KVAGNITTDHISPA----------------------------GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFA 52

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 547883143  89 RIFYRNAINIG-LPI-IECEEAAEKIDNGDEVEID 121
Cdd:cd00404   53 RIFFRNLVDQGlLPLeFADPEDYLKLHTGDELDIY 87
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 3-102 1.71e-17

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: 73.55  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143    3 ACGKVHKygDNVDTDVIIPARYLNTPDMQELAQHCMEDIDVDFAKNVQKGDIM------------------VAKSNFGCG 64
Cdd:pfam00694  10 KTTPDFN--SNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPdfydaamrykqhgapivvIGGKNFGCG 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 547883143   65 SSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPI 102
Cdd:pfam00694  88 SSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGlLPL 126
PRK14812 PRK14812
hypothetical protein; Provisional
 64-154 1.19e-07

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 47.79  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  64 GSSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPIIECEEAAEKIDN---GDEVEIDFDSGVITNKTKNETYQGQ 139
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGmLPIVQPREVREKLAQlkpTDQVTVDLEQQKIISPVEEFTFEID 82

                         90
                 ....*....|....*.
gi 547883143 140 S-FPEFLINIINSNGL 154
Cdd:PRK14812  83 SeWKHKLLNSLDDIGI 98
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 54-121 1.78e-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: 42.46  E-value: 1.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547883143  54 IMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPIIECEEAA-EKIDNGDEVEID 121
Cdd:cd01578   72 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGlLPLTFADPADyDKIHPDDKVDIL 141
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 54-125 2.23e-04

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 40.38  E-value: 2.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547883143  54 IMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPI--IECEEAAEKIDNGDE-VEIDFDSG 125
Cdd:PTZ00092 774 IVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGiLPLqfLNGENADSLGLTGKEqFSIDLNSG 849
PLN00070 PLN00070
aconitate hydratase
 47-113 2.65e-04

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 40.17  E-value: 2.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547883143  47 KNVQKGDIMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFARIFYRNAINIGLpIIECEEAAEKID 113
Cdd:PLN00070 803 KSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGI-IPLCFKSGEDAD 868
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 54-90 3.76e-04

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: 39.70  E-value: 3.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 547883143  54 IMVAKSNFGCGSSREHApAaiKAS---GISCVIAKTFARI 90
Cdd:COG1048  763 VVLAGKEYGTGSSRDWA-A--KGTrllGVKAVIAESFERI 799
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 54-118 4.79e-04

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: 38.41  E-value: 4.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547883143  54 IMVAKSNFGCGSSREHAPAAIKASGISCVIAKTFARIFYRNAINIG-LPI-IECEEAAEKID-NGDEV 118
Cdd:cd01580   99 VILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGiLPLqFPPGENADSLGlTGEET 166
 
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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