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Conserved domains on  [gi|501284105|ref|WP_012327123|]
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3-isopropylmalate dehydratase small subunit [Shewanella woodyi]

Protein Classification

3-isopropylmalate dehydratase small subunit( domain architecture ID 10011702)

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 Symbol:  leuD
Gene Ontology:  GO:0003861|GO:0009098
PubMed:  20938981
SCOP:  4003492

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-200 3.92e-134

3-isopropylmalate dehydratase small subunit;


:

Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 373.69  E-value: 3.92e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDagDEPNPEFTLNQSRYKGASILISKENFG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDD--GQPNPDFVLNQPRYQGASILLAGDNFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  81 CGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVQANEGAEITVDLEGLTVTSPSGaVF 160
Cdd:PRK01641  79 CGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVTAPDK-TF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 501284105 161 SFEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAWK 200
Cdd:PRK01641 158 PFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFR 197
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-200 3.92e-134

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 373.69  E-value: 3.92e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDagDEPNPEFTLNQSRYKGASILISKENFG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDD--GQPNPDFVLNQPRYQGASILLAGDNFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  81 CGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVQANEGAEITVDLEGLTVTSPSGaVF 160
Cdd:PRK01641  79 CGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVTAPDK-TF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 501284105 161 SFEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAWK 200
Cdd:PRK01641 158 PFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFR 197
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-199 1.32e-115

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: 326.74  E-value: 1.32e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   2 EAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDdagdEPNPEFTLNQSRYKGASILISKENFGC 81
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR----SPDPDFVLNQPRYQGADILVAGRNFGC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  82 GSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVQANEGAEITVDLEGLTVTSPSGAVFS 161
Cdd:COG0066   77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTNGTGETYP 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 501284105 162 FEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAW 199
Cdd:COG0066  157 FEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAW 194
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 1-189 9.20e-97

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: 279.01  E-value: 9.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105    1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDAGDEPNPEFTLNQSRYKGASILISKENFG 80
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDANGKEPNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   81 CGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVqANEGAEITVDLEGLTVTSPSGAVF 160
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQV-ENQGLQMTVDLENQLIHDSEGKVY 159

                         170       180
                  ....*....|....*....|....*....
gi 501284105  161 SFEIAGSARHNMLNGLDAIGLTLAYDVQI 189
Cdd:TIGR00171 160 SFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 1-125 3.80e-48

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: 153.68  E-value: 3.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105    1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDAG--DEPNPEFTLNQSRYK--GASILIS- 75
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYlpDGENPDFYDAAMRYKqhGAPIVVIg 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501284105   76 KENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSD 125
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 14-147 1.94e-43

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: 140.42  E-value: 1.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  14 IDSANVDTDQIIPKQFLskvtrdgfgvhlfhdwrylddagdepnpeftlnqsrykgASILISKENFGCGSSREHAPWALA 93
Cdd:cd01577    1 LFGDNIDTDQIIPARFL---------------------------------------GDIIVAGKNFGCGSSREHAPWALK 41

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501284105  94 DFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVqqlmDEVQANEGAEITVDL 147
Cdd:cd01577   42 DAGIRAVIAESFARIFFRNAINNGLLPVTLADEDV----EEVEAKPGDEVEVDL 91
HacB2_Meth NF040625
homoaconitase small subunit;
18-185 2.42e-28

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 104.02  E-value: 2.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  18 NVDTDQIIPKQFLSKVTRDGFGVHLFHDWRylddagdepnPEFTLNqsrYKGASILISKENFGCGSSREHAPWALADFGL 97
Cdd:NF040625  14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER----------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  98 RAIIAPSFADIFYGNSINNGlLPVRLSDVEvqqlmdevqANEGAEITVDLE-GLTVTSPSGAVFSFEiagSARHNMLNGL 176
Cdd:NF040625  81 SAIIAKSFARIFYRNAINIG-LPVIVADIE---------ADDGDILSIDLEkGIIKNKTTGEEFKIQ---PFKEFMLEIL 147


                 ....*....
gi 501284105 177 DAIGLTLAY 185
Cdd:NF040625 148 EDGGLVNHY 156
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-200 3.92e-134

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 373.69  E-value: 3.92e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDagDEPNPEFTLNQSRYKGASILISKENFG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDD--GQPNPDFVLNQPRYQGASILLAGDNFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  81 CGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVQANEGAEITVDLEGLTVTSPSGaVF 160
Cdd:PRK01641  79 CGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVTAPDK-TF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 501284105 161 SFEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAWK 200
Cdd:PRK01641 158 PFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFR 197
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-199 1.32e-115

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: 326.74  E-value: 1.32e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   2 EAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDdagdEPNPEFTLNQSRYKGASILISKENFGC 81
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR----SPDPDFVLNQPRYQGADILVAGRNFGC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  82 GSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVQANEGAEITVDLEGLTVTSPSGAVFS 161
Cdd:COG0066   77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTNGTGETYP 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 501284105 162 FEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAW 199
Cdd:COG0066  157 FEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAW 194
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 1-189 9.20e-97

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: 279.01  E-value: 9.20e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105    1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDAGDEPNPEFTLNQSRYKGASILISKENFG 80
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDANGKEPNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   81 CGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQLMDEVqANEGAEITVDLEGLTVTSPSGAVF 160
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQV-ENQGLQMTVDLENQLIHDSEGKVY 159

                         170       180
                  ....*....|....*....|....*....
gi 501284105  161 SFEIAGSARHNMLNGLDAIGLTLAYDVQI 189
Cdd:TIGR00171 160 SFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 1-125 3.80e-48

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: 153.68  E-value: 3.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105    1 MEAFTKHTGLAVMIDSANVDTDQIIPKQFLSKVTRDGFGVHLFHDWRYLDDAG--DEPNPEFTLNQSRYK--GASILIS- 75
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYlpDGENPDFYDAAMRYKqhGAPIVVIg 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501284105   76 KENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSD 125
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 14-147 1.94e-43

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: 140.42  E-value: 1.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  14 IDSANVDTDQIIPKQFLskvtrdgfgvhlfhdwrylddagdepnpeftlnqsrykgASILISKENFGCGSSREHAPWALA 93
Cdd:cd01577    1 LFGDNIDTDQIIPARFL---------------------------------------GDIIVAGKNFGCGSSREHAPWALK 41

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501284105  94 DFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVqqlmDEVQANEGAEITVDL 147
Cdd:cd01577   42 DAGIRAVIAESFARIFFRNAINNGLLPVTLADEDV----EEVEAKPGDEVEVDL 91
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 18-163 1.08e-34

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 120.32  E-value: 1.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  18 NVDTDQIIPKQFLSKVTRDGFGVHLFHDWRylddagdepnPEFTlnqSRYKGASILISKENFGCGSSREHAPWALADFGL 97
Cdd:PRK00439  10 NIDTDVIIPARYLNTSDPQELAKHCMEDLD----------PEFA---KKVKPGDIIVAGKNFGCGSSREHAPIALKAAGV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501284105  98 RAIIAPSFADIFYGNSINNGlLPVrlsdVEVQQLMDEVqaNEGAEITVDLEGLTVTSPS-GAVFSFE 163
Cdd:PRK00439  77 SAVIAKSFARIFYRNAINIG-LPV----LECDEAVDKI--EDGDEVEVDLETGVITNLTtGEEYKFK 136
PRK14812 PRK14812
hypothetical protein; Provisional
 82-199 4.00e-31

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 109.81  E-value: 4.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  82 GSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVrLSDVEVQQLMDEVQANEgaEITVDLEGLTVTSPSGAvFS 161
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI-VQPREVREKLAQLKPTD--QVTVDLEQQKIISPVEE-FT 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501284105 162 FEIAGSARHNMLNGLDAIGLTLAYDVQIASYESQLPAW 199
Cdd:PRK14812  79 FEIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAY 116
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 18-163 2.66e-30

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: 108.66  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   18 NVDTDQIIPKQFLSKVTRDGFGVHLFhdwrylddagDEPNPEFTlnqSRYKGASILISKENFGCGSSREHAPWALADFGL 97
Cdd:TIGR02087   9 DIDTDEIIPGRYLRTTDPDELASHAM----------EGIDPEFA---KKVRPGDVIVAGKNFGCGSSREQAALALKAAGI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501284105   98 RAIIAPSFADIFYGNSINNGlLPVRLSDVEVQqlmdevqaNEGAEITVDLEGLTVTSPSGAVFSFE 163
Cdd:TIGR02087  76 AAVIAESFARIFYRNAINIG-LPLIEAKTEGI--------KDGDEVTVDLETGEIRVNGNEEYKGE 132
HacB2_Meth NF040625
homoaconitase small subunit;
18-185 2.42e-28

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 104.02  E-value: 2.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  18 NVDTDQIIPKQFLSKVTRDGFGVHLFHDWRylddagdepnPEFTLNqsrYKGASILISKENFGCGSSREHAPWALADFGL 97
Cdd:NF040625  14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER----------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  98 RAIIAPSFADIFYGNSINNGlLPVRLSDVEvqqlmdevqANEGAEITVDLE-GLTVTSPSGAVFSFEiagSARHNMLNGL 176
Cdd:NF040625  81 SAIIAKSFARIFYRNAINIG-LPVIVADIE---------ADDGDILSIDLEkGIIKNKTTGEEFKIQ---PFKEFMLEIL 147


                 ....*....
gi 501284105 177 DAIGLTLAY 185
Cdd:NF040625 148 EDGGLVNHY 156
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 18-148 2.51e-26

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: 98.71  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105   18 NVDTDQIIPKQFLSKVTRDGFGVHLFHDWRylddagdepnPEFtlnQSRYKGASILISKENFGCGSSREHAPWALADFGL 97
Cdd:TIGR02084   9 NVDTDVIIPARYLNTSDPKELAKHCMEDLD----------KDF---VKKVKEGDIIVAGENFGCGSSREHAPIAIKASGI 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501284105   98 RAIIAPSFADIFYGNSINNGlLPVrlsdVEVQQLMDEVQanEGAEITVDLE 148
Cdd:TIGR02084  76 SCVIAKSFARIFYRNAINIG-LPI----VESEEAVDEIE--EGDEVEVDLE 119
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 17-153 3.92e-25

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 96.03  E-value: 3.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  17 ANVDTDQIIPKQFLS-KVTRDGFGVHLFHDWRylddagdepnPEFTlnqSRYKGASILISKENFGCGSSREHAPWALADF 95
Cdd:PRK14023   9 DNINTDDILPGKYAPfMVGEDRFHNYAFAHLR----------PEFA---STVRPGDILVAGRNFGLGSSREYAPEALKML 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501284105  96 GLRAIIAPSFADIFYGNSINNGLLPVRLSDVeVQQLMDevqaneGAEITVDLEGLTVT 153
Cdd:PRK14023  76 GIGAIIAKSYARIFYRNLVNLGIPPFESEEV-VDALED------GDEVELDLETGVLT 126
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 18-149 1.94e-22

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 90.69  E-value: 1.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  18 NVDTDQIIPKQFLSKV-----TRDGFGVHLFHDwryLDDAGDEPNPEFTLNQSRYkgaSILISKENFGCGSSREHAPWAL 92
Cdd:PLN00072  79 NIDTDQIIPAEYLTLVpskpdEYEKLGSYALIG---LPAFYKTRFVEPGEMKTKY---SIIIGGENFGCGSSREHAPVAL 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501284105  93 ADFGLRAIIAPSFADIFYGNSINNGllpvrlsdvEVQQLMDEVQANE----GAEITVDLEG 149
Cdd:PLN00072 153 GAAGAKAVVAESYARIFFRNSVATG---------EVYPLESEVRICEecktGDVVTVELGN 204
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 69-146 7.27e-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: 74.81  E-value: 7.27e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501284105  69 GASILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEvqqlmDEVQANEGAEITVD 146
Cdd:cd00404   15 GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE-----DYLKLHTGDELDIY 87
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 15-144 9.60e-14

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: 65.00  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  15 DSANVDTDQIIPKQFlskvtrdgfgvhlfhdwRYLDD---------AGDEPNPEFTlnqSRYKGASILISKENFGCGSSR 85
Cdd:cd01674    2 DADNLNTDGIYPGKY-----------------TYQDDitpekmaevCMENYDSEFS---TKTKQGDILVSGFNFGTGSSR 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501284105  86 EHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVeVQQLMdEVQANEGAEIT 144
Cdd:cd01674   62 EQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIELPFL-VQKLR-EAFANESKELT 118
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 57-127 5.01e-13

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: 62.84  E-value: 5.01e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501284105  57 NPEFTlNQSRYKGASILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVE 127
Cdd:cd01579   37 DPTFA-ERAKAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADED 106
PRK07229 PRK07229
aconitate hydratase; Validated
 68-159 2.40e-12

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 64.78  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  68 KGASILISKENFGCGSSREHApwALAD--FGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEvqqlmDEVQANEGAEItv 145
Cdd:PRK07229 522 QGGGIVVGGENYGQGSSREHA--ALAPryLGVKAVLAKSFARIHKANLINFGILPLTFADPA-----DYDKIEEGDVL-- 592

                         90
                 ....*....|....
gi 501284105 146 DLEGLTVTSPSGAV 159
Cdd:PRK07229 593 EIEDLREFLPGGPL 606
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 71-155 1.83e-08

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: 51.32  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  71 SILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDvevQQLMDEVQANEgaeiTVDLEGL 150
Cdd:cd01578   71 WVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAD---PADYDKIHPDD----KVDILGL 143


                 ....*
gi 501284105 151 TVTSP 155
Cdd:cd01578  144 TDFAP 148
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 66-163 1.86e-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: 41.63  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501284105  66 RYKGA---SILISKENFGCGSSREHA---PwALAdfGLRAIIAPSFADIFYGNSINNGLLPVRLSD-------------- 125
Cdd:COG1048  754 RYKAEgtpLVVLAGKEYGTGSSRDWAakgT-RLL--GVKAVIAESFERIHRSNLVGMGVLPLQFPEgesaeslgltgdet 830

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 501284105 126 VEVQQLMDEVQanEGAEITVdleglTVTSPSGAVFSFE 163
Cdd:COG1048  831 FDIEGLDEGLA--PGKTVTV-----TATRADGSTEEFP 861
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 66-130 4.23e-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: 39.57  E-value: 4.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501284105  66 RYKGAS---ILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLPVRLSDVEVQQ 130
Cdd:cd01580   90 RYKEEGvplVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENAD 157
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 72-120 2.63e-03

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 38.07  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 501284105  72 ILISKENFGCGSSREHAPWALADFGLRAIIAPSFADIFYGNSINNGLLP 120
Cdd:PTZ00092 774 IVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILP 822
 
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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