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Conserved domains on  [gi|579438220|gb|EUU86989|]
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3-isopropylmalate dehydratase small subunit [Staphylococcus aureus M0179]

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;
5-190 1.30e-122

3-isopropylmalate dehydratase small subunit;


:

Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 344.03  E-value: 1.30e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPDGSDNPDFNPNKPQYKGASILITGDNFGCGS 84
Cdd:PRK01641   2 EKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  85 SREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY------EEIEIDLPNQTVSSPDKRFHFEI 158
Cdd:PRK01641  82 SREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLveanpgAELTVDLEAQTVTAPDKTFPFEI 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 579438220 159 DETWKNKLVNGLDDIAITLQYESLIEKYEKSL 190
Cdd:PRK01641 162 DPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
5-190 1.30e-122

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 344.03  E-value: 1.30e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPDGSDNPDFNPNKPQYKGASILITGDNFGCGS 84
Cdd:PRK01641   2 EKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  85 SREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY------EEIEIDLPNQTVSSPDKRFHFEI 158
Cdd:PRK01641  82 SREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLveanpgAELTVDLEAQTVTAPDKTFPFEI 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 579438220 159 DETWKNKLVNGLDDIAITLQYESLIEKYEKSL 190
Cdd:PRK01641 162 DPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 5-190 2.56e-96

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: 277.44  E-value: 2.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPdgSDNPDFNPNKPQYKGASILITGDNFGCGS 84
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR--SPDPDFVLNQPRYQGADILVAGRNFGCGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  85 SREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY------EEIEIDLPNQTVSSPDKR-FHFE 157
Cdd:COG0066   79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAieanpgDELTVDLEAGTVTNGTGEtYPFE 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 579438220 158 IDETWKNKLVNGLDDIAITLQYESLIEKYEKSL 190
Cdd:COG0066  159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKR 191
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 4-183 1.33e-72

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: 217.38  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220    4 IKPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPD-GSD-NPDFNPNKPQYKGASILITGDNFG 81
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDAnGKEpNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   82 CGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVL-EKSAREHLAQYE----EIEIDLPNQTVSSPD-KRFH 155
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLsYDEVKELFGQVEnqglQMTVDLENQLIHDSEgKVYS 160

                         170       180
                  ....*....|....*....|....*...
gi 579438220  156 FEIDETWKNKLVNGLDDIAITLQYESLI 183
Cdd:TIGR00171 161 FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 5-124 4.87e-41

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: 135.19  E-value: 4.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220    5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYL----PDGSDNPDFNPNKPQYK--GASIL-ITG 77
Cdd:pfam00694   2 PVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGkvryLPDGENPDFYDAAMRYKqhGAPIVvIGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 579438220   78 DNFGCGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVL 124
Cdd:pfam00694  82 KNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEF 128
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 17-142 7.87e-37

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: 123.08  E-value: 7.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  17 LFNDNIDTDQIIPKVHLkrisksgfgpfafdewrylpdgsdnpdfnpnkpqykgASILITGDNFGCGSSREHAAWALKDY 96
Cdd:cd01577    1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 579438220  97 GFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQYE--EIEIDL 142
Cdd:cd01577   44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPgdEVEVDL 91
HacB2_Meth NF040625
homoaconitase small subunit;
11-179 3.13e-18

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 77.44  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  11 KGKiVPLFNDNIDTDQIIPKVHLKrisksgfgPFAFDEW-RYLPDGSDnPDFNPNkpqYKGASILITGDNFGCGSSREHA 89
Cdd:NF040625   5 KGK-VWKFGDNIDTDVIIPGRYLR--------TFNPDDLaSHVMEGER-PDFTKN---VQKGDIIVAGWNFGCGSSREQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  90 AWALKDYGFHIIIAGSFSDIFYMNCTkNAMLPIVLEKSAREhlaQYEEIEIDLPNQTVSSPDKRFHFEIdETWKNKLVNG 169
Cdd:NF040625  72 PVAIKHAGVSAIIAKSFARIFYRNAI-NIGLPVIVADIEAD---DGDILSIDLEKGIIKNKTTGEEFKI-QPFKEFMLEI 146

                        170
                 ....*....|
gi 579438220 170 LDDIAITLQY 179
Cdd:NF040625 147 LEDGGLVNHY 156
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
5-190 1.30e-122

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 344.03  E-value: 1.30e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPDGSDNPDFNPNKPQYKGASILITGDNFGCGS 84
Cdd:PRK01641   2 EKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  85 SREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY------EEIEIDLPNQTVSSPDKRFHFEI 158
Cdd:PRK01641  82 SREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLveanpgAELTVDLEAQTVTAPDKTFPFEI 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 579438220 159 DETWKNKLVNGLDDIAITLQYESLIEKYEKSL 190
Cdd:PRK01641 162 DPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 5-190 2.56e-96

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: 277.44  E-value: 2.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPdgSDNPDFNPNKPQYKGASILITGDNFGCGS 84
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR--SPDPDFVLNQPRYQGADILVAGRNFGCGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  85 SREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY------EEIEIDLPNQTVSSPDKR-FHFE 157
Cdd:COG0066   79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAieanpgDELTVDLEAGTVTNGTGEtYPFE 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 579438220 158 IDETWKNKLVNGLDDIAITLQYESLIEKYEKSL 190
Cdd:COG0066  159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKR 191
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 4-183 1.33e-72

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: 217.38  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220    4 IKPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYLPD-GSD-NPDFNPNKPQYKGASILITGDNFG 81
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDAnGKEpNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   82 CGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVL-EKSAREHLAQYE----EIEIDLPNQTVSSPD-KRFH 155
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLsYDEVKELFGQVEnqglQMTVDLENQLIHDSEgKVYS 160

                         170       180
                  ....*....|....*....|....*...
gi 579438220  156 FEIDETWKNKLVNGLDDIAITLQYESLI 183
Cdd:TIGR00171 161 FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 5-124 4.87e-41

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: 135.19  E-value: 4.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220    5 KPITTYKGKIVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRYL----PDGSDNPDFNPNKPQYK--GASIL-ITG 77
Cdd:pfam00694   2 PVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGkvryLPDGENPDFYDAAMRYKqhGAPIVvIGG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 579438220   78 DNFGCGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVL 124
Cdd:pfam00694  82 KNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEF 128
PRK14812 PRK14812
hypothetical protein; Provisional
 83-188 1.26e-39

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 131.38  E-value: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  83 GSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQY---EEIEIDLPNQTVSSPDKRFHFEID 159
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLkptDQVTVDLEQQKIISPVEEFTFEID 82

                         90       100
                 ....*....|....*....|....*....
gi 579438220 160 ETWKNKLVNGLDDIAITLQYESLIEKYEK 188
Cdd:PRK14812  83 SEWKHKLLNSLDDIGITLQYEELIAAYEK 111
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 17-142 7.87e-37

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: 123.08  E-value: 7.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  17 LFNDNIDTDQIIPKVHLkrisksgfgpfafdewrylpdgsdnpdfnpnkpqykgASILITGDNFGCGSSREHAAWALKDY 96
Cdd:cd01577    1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 579438220  97 GFHIIIAGSFSDIFYMNCTKNAMLPIVLEKSAREHLAQYE--EIEIDL 142
Cdd:cd01577   44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPgdEVEVDL 91
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 11-142 4.70e-25

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 95.28  E-value: 4.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  11 KGKiVPLFNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRylpdgsdnPDFnPNKPQyKGAsILITGDNFGCGSSREHAA 90
Cdd:PRK00439   1 KGR-VWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLD--------PEF-AKKVK-PGD-IIVAGKNFGCGSSREHAP 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 579438220  91 WALKDYGFHIIIAGSFSDIFYMNCTkNAMLPIVLEKSAREHLAQYEEIEIDL 142
Cdd:PRK00439  69 IALKAAGVSAVIAKSFARIFYRNAI-NIGLPVLECDEAVDKIEDGDEVEVDL 119
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 18-152 1.18e-23

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: 91.33  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   18 FNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRylpdgsdnPDFnpnKPQYKGASILITGDNFGCGSSREHAAWALKDYG 97
Cdd:TIGR02087   6 FGDDIDTDEIIPGRYLRTTDPDELASHAMEGID--------PEF---AKKVRPGDVIVAGKNFGCGSSREQAALALKAAG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 579438220   98 FHIIIAGSFSDIFYMNCTKNAMLPIVLEKsarEHLAQYEEIEIDLPNQTVSSPDK 152
Cdd:TIGR02087  75 IAAVIAESFARIFYRNAINIGLPLIEAKT---EGIKDGDEVTVDLETGEIRVNGN 126
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 18-144 1.07e-21

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: 86.38  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220   18 FNDNIDTDQIIPKVHLKRISKSGFGPFAFDEWRylpdgsdnPDFnpnKPQYKGASILITGDNFGCGSSREHAAWALKDYG 97
Cdd:TIGR02084   6 YGDNVDTDVIIPARYLNTSDPKELAKHCMEDLD--------KDF---VKKVKEGDIIVAGENFGCGSSREHAPIAIKASG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 579438220   98 FHIIIAGSFSDIFYMNCTkNAMLPIVLEKSAREHLAQYEEIEIDLPN 144
Cdd:TIGR02084  75 ISCVIAKSFARIFYRNAI-NIGLPIVESEEAVDEIEEGDEVEVDLEK 120
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 18-163 2.21e-20

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 83.31  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  18 FNDNIDTDQIIPkvhlkriskSGFGPFAF--DEWRYLPDGSDNPDFNPNkpqYKGASILITGDNFGCGSSREHAAWALKD 95
Cdd:PRK14023   7 FGDNINTDDILP---------GKYAPFMVgeDRFHNYAFAHLRPEFAST---VRPGDILVAGRNFGLGSSREYAPEALKM 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579438220  96 YGFHIIIAGSFSDIFYMNCTkNAMLPIVLEKSAREHLAQYEEIEIDLPNQTVSSPDKRFHFE-----IDETWK 163
Cdd:PRK14023  75 LGIGAIIAKSYARIFYRNLV-NLGIPPFESEEVVDALEDGDEVELDLETGVLTRGGETFQLRpppefLLEALK 146
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 20-114 2.00e-18

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 79.90  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  20 DNIDTDQIIPKVHLKRI-SK----SGFGPFAFDEwryLPDGSDNPDFNPNKPQYKgASILITGDNFGCGSSREHAAWALK 94
Cdd:PLN00072  78 DNIDTDQIIPAEYLTLVpSKpdeyEKLGSYALIG---LPAFYKTRFVEPGEMKTK-YSIIIGGENFGCGSSREHAPVALG 153

                         90       100
                 ....*....|....*....|
gi 579438220  95 DYGFHIIIAGSFSDIFYMNC 114
Cdd:PLN00072 154 AAGAKAVVAESYARIFFRNS 173
HacB2_Meth NF040625
homoaconitase small subunit;
11-179 3.13e-18

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 77.44  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  11 KGKiVPLFNDNIDTDQIIPKVHLKrisksgfgPFAFDEW-RYLPDGSDnPDFNPNkpqYKGASILITGDNFGCGSSREHA 89
Cdd:NF040625   5 KGK-VWKFGDNIDTDVIIPGRYLR--------TFNPDDLaSHVMEGER-PDFTKN---VQKGDIIVAGWNFGCGSSREQA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  90 AWALKDYGFHIIIAGSFSDIFYMNCTkNAMLPIVLEKSAREhlaQYEEIEIDLPNQTVSSPDKRFHFEIdETWKNKLVNG 169
Cdd:NF040625  72 PVAIKHAGVSAIIAKSFARIFYRNAI-NIGLPVIVADIEAD---DGDILSIDLEKGIIKNKTTGEEFKI-QPFKEFMLEI 146

                        170
                 ....*....|
gi 579438220 170 LDDIAITLQY 179
Cdd:NF040625 147 LEDGGLVNHY 156
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 70-141 9.16e-14

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: 63.64  E-value: 9.16e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579438220  70 GASILITGDNFGCGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPivLEKSAREH---LAQYEEIEID 141
Cdd:cd00404   15 GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLP--LEFADPEDylkLHTGDELDIY 87
PRK07229 PRK07229
aconitate hydratase; Validated
 20-145 2.19e-12

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 64.40  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  20 DNIDTDQIIP---KV-----HLKRISKSGFGPFafdewrylpdgsdNPDFnPNKPQYKGASILITGDNFGCGSSREHAAW 91
Cdd:PRK07229 479 DNITTDHIMPagaKWlpyrsNIPNISEFVFEGV-------------DNTF-PERAKEQGGGIVVGGENYGQGSSREHAAL 544

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 579438220  92 ALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVLE-KSAREHLAQYEEIEI-DLPNQ 145
Cdd:PRK07229 545 APRYLGVKAVLAKSFARIHKANLINFGILPLTFAdPADYDKIEEGDVLEIeDLREF 600
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 20-142 5.01e-12

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: 60.14  E-value: 5.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579438220  20 DNIDTDQIIP---KVHLKRISKSGFGPFAFdewRYLpdgsdNPDFnPNKPQYKGASILITGDNFGCGSSREHAAWALKDY 96
Cdd:cd01579    4 DNITTDHIMPagaKVLPLRSNIPAISEFVF---HRV-----DPTF-AERAKAAGPGFIVGGENYGQGSSREHAALAPMYL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 579438220  97 GFHIIIAGSFSDIFYMNCTKNAMLPIVL-EKSAREHLAQYEEIEIDL 142
Cdd:cd01579   75 GVRAVLAKSFARIHRANLINFGILPLTFaDEDDYDRFEQGDQLELPL 121
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 69-124 5.93e-12

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: 59.99  E-value: 5.93e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 579438220  69 KGASILITGDNFGCGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPIVL 124
Cdd:cd01674   44 KQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIEL 99
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 67-122 2.80e-06

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: 45.15  E-value: 2.80e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 579438220  67 QYKGASI--LITGD-NFGCGSSREHAAWALKDYGFHIIIAGSFSDIFYMNCTKNAMLPI 122
Cdd:cd01578   63 DYKAHGIkwVVIGDeNYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 121
 
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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