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Conserved domains on  [gi|2410729180|ref|WP_268541730|]
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3-isopropylmalate dehydratase small subunit [Candidatus Nitrosotenuis cloacae]

Protein Classification

3-isopropylmalate dehydratase small subunit( domain architecture ID 1030)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aconitase_swivel super family cl00215
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 3-158 1.68e-72

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.


The actual alignment was detected with superfamily member PRK00439:

Pssm-ID: 469664 [Multi-domain]  Cd Length: 163  Bit Score: 214.69  E-value: 1.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYeRDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:PRK00439    2 GRVWKF-GDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAFLLpIEIDEqTYQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPV-LECDE-AVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEY 154
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 3-158 1.68e-72

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 214.69  E-value: 1.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYeRDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:PRK00439    2 GRVWKF-GDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAFLLpIEIDEqTYQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPV-LECDE-AVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEY 154
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 3-158 6.83e-61

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: 185.32  E-value: 6.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYErDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:TIGR02087   1 GRVWKFG-DDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAfLLPIEIDEQTyqkISDGDKIEVDTQKNEIKnLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:TIGR02087  80 AESFARIFYRNAINIG-LPLIEAKTEG---IKDGDEVTVDLETGEIR-VNGNEEYKGEPLPDFLLEILREGGLLEY 150
HacB2_Meth NF040625
homoaconitase small subunit;
1-158 2.25e-54

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 168.74  E-value: 2.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYeRDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKG 80
Cdd:NF040625    4 IKGKVWKF-GDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410729180  81 VLAVSFARIFYRNAVDGAflLPIEIDEqtyQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:NF040625   83 IIAKSFARIFYRNAINIG--LPVIVAD---IEADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNH 155
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 1-135 2.84e-53

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: 167.27  E-value: 2.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAMEGI------DPNF---HSRVKMGDYIVSGKNFGCGSSREHAPI 71
Cdd:COG0066     6 LTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFvlnQPRYQGADILVAGRNFGCGSSREHAPW 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2410729180  72 ALSHCGIKGVLAVSFARIFYRNAVD-GafLLPIEIDEQTYQKI------SDGDKIEVDTQKNEIKNLTKNE 135
Cdd:COG0066    86 ALKDYGFRAVIAPSFADIFYRNAINnG--LLPIELPEEAVDALfaaieaNPGDELTVDLEAGTVTNGTGET 154
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-158 7.69e-48

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 152.20  E-value: 7.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYErDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKG 80
Cdd:NF040604    3 IKGRVHKFG-DDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIKA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410729180  81 VLAVSFARIFYRNAVDGAfLLPIEIDEQTyQKISDGDKIEVDTQKNEIKnLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:NF040604   82 VIAESFARIFYRNAINIG-LIPIVCKGIT-KEVKDGDIIEIDLENEKII-INDKKTLNCEVPKGIEKEILDAGGLINY 156
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.18e-35

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: 118.85  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   9 ERDNIDTDVILPGQYLklhdydeiakhamegidpnfhsrvkmGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFAR 88
Cdd:cd01577     2 FGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFAR 55

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2410729180  89 IFYRNAVDGaFLLPIEIDEQTYQKI--SDGDKIEVD 122
Cdd:cd01577    56 IFFRNAINN-GLLPVTLADEDVEEVeaKPGDEVEVD 90
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 2-108 8.33e-21

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: 82.41  E-value: 8.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   2 TGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDY------------------IVSGKNFGCG 63
Cdd:pfam00694   8 KGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENpdfydaamrykqhgapivVIGGKNFGCG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2410729180  64 SSREHAPIALSHCGIKGVLAVSFARIFYRNAVDGAfLLPIEIDEQ 108
Cdd:pfam00694  88 SSREHAAWALRDLGIKAVIAESFARIHRNNLIKNG-LLPLEFPEE 131
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 3-158 1.68e-72

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 214.69  E-value: 1.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYeRDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:PRK00439    2 GRVWKF-GDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAFLLpIEIDEqTYQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:PRK00439   81 AKSFARIFYRNAINIGLPV-LECDE-AVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEY 154
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 3-158 6.83e-61

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: 185.32  E-value: 6.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYErDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:TIGR02087   1 GRVWKFG-DDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAfLLPIEIDEQTyqkISDGDKIEVDTQKNEIKnLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:TIGR02087  80 AESFARIFYRNAINIG-LPLIEAKTEG---IKDGDEVTVDLETGEIR-VNGNEEYKGEPLPDFLLEILREGGLLEY 150
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 3-158 1.60e-58

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: 179.22  E-value: 1.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   3 GNVIKYErDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVL 82
Cdd:TIGR02084   1 GKVHKYG-DNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410729180  83 AVSFARIFYRNAVDGAflLPIEIDEQTYQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:TIGR02084  80 AKSFARIFYRNAINIG--LPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNY 153
HacB2_Meth NF040625
homoaconitase small subunit;
1-158 2.25e-54

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 168.74  E-value: 2.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYeRDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKG 80
Cdd:NF040625    4 IKGKVWKF-GDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410729180  81 VLAVSFARIFYRNAVDGAflLPIEIDEqtyQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:NF040625   83 IIAKSFARIFYRNAINIG--LPVIVAD---IEADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVNH 155
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 1-135 2.84e-53

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: 167.27  E-value: 2.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAMEGI------DPNF---HSRVKMGDYIVSGKNFGCGSSREHAPI 71
Cdd:COG0066     6 LTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFvlnQPRYQGADILVAGRNFGCGSSREHAPW 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2410729180  72 ALSHCGIKGVLAVSFARIFYRNAVD-GafLLPIEIDEQTYQKI------SDGDKIEVDTQKNEIKNLTKNE 135
Cdd:COG0066    86 ALKDYGFRAVIAPSFADIFYRNAINnG--LLPIELPEEAVDALfaaieaNPGDELTVDLEAGTVTNGTGET 154
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-158 7.69e-48

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 152.20  E-value: 7.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYErDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKG 80
Cdd:NF040604    3 IKGRVHKFG-DDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIKA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410729180  81 VLAVSFARIFYRNAVDGAfLLPIEIDEQTyQKISDGDKIEVDTQKNEIKnLTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:NF040604   82 VIAESFARIFYRNAINIG-LIPIVCKGIT-KEVKDGDIIEIDLENEKII-INDKKTLNCEVPKGIEKEILDAGGLINY 156
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 10-158 1.62e-40

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 136.53  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  10 RDNIDTDVILPGQYLKL-----HDYDEIAKHAMEGIdPNFHSR--VKMGD------YIVSGKNFGCGSSREHAPIALSHC 76
Cdd:PLN00072   77 GDNIDTDQIIPAEYLTLvpskpDEYEKLGSYALIGL-PAFYKTrfVEPGEmktkysIIIGGENFGCGSSREHAPVALGAA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  77 GIKGVLAVSFARIFYRNAVDGAFLLPIEIDEQTYQKISDGDKIEVDTQKNEIKNLTKNETYKMKPFSDiVSKIIAAGGLF 156
Cdd:PLN00072  156 GAKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVELGNSVLINHTTGKEYKLKPIGD-AGPVIDAGGIF 234


                  ..
gi 2410729180 157 KY 158
Cdd:PLN00072  235 AY 236
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 1.18e-35

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: 118.85  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   9 ERDNIDTDVILPGQYLklhdydeiakhamegidpnfhsrvkmGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFAR 88
Cdd:cd01577     2 FGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFAR 55

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2410729180  89 IFYRNAVDGaFLLPIEIDEQTYQKI--SDGDKIEVD 122
Cdd:cd01577    56 IFFRNAINN-GLLPVTLADEDVEEVeaKPGDEVEVD 90
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 11-158 1.43e-34

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 118.75  E-value: 1.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  11 DNIDTDVILPGQYLK-LHDYDEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFARI 89
Cdd:PRK14023    9 DNINTDDILPGKYAPfMVGEDRFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2410729180  90 FYRNAVDGAfLLPIEIDEQTYQkISDGDKIEVDTQKNEIKnlTKNETYKMKPFSDIVSKIIAAGGLFKY 158
Cdd:PRK14023   89 FYRNLVNLG-IPPFESEEVVDA-LEDGDEVELDLETGVLT--RGGETFQLRPPPEFLLEALKEGSILEY 153
PRK07229 PRK07229
aconitate hydratase; Validated
 11-158 3.41e-30

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 114.47  E-value: 3.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  11 DNIDTDVILPG--QYLKLH-DYDEIAKHAMEGIDPNFHSRVK--MGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVS 85
Cdd:PRK07229  479 DNITTDHIMPAgaKWLPYRsNIPNISEFVFEGVDNTFPERAKeqGGGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKS 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  86 FARIFYRNAVD-GafLLPIEI-DEQTYQKISDGDKIEVDTQKN-------EIKNLTKNETYKMK-PFSDIVSKIIAAGGL 155
Cdd:PRK07229  559 FARIHKANLINfG--ILPLTFaDPADYDKIEEGDVLEIEDLREflpggplTVVNVTKDEEIEVRhTLSERQIEILLAGGA 636


                  ...
gi 2410729180 156 FKY 158
Cdd:PRK07229  637 LNL 639
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
2-142 2.90e-29

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 105.98  E-value: 2.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   2 TGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAME--------GIDPNF---HSRVKMGDYIVSGKNFGCGSSREHAP 70
Cdd:PRK01641    8 TGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDdwrylddgQPNPDFvlnQPRYQGASILLAGDNFGCGSSREHAP 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2410729180  71 IALSHCGIKGVLAVSFARIFYRNAV-DGafLLPIEIDEQTYQKISD------GDKIEVDTQKNEIKnlTKNETYkmkPF 142
Cdd:PRK01641   88 WALADYGFRAVIAPSFADIFYNNCFkNG--LLPIVLPEEDVDELFKlveanpGAELTVDLEAQTVT--APDKTF---PF 159
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 11-122 1.49e-28

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: 101.75  E-value: 1.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  11 DNIDTDVILPG--QYLKLH-DYDEIAKHAMEGIDPNFHSRVKMGD--YIVSGKNFGCGSSREHAPIALSHCGIKGVLAVS 85
Cdd:cd01579     4 DNITTDHIMPAgaKVLPLRsNIPAISEFVFHRVDPTFAERAKAAGpgFIVGGENYGQGSSREHAALAPMYLGVRAVLAKS 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2410729180  86 FARIFYRNAVDGAfLLPIEI-DEQTYQKISDGDKIEVD 122
Cdd:cd01579    84 FARIHRANLINFG-ILPLTFaDEDDYDRFEQGDQLELP 120
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 11-140 7.81e-24

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: 90.04  E-value: 7.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  11 DNIDTDVILPGQYLKLHDY--DEIAKHAMEGIDPNFHSRVKMGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFAR 88
Cdd:cd01674     4 DNLNTDGIYPGKYTYQDDItpEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGN 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2410729180  89 IFYRNAVDGAfLLPIEideqtyqkISDGDKIEVDTQKNEIKNLTKNETYKMK 140
Cdd:cd01674    84 IFSRNSINNA-LLSIE--------LPFLVQKLREAFANESKELTRRTGWKLK 126
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 1-142 4.28e-23

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: 89.87  E-value: 4.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   1 MTGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAM--------EGIDPNFHSRVKMGDY-----IVSGKNFGCGSSRE 67
Cdd:TIGR00171   7 HTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFfdwrfldaNGKEPNPDFVLNQPQYqgasiLLARENFGCGSSRE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  68 HAPIALSHCGIKGVLAVSFARIFYRNAVDGAfLLPIEIDEQTYQKI-----SDGDKIEVDTQKNEIKNLTKNE-TYKMKP 141
Cdd:TIGR00171  87 HAPWALDDYGFKVIIAPSFADIFYNNSFKNG-LLPIRLSYDEVKELfgqveNQGLQMTVDLENQLIHDSEGKVySFEIDP 165


                  .
gi 2410729180 142 F 142
Cdd:TIGR00171 166 F 166
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 2-108 8.33e-21

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: 82.41  E-value: 8.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180   2 TGNVIKYERDNIDTDVILPGQYLKLHDYDEIAKHAMEGIDPNFHSRVKMGDY------------------IVSGKNFGCG 63
Cdd:pfam00694   8 KGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENpdfydaamrykqhgapivVIGGKNFGCG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2410729180  64 SSREHAPIALSHCGIKGVLAVSFARIFYRNAVDGAfLLPIEIDEQ 108
Cdd:pfam00694  88 SSREHAAWALRDLGIKAVIAESFARIHRNNLIKNG-LLPLEFPEE 131
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 11-122 4.42e-19

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


Pssm-ID: 238236 [Multi-domain]  Cd Length: 88  Bit Score: 76.74  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  11 DNIDTDVILPGQylklhdydeiakhamegidpnfhsrvkmGDYIVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFARIF 90
Cdd:cd00404     4 GNITTDHISPAG----------------------------PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIF 55

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2410729180  91 YRNAVDGAfLLPIEIDE-QTYQKISDGDKIEVD 122
Cdd:cd00404    56 FRNLVDQG-LLPLEFADpEDYLKLHTGDELDIY 87
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 54-122 1.58e-07

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: 47.85  E-value: 1.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  54 IVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFARIFYRNaVDGAFLLPIEI-DEQTYQKISDGDKIEVD 122
Cdd:cd01578    73 VIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN-LKKQGLLPLTFaDPADYDKIHPDDKVDIL 141
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 54-89 1.99e-07

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


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 49.33  E-value: 1.99e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2410729180  54 IVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFARI 89
Cdd:COG1048   764 VLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERI 799
acnA PRK12881
aconitate hydratase AcnA;
54-129 4.84e-06

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 45.31  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  54 IVSGKNFGCGSSREHAPIALSHCGIKGVLAVSFARIFYRNAVdGAFLLPIE----IDEQTYqKISDGDKIEVDTQKNEIK 129
Cdd:PRK12881  763 VIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLV-GMGVLPLQfkggDSRQSL-GLTGGETFDIEGLPGEIK 840
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 54-105 5.70e-06

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


Pssm-ID: 238812 [Multi-domain]  Cd Length: 171  Bit Score: 43.80  E-value: 5.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2410729180  54 IVSGKNFGCGSSREHA---PIALshcGIKGVLAVSFARIFYRNAVdGAFLLPIEI 105
Cdd:cd01580   100 ILAGKEYGSGSSRDWAakgPFLL---GVKAVIAESFERIHRSNLV-GMGILPLQF 150
PRK14812 PRK14812
hypothetical protein; Provisional
 63-139 1.38e-05

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 42.02  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  63 GSSREHAPIALSHCGIKGVLAVSFARIFYRNAVDGAFL---LPIEIDEQTYQkISDGDKIEVDTQKNEIKNLTKNETYKM 139
Cdd:PRK14812    3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLpivQPREVREKLAQ-LKPTDQVTVDLEQQKIISPVEEFTFEI 81
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 54-104 4.54e-05

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 42.31  E-value: 4.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2410729180  54 IVSGKNFGCGSSREHA---PIALshcGIKGVLAVSFARIFYRNAVdGAFLLPIE 104
Cdd:PTZ00092  775 VLAGKEYGSGSSRDWAakgPYLQ---GVKAVIAESFERIHRSNLV-GMGILPLQ 824
PRK09238 PRK09238
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
 81-154 1.79e-04

bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated


Pssm-ID: 236424 [Multi-domain]  Cd Length: 835  Bit Score: 40.55  E-value: 1.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2410729180  81 VLAVSFARIFYRNAVD-GAflLPIEIDeqtYQKISDGDKIEVDTQKNEIKNLTKNE--TYKMKPfsDIVSKIIAAGG 154
Cdd:PRK09238  263 VLGGKIAPIFFNTMEDsGA--LPIELD---VSKLNMGDVIDIYPYKGKIRNETGEViaTFKLKT--DVLLDEVRAGG 332
PLN00070 PLN00070
aconitate hydratase
 25-103 3.12e-03

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 37.09  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410729180  25 KLHDYDEIAKHAMEGIDPnfhsrvkmgdYIVSGKNFGCGSSREHA---PIALshcGIKGVLAVSFARIFYRNAVdGAFLL 101
Cdd:PLN00070  792 KLSVFDAAMKYKSEGHDT----------IILAGAEYGSGSSRDWAakgPMLL---GVKAVIAKSFERIHRSNLV-GMGII 857


                  ..
gi 2410729180 102 PI 103
Cdd:PLN00070  858 PL 859
 
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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