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Conserved domains on  [gi|499170190|ref|WP_010868466|]
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3-isopropylmalate dehydratase small subunit [Pyrococcus abyssi]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-164 7.25e-115

3-isopropylmalate dehydratase small subunit; Reviewed


:

Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 322.16  E-value: 7.25e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   4 RGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVI 83
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  84 AKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKRRLK 163
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 .
gi 499170190 164 G 164
Cdd:PRK00439 161 F 161
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-164 7.25e-115

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 322.16  E-value: 7.25e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   4 RGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVI 83
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  84 AKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKRRLK 163
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 .
gi 499170190 164 G 164
Cdd:PRK00439 161 F 161
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-160 5.25e-104

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: 294.39  E-value: 5.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190    5 GRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499170190   85 KSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKR 160
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVKK 156
HacB2_Meth NF040625
homoaconitase small subunit;
1-156 4.44e-78

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 229.21  E-value: 4.44e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   1 MRVRGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVS 80
Cdd:NF040625   2 EIIKGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499170190  81 CVIAKSFARIFYRNAINIGLPILEAPQAVDRietGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVE 156
Cdd:NF040625  82 AIIAKSFARIFYRNAINIGLPVIVADIEADD---GDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVN 154
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-152 1.20e-75

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: 223.90  E-value: 1.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   2 RVRGRAWKY-GDNIDTDVIIPARYLNTSDPKELAKHVLEDL------DPEF---RSKMKPGDIIVAGENFGCGSSREHAP 71
Cdd:COG0066    5 TLTGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFvlnQPRYQGADILVAGRNFGCGSSREHAP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  72 LAIKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQA-VDRI------ETGDELEVDFSSGEIRNLTkGEVYRAnPFPDF 144
Cdd:COG0066   85 WALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEaVDALfaaieaNPGDELTVDLEAGTVTNGT-GETYPF-EIDPF 162


                 ....*...
gi 499170190 145 IMEIIKAG 152
Cdd:COG0066  163 RRECLLNG 170
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-160 1.74e-60

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 184.55  E-value: 1.74e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   1 MRVRGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVS 80
Cdd:NF040604   1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  81 CVIAKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPfPDFIMEIIKAGGLVEWAKR 160
Cdd:NF040604  81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKIIINDKKTLNCEVP-KGIEKEILDAGGLINYAKK 159
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 7.65e-46

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: 145.04  E-value: 7.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   9 KYGDNIDTDVIIPARYLntsdpkelakhvledldpefrskmkpGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFA 88
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499170190  89 RIFYRNAINIG-LPILEAPQAVDRIE--TGDELEVDF 122
Cdd:cd01577   55 RIFFRNAINNGlLPVTLADEDVEEVEakPGDEVEVDL 91
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 12-108 3.05e-23

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: 88.58  E-value: 3.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   12 DNIDTDVIIPARYLNTSDPKELAKHVLEDL-----------------DPEFRSKMKPGDIIV-AGENFGCGSSREHAPLA 73
Cdd:pfam00694  17 SNVDTDLIIPKQFLGTIANIGIGNINFEGWrygkvrylpdgenpdfyDAAMRYKQHGAPIVViGGKNFGCGSSREHAAWA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499170190   74 IKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQA 108
Cdd:pfam00694  97 LRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
 
Name Accession Description Interval E-value
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 4-164 7.25e-115

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 322.16  E-value: 7.25e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   4 RGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVI 83
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNTSDPQELAKHCMEDLDPEFAKKVKPGDIIVAGKNFGCGSSREHAPIALKAAGVSAVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  84 AKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKRRLK 163
Cdd:PRK00439  81 AKSFARIFYRNAINIGLPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEFMLEILKAGGLIEYLKKKGR 160


                 .
gi 499170190 164 G 164
Cdd:PRK00439 161 F 161
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 5-160 5.25e-104

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: 294.39  E-value: 5.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190    5 GRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIA 84
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISCVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499170190   85 KSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVEWAKR 160
Cdd:TIGR02084  81 KSFARIFYRNAINIGLPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEFLQKIMKAGGLLNYVKK 156
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 5-161 1.30e-81

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: 237.71  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190    5 GRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIA 84
Cdd:TIGR02087   1 GRVWKFGDDIDTDEIIPGRYLRTTDPDELASHAMEGIDPEFAKKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAAVIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499170190   85 KSFARIFYRNAINIGLPILEAPqaVDRIETGDELEVDFSSGEIRnLTKGEVYRANPFPDFIMEIIKAGGLVEWAKRR 161
Cdd:TIGR02087  81 ESFARIFYRNAINIGLPLIEAK--TEGIKDGDEVTVDLETGEIR-VNGNEEYKGEPLPDFLLEILREGGLLEYLKKR 154
HacB2_Meth NF040625
homoaconitase small subunit;
1-156 4.44e-78

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 229.21  E-value: 4.44e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   1 MRVRGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVS 80
Cdd:NF040625   2 EIIKGKVWKFGDNIDTDVIIPGRYLRTFNPDDLASHVMEGERPDFTKNVQKGDIIVAGWNFGCGSSREQAPVAIKHAGVS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499170190  81 CVIAKSFARIFYRNAINIGLPILEAPQAVDRietGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGGLVE 156
Cdd:NF040625  82 AIIAKSFARIFYRNAINIGLPVIVADIEADD---GDILSIDLEKGIIKNKTTGEEFKIQPFKEFMLEILEDGGLVN 154
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-152 1.20e-75

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: 223.90  E-value: 1.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   2 RVRGRAWKY-GDNIDTDVIIPARYLNTSDPKELAKHVLEDL------DPEF---RSKMKPGDIIVAGENFGCGSSREHAP 71
Cdd:COG0066    5 TLTGRAVPLdGDNIDTDQIIPARFLKTIDREGLGKHLFEDWrydrspDPDFvlnQPRYQGADILVAGRNFGCGSSREHAP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  72 LAIKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQA-VDRI------ETGDELEVDFSSGEIRNLTkGEVYRAnPFPDF 144
Cdd:COG0066   85 WALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEaVDALfaaieaNPGDELTVDLEAGTVTNGT-GETYPF-EIDPF 162


                 ....*...
gi 499170190 145 IMEIIKAG 152
Cdd:COG0066  163 RRECLLNG 170
HacB_Meth NF040604
homoaconitase small subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 1-160 1.74e-60

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


Pssm-ID: 468577 [Multi-domain]  Cd Length: 159  Bit Score: 184.55  E-value: 1.74e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   1 MRVRGRAWKYGDNIDTDVIIPARYLNTSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVS 80
Cdd:NF040604   1 MIIKGRVHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDEDFPKKVKEGDIIVAGENFGCGSSREQAPIAIKYCGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  81 CVIAKSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPfPDFIMEIIKAGGLVEWAKR 160
Cdd:NF040604  81 AVIAESFARIFYRNAINIGLIPIVCKGITKEVKDGDIIEIDLENEKIIINDKKTLNCEVP-KGIEKEILDAGGLINYAKK 159
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 6-164 4.76e-55

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 170.75  E-value: 4.76e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   6 RAWKYGDNIDTDVIIPARYLN-TSDPKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIA 84
Cdd:PRK14023   3 RVWKFGDNINTDDILPGKYAPfMVGEDRFHNYAFAHLRPEFASTVRPGDILVAGRNFGLGSSREYAPEALKMLGIGAIIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  85 KSFARIFYRNAINIGLPILEAPQAVDRIETGDELEVDFSSGEIRnlTKGEVYRANPFPDFIMEIIKAGGLVEWAK--RRL 162
Cdd:PRK14023  83 KSYARIFYRNLVNLGIPPFESEEVVDALEDGDEVELDLETGVLT--RGGETFQLRPPPEFLLEALKEGSILEYYRkhGRF 160


                 ..
gi 499170190 163 KG 164
Cdd:PRK14023 161 PG 162
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 9-122 7.65e-46

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: 145.04  E-value: 7.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   9 KYGDNIDTDVIIPARYLntsdpkelakhvledldpefrskmkpGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFA 88
Cdd:cd01577    1 LFGDNIDTDQIIPARFL--------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFA 54

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499170190  89 RIFYRNAINIG-LPILEAPQAVDRIE--TGDELEVDF 122
Cdd:cd01577   55 RIFFRNAINNGlLPVTLADEDVEEVEakPGDEVEVDL 91
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 3-160 4.62e-40

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 135.37  E-value: 4.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   3 VRGRAWKYGDNIDTDVIIPARYLNT--SDPKE---LAKHVLEDLDPEFRSK-MKPGD------IIVAGENFGCGSSREHA 70
Cdd:PLN00072  69 FHGLCFVVGDNIDTDQIIPAEYLTLvpSKPDEyekLGSYALIGLPAFYKTRfVEPGEmktkysIIIGGENFGCGSSREHA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  71 PLAIKAAGVSCVIAKSFARIFYRNAINIG--LPILEAPQAVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDfIMEI 148
Cdd:PLN00072 149 PVALGAAGAKAVVAESYARIFFRNSVATGevYPLESEVRICEECKTGDVVTVELGNSVLINHTTGKEYKLKPIGD-AGPV 227

                        170
                 ....*....|..
gi 499170190 149 IKAGGLVEWAKR 160
Cdd:PLN00072 228 IDAGGIFAYARK 239
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
11-121 1.63e-35

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 122.16  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  11 GDNIDTDVIIPARYLNTSDPKELAKHVLED--------LDPEF---RSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGV 79
Cdd:PRK01641  16 RANVDTDQIIPKQFLKRITRTGFGKGLFDDwrylddgqPNPDFvlnQPRYQGASILLAGDNFGCGSSREHAPWALADYGF 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499170190  80 SCVIAKSFARIFYRNAINIGLPILEAPQAV-----DRIET--GDELEVD 121
Cdd:PRK01641  96 RAVIAPSFADIFYNNCFKNGLLPIVLPEEDvdelfKLVEAnpGAELTVD 144
PRK07229 PRK07229
aconitate hydratase; Validated
 9-164 1.20e-33

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 124.49  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   9 KYGDNIDTDVIIPA--RYLN-TSDPKELAKHVLEDLDPEF--RSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVI 83
Cdd:PRK07229 476 KVGDNITTDHIMPAgaKWLPyRSNIPNISEFVFEGVDNTFpeRAKEQGGGIVVGGENYGQGSSREHAALAPRYLGVKAVL 555

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  84 AKSFARIFYRNAINIG-LP-ILEAPQAVDRIETGDELEV----DFSSG---EIRNLTKGEVYRAN-PFPDFIMEIIKAGG 153
Cdd:PRK07229 556 AKSFARIHKANLINFGiLPlTFADPADYDKIEEGDVLEIedlrEFLPGgplTVVNVTKDEEIEVRhTLSERQIEILLAGG 635

                        170
                 ....*....|.
gi 499170190 154 LVEWAKRRLKG 164
Cdd:PRK07229 636 ALNLIKKKLAA 646
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 12-114 3.84e-32

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: 111.61  E-value: 3.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  12 DNIDTDVIIPARYLNTSD--PKELAKHVLEDLDPEFRSKMKPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFAR 89
Cdd:cd01674    4 DNLNTDGIYPGKYTYQDDitPEKMAEVCMENYDSEFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGN 83

                         90       100
                 ....*....|....*....|....*
gi 499170190  90 IFYRNAINIGLPILEAPQAVDRIET 114
Cdd:cd01674   84 IFSRNSINNALLSIELPFLVQKLRE 108
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 9-121 7.77e-31

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: 107.91  E-value: 7.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   9 KYGDNIDTDVIIPA--RYLN-TSDPKELAKHVLEDLDPEFRSKMKPGD--IIVAGENFGCGSSREHAPLAIKAAGVSCVI 83
Cdd:cd01579    1 KVGDNITTDHIMPAgaKVLPlRSNIPAISEFVFHRVDPTFAERAKAAGpgFIVGGENYGQGSSREHAALAPMYLGVRAVL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499170190  84 AKSFARIFYRNAINIG-LPI-LEAPQAVDRIETGDELEVD 121
Cdd:cd01579   81 AKSFARIHRANLINFGiLPLtFADEDDYDRFEQGDQLELP 120
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 9-121 1.76e-23

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: 87.91  E-value: 1.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   9 KYGDNIDTDVIIPArylntsdpkelakhvledldpefrskmkPGDIIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFA 88
Cdd:cd00404    1 KVAGNITTDHISPA----------------------------GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFA 52

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499170190  89 RIFYRNAINIGLPILE--APQAVDRIETGDELEVD 121
Cdd:cd00404   53 RIFFRNLVDQGLLPLEfaDPEDYLKLHTGDELDIY 87
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 12-108 3.05e-23

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: 88.58  E-value: 3.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   12 DNIDTDVIIPARYLNTSDPKELAKHVLEDL-----------------DPEFRSKMKPGDIIV-AGENFGCGSSREHAPLA 73
Cdd:pfam00694  17 SNVDTDLIIPKQFLGTIANIGIGNINFEGWrygkvrylpdgenpdfyDAAMRYKQHGAPIVViGGKNFGCGSSREHAAWA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499170190   74 IKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQA 108
Cdd:pfam00694  97 LRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 13-137 1.16e-22

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: 88.72  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190   13 NIDTDVIIPARYLNTSDPKELAKHVLED---LD-------PEFRSKMKP---GDIIVAGENFGCGSSREHAPLAIKAAGV 79
Cdd:TIGR00171  18 NVDTDAIIPKQFLKRITRTGFGKHLFFDwrfLDangkepnPDFVLNQPQyqgASILLARENFGCGSSREHAPWALDDYGF 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499170190   80 SCVIAKSFARIFYRNAINIG-LPILEAPQAVDRI-----ETGDELEVDFSSGEIRNlTKGEVYR 137
Cdd:TIGR00171  98 KVIIAPSFADIFYNNSFKNGlLPIRLSYDEVKELfgqveNQGLQMTVDLENQLIHD-SEGKVYS 160
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 54-90 7.53e-10

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: 56.27  E-value: 7.53e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARI 90
Cdd:COG1048  763 VVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERI 799
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 54-162 3.01e-09

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 54.63  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQAVDRIE---TGDEL-EVDFSSGEIRN 129
Cdd:PTZ00092 774 IVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNGENADSlglTGKEQfSIDLNSGELKP 853

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499170190 130 LTKGEVYRANP--FP-----DFIMEI--IKAGGLVEWAKRRL 162
Cdd:PTZ00092 854 GQDVTVKTDTGktFDtilriDTEVEVeyFKHGGILQYVLRKL 895
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 54-121 7.05e-09

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: 51.70  E-value: 7.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIG-LPILEA-PQAVDRIETGDELEVD 121
Cdd:cd01578   72 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGlLPLTFAdPADYDKIHPDDKVDIL 141
acnA PRK12881
aconitate hydratase AcnA;
54-128 8.74e-09

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 53.40  E-value: 8.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIG-LPiLEAPQAVDR----IETGDELEVDFSSGEIR 128
Cdd:PRK12881 762 VVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGvLP-LQFKGGDSRqslgLTGGETFDIEGLPGEIK 840
PRK09238 PRK09238
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
 75-153 3.18e-07

bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated


Pssm-ID: 236424 [Multi-domain]  Cd Length: 835  Bit Score: 48.64  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  75 KAAGVscVIAKSFARIFYRNAINIG-LPIlEAPqaVDRIETGDELEVDFSSGEIRNLTKGEVYRANPFPDFIMEIIKAGG 153
Cdd:PRK09238 258 RAGGV--VLGGKIAPIFFNTMEDSGaLPI-ELD--VSKLNMGDVIDIYPYKGKIRNETGEVIATFKLKTDVLLDEVRAGG 332
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 54-117 7.07e-07

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: 46.50  E-value: 7.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIGLPILEAPQAVDRIE---TGDE 117
Cdd:cd01580   99 VILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSlglTGEE 165
PRK09277 PRK09277
aconitate hydratase AcnA;
54-117 1.02e-06

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 47.43  E-value: 1.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIG-LPiLEAPQAVDRIE---TGDE 117
Cdd:PRK09277 761 VVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGvLP-LQFKPGESRKTlglDGTE 827
PLN00070 PLN00070
aconitate hydratase
 54-100 5.02e-06

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 45.57  E-value: 5.02e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499170190  54 IIVAGENFGCGSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIGL 100
Cdd:PLN00070 810 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGI 856
PRK14812 PRK14812
hypothetical protein; Provisional
 64-148 9.84e-06

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 42.79  E-value: 9.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  64 GSSREHAPLAIKAAGVSCVIAKSFARIFYRNAINIG-LPIL---EAPQAVDRIETGDELEVDFSSGEIrnltkgevyrAN 139
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGmLPIVqprEVREKLAQLKPTDQVTVDLEQQKI----------IS 72


                 ....*....
gi 499170190 140 PFPDFIMEI 148
Cdd:PRK14812  73 PVEEFTFEI 81
PykA2 COG3848
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
44-125 6.65e-05

Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];


Pssm-ID: 443058  Cd Length: 321  Bit Score: 41.81  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499170190  44 EFRSKMKPGDIIVAGEnfgcgSSREHAPLAIKAAGVscVIAK----SFARIFyrnAINIGLP-ILEAPQAVDRIETGDEL 118
Cdd:COG3848  235 EALEKFEEGDILVVPS-----TDAEFVPAIEKAAGI--ITEEggltSHAAIV---GLELGIPvIVGAEGATEILKDGQVV 304


                 ....*..
gi 499170190 119 EVDFSSG 125
Cdd:COG3848  305 TVDAERG 311
 
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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