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Conserved domains on  [gi|651990614|ref|WP_026698277|]
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3-isopropylmalate dehydratase small subunit [Alkalicoccus chagannorensis]

Protein Classification

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

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

CATH:  3.20.19.10
EC:  4.2.1.33
Gene Symbol:  leuD
Gene Ontology:  GO:0003861|GO:0009098
PubMed:  20938981
SCOP:  4003492

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-193 9.64e-121

3-isopropylmalate dehydratase small subunit;


:

Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 339.80  E-value: 9.64e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFHDDGTPREDFSLNNPVYEAASILVAGENFGCG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  81 SSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAE-SSSYHLTADLEAQRVYDNqGFEASF 159
Cdd:PRK01641  81 SSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEaNPGAELTVDLEAQTVTAP-DKTFPF 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 651990614 160 DITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:PRK01641 160 EIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-193 9.64e-121

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 339.80  E-value: 9.64e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFHDDGTPREDFSLNNPVYEAASILVAGENFGCG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  81 SSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAE-SSSYHLTADLEAQRVYDNqGFEASF 159
Cdd:PRK01641  81 SSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEaNPGAELTVDLEAQTVTAP-DKTFPF 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 651990614 160 DITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:PRK01641 160 EIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-193 1.56e-109

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: 310.95  E-value: 1.56e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   2 EPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFhdDGTPREDFSLNNPVYEAASILVAGENFGCGS 81
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRY--DRSPDPDFVLNQPRYQGADILVAGRNFGCGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  82 SREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAESSS-YHLTADLEAQRVYDNQGFEASFD 160
Cdd:COG0066   79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPgDELTVDLEAGTVTNGTGETYPFE 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 651990614 161 ITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:COG0066  159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKR 191
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 1-186 2.28e-91

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: 265.14  E-value: 2.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614    1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFHDD-GT-PREDFSLNNPVYEAASILVAGENFG 78
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDAnGKePNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   79 CGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAESSSYHLTADLEAQRVYDNQGFEAS 158
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVENQGLQMTVDLENQLIHDSEGKVYS 160

                         170       180
                  ....*....|....*....|....*...
gi 651990614  159 FDITSYMREMLLNGWDEISVTLTHEDKI 186
Cdd:TIGR00171 161 FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 1-124 4.88e-45

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: 145.59  E-value: 4.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614    1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRF----HDDGTPREDFSLNNPVY--EAASILV-A 73
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYgkvrYLPDGENPDFYDAAMRYkqHGAPIVViG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 651990614   74 GENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQE 124
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 14-144 1.57e-43

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 140.42  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  14 INRSNIDTDQIIPKQFLkrierqgfgqflfynwrfhddgtpredfslnnpvyeaASILVAGENFGCGSSREHAPWALQDF 93
Cdd:cd01577    1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 651990614  94 GFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEaimTAAESSSYHLTADL 144
Cdd:cd01577   44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVE---EVEAKPGDEVEVDL 91
HacB2_Meth NF040625
homoaconitase small subunit;
16-110 2.79e-19

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 80.14  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  16 RSNIDTDQIIPKQFLKRIERQGFGQflfynwrfHDDGTPREDFSLNnpvYEAASILVAGENFGCGSSREHAPWALQDFGF 95
Cdd:NF040625  12 GDNIDTDVIIPGRYLRTFNPDDLAS--------HVMEGERPDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80

                         90
                 ....*....|....*
gi 651990614  96 RVIIAPSFADIFYNN 110
Cdd:NF040625  81 SAIIAKSFARIFYRN 95
 
Name Accession Description Interval E-value
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
1-193 9.64e-121

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 339.80  E-value: 9.64e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFHDDGTPREDFSLNNPVYEAASILVAGENFGCG 80
Cdd:PRK01641   1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  81 SSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAE-SSSYHLTADLEAQRVYDNqGFEASF 159
Cdd:PRK01641  81 SSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEaNPGAELTVDLEAQTVTAP-DKTFPF 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 651990614 160 DITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:PRK01641 160 EIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKR 193
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 2-193 1.56e-109

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: 310.95  E-value: 1.56e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   2 EPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFhdDGTPREDFSLNNPVYEAASILVAGENFGCGS 81
Cdd:COG0066    1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRY--DRSPDPDFVLNQPRYQGADILVAGRNFGCGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  82 SREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAESSS-YHLTADLEAQRVYDNQGFEASFD 160
Cdd:COG0066   79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPgDELTVDLEAGTVTNGTGETYPFE 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 651990614 161 ITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:COG0066  159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKR 191
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 1-186 2.28e-91

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: 265.14  E-value: 2.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614    1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRFHDD-GT-PREDFSLNNPVYEAASILVAGENFG 78
Cdd:TIGR00171   1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDAnGKePNPDFVLNQPQYQGASILLARENFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   79 CGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAIMTAAESSSYHLTADLEAQRVYDNQGFEAS 158
Cdd:TIGR00171  81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVENQGLQMTVDLENQLIHDSEGKVYS 160

                         170       180
                  ....*....|....*....|....*...
gi 651990614  159 FDITSYMREMLLNGWDEISVTLTHEDKI 186
Cdd:TIGR00171 161 FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 1-124 4.88e-45

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: 145.59  E-value: 4.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614    1 MEPIQQHEGLVYPINRSNIDTDQIIPKQFLKRIERQGFGQFLFYNWRF----HDDGTPREDFSLNNPVY--EAASILV-A 73
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYgkvrYLPDGENPDFYDAAMRYkqHGAPIVViG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 651990614   74 GENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQE 124
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 14-144 1.57e-43

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 140.42  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  14 INRSNIDTDQIIPKQFLkrierqgfgqflfynwrfhddgtpredfslnnpvyeaASILVAGENFGCGSSREHAPWALQDF 93
Cdd:cd01577    1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 651990614  94 GFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEaimTAAESSSYHLTADL 144
Cdd:cd01577   44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVE---EVEAKPGDEVEVDL 91
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 18-172 1.86e-26

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 98.75  E-value: 1.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  18 NIDTDQIIPKQFLKRIERQGFGQFLFynwrfHDdgtPREDFSLNnpvYEAASILVAGENFGCGSSREHAPWALQDFGFRV 97
Cdd:PRK00439  10 NIDTDVIIPARYLNTSDPQELAKHCM-----ED---LDPEFAKK---VKPGDIIVAGKNFGCGSSREHAPIALKAAGVSA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 651990614  98 IIAPSFADIFYNNCSKNGiLPIALKQEEVEAIMTAAEsssyhLTADLEAQRVYD-NQGFEASFD-ITSYMREMLLNG 172
Cdd:PRK00439  79 VIAKSFARIFYRNAINIG-LPVLECDEAVDKIEDGDE-----VEVDLETGVITNlTTGEEYKFKpIPEFMLEILKAG 149
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 18-127 3.73e-25

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: 95.18  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   18 NIDTDQIIPKQFLKRIERQGFGQFLFYNwrfhddgtPREDFSLNnpvYEAASILVAGENFGCGSSREHAPWALQDFGFRV 97
Cdd:TIGR02087   9 DIDTDEIIPGRYLRTTDPDELASHAMEG--------IDPEFAKK---VRPGDVIVAGKNFGCGSSREQAALALKAAGIAA 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 651990614   98 IIAPSFADIFYNNCSKNGILPIALKQEEVE 127
Cdd:TIGR02087  78 VIAESFARIFYRNAINIGLPLIEAKTEGIK 107
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 9-115 3.25e-23

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 92.61  E-value: 3.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   9 GLVYpINRSNIDTDQIIPKQFL-----KRIERQGFGQF------LFYNWRFHDDGTPREDFSlnnpvyeaasILVAGENF 77
Cdd:PLN00072  71 GLCF-VVGDNIDTDQIIPAEYLtlvpsKPDEYEKLGSYaliglpAFYKTRFVEPGEMKTKYS----------IIIGGENF 139

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 651990614  78 GCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNG 115
Cdd:PLN00072 140 GCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATG 177
PRK14812 PRK14812
hypothetical protein; Provisional
 80-193 5.96e-23

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 88.62  E-value: 5.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  80 GSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQEEVEAImtAAESSSYHLTADLEAQRVYDNQGfEASF 159
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKL--AQLKPTDQVTVDLEQQKIISPVE-EFTF 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 651990614 160 DITSYMREMLLNGWDEISVTLTHEDKISQFEAAR 193
Cdd:PRK14812  80 EIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQR 113
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 18-136 1.01e-20

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The 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: 84.07  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614   18 NIDTDQIIPKQFLKRIERQGFGQflfynwrfHDDGTPREDFSlnNPVYEAaSILVAGENFGCGSSREHAPWALQDFGFRV 97
Cdd:TIGR02084   9 NVDTDVIIPARYLNTSDPKELAK--------HCMEDLDKDFV--KKVKEG-DIIVAGENFGCGSSREHAPIAIKASGISC 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 651990614   98 IIAPSFADIFYNNCSKNGiLPIALKQEEVEAIMTAAESS 136
Cdd:TIGR02084  78 VIAKSFARIFYRNAINIG-LPIVESEEAVDEIEEGDEVE 115
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 18-118 1.03e-19

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 81.39  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  18 NIDTDQIIPKQFLKRIerqgFGQFLFYNWRFHDdgtPREDFSlnnPVYEAASILVAGENFGCGSSREHAPWALQDFGFRV 97
Cdd:PRK14023  10 NINTDDILPGKYAPFM----VGEDRFHNYAFAH---LRPEFA---STVRPGDILVAGRNFGLGSSREYAPEALKMLGIGA 79

                         90       100
                 ....*....|....*....|.
gi 651990614  98 IIAPSFADIFYNNCSKNGILP 118
Cdd:PRK14023  80 IIAKSYARIFYRNLVNLGIPP 100
HacB2_Meth NF040625
homoaconitase small subunit;
16-110 2.79e-19

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 80.14  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  16 RSNIDTDQIIPKQFLKRIERQGFGQflfynwrfHDDGTPREDFSLNnpvYEAASILVAGENFGCGSSREHAPWALQDFGF 95
Cdd:NF040625  12 GDNIDTDVIIPGRYLRTFNPDDLAS--------HVMEGERPDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80

                         90
                 ....*....|....*
gi 651990614  96 RVIIAPSFADIFYNN 110
Cdd:NF040625  81 SAIIAKSFARIFYRN 95
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 70-119 1.89e-16

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: 70.96  E-value: 1.89e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 651990614  70 ILVAGENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPI 119
Cdd:cd00404   18 VVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPL 67
PRK07229 PRK07229
aconitate hydratase; Validated
 69-172 6.65e-14

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 69.02  E-value: 6.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  69 SILVAGENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQE------------EVEAIMTAAESS 136
Cdd:PRK07229 525 GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPadydkieegdvlEIEDLREFLPGG 604

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 651990614 137 syhltaDLEAQRVYDNQGFEASFDITSYMREMLLNG 172
Cdd:PRK07229 605 ------PLTVVNVTKDEEIEVRHTLSERQIEILLAG 634
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 18-125 1.08e-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: 62.07  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  18 NIDTDQIIPK-----QFLKRIERqgFGQFLFYnwRFHDDGTPREDFSlnnpvyeAASILVAGENFGCGSSREHAPWALQD 92
Cdd:cd01579    5 NITTDHIMPAgakvlPLRSNIPA--ISEFVFH--RVDPTFAERAKAA-------GPGFIVGGENYGQGSSREHAALAPMY 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 651990614  93 FGFRVIIAPSFADIFYNNCSKNGILPIALKQEE 125
Cdd:cd01579   74 LGVRAVLAKSFARIHRANLINFGILPLTFADED 106
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 18-141 1.53e-09

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: 53.83  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  18 NIDTDQIIPKQFlkrierqgfgqflfynwRFHDDGTPREDFSLNNPVYEAAS--------ILVAGENFGCGSSREHAPWA 89
Cdd:cd01674    5 NLNTDGIYPGKY-----------------TYQDDITPEKMAEVCMENYDSEFstktkqgdILVSGFNFGTGSSREQAATA 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 651990614  90 LQDFGFRVIIAPSFADIFYNNCSKNGILPIALKqEEVEAIMTAAESSSYHLT 141
Cdd:cd01674   68 LLAKGIPLVVSGSFGNIFSRNSINNALLSIELP-FLVQKLREAFANESKELT 118
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 69-119 1.56e-08

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 51.32  E-value: 1.56e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 651990614  69 SILVAGENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPI 119
Cdd:cd01578   71 WVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 121
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 63-125 1.44e-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: 50.49  E-value: 1.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651990614  63 PVYEAA---------SILVAGENFGCGSSREHA---PwALQdfGFRVIIAPSFADIFYNNCSKNGILPIALKQEE 125
Cdd:COG1048  747 SIYDAAmrykaegtpLVVLAGKEYGTGSSRDWAakgT-RLL--GVKAVIAESFERIHRSNLVGMGVLPLQFPEGE 818
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 63-125 6.26e-07

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 48.85  E-value: 6.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 651990614  63 PVYEAAS---------ILVAGENFGCGSSREhapWA-----LQdfGFRVIIAPSFADIFYNNCSKNGILPIALKQEE 125
Cdd:PTZ00092 758 SIYDAAEkykqegvplIVLAGKEYGSGSSRD---WAakgpyLQ--GVKAVIAESFERIHRSNLVGMGILPLQFLNGE 829
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 63-125 9.98e-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: 46.89  E-value: 9.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651990614  63 PVYEAAS---------ILVAGENFGCGSSREhapWALQD---FGFRVIIAPSFADIFYNNCSKNGILPIALKQEE 125
Cdd:cd01580   83 SIYDAAMrykeegvplVILAGKEYGSGSSRD---WAAKGpflLGVKAVIAESFERIHRSNLVGMGILPLQFPPGE 154
acnA PRK12881
aconitate hydratase AcnA;
63-122 3.12e-05

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 43.77  E-value: 3.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651990614  63 PVYEAA---------SILVAGENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALK 122
Cdd:PRK12881 746 SIYDAAmryqaagtpLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFK 814
PLN00070 PLN00070
aconitate hydratase
 64-145 1.56e-04

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 41.71  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990614  64 VYEAA---------SILVAGENFGCGSSREHAPWALQDFGFRVIIAPSFADIFYNNCSKNGILPIALKQ-EEVEAI-MTA 132
Cdd:PLN00070 795 VFDAAmkykseghdTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSgEDADTLgLTG 874

                         90
                 ....*....|...
gi 651990614 133 AESSSYHLTADLE 145
Cdd:PLN00070 875 HERYTIDLPSNIS 887
PRK09277 PRK09277
aconitate hydratase AcnA;
63-125 3.90e-04

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 40.49  E-value: 3.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651990614  63 PVYEAAS---------ILVAGENFGCGSSREhapWA------LqdfGFRVIIAPSFADIFYNNCSKNGILPIALKQEE 125
Cdd:PRK09277 745 SIYDAAMkykeegtplVVIAGKEYGTGSSRD---WAakgtrlL---GVKAVIAESFERIHRSNLVGMGVLPLQFKPGE 816
 
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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