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Conserved domains on  [gi|15224221|ref|NP_181837|]
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Aconitase/3-isopropylmalate dehydratase protein [Arabidopsis thaliana]

Protein Classification

PLN00072 family protein( domain architecture ID 11476369)

PLN00072 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 1-249 9.75e-153

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


:

Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 425.04  E-value: 9.75e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    1 MAASLQSANPTLSRTLASPNKPSSFATFRsPFLRFNSTSVASNFKPLVSREASSSFVTRSAAEPQERKTFHGLCYVVGDN 80
Cdd:PLN00072   1 MAASQQSANPTLAPSLASTNKSSSSATPR-PFLRFSSTSSIFPFKPLTTSSGTSSPTISDSAESTSSTTFHGLCFVVGDN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   81 IDTDQIIPAEFLTLVPSNPEEYEKLGSYALVGLPASYKERFVQPGEMKTKYSIIIGGENFGCGSSREHAPVCLGAAGAKA 160
Cdd:PLN00072  80 IDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFGCGSSREHAPVALGAAGAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  161 VVAQSYARIFFRNSVATGEVYPLDSEVRVCDECTTGDVATVELreGDSILINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 240
Cdd:PLN00072 160 VVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVEL--GNSVLINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 237


                 ....*....
gi 15224221  241 RKAGMIPSA 249
Cdd:PLN00072 238 RKTGMIPSA 246
 
Name Accession Description Interval E-value
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 1-249 9.75e-153

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 425.04  E-value: 9.75e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    1 MAASLQSANPTLSRTLASPNKPSSFATFRsPFLRFNSTSVASNFKPLVSREASSSFVTRSAAEPQERKTFHGLCYVVGDN 80
Cdd:PLN00072   1 MAASQQSANPTLAPSLASTNKSSSSATPR-PFLRFSSTSSIFPFKPLTTSSGTSSPTISDSAESTSSTTFHGLCFVVGDN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   81 IDTDQIIPAEFLTLVPSNPEEYEKLGSYALVGLPASYKERFVQPGEMKTKYSIIIGGENFGCGSSREHAPVCLGAAGAKA 160
Cdd:PLN00072  80 IDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFGCGSSREHAPVALGAAGAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  161 VVAQSYARIFFRNSVATGEVYPLDSEVRVCDECTTGDVATVELreGDSILINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 240
Cdd:PLN00072 160 VVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVEL--GNSVLINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 237


                 ....*....
gi 15224221  241 RKAGMIPSA 249
Cdd:PLN00072 238 RKTGMIPSA 246
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 72-242 1.42e-36

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: 126.83  E-value: 1.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    72 GLCYVVGDNIDTDQIIPAEFLTlvPSNPEEyekLGSYALVGLPASYKERfVQPGemktkySIIIGGENFGCGSSREHAPV 151
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLN--TSDPKE---LAKHCMEDLDKDFVKK-VKEG------DIIVAGENFGCGSSREHAPI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   152 CLGAAGAKAVVAQSYARIFFRNSVATGevYPLDSEVRVCDECTTGDVATVELREGdsILINHTTGKEYKLKPIGD-AGPV 230
Cdd:TIGR02084  69 AIKASGISCVIAKSFARIFYRNAINIG--LPIVESEEAVDEIEEGDEVEVDLEKG--IIKNLTKGKEYKATPFPEfLQKI 144

                         170
                  ....*....|..
gi 15224221   231 IDAGGIFAYARK 242
Cdd:TIGR02084 145 MKAGGLLNYVKK 156
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 65-212 2.31e-29

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: 109.11  E-value: 2.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  65 QERKTFHGLCYVV-GDNIDTDQIIPAEFLTLVpsNPEEyekLGSYALVGLPASYKER--FV------QPGemktkySIII 135
Cdd:COG0066   1 EKFTTLTGRAVPLdGDNIDTDQIIPARFLKTI--DREG---LGKHLFEDWRYDRSPDpdFVlnqpryQGA------DILV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221 136 GGENFGCGSSREHAPVCLgaagakavvAQ---------SYARIFFRNSVATGevYPLdseVRVCDECTTGDVATVELREG 206
Cdd:COG0066  70 AGRNFGCGSSREHAPWAL---------KDygfraviapSFADIFYRNAINNG--LLP---IELPEEAVDALFAAIEANPG 135


                ....*.
gi 15224221 207 DSILIN 212
Cdd:COG0066 136 DELTVD 141
HacB2_Meth NF040625
homoaconitase small subunit;
78-226 5.54e-29

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 107.10  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   78 GDNIDTDQIIPAEFLTLVpsNPEEyekLGSYALVGLPASYKERfVQPGEmktkysIIIGGENFGCGSSREHAPVCLGAAG 157
Cdd:NF040625  12 GDNIDTDVIIPGRYLRTF--NPDD---LASHVMEGERPDFTKN-VQKGD------IIVAGWNFGCGSSREQAPVAIKHAG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  158 AKAVVAQSYARIFFRNSVATGevYPldseVRVCD-ECTTGDVATVELREGdsILINHTTGKEYKLKPIGD 226
Cdd:NF040625  80 VSAIIAKSFARIFYRNAINIG--LP----VIVADiEADDGDILSIDLEKG--IIKNKTTGEEFKIQPFKE 141
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 76-203 1.19e-27

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: 101.51  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  76 VVGDNIDTDQIIPAEFLtlvpsnpeeyeklgsyalvglpasykerfvqpgemktkYSIIIGGENFGCGSSREHAPVCLGA 155
Cdd:cd01577   1 LFGDNIDTDQIIPARFL--------------------------------------GDIIVAGKNFGCGSSREHAPWALKD 42

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15224221 156 AGAKAVVAQSYARIFFRNSVATGeVYPLDSEVRVCDECTTGDVATVEL 203
Cdd:cd01577  43 AGIRAVIAESFARIFFRNAINNG-LLPVTLADEDVEEVEAKPGDEVEV 89
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 79-183 2.21e-11

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: 59.69  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    79 DNIDTDQIIPAEFL-----TLVPSNPEEYEKLGSYalVGLPASYKERFVQpGEMKTKYS----IIIGGENFGCGSSREHA 149
Cdd:pfam00694  17 SNVDTDLIIPKQFLgtianIGIGNINFEGWRYGKV--RYLPDGENPDFYD-AAMRYKQHgapiVVIGGKNFGCGSSREHA 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15224221   150 PVCLGAAGAKAVVAQSYARIFFRNSVATGeVYPL 183
Cdd:pfam00694  94 AWALRDLGIKAVIAESFARIHRNNLIKNG-LLPL 126
 
Name Accession Description Interval E-value
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 1-249 9.75e-153

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 425.04  E-value: 9.75e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    1 MAASLQSANPTLSRTLASPNKPSSFATFRsPFLRFNSTSVASNFKPLVSREASSSFVTRSAAEPQERKTFHGLCYVVGDN 80
Cdd:PLN00072   1 MAASQQSANPTLAPSLASTNKSSSSATPR-PFLRFSSTSSIFPFKPLTTSSGTSSPTISDSAESTSSTTFHGLCFVVGDN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   81 IDTDQIIPAEFLTLVPSNPEEYEKLGSYALVGLPASYKERFVQPGEMKTKYSIIIGGENFGCGSSREHAPVCLGAAGAKA 160
Cdd:PLN00072  80 IDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFGCGSSREHAPVALGAAGAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  161 VVAQSYARIFFRNSVATGEVYPLDSEVRVCDECTTGDVATVELreGDSILINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 240
Cdd:PLN00072 160 VVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVEL--GNSVLINHTTGKEYKLKPIGDAGPVIDAGGIFAYA 237


                 ....*....
gi 15224221  241 RKAGMIPSA 249
Cdd:PLN00072 238 RKTGMIPSA 246
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 71-247 7.92e-42

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 140.35  E-value: 7.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   71 HGLCYVVGDNIDTDQIIPAEFLTLvpSNPEEyekLGSYALVGLPASYKERfVQPGEmktkysIIIGGENFGCGSSREHAP 150
Cdd:PRK00439   1 KGRVWKFGDNIDTDVIIPARYLNT--SDPQE---LAKHCMEDLDPEFAKK-VKPGD------IIVAGKNFGCGSSREHAP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  151 VCLGAAGAKAVVAQSYARIFFRNSVATGevYPldseVRVCDECT----TGDVATVELREGdsILINHTTGKEYKLKPIGD 226
Cdd:PRK00439  69 IALKAAGVSAVIAKSFARIFYRNAINIG--LP----VLECDEAVdkieDGDEVEVDLETG--VITNLTTGEEYKFKPIPE 140

                        170       180
                 ....*....|....*....|..
gi 15224221  227 -AGPVIDAGGIFAYARKAGMIP 247
Cdd:PRK00439 141 fMLEILKAGGLIEYLKKKGRFP 162
leud TIGR02084
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 72-242 1.42e-36

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: 126.83  E-value: 1.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    72 GLCYVVGDNIDTDQIIPAEFLTlvPSNPEEyekLGSYALVGLPASYKERfVQPGemktkySIIIGGENFGCGSSREHAPV 151
Cdd:TIGR02084   1 GKVHKYGDNVDTDVIIPARYLN--TSDPKE---LAKHCMEDLDKDFVKK-VKEG------DIIVAGENFGCGSSREHAPI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   152 CLGAAGAKAVVAQSYARIFFRNSVATGevYPLDSEVRVCDECTTGDVATVELREGdsILINHTTGKEYKLKPIGD-AGPV 230
Cdd:TIGR02084  69 AIKASGISCVIAKSFARIFYRNAINIG--LPIVESEEAVDEIEEGDEVEVDLEKG--IIKNLTKGKEYKATPFPEfLQKI 144

                         170
                  ....*....|..
gi 15224221   231 IDAGGIFAYARK 242
Cdd:TIGR02084 145 MKAGGLLNYVKK 156
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 72-243 7.59e-30

3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.


Pssm-ID: 273961 [Multi-domain]  Cd Length: 154  Bit Score: 109.05  E-value: 7.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    72 GLCYVVGDNIDTDQIIPAEFLTLVpsnpeEYEKLGSYALVGLPASYKERfVQPGEmktkysIIIGGENFGCGSSREHAPV 151
Cdd:TIGR02087   1 GRVWKFGDDIDTDEIIPGRYLRTT-----DPDELASHAMEGIDPEFAKK-VRPGD------VIVAGKNFGCGSSREQAAL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   152 CLGAAGAKAVVAQSYARIFFRNSVATGeVYPLDSEVRVCDEcttGDVATVELREGDSILinhTTGKEYKLKPIGD-AGPV 230
Cdd:TIGR02087  69 ALKAAGIAAVIAESFARIFYRNAINIG-LPLIEAKTEGIKD---GDEVTVDLETGEIRV---NGNEEYKGEPLPDfLLEI 141

                         170
                  ....*....|...
gi 15224221   231 IDAGGIFAYARKA 243
Cdd:TIGR02087 142 LREGGLLEYLKKR 154
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 65-212 2.31e-29

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: 109.11  E-value: 2.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  65 QERKTFHGLCYVV-GDNIDTDQIIPAEFLTLVpsNPEEyekLGSYALVGLPASYKER--FV------QPGemktkySIII 135
Cdd:COG0066   1 EKFTTLTGRAVPLdGDNIDTDQIIPARFLKTI--DREG---LGKHLFEDWRYDRSPDpdFVlnqpryQGA------DILV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221 136 GGENFGCGSSREHAPVCLgaagakavvAQ---------SYARIFFRNSVATGevYPLdseVRVCDECTTGDVATVELREG 206
Cdd:COG0066  70 AGRNFGCGSSREHAPWAL---------KDygfraviapSFADIFYRNAINNG--LLP---IELPEEAVDALFAAIEANPG 135


                ....*.
gi 15224221 207 DSILIN 212
Cdd:COG0066 136 DELTVD 141
HacB2_Meth NF040625
homoaconitase small subunit;
78-226 5.54e-29

homoaconitase small subunit;


Pssm-ID: 468597 [Multi-domain]  Cd Length: 161  Bit Score: 107.10  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   78 GDNIDTDQIIPAEFLTLVpsNPEEyekLGSYALVGLPASYKERfVQPGEmktkysIIIGGENFGCGSSREHAPVCLGAAG 157
Cdd:NF040625  12 GDNIDTDVIIPGRYLRTF--NPDD---LASHVMEGERPDFTKN-VQKGD------IIVAGWNFGCGSSREQAPVAIKHAG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  158 AKAVVAQSYARIFFRNSVATGevYPldseVRVCD-ECTTGDVATVELREGdsILINHTTGKEYKLKPIGD 226
Cdd:NF040625  80 VSAIIAKSFARIFYRNAINIG--LP----VIVADiEADDGDILSIDLEKG--IIKNKTTGEEFKIQPFKE 141
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 76-203 1.19e-27

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: 101.51  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  76 VVGDNIDTDQIIPAEFLtlvpsnpeeyeklgsyalvglpasykerfvqpgemktkYSIIIGGENFGCGSSREHAPVCLGA 155
Cdd:cd01577   1 LFGDNIDTDQIIPARFL--------------------------------------GDIIVAGKNFGCGSSREHAPWALKD 42

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15224221 156 AGAKAVVAQSYARIFFRNSVATGeVYPLDSEVRVCDECTTGDVATVEL 203
Cdd:cd01577  43 AGIRAVIAESFARIFFRNAINNG-LLPVTLADEDVEEVEAKPGDEVEV 89
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 78-250 1.10e-20

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 85.63  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   78 GDNIDTDQIIPAEFLTLVPSNpeeyEKLGSYALVGLPASYKERfVQPGEmktkysIIIGGENFGCGSSREHAPVCLGAAG 157
Cdd:PRK14023   8 GDNINTDDILPGKYAPFMVGE----DRFHNYAFAHLRPEFAST-VRPGD------ILVAGRNFGLGSSREYAPEALKMLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  158 AKAVVAQSYARIFFRNSVATGeVYPLDSEvRVCDECTTGDVATVELREGdsILInhTTGKEYKLKPIGD-AGPVIDAGGI 236
Cdd:PRK14023  77 IGAIIAKSYARIFYRNLVNLG-IPPFESE-EVVDALEDGDEVELDLETG--VLT--RGGETFQLRPPPEfLLEALKEGSI 150

                        170
                 ....*....|....
gi 15224221  237 FAYARKAGMIPSAA 250
Cdd:PRK14023 151 LEYYRKHGRFPGEV 164
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
68-178 1.79e-16

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 75.16  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   68 KTFHGLCYVV-GDNIDTDQIIPAEFLTLVpsnpeEYEKLGSYALvglpasYKERFVQPGEM-------KTKY---SIIIG 136
Cdd:PRK01641   5 TTHTGLAVPLdRANVDTDQIIPKQFLKRI-----TRTGFGKGLF------DDWRYLDDGQPnpdfvlnQPRYqgaSILLA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15224221  137 GENFGCGSSREHAPVCLGAAGAKAVVAQSYARIFFRNSVATG 178
Cdd:PRK01641  74 GDNFGCGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNG 115
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 76-183 3.67e-13

Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.


Pssm-ID: 238811 [Multi-domain]  Cd Length: 121  Bit Score: 64.38  E-value: 3.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  76 VVGDNIDTDQIIPA--EFLTLVPSNPEeyekLGSYALVGLPASYKERfvqpgEMKTKYSIIIGGENFGCGSSREHAPVCL 153
Cdd:cd01579   1 KVGDNITTDHIMPAgaKVLPLRSNIPA----ISEFVFHRVDPTFAER-----AKAAGPGFIVGGENYGQGSSREHAALAP 71

                        90       100       110
                ....*....|....*....|....*....|
gi 15224221 154 GAAGAKAVVAQSYARIFFRNSVATGeVYPL 183
Cdd:cd01579  72 MYLGVRAVLAKSFARIHRANLINFG-ILPL 100
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 80-178 3.22e-12

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: 63.30  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    80 NIDTDQIIPAEFLTLVpsnpeeyEKLGsyalVGLPASYKERF--VQPGEMKTKY----------SIIIGGENFGCGSSRE 147
Cdd:TIGR00171  18 NVDTDAIIPKQFLKRI-------TRTG----FGKHLFFDWRFldANGKEPNPDFvlnqpqyqgaSILLARENFGCGSSRE 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15224221   148 HAPVCLGAAGAKAVVAQSYARIFFRNSVATG 178
Cdd:TIGR00171  87 HAPWALDDYGFKVIIAPSFADIFYNNSFKNG 117
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 79-183 2.21e-11

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: 59.69  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221    79 DNIDTDQIIPAEFL-----TLVPSNPEEYEKLGSYalVGLPASYKERFVQpGEMKTKYS----IIIGGENFGCGSSREHA 149
Cdd:pfam00694  17 SNVDTDLIIPKQFLgtianIGIGNINFEGWRYGKV--RYLPDGENPDFYD-AAMRYKQHgapiVVIGGKNFGCGSSREHA 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15224221   150 PVCLGAAGAKAVVAQSYARIFFRNSVATGeVYPL 183
Cdd:pfam00694  94 AWALRDLGIKAVIAESFARIHRNNLIKNG-LLPL 126
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 76-201 2.31e-11

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: 58.63  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  76 VVGDNIDTDQIIPAEfltlvpsnpeeyeklgsyalvglpasykerfvqPGemktkysIIIGGENFGCGSSREHAPVCLGA 155
Cdd:cd00404   1 KVAGNITTDHISPAG---------------------------------PG-------VVIGDENYGTGSSREHAALELRL 40

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15224221 156 AGAKAVVAQSYARIFFRNSVATGEVyPLD-SEVRVCDECTTGDVATV 201
Cdd:cd00404  41 LGGRAVIAKSFARIFFRNLVDQGLL-PLEfADPEDYLKLHTGDELDI 86
PRK07229 PRK07229
aconitate hydratase; Validated
 77-242 3.73e-10

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 59.39  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221   77 VGDNIDTDQIIPA--EFLTLvPSNpeeYEKLGSYALVGLPASYKERFVQPGEmktkySIIIGGENFGCGSSREHAPVCLG 154
Cdd:PRK07229 477 VGDNITTDHIMPAgaKWLPY-RSN---IPNISEFVFEGVDNTFPERAKEQGG-----GIVVGGENYGQGSSREHAALAPR 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  155 AAGAKAVVAQSYARIFFRNSVATGeVYPL---DSE----VRVCDECTTGDVATvELREGDSILINHTTGKEYKLKPigDA 227
Cdd:PRK07229 548 YLGVKAVLAKSFARIHKANLINFG-ILPLtfaDPAdydkIEEGDVLEIEDLRE-FLPGGPLTVVNVTKDEEIEVRH--TL 623

                        170
                 ....*....|....*....
gi 15224221  228 GP----VIDAGGIFAYARK 242
Cdd:PRK07229 624 SErqieILLAGGALNLIKK 642
Homoaconitase_Swivel cd01674
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ...
 79-175 8.16e-08

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: 49.98  E-value: 8.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224221  79 DNIDTDQIIPAEFLTLVPSNPEEYEKLgsyalVGLPASYKERF-VQPGEmktkysIIIGGENFGCGSSREHAPVCLGAAG 157
Cdd:cd01674   4 DNLNTDGIYPGKYTYQDDITPEKMAEV-----CMENYDSEFSTkTKQGD------ILVSGFNFGTGSSREQAATALLAKG 72

                        90
                ....*....|....*...
gi 15224221 158 AKAVVAQSYARIFFRNSV 175
Cdd:cd01674  73 IPLVVSGSFGNIFSRNSI 90
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 133-149 2.91e-03

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: 38.55  E-value: 2.91e-03
                        10
                ....*....|....*..
gi 15224221 133 IIIGGENFGCGSSREHA 149
Cdd:COG1048 763 VVLAGKEYGTGSSRDWA 779
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 132-169 8.44e-03

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: 35.91  E-value: 8.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15224221 132 SIIIGGENFGCGSSREHAPVCLGAAGAKAVVAQSYARI 169
Cdd:cd01578  71 WVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARI 108
 
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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