|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
1-253 |
1.50e-154 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 429.66 E-value: 1.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 1 MATSQQFLNPTLFKSLASSNKNSCTLCPSPFLQLKSASTIFNYKPLTSSSATIITRVaassSDSGESITRETFHGLCFVL 80
Cdd:PLN00072 1 MAASQQSANPTLAPSLASTNKSSSSATPRPFLRFSSTSSIFPFKPLTTSSGTSSPTI----SDSAESTSSTTFHGLCFVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 81 KDNIDTDQIIPAEYGTLIPSIPEDREKLGSFALNGLPKFYNERFVVPGEMKSKYSVIIGGDNFGCGSSREHAPVCLGAAG 160
Cdd:PLN00072 77 GDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFGCGSSREHAPVALGAAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 161 AKAVVAESYARIFFRNCVATGEIFPLESEVRICDECKTGDVVTIEHkedGSSLLINHTTRKEYKLKPLGDAGPVIDAGGI 240
Cdd:PLN00072 157 AKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVEL---GNSVLINHTTGKEYKLKPIGDAGPVIDAGGI 233
|
250
....*....|...
gi 15231608 241 FAYARKAGMIPSA 253
Cdd:PLN00072 234 FAYARKTGMIPSA 246
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
72-204 |
1.82e-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: 109.49 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 72 TFHGLCFVL-KDNIDTDQIIPAEYGTLIpsipeDREKLGSFALNGLPKFYNER--FVVPgemKSKY---SVIIGGDNFGC 145
Cdd:COG0066 5 TLTGRAVPLdGDNIDTDQIIPARFLKTI-----DREGLGKHLFEDWRYDRSPDpdFVLN---QPRYqgaDILVAGRNFGC 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231608 146 GSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGeIFPLESEVRICD------ECKTGDVVTI 204
Cdd:COG0066 77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNG-LLPIELPEEAVDalfaaiEANPGDELTV 140
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
75-246 |
1.47e-28 |
|
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: 106.03 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 75 GLCFVLKDNIDTDQIIPAEYgtLIPSIPEDrekLGSFALNGL-PKFYNErfVVPGemkskySVIIGGDNFGCGSSREHAP 153
Cdd:TIGR02084 1 GKVHKYGDNVDTDVIIPARY--LNTSDPKE---LAKHCMEDLdKDFVKK--VKEG------DIIVAGENFGCGSSREHAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 154 VCLGAAGAKAVVAESYARIFFRNCVATGeiFP-LESEvRICDECKTGDVVTIEHKEdgsSLLINHTTRKEYKLKPLGD-A 231
Cdd:TIGR02084 68 IAIKASGISCVIAKSFARIFYRNAINIG--LPiVESE-EAVDEIEEGDEVEVDLEK---GIIKNLTKGKEYKATPFPEfL 141
|
170
....*....|....*
gi 15231608 232 GPVIDAGGIFAYARK 246
Cdd:TIGR02084 142 QKIMKAGGLLNYVKK 156
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
79-205 |
1.06e-25 |
|
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: 96.50 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 79 VLKDNIDTDQIIPAEYgtlipsipedrekLGSfalnglpkfynerfvvpgemkskysVIIGGDNFGCGSSREHAPVCLGA 158
Cdd:cd01577 1 LFGDNIDTDQIIPARF-------------LGD-------------------------IIVAGKNFGCGSSREHAPWALKD 42
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15231608 159 AGAKAVVAESYARIFFRNCVATGeIFPLESEVRICDECKTGDVVTIE 205
Cdd:cd01577 43 AGIRAVIAESFARIFFRNAINNG-LLPVTLADEDVEEVEAKPGDEVE 88
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
82-230 |
1.84e-21 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 87.46 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 82 DNIDTDQIIPAEYgtLIPSIPEDrekLGSFALNGlpkfynERFVVPGEMKsKYSVIIGGDNFGCGSSREHAPVCLGAAGA 161
Cdd:NF040625 13 DNIDTDVIIPGRY--LRTFNPDD---LASHVMEG------ERPDFTKNVQ-KGDIIVAGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 162 KAVVAESYARIFFRNCVATGeiFPleseVRICD-ECKTGDVVTIEhKEDGssLLINHTTRKEYKLKPLGD 230
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIG--LP----VIVADiEADDGDILSID-LEKG--IIKNKTTGEEFKIQPFKE 141
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
81-187 |
4.94e-12 |
|
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: 61.61 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 81 KDNIDTDQIIPaeygtlipsipedREKLGSFALNGLPK--FYNERF-------------VVPGEMKSKYS----VIIGGD 141
Cdd:pfam00694 16 NSNVDTDLIIP-------------KQFLGTIANIGIGNinFEGWRYgkvrylpdgenpdFYDAAMRYKQHgapiVVIGGK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15231608 142 NFGCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGeIFPLE 187
Cdd:pfam00694 83 NFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNG-LLPLE 127
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
1-253 |
1.50e-154 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 429.66 E-value: 1.50e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 1 MATSQQFLNPTLFKSLASSNKNSCTLCPSPFLQLKSASTIFNYKPLTSSSATIITRVaassSDSGESITRETFHGLCFVL 80
Cdd:PLN00072 1 MAASQQSANPTLAPSLASTNKSSSSATPRPFLRFSSTSSIFPFKPLTTSSGTSSPTI----SDSAESTSSTTFHGLCFVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 81 KDNIDTDQIIPAEYGTLIPSIPEDREKLGSFALNGLPKFYNERFVVPGEMKSKYSVIIGGDNFGCGSSREHAPVCLGAAG 160
Cdd:PLN00072 77 GDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYKTRFVEPGEMKTKYSIIIGGENFGCGSSREHAPVALGAAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 161 AKAVVAESYARIFFRNCVATGEIFPLESEVRICDECKTGDVVTIEHkedGSSLLINHTTRKEYKLKPLGDAGPVIDAGGI 240
Cdd:PLN00072 157 AKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVEL---GNSVLINHTTGKEYKLKPIGDAGPVIDAGGI 233
|
250
....*....|...
gi 15231608 241 FAYARKAGMIPSA 253
Cdd:PLN00072 234 FAYARKTGMIPSA 246
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
74-251 |
7.01e-35 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 122.63 E-value: 7.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 74 HGLCFVLKDNIDTDQIIPAEYgtLIPSIPEDrekLGSFALNGL-PKFYNErfVVPGEmkskysVIIGGDNFGCGSSREHA 152
Cdd:PRK00439 1 KGRVWKFGDNIDTDVIIPARY--LNTSDPQE---LAKHCMEDLdPEFAKK--VKPGD------IIVAGKNFGCGSSREHA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 153 PVCLGAAGAKAVVAESYARIFFRNCVATGeiFP-LESEvRICDECKTGDVVTIEHKedgSSLLINHTTRKEYKLKPLGD- 230
Cdd:PRK00439 68 PIALKAAGVSAVIAKSFARIFYRNAINIG--LPvLECD-EAVDKIEDGDEVEVDLE---TGVITNLTTGEEYKFKPIPEf 141
|
170 180
....*....|....*....|.
gi 15231608 231 AGPVIDAGGIFAYARKAGMIP 251
Cdd:PRK00439 142 MLEILKAGGLIEYLKKKGRFP 162
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
72-204 |
1.82e-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: 109.49 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 72 TFHGLCFVL-KDNIDTDQIIPAEYGTLIpsipeDREKLGSFALNGLPKFYNER--FVVPgemKSKY---SVIIGGDNFGC 145
Cdd:COG0066 5 TLTGRAVPLdGDNIDTDQIIPARFLKTI-----DREGLGKHLFEDWRYDRSPDpdFVLN---QPRYqgaDILVAGRNFGC 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231608 146 GSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGeIFPLESEVRICD------ECKTGDVVTI 204
Cdd:COG0066 77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNG-LLPIELPEEAVDalfaaiEANPGDELTV 140
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
75-246 |
1.47e-28 |
|
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: 106.03 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 75 GLCFVLKDNIDTDQIIPAEYgtLIPSIPEDrekLGSFALNGL-PKFYNErfVVPGemkskySVIIGGDNFGCGSSREHAP 153
Cdd:TIGR02084 1 GKVHKYGDNVDTDVIIPARY--LNTSDPKE---LAKHCMEDLdKDFVKK--VKEG------DIIVAGENFGCGSSREHAP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 154 VCLGAAGAKAVVAESYARIFFRNCVATGeiFP-LESEvRICDECKTGDVVTIEHKEdgsSLLINHTTRKEYKLKPLGD-A 231
Cdd:TIGR02084 68 IAIKASGISCVIAKSFARIFYRNAINIG--LPiVESE-EAVDEIEEGDEVEVDLEK---GIIKNLTKGKEYKATPFPEfL 141
|
170
....*....|....*
gi 15231608 232 GPVIDAGGIFAYARK 246
Cdd:TIGR02084 142 QKIMKAGGLLNYVKK 156
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
82-247 |
2.66e-26 |
|
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: 100.19 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 82 DNIDTDQIIPAEYGTLIpsipeDREKLGSFALNGL-PKFYNErfVVPGEmkskysVIIGGDNFGCGSSREHAPVCLGAAG 160
Cdd:TIGR02087 8 DDIDTDEIIPGRYLRTT-----DPDELASHAMEGIdPEFAKK--VRPGD------VIVAGKNFGCGSSREQAALALKAAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 161 AKAVVAESYARIFFRNCVATGeIFPLESEVricDECKTGDVVTIehkeDGSSLLINHTTRKEYKLKPLGD-AGPVIDAGG 239
Cdd:TIGR02087 75 IAAVIAESFARIFYRNAINIG-LPLIEAKT---EGIKDGDEVTV----DLETGEIRVNGNEEYKGEPLPDfLLEILREGG 146
|
....*...
gi 15231608 240 IFAYARKA 247
Cdd:TIGR02087 147 LLEYLKKR 154
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
79-205 |
1.06e-25 |
|
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: 96.50 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 79 VLKDNIDTDQIIPAEYgtlipsipedrekLGSfalnglpkfynerfvvpgemkskysVIIGGDNFGCGSSREHAPVCLGA 158
Cdd:cd01577 1 LFGDNIDTDQIIPARF-------------LGD-------------------------IIVAGKNFGCGSSREHAPWALKD 42
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15231608 159 AGAKAVVAESYARIFFRNCVATGeIFPLESEVRICDECKTGDVVTIE 205
Cdd:cd01577 43 AGIRAVIAESFARIFFRNAINNG-LLPVTLADEDVEEVEAKPGDEVE 88
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
82-230 |
1.84e-21 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 87.46 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 82 DNIDTDQIIPAEYgtLIPSIPEDrekLGSFALNGlpkfynERFVVPGEMKsKYSVIIGGDNFGCGSSREHAPVCLGAAGA 161
Cdd:NF040625 13 DNIDTDVIIPGRY--LRTFNPDD---LASHVMEG------ERPDFTKNVQ-KGDIIVAGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 162 KAVVAESYARIFFRNCVATGeiFPleseVRICD-ECKTGDVVTIEhKEDGssLLINHTTRKEYKLKPLGD 230
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIG--LP----VIVADiEADDGDILSID-LEKG--IIKNKTTGEEFKIQPFKE 141
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
82-253 |
2.38e-20 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 84.85 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 82 DNIDTDQIIPAEYGTLIpsIPEDREKLGSFAlNGLPKFYNErfVVPGEmkskysVIIGGDNFGCGSSREHAPVCLGAAGA 161
Cdd:PRK14023 9 DNINTDDILPGKYAPFM--VGEDRFHNYAFA-HLRPEFAST--VRPGD------ILVAGRNFGLGSSREYAPEALKMLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 162 KAVVAESYARIFFRNCVATGeIFPLESEvRICDECKTGDVVTIEHKedgSSLLINHTTRkeYKLKPLGD-AGPVIDAGGI 240
Cdd:PRK14023 78 GAIIAKSYARIFYRNLVNLG-IPPFESE-EVVDALEDGDEVELDLE---TGVLTRGGET--FQLRPPPEfLLEALKEGSI 150
|
170
....*....|...
gi 15231608 241 FAYARKAGMIPSA 253
Cdd:PRK14023 151 LEYYRKHGRFPGE 163
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
66-181 |
6.22e-19 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 81.71 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 66 ESITRETfhGLCFVLK-DNIDTDQIIPAEYGTLIpsipeDREKLGSFAlnglpkFYNERFVVPGEM-------KSKY--- 134
Cdd:PRK01641 2 EKFTTHT--GLAVPLDrANVDTDQIIPKQFLKRI-----TRTGFGKGL------FDDWRYLDDGQPnpdfvlnQPRYqga 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15231608 135 SVIIGGDNFGCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATG 181
Cdd:PRK01641 69 SILLAGDNFGCGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNG 115
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
79-187 |
2.55e-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: 64.77 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 79 VLKDNIDTDQIIPA--EYGTLIPSIPEdrekLGSFALNGLPKFYNERfvvpgEMKSKYSVIIGGDNFGCGSSREHAPVCL 156
Cdd:cd01579 1 KVGDNITTDHIMPAgaKVLPLRSNIPA----ISEFVFHRVDPTFAER-----AKAAGPGFIVGGENYGQGSSREHAALAP 71
|
90 100 110
....*....|....*....|....*....|.
gi 15231608 157 GAAGAKAVVAESYARIFFRNCVATGeIFPLE 187
Cdd:cd01579 72 MYLGVRAVLAKSFARIHRANLINFG-ILPLT 101
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
79-204 |
8.76e-13 |
|
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: 62.49 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 79 VLKDNIDTDQIIPAEYGtlipsipedreklgsfalnglpkfynerfvvpgemkskysVIIGGDNFGCGSSREHAPVCLGA 158
Cdd:cd00404 1 KVAGNITTDHISPAGPG----------------------------------------VVIGDENYGTGSSREHAALELRL 40
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15231608 159 AGAKAVVAESYARIFFRNCVATGeIFPLESEVRI-CDECKTGDVVTI 204
Cdd:cd00404 41 LGGRAVIAKSFARIFFRNLVDQG-LLPLEFADPEdYLKLHTGDELDI 86
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
72-181 |
1.08e-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: 64.84 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 72 TFHGLCFVL-KDNIDTDQIIPAEYGTLIpsipeDREKLGSFALNGLpKFYNER-------FVVPGEMKSKYSVIIGGDNF 143
Cdd:TIGR00171 6 SHTGLVAPLdAANVDTDAIIPKQFLKRI-----TRTGFGKHLFFDW-RFLDANgkepnpdFVLNQPQYQGASILLARENF 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 15231608 144 GCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATG 181
Cdd:TIGR00171 80 GCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNG 117
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
81-187 |
4.94e-12 |
|
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: 61.61 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 81 KDNIDTDQIIPaeygtlipsipedREKLGSFALNGLPK--FYNERF-------------VVPGEMKSKYS----VIIGGD 141
Cdd:pfam00694 16 NSNVDTDLIIP-------------KQFLGTIANIGIGNinFEGWRYgkvrylpdgenpdFYDAAMRYKQHgapiVVIGGK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15231608 142 NFGCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGeIFPLE 187
Cdd:pfam00694 83 NFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNG-LLPLE 127
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
80-246 |
4.99e-10 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 59.39 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 80 LKDNIDTDQIIPAEYGTL-----IPSIPEdreklgsFALNGLPKFYNERfvvpgeMKSKY-SVIIGGDNFGCGSSREHAP 153
Cdd:PRK07229 477 VGDNITTDHIMPAGAKWLpyrsnIPNISE-------FVFEGVDNTFPER------AKEQGgGIVVGGENYGQGSSREHAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 154 VCLGAAGAKAVVAESYARIFFRNCVATGeIFPLEsevrICDE-----CKTGDVVTI----EHKEDGSSLLINHTTRKEYK 224
Cdd:PRK07229 544 LAPRYLGVKAVLAKSFARIHKANLINFG-ILPLT----FADPadydkIEEGDVLEIedlrEFLPGGPLTVVNVTKDEEIE 618
|
170 180
....*....|....*....|....*.
gi 15231608 225 LKPlgDAGP----VIDAGGIFAYARK 246
Cdd:PRK07229 619 VRH--TLSErqieILLAGGALNLIKK 642
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
82-183 |
8.06e-07 |
|
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: 46.90 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231608 82 DNIDTDQIIPAEYgTLIPSIPedREKLGSFA-LNGLPKFynerfvvpGEMKSKYSVIIGGDNFGCGSSREHAPVCLGAAG 160
Cdd:cd01674 4 DNLNTDGIYPGKY-TYQDDIT--PEKMAEVCmENYDSEF--------STKTKQGDILVSGFNFGTGSSREQAATALLAKG 72
|
90 100
....*....|....*....|....*
gi 15231608 161 AKAVVAESYARIFFRNCV--ATGEI 183
Cdd:cd01674 73 IPLVVSGSFGNIFSRNSInnALLSI 97
|
|
| |
