|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
3-180 |
1.51e-107 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 307.56 E-value: 1.51e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVDDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYAMIGLPDRY-GKFIESGEQKTRYPIIIAGENFGCGSSRE 81
Cdd:PLN00072 67 TTFHGLCFVVGDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYkTRFVEPGEMKTKYSIIIGGENFGCGSSRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 82 HAPIALGAAGVTAVVALSYARIFFRNCSATGELYPMESVDRLCDLFATGQEVTVDFTAEQIVNHTLDRTFSLKPLGEVGP 161
Cdd:PLN00072 147 HAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVELGNSVLINHTTGKEYKLKPIGDAGP 226
|
170
....*....|....*....
gi 504991645 162 VIDAGGLFEYARQTGMIAA 180
Cdd:PLN00072 227 VIDAGGIFAYARKTGMIPS 245
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
3-180 |
4.75e-45 |
|
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: 147.24 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVD-DNIDTDQIIPAEYLTLVpsKPDEyekLGSYAMIGLpdRYGK-----FIESGEQKTRYPIIIAGENFGC 76
Cdd:COG0066 4 TTLTGRAVPLDgDNIDTDQIIPARFLKTI--DREG---LGKHLFEDW--RYDRspdpdFVLNQPRYQGADILVAGRNFGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 77 GSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGELY---PMESVDRLCDLFAT--GQEVTVDFTAEQIVNHTlDRTF 151
Cdd:COG0066 77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPielPEEAVDALFAAIEAnpGDELTVDLEAGTVTNGT-GETY 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 504991645 152 SLKplgevgpvIDAG-------GLFEYA---RQTGMIAA 180
Cdd:COG0066 156 PFE--------IDPFrrecllnGLDDIGltlKHADAIAA 186
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
7-174 |
2.67e-39 |
|
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: 131.45 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 7 GQIFVVDDNIDTDQIIPAEYLTlvPSKPDEyekLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREHAPIA 86
Cdd:TIGR02084 1 GKVHKYGDNVDTDVIIPARYLN--TSDPKE---LAKHCMEDLDKDFVKKVKEGD------IIVAGENFGCGSSREHAPIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 87 LGAAGVTAVVALSYARIFFRNCSATGelYPMESVDRLCDLFATGQEVTVDFTAEQIVNHTLDRTFSLKPLGE-VGPVIDA 165
Cdd:TIGR02084 70 IKASGISCVIAKSFARIFYRNAINIG--LPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEfLQKIMKA 147
|
....*....
gi 504991645 166 GGLFEYARQ 174
Cdd:TIGR02084 148 GGLLNYVKK 156
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-137 |
9.12e-33 |
|
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: 112.30 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYLtlvpskpdeyeklgsyamiglpdrygkfiesgeqktrYPIIIAGENFGCGSSREHAPIALGAAGVT 93
Cdd:cd01577 4 DNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIR 46
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504991645 94 AVVALSYARIFFRNCSATGeLYPMESVDRLCD--LFATGQEVTVDF 137
Cdd:cd01577 47 AVIAESFARIFFRNAINNG-LLPVTLADEDVEevEAKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
3-168 |
2.85e-32 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 113.27 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVDDNIDTDQIIPAEYLTLVpsKPDEyekLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREH 82
Cdd:NF040625 2 EIIKGKVWKFGDNIDTDVIIPGRYLRTF--NPDD---LASHVMEGERPDFTKNVQKGD------IIVAGWNFGCGSSREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 83 APIALGAAGVTAVVALSYARIFFRNCSATGelYPMESVDRLCDlfaTGQEVTVDFTAEQIVNHTLDRTFSLKPLGE-VGP 161
Cdd:NF040625 71 APVAIKHAGVSAIIAKSFARIFYRNAINIG--LPVIVADIEAD---DGDILSIDLEKGIIKNKTTGEEFKIQPFKEfMLE 145
|
....*..
gi 504991645 162 VIDAGGL 168
Cdd:NF040625 146 ILEDGGL 152
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
14-107 |
4.33e-14 |
|
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: 65.47 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYL-TLV----------PSKPDEYEKLGSYAMIGLPDRYGKFIESGeqktRYPIIIAGENFGCGSSREH 82
Cdd:pfam00694 17 SNVDTDLIIPKQFLgTIAnigigninfeGWRYGKVRYLPDGENPDFYDAAMRYKQHG----APIVVIGGKNFGCGSSREH 92
|
90 100
....*....|....*....|....*
gi 504991645 83 APIALGAAGVTAVVALSYARIFFRN 107
Cdd:pfam00694 93 AAWALRDLGIKAVIAESFARIHRNN 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
3-180 |
1.51e-107 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 307.56 E-value: 1.51e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVDDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYAMIGLPDRY-GKFIESGEQKTRYPIIIAGENFGCGSSRE 81
Cdd:PLN00072 67 TTFHGLCFVVGDNIDTDQIIPAEYLTLVPSKPDEYEKLGSYALIGLPAFYkTRFVEPGEMKTKYSIIIGGENFGCGSSRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 82 HAPIALGAAGVTAVVALSYARIFFRNCSATGELYPMESVDRLCDLFATGQEVTVDFTAEQIVNHTLDRTFSLKPLGEVGP 161
Cdd:PLN00072 147 HAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVRICEECKTGDVVTVELGNSVLINHTTGKEYKLKPIGDAGP 226
|
170
....*....|....*....
gi 504991645 162 VIDAGGLFEYARQTGMIAA 180
Cdd:PLN00072 227 VIDAGGIFAYARKTGMIPS 245
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
1-176 |
3.62e-49 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 156.53 E-value: 3.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 1 MGKVisgqiFVVDDNIDTDQIIPAEYLTLvpSKPDEyekLGSYAMIGL-PDRYGKFiESGEqktrypIIIAGENFGCGSS 79
Cdd:PRK00439 1 KGRV-----WKFGDNIDTDVIIPARYLNT--SDPQE---LAKHCMEDLdPEFAKKV-KPGD------IIVAGKNFGCGSS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 80 REHAPIALGAAGVTAVVALSYARIFFRNCSATGelYPMESVDRLCDLFATGQEVTVDFTAEQIVNHTLDRTFSLKPLGE- 158
Cdd:PRK00439 64 REHAPIALKAAGVSAVIAKSFARIFYRNAINIG--LPVLECDEAVDKIEDGDEVEVDLETGVITNLTTGEEYKFKPIPEf 141
|
170
....*....|....*...
gi 504991645 159 VGPVIDAGGLFEYARQTG 176
Cdd:PRK00439 142 MLEILKAGGLIEYLKKKG 159
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
3-180 |
4.75e-45 |
|
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: 147.24 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVD-DNIDTDQIIPAEYLTLVpsKPDEyekLGSYAMIGLpdRYGK-----FIESGEQKTRYPIIIAGENFGC 76
Cdd:COG0066 4 TTLTGRAVPLDgDNIDTDQIIPARFLKTI--DREG---LGKHLFEDW--RYDRspdpdFVLNQPRYQGADILVAGRNFGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 77 GSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGELY---PMESVDRLCDLFAT--GQEVTVDFTAEQIVNHTlDRTF 151
Cdd:COG0066 77 GSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPielPEEAVDALFAAIEAnpGDELTVDLEAGTVTNGT-GETY 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 504991645 152 SLKplgevgpvIDAG-------GLFEYA---RQTGMIAA 180
Cdd:COG0066 156 PFE--------IDPFrrecllnGLDDIGltlKHADAIAA 186
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
7-174 |
2.67e-39 |
|
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: 131.45 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 7 GQIFVVDDNIDTDQIIPAEYLTlvPSKPDEyekLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREHAPIA 86
Cdd:TIGR02084 1 GKVHKYGDNVDTDVIIPARYLN--TSDPKE---LAKHCMEDLDKDFVKKVKEGD------IIVAGENFGCGSSREHAPIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 87 LGAAGVTAVVALSYARIFFRNCSATGelYPMESVDRLCDLFATGQEVTVDFTAEQIVNHTLDRTFSLKPLGE-VGPVIDA 165
Cdd:TIGR02084 70 IKASGISCVIAKSFARIFYRNAINIG--LPIVESEEAVDEIEEGDEVEVDLEKGIIKNLTKGKEYKATPFPEfLQKIMKA 147
|
....*....
gi 504991645 166 GGLFEYARQ 174
Cdd:TIGR02084 148 GGLLNYVKK 156
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
7-175 |
1.70e-35 |
|
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: 121.37 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 7 GQIFVVDDNIDTDQIIPAEYLTLVpsKPDEyekLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREHAPIA 86
Cdd:TIGR02087 1 GRVWKFGDDIDTDEIIPGRYLRTT--DPDE---LASHAMEGIDPEFAKKVRPGD------VIVAGKNFGCGSSREQAALA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 87 LGAAGVTAVVALSYARIFFRNCSATGeLYPMESVdrlCDLFATGQEVTVDFTAEQIVNhTLDRTFSLKPLGEVG-PVIDA 165
Cdd:TIGR02087 70 LKAAGIAAVIAESFARIFYRNAINIG-LPLIEAK---TEGIKDGDEVTVDLETGEIRV-NGNEEYKGEPLPDFLlEILRE 144
|
170
....*....|
gi 504991645 166 GGLFEYARQT 175
Cdd:TIGR02087 145 GGLLEYLKKR 154
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-137 |
9.12e-33 |
|
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: 112.30 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYLtlvpskpdeyeklgsyamiglpdrygkfiesgeqktrYPIIIAGENFGCGSSREHAPIALGAAGVT 93
Cdd:cd01577 4 DNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDAGIR 46
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504991645 94 AVVALSYARIFFRNCSATGeLYPMESVDRLCD--LFATGQEVTVDF 137
Cdd:cd01577 47 AVIAESFARIFFRNAINNG-LLPVTLADEDVEevEAKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
3-168 |
2.85e-32 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 113.27 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVDDNIDTDQIIPAEYLTLVpsKPDEyekLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREH 82
Cdd:NF040625 2 EIIKGKVWKFGDNIDTDVIIPGRYLRTF--NPDD---LASHVMEGERPDFTKNVQKGD------IIVAGWNFGCGSSREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 83 APIALGAAGVTAVVALSYARIFFRNCSATGelYPMESVDRLCDlfaTGQEVTVDFTAEQIVNHTLDRTFSLKPLGE-VGP 161
Cdd:NF040625 71 APVAIKHAGVSAIIAKSFARIFYRNAINIG--LPVIVADIEAD---DGDILSIDLEKGIIKNKTTGEEFKIQPFKEfMLE 145
|
....*..
gi 504991645 162 VIDAGGL 168
Cdd:NF040625 146 ILEDGGL 152
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
14-152 |
1.32e-30 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 110.22 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYLTLVpskpdEYEKLGSYAMIGlpDRYgkfIESGEQ-------KTRY---PIIIAGENFGCGSSREHA 83
Cdd:PRK01641 17 ANVDTDQIIPKQFLKRI-----TRTGFGKGLFDD--WRY---LDDGQPnpdfvlnQPRYqgaSILLAGDNFGCGSSREHA 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504991645 84 PIALGAAGVTAVVALSYARIFFRNCSATGEL---YPMESVDRLCDLFAT--GQEVTVDFTAEQIvnHTLDRTFS 152
Cdd:PRK01641 87 PWALADYGFRAVIAPSFADIFYNNCFKNGLLpivLPEEDVDELFKLVEAnpGAELTVDLEAQTV--TAPDKTFP 158
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
14-176 |
1.87e-28 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 103.73 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYLTLVPSKpdeyEKLGSYAMIGLPDRYGKFIESGEqktrypIIIAGENFGCGSSREHAPIALGAAGVT 93
Cdd:PRK14023 9 DNINTDDILPGKYAPFMVGE----DRFHNYAFAHLRPEFASTVRPGD------ILVAGRNFGLGSSREYAPEALKMLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 94 AVVALSYARIFFRNCSATGeLYPMESVDrLCDLFATGQEVTVDFTAEQIVNHtlDRTFSLKPLGE-VGPVIDAGGLFEYA 172
Cdd:PRK14023 79 AIIAKSYARIFYRNLVNLG-IPPFESEE-VVDALEDGDEVELDLETGVLTRG--GETFQLRPPPEfLLEALKEGSILEYY 154
|
....
gi 504991645 173 RQTG 176
Cdd:PRK14023 155 RKHG 158
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
3-155 |
4.73e-19 |
|
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: 79.86 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 3 KVISGQIFVVDD-NIDTDQIIPAEYLTLVpskpdEYEKLGSYAMIG--LPDRYGK-----FIESGEQKTRYPIIIAGENF 74
Cdd:TIGR00171 5 KSHTGLVAPLDAaNVDTDAIIPKQFLKRI-----TRTGFGKHLFFDwrFLDANGKepnpdFVLNQPQYQGASILLARENF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 75 GCGSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGEL---YPMESVDRLCDLFAT-GQEVTVDFTAEQI-VNHTLDR 149
Cdd:TIGR00171 80 GCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLpirLSYDEVKELFGQVENqGLQMTVDLENQLIhDSEGKVY 159
|
....*.
gi 504991645 150 TFSLKP 155
Cdd:TIGR00171 160 SFEIDP 165
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
11-136 |
4.17e-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: 69.80 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 11 VVDDNIDTDQIIPAEYLtlvpskpdeyeklgsyamiglpdrygkfiesgeqktrypIIIAGENFGCGSSREHAPIALGAA 90
Cdd:cd00404 1 KVAGNITTDHISPAGPG---------------------------------------VVIGDENYGTGSSREHAALELRLL 41
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 504991645 91 GVTAVVALSYARIFFRNCSATGELyPME-SVDRLCDLFATGQEVTVD 136
Cdd:cd00404 42 GGRAVIAKSFARIFFRNLVDQGLL-PLEfADPEDYLKLHTGDELDIY 87
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
11-136 |
2.76e-14 |
|
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: 65.92 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 11 VVDDNIDTDQIIPA--EYLTLVPSKPdeyeKLGSYAMIGLPDRYGKFIESGEQKtrypIIIAGENFGCGSSREHAPIALG 88
Cdd:cd01579 1 KVGDNITTDHIMPAgaKVLPLRSNIP----AISEFVFHRVDPTFAERAKAAGPG----FIVGGENYGQGSSREHAALAPM 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 504991645 89 AAGVTAVVALSYARIFFRNCSATGELyPMESVDRL-CDLFATGQEVTVD 136
Cdd:cd01579 73 YLGVRAVLAKSFARIHRANLINFGIL-PLTFADEDdYDRFEQGDQLELP 120
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
14-107 |
4.33e-14 |
|
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: 65.47 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYL-TLV----------PSKPDEYEKLGSYAMIGLPDRYGKFIESGeqktRYPIIIAGENFGCGSSREH 82
Cdd:pfam00694 17 SNVDTDLIIPKQFLgTIAnigigninfeGWRYGKVRYLPDGENPDFYDAAMRYKQHG----APIVVIGGKNFGCGSSREH 92
|
90 100
....*....|....*....|....*
gi 504991645 83 APIALGAAGVTAVVALSYARIFFRN 107
Cdd:pfam00694 93 AAWALRDLGIKAVIAESFARIHRNN 117
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
14-133 |
1.26e-13 |
|
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: 64.23 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPAEYLTLVPSKPdeyEKLGSYAMiglpDRYGKfiESGEQKTRYPIIIAGENFGCGSSREHAPIALGAAGVT 93
Cdd:cd01674 4 DNLNTDGIYPGKYTYQDDITP---EKMAEVCM----ENYDS--EFSTKTKQGDILVSGFNFGTGSSREQAATALLAKGIP 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 504991645 94 AVVALSYARIFFRNC--SATGELYPMESVDRLCDLFATGQEV 133
Cdd:cd01674 75 LVVSGSFGNIFSRNSinNALLSIELPFLVQKLREAFANESKE 116
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
12-174 |
1.88e-11 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 61.70 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 12 VDDNIDTDQIIPA--EYLTL---VPskpdeyeKLGSYAMIGL-PDRYGKFIESGEQktrypIIIAGENFGCGSSREHAPI 85
Cdd:PRK07229 477 VGDNITTDHIMPAgaKWLPYrsnIP-------NISEFVFEGVdNTFPERAKEQGGG-----IVVGGENYGQGSSREHAAL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 86 ALGAAGVTAVVALSYARIFFRNCSATGELyPMESVDRL-CDLFATGQEVTVDFTAEQ-------IVNHTLDRTFSLKPlg 157
Cdd:PRK07229 545 APRYLGVKAVLAKSFARIHKANLINFGIL-PLTFADPAdYDKIEEGDVLEIEDLREFlpggpltVVNVTKDEEIEVRH-- 621
|
170 180
....*....|....*....|.
gi 504991645 158 EVGP----VIDAGGLFEYARQ 174
Cdd:PRK07229 622 TLSErqieILLAGGALNLIKK 642
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
14-148 |
2.43e-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: 58.58 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPA----------EYLTLVPSKPDEYEKLGSY------AMIG-----------LPDR---YGKFIESGEQKT 63
Cdd:COG1048 668 DSITTDHISPAgaikadspagRYLLEHGVEPKDFNSYGSRrgnhevMMRGtfaniriknllAPGTeggYTKHQPTGEVMS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 64 ------RY-----P-IIIAGENFGCGSSREHApiALGAA--GVTAVVALSYARI--------------FFRNCSA----- 110
Cdd:COG1048 748 iydaamRYkaegtPlVVLAGKEYGTGSSRDWA--AKGTRllGVKAVIAESFERIhrsnlvgmgvlplqFPEGESAeslgl 825
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504991645 111 TG-ELYpmeSVDRLCDLFATGQEVTV-----DFTAEQI-VNHTLD 148
Cdd:COG1048 826 TGdETF---DIEGLDEGLAPGKTVTVtatraDGSTEEFpVLHRID 867
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
11-103 |
5.77e-07 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 48.78 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 11 VVDDNIDTDQIIPA----------EYLTlvpSKPDEYEKLGSYA----------------------MI-GLPDRYGKFIE 57
Cdd:PRK12881 664 VLGDSITTDHISPAgaikadspagKYLK---ENGVPKADFNSYGsrrgnhevmmrgtfanvriknlMIpGKEGGLTLHQP 740
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 58 SGEQKT------RY-----P-IIIAGENFGCGSSREHApiALGA--AGVTAVVALSYARI 103
Cdd:PRK12881 741 SGEVLSiydaamRYqaagtPlVVIAGEEYGTGSSRDWA--AKGTrlLGVKAVIAESFERI 798
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
14-103 |
1.11e-06 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 46.50 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPA----------EYLTLVPSKPDEYEKLGS------------YAMIGL-----PDRYGKFI---ESGEQKT 63
Cdd:cd01580 4 DSVTTDHISPAgsiakdspagKYLAERGVKPRDFNSYGSrrgndevmmrgtFANIRLrnklvPGTEGGTThhpPTGEVMS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504991645 64 RYP------------IIIAGENFGCGSSREHApiALGAA--GVTAVVALSYARI 103
Cdd:cd01580 84 IYDaamrykeegvplVILAGKEYGSGSSRDWA--AKGPFllGVKAVIAESFERI 135
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
14-103 |
1.04e-05 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 44.73 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 14 DNIDTDQIIPA----------EYLTlvpSKPDEYEKLGSYA---------MIG-----------LPDR---YGKFIESGE 60
Cdd:PRK09277 666 DSITTDHISPAgaikadspagKYLL---EHGVEPKDFNSYGsrrgnhevmMRGtfanirirnemVPGVeggYTRHFPEGE 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504991645 61 QKT------RY-----P-IIIAGENFGCGSSREHApiALGA--AGVTAVVALSYARI 103
Cdd:PRK09277 743 VMSiydaamKYkeegtPlVVIAGKEYGTGSSRDWA--AKGTrlLGVKAVIAESFERI 797
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
67-114 |
1.49e-05 |
|
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: 42.84 E-value: 1.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504991645 67 IIIAGENFGCGSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGEL 114
Cdd:cd01578 72 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLL 119
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
61-135 |
2.02e-05 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 44.23 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 61 QKTRYP-IIIAGENFGCGSSREHApiALGAA--GVTAVVALSYARI--------------FFRNCSA-----TG-ELYpm 117
Cdd:PTZ00092 767 KQEGVPlIVLAGKEYGSGSSRDWA--AKGPYlqGVKAVIAESFERIhrsnlvgmgilplqFLNGENAdslglTGkEQF-- 842
|
90
....*....|....*...
gi 504991645 118 eSVDRLCDLFATGQEVTV 135
Cdd:PTZ00092 843 -SIDLNSGELKPGQDVTV 859
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
77-153 |
4.62e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 41.25 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 77 GSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGEL---YPMESVDRLCDLFATGQeVTVDFTAEQIVNHTLDRTFSL 153
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLpivQPREVREKLAQLKPTDQ-VTVDLEQQKIISPVEEFTFEI 81
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
67-169 |
3.19e-03 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 37.48 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504991645 67 IIIAGENFGCGSSREHAPIALGAAGVTAVVALSYARIFFRNCSATGeLYPmesvdrLCdlFATGQEV-TVDFTAEQIVNH 145
Cdd:PLN00070 810 IILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMG-IIP------LC--FKSGEDAdTLGLTGHERYTI 880
|
90 100
....*....|....*....|....*
gi 504991645 146 TLDRTFS-LKPLGEVGPVIDAGGLF 169
Cdd:PLN00070 881 DLPSNISeIKPGQDVTVTTDNGKSF 905
|
|
| |
