|
Name |
Accession |
Description |
Interval |
E-value |
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
1-199 |
2.80e-142 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 394.49 E-value: 2.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDagQQPNPEFVMNEARYQGASILLARENFG 80
Cdd:PRK01641 1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDD--GQPNPDFVLNQPRYQGASILLAGDNFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 81 CGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEANEGAEITVDLEAMKVSANGKEYS 160
Cdd:PRK01641 79 CGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVTAPDKTFP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 857965131 161 FEIDEFRRHCLLNGLDNIGLTLQHADKISEFEAKIPSFL 199
Cdd:PRK01641 159 FEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFR 197
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
4-199 |
1.89e-118 |
|
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: 334.06 E-value: 1.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 4 FQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDdagqQPNPEFVMNEARYQGASILLARENFGCGS 83
Cdd:COG0066 3 FTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR----SPDPDFVLNQPRYQGADILVAGRNFGCGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 84 SREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEANEGAEITVDLEAMKVSA-NGKEYSFE 162
Cdd:COG0066 79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTNgTGETYPFE 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 857965131 163 IDEFRRHCLLNGLDNIGLTLQHADKISEFEAKIPSFL 199
Cdd:COG0066 159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAWL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
1-188 |
2.44e-114 |
|
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: 323.31 E-value: 2.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDAGQQPNPEFVMNEARYQGASILLARENFG 80
Cdd:TIGR00171 1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDANGKEPNPDFVLNQPQYQGASILLARENFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 81 CGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEaNEGAEITVDLEAMKVSA-NGKEY 159
Cdd:TIGR00171 81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVE-NQGLQMTVDLENQLIHDsEGKVY 159
|
170 180
....*....|....*....|....*....
gi 857965131 160 SFEIDEFRRHCLLNGLDNIGLTLQHADKI 188
Cdd:TIGR00171 160 SFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
1-126 |
4.18e-48 |
|
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: 153.68 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDAGQ--QPNPEFVMNEARYQ--GASILLAR 76
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLpdGENPDFYDAAMRYKqhGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 857965131 77 -ENFGCGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQ 126
Cdd:pfam00694 81 gKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-147 |
3.10e-42 |
|
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: 137.33 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 14 LDTANIDTDAIIPKQFLqkvnrigfgkhlfhdwrflddagqqpnpefvmnearyqgASILLARENFGCGSSREHAPWALA 93
Cdd:cd01577 1 LFGDNIDTDQIIPARFL---------------------------------------GDIIVAGKNFGCGSSREHAPWALK 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 857965131 94 DYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDElfqfVEANEGAEITVDL 147
Cdd:cd01577 42 DAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE----VEAKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
18-180 |
7.54e-24 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 92.47 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKVNRIGFGKHLFHDWRflddagqqpnPEFVMNearYQGASILLARENFGCGSSREHAPWALADYGI 97
Cdd:NF040625 14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER----------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 98 QVMIAPSFADIFYGNSINNQMvPVRLTEqevdelfqfVEANEGAEITVDLEA--MKVSANGKEYSFE-IDEFrrhcLLNG 174
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIGL-PVIVAD---------IEADDGDILSIDLEKgiIKNKTTGEEFKIQpFKEF----MLEI 146
|
....*.
gi 857965131 175 LDNIGL 180
Cdd:NF040625 147 LEDGGL 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
1-199 |
2.80e-142 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 394.49 E-value: 2.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDagQQPNPEFVMNEARYQGASILLARENFG 80
Cdd:PRK01641 1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDD--GQPNPDFVLNQPRYQGASILLAGDNFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 81 CGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEANEGAEITVDLEAMKVSANGKEYS 160
Cdd:PRK01641 79 CGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVTAPDKTFP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 857965131 161 FEIDEFRRHCLLNGLDNIGLTLQHADKISEFEAKIPSFL 199
Cdd:PRK01641 159 FEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFR 197
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
4-199 |
1.89e-118 |
|
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: 334.06 E-value: 1.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 4 FQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDdagqQPNPEFVMNEARYQGASILLARENFGCGS 83
Cdd:COG0066 3 FTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR----SPDPDFVLNQPRYQGADILVAGRNFGCGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 84 SREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEANEGAEITVDLEAMKVSA-NGKEYSFE 162
Cdd:COG0066 79 SREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTNgTGETYPFE 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 857965131 163 IDEFRRHCLLNGLDNIGLTLQHADKISEFEAKIPSFL 199
Cdd:COG0066 159 IDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPAWL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
1-188 |
2.44e-114 |
|
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: 323.31 E-value: 2.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDAGQQPNPEFVMNEARYQGASILLARENFG 80
Cdd:TIGR00171 1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLDANGKEPNPDFVLNQPQYQGASILLARENFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 81 CGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEaNEGAEITVDLEAMKVSA-NGKEY 159
Cdd:TIGR00171 81 CGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVE-NQGLQMTVDLENQLIHDsEGKVY 159
|
170 180
....*....|....*....|....*....
gi 857965131 160 SFEIDEFRRHCLLNGLDNIGLTLQHADKI 188
Cdd:TIGR00171 160 SFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
1-126 |
4.18e-48 |
|
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: 153.68 E-value: 4.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 1 MSGFQQHTGLVVPLDTANIDTDAIIPKQFLQKVNRIGFGKHLFHDWRFLDDAGQ--QPNPEFVMNEARYQ--GASILLAR 76
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLpdGENPDFYDAAMRYKqhGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 857965131 77 -ENFGCGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQ 126
Cdd:pfam00694 81 gKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-147 |
3.10e-42 |
|
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: 137.33 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 14 LDTANIDTDAIIPKQFLqkvnrigfgkhlfhdwrflddagqqpnpefvmnearyqgASILLARENFGCGSSREHAPWALA 93
Cdd:cd01577 1 LFGDNIDTDQIIPARFL---------------------------------------GDIIVAGKNFGCGSSREHAPWALK 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 857965131 94 DYGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDElfqfVEANEGAEITVDL 147
Cdd:cd01577 42 DAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE----VEAKPGDEVEVDL 91
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
18-193 |
2.99e-33 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 116.46 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKVNRIGFGKHLFHDWRflddagqqpnPEFVmneARYQGASILLARENFGCGSSREHAPWALADYGI 97
Cdd:PRK00439 10 NIDTDVIIPARYLNTSDPQELAKHCMEDLD----------PEFA---KKVKPGDIIVAGKNFGCGSSREHAPIALKAAGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 98 QVMIAPSFADIFYGNSINNQmVPVRLTEQEVDELfqfveaNEGAEITVDLEA--MKVSANGKEYSFE-IDEFrrhcLLNG 174
Cdd:PRK00439 77 SAVIAKSFARIFYRNAINIG-LPVLECDEAVDKI------EDGDEVEVDLETgvITNLTTGEEYKFKpIPEF----MLEI 145
|
170
....*....|....*....
gi 857965131 175 LDNIGLtLQHADKISEFEA 193
Cdd:PRK00439 146 LKAGGL-IEYLKKKGRFPG 163
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
82-198 |
2.31e-30 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 107.88 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 82 GSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVrLTEQEVDElfQFVEANEGAEITVDLEAMKVSANGKEYSF 161
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPI-VQPREVRE--KLAQLKPTDQVTVDLEQQKIISPVEEFTF 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 857965131 162 EIDEFRRHCLLNGLDNIGLTLQHADKISEFEAKIPSF 198
Cdd:PRK14812 80 EIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAY 116
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
18-160 |
1.24e-26 |
|
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: 99.48 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKVNRIGFGKHLFHDWRflddagqqpnPEFVmneARYQGASILLARENFGCGSSREHAPWALADYGI 97
Cdd:TIGR02084 9 NVDTDVIIPARYLNTSDPKELAKHCMEDLD----------KDFV---KKVKEGDIIVAGENFGCGSSREHAPIAIKASGI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 857965131 98 QVMIAPSFADIFYGNSINNQMvPVRLTEQEVDELfqfveaNEGAEITVDLE--AMKVSANGKEYS 160
Cdd:TIGR02084 76 SCVIAKSFARIFYRNAINIGL-PIVESEEAVDEI------EEGDEVEVDLEkgIIKNLTKGKEYK 133
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
18-174 |
1.26e-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: 96.72 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKVNRIGFGKHLFHDWRflddagqqpnPEFVMNearYQGASILLARENFGCGSSREHAPWALADYGI 97
Cdd:TIGR02087 9 DIDTDEIIPGRYLRTTDPDELASHAMEGID----------PEFAKK---VRPGDVIVAGKNFGCGSSREQAALALKAAGI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857965131 98 QVMIAPSFADIFYGNSINNQMVPVRLTEQEVdelfqfveaNEGAEITVDLEAMKV-SANGKEYSFE-IDEFRRHCLLNG 174
Cdd:TIGR02087 76 AAVIAESFARIFYRNAINIGLPLIEAKTEGI---------KDGDEVTVDLETGEIrVNGNEEYKGEpLPDFLLEILREG 145
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
18-180 |
7.54e-24 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 92.47 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKVNRIGFGKHLFHDWRflddagqqpnPEFVMNearYQGASILLARENFGCGSSREHAPWALADYGI 97
Cdd:NF040625 14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER----------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 98 QVMIAPSFADIFYGNSINNQMvPVRLTEqevdelfqfVEANEGAEITVDLEA--MKVSANGKEYSFE-IDEFrrhcLLNG 174
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIGL-PVIVAD---------IEADDGDILSIDLEKgiIKNKTTGEEFKIQpFKEF----MLEI 146
|
....*.
gi 857965131 175 LDNIGL 180
Cdd:NF040625 147 LEDGGL 152
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
18-159 |
5.88e-20 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 84.14 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIPKQFLQKV-------NRIG----FGKHLFHDWRFLDDaGQqpnpefvmNEARYqgaSILLARENFGCGSSRE 86
Cdd:PLN00072 79 NIDTDQIIPAEYLTLVpskpdeyEKLGsyalIGLPAFYKTRFVEP-GE--------MKTKY---SIIIGGENFGCGSSRE 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857965131 87 HAPWALADYGIQVMIAPSFADIFYGNSI-NNQMVPVRlTEQEVDElfqfvEANEGAEITVDLEAMKVS--ANGKEY 159
Cdd:PLN00072 147 HAPVALGAAGAKAVVAESYARIFFRNSVaTGEVYPLE-SEVRICE-----ECKTGDVVTVELGNSVLInhTTGKEY 216
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
17-162 |
1.44e-19 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 81.39 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 17 ANIDTDAIIPKQFLQKVnrigFGKHLFHDWRFLddagqQPNPEFVmneARYQGASILLARENFGCGSSREHAPWALADYG 96
Cdd:PRK14023 9 DNINTDDILPGKYAPFM----VGEDRFHNYAFA-----HLRPEFA---STVRPGDILVAGRNFGLGSSREYAPEALKMLG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857965131 97 IQVMIAPSFADIFYGNSINNQMVPVRlTEQEVDELfqfveaNEGAEITVDLEAMKVSANGKEYSFE 162
Cdd:PRK14023 77 IGAIIAKSYARIFYRNLVNLGIPPFE-SEEVVDAL------EDGDEVELDLETGVLTRGGETFQLR 135
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
69-146 |
1.36e-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: 63.64 E-value: 1.36e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 857965131 69 GASILLARENFGCGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVPVrlteqEVDELFQFVEANEGAEITVD 146
Cdd:cd00404 15 GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPL-----EFADPEDYLKLHTGDELDIY 87
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
18-133 |
1.61e-11 |
|
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: 58.99 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 18 NIDTDAIIP---KQFLQKVNRIGFGKHLFHdwRFlddagqqpNPEFVmNEARYQGASILLARENFGCGSSREHAPWALAD 94
Cdd:cd01579 5 NITTDHIMPagaKVLPLRSNIPAISEFVFH--RV--------DPTFA-ERAKAAGPGFIVGGENYGQGSSREHAALAPMY 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 857965131 95 YGIQVMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQ 133
Cdd:cd01579 74 LGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFE 112
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
15-123 |
3.74e-11 |
|
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: 58.07 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 15 DTANIDTDAIIPkqflqkvnrigfGKHLFHDwrfldDAGQQPNPEFVMNEARYQGAS------ILLARENFGCGSSREHA 88
Cdd:cd01674 2 DADNLNTDGIYP------------GKYTYQD-----DITPEKMAEVCMENYDSEFSTktkqgdILVSGFNFGTGSSREQA 64
|
90 100 110
....*....|....*....|....*....|....*
gi 857965131 89 PWALADYGIQVMIAPSFADIFYGNSINNQMVPVRL 123
Cdd:cd01674 65 ATALLAKGIPLVVSGSFGNIFSRNSINNALLSIEL 99
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
58-149 |
3.76e-10 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 58.23 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857965131 58 PEFVMnEARYQGASILLARENFGCGSSREHApwALAD-Y-GIQVMIAPSFADIFYGNSINNQMVPVRLTE-------QEV 128
Cdd:PRK07229 513 NTFPE-RAKEQGGGIVVGGENYGQGSSREHA--ALAPrYlGVKAVLAKSFARIHKANLINFGILPLTFADpadydkiEEG 589
|
90 100 110
....*....|....*....|....*....|....
gi 857965131 129 DEL-------------FQFVEANEGAEITVDLEA 149
Cdd:PRK07229 590 DVLeiedlreflpggpLTVVNVTKDEEIEVRHTL 623
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
61-120 |
1.57e-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: 37.45 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 857965131 61 VMNEARYQGA----SILLARENFGCGSSREHAPWALADYGIQVMIAPSFADIFYGNSINNQMVP 120
Cdd:cd01578 57 VPDTARDYKAhgikWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLP 120
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
66-108 |
3.51e-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: 37.78 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 857965131 66 RYQGA---SILLARENFGCGSSREHA---PwALAdyGIQVMIAPSFADI 108
Cdd:COG1048 754 RYKAEgtpLVVLAGKEYGTGSSRDWAakgT-RLL--GVKAVIAESFERI 799
|
|
| |
