|
Name |
Accession |
Description |
Interval |
E-value |
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
1-210 |
9.33e-147 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 406.05 E-value: 9.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDVGQPgqdnskrplNPDFVLNQPRYQGASVL 80
Cdd:PRK01641 1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQP---------NPDFVLNQPRYQGASIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 81 LARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEANEGYQLSIDLAAQTVT 160
Cdd:PRK01641 72 LAGDNFGCGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598316 161 RPDgKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAIRAFEDGYRQQQPWL 210
Cdd:PRK01641 152 APD-KTFPFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
2-210 |
6.42e-125 |
|
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: 350.63 E-value: 6.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 2 KPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLdvgqpgqdnskRPLNPDFVLNQPRYQGASVLL 81
Cdd:COG0066 1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYD-----------RSPDPDFVLNQPRYQGADILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 82 ARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEANEGYQLSIDLAAQTVTR 161
Cdd:COG0066 70 AGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598316 162 PDGKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAIRAFEDGYRQqqpWL 210
Cdd:COG0066 150 GTGETYPFEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPA---WL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
1-196 |
8.14e-107 |
|
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: 304.82 E-value: 8.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDvgqpgqDNSKRPlNPDFVLNQPRYQGASVL 80
Cdd:TIGR00171 1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLD------ANGKEP-NPDFVLNQPQYQGASIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 81 LARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEaNEGYQLSIDLAAQTVT 160
Cdd:TIGR00171 74 LARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVE-NQGLQMTVDLENQLIH 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598316 161 RPDGKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAI 196
Cdd:TIGR00171 153 DSEGKVYSFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
1-133 |
3.07e-51 |
|
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: 161.76 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDV-GQPGQDNskrplnPDFVLNQPRYQGAS- 78
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVrYLPDGEN------PDFYDAAMRYKQHGa 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598316 79 --VLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEA 133
Cdd:pfam00694 75 piVVIGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-154 |
7.78e-45 |
|
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: 144.27 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 14 LDRANVDTDQIIPKQFLksikrtgfgpnlfdewryldvgqpgqdnskrplnpdfvlnqpryqgASVLLARENFGCGSSRE 93
Cdd:cd01577 1 LFGDNIDTDQIIPARFL----------------------------------------------GDIIVAGKNFGCGSSRE 34
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598316 94 HAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDElfrqVEANEGYQLSIDL 154
Cdd:cd01577 35 HAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE----VEAKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
16-188 |
2.86e-21 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 85.92 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 16 RANVDTDQIIPKQFLksikRTgFGPNlfdewrylDVGqpgqDNSKRPLNPDFVLNqprYQGASVLLARENFGCGSSREHA 95
Cdd:NF040625 12 GDNIDTDVIIPGRYL----RT-FNPD--------DLA----SHVMEGERPDFTKN---VQKGDIIVAGWNFGCGSSREQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 96 PWALDEYGFRTVIAPSYADIFFNNSFKNGlLPIILPEaevdelfrqVEANEGYQLSIDLA-AQTVTRPDGKVlgFEVDPF 174
Cdd:NF040625 72 PVAIKHAGVSAIIAKSFARIFYRNAINIG-LPVIVAD---------IEADDGDILSIDLEkGIIKNKTTGEE--FKIQPF 139
|
170
....*....|....
gi 15598316 175 RKHcLLNGLDDIGL 188
Cdd:NF040625 140 KEF-MLEILEDGGL 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
1-210 |
9.33e-147 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 406.05 E-value: 9.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDVGQPgqdnskrplNPDFVLNQPRYQGASVL 80
Cdd:PRK01641 1 MEKFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQP---------NPDFVLNQPRYQGASIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 81 LARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEANEGYQLSIDLAAQTVT 160
Cdd:PRK01641 72 LAGDNFGCGSSREHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEANPGAELTVDLEAQTVT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598316 161 RPDgKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAIRAFEDGYRQQQPWL 210
Cdd:PRK01641 152 APD-KTFPFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
2-210 |
6.42e-125 |
|
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: 350.63 E-value: 6.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 2 KPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLdvgqpgqdnskRPLNPDFVLNQPRYQGASVLL 81
Cdd:COG0066 1 EKFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYD-----------RSPDPDFVLNQPRYQGADILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 82 ARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEANEGYQLSIDLAAQTVTR 161
Cdd:COG0066 70 AGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANPGDELTVDLEAGTVTN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598316 162 PDGKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAIRAFEDGYRQqqpWL 210
Cdd:COG0066 150 GTGETYPFEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRPA---WL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
1-196 |
8.14e-107 |
|
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: 304.82 E-value: 8.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDvgqpgqDNSKRPlNPDFVLNQPRYQGASVL 80
Cdd:TIGR00171 1 MAPFKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFLD------ANGKEP-NPDFVLNQPQYQGASIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 81 LARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQVEaNEGYQLSIDLAAQTVT 160
Cdd:TIGR00171 74 LARENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVE-NQGLQMTVDLENQLIH 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598316 161 RPDGKVLGFEVDPFRKHCLLNGLDDIGLTLQDADAI 196
Cdd:TIGR00171 153 DSEGKVYSFEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
1-133 |
3.07e-51 |
|
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: 161.76 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 1 MKPYTQTTGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDV-GQPGQDNskrplnPDFVLNQPRYQGAS- 78
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVrYLPDGEN------PDFYDAAMRYKQHGa 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598316 79 --VLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEA 133
Cdd:pfam00694 75 piVVIGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
14-154 |
7.78e-45 |
|
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: 144.27 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 14 LDRANVDTDQIIPKQFLksikrtgfgpnlfdewryldvgqpgqdnskrplnpdfvlnqpryqgASVLLARENFGCGSSRE 93
Cdd:cd01577 1 LFGDNIDTDQIIPARFL----------------------------------------------GDIIVAGKNFGCGSSRE 34
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598316 94 HAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDElfrqVEANEGYQLSIDL 154
Cdd:cd01577 35 HAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE----VEAKPGDEVEVDL 91
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
89-208 |
1.14e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 101.34 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 89 GSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEaEVDELFRQVEANEgyQLSIDLAAQTVTRPDGKvLG 168
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPR-EVREKLAQLKPTD--QVTVDLEQQKIISPVEE-FT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15598316 169 FEVDPFRKHCLLNGLDDIGLTLQDADAIRAFEdgyrQQQP 208
Cdd:PRK14812 79 FEIDSEWKHKLLNSLDDIGITLQYEELIAAYE----KQRP 114
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
18-174 |
2.20e-27 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 101.83 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 18 NVDTDQIIPKQFLksikrtgfgpNLFDEwRYLdvgqpgQDNSKRPLNPDFVlnqPRYQGASVLLARENFGCGSSREHAPW 97
Cdd:PRK00439 10 NIDTDVIIPARYL----------NTSDP-QEL------AKHCMEDLDPEFA---KKVKPGDIIVAGKNFGCGSSREHAPI 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598316 98 ALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAeVDELfrqveaNEGYQLSIDLAAQTVTRPD-GKVLGFE-VDPF 174
Cdd:PRK00439 70 ALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEA-VDKI------EDGDEVEVDLETGVITNLTtGEEYKFKpIPEF 141
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
18-170 |
1.15e-21 |
|
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: 86.71 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 18 NVDTDQIIPKQFLKSIKRTGFGPNLFDewryldvgqpgqdnskrPLNPDFVLNqprYQGASVLLARENFGCGSSREHAPW 97
Cdd:TIGR02087 9 DIDTDEIIPGRYLRTTDPDELASHAME-----------------GIDPEFAKK---VRPGDVIVAGKNFGCGSSREQAAL 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598316 98 ALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVdelfrqveaNEGYQLSIDLAAQTVTRPDGKVLGFE 170
Cdd:TIGR02087 69 ALKAAGIAAVIAESFARIFYRNAINIGLPLIEAKTEGI---------KDGDEVTVDLETGEIRVNGNEEYKGE 132
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
16-188 |
2.86e-21 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 85.92 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 16 RANVDTDQIIPKQFLksikRTgFGPNlfdewrylDVGqpgqDNSKRPLNPDFVLNqprYQGASVLLARENFGCGSSREHA 95
Cdd:NF040625 12 GDNIDTDVIIPGRYL----RT-FNPD--------DLA----SHVMEGERPDFTKN---VQKGDIIVAGWNFGCGSSREQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 96 PWALDEYGFRTVIAPSYADIFFNNSFKNGlLPIILPEaevdelfrqVEANEGYQLSIDLA-AQTVTRPDGKVlgFEVDPF 174
Cdd:NF040625 72 PVAIKHAGVSAIIAKSFARIFYRNAINIG-LPVIVAD---------IEADDGDILSIDLEkGIIKNKTTGEE--FKIQPF 139
|
170
....*....|....
gi 15598316 175 RKHcLLNGLDDIGL 188
Cdd:NF040625 140 KEF-MLEILEDGGL 152
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
18-154 |
1.74e-20 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 83.69 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 18 NVDTDQIIPKqflksikrtgfgpnlfdewRYLDVGQPGQ--DNSKRPLNPDFVlnqPRYQGASVLLARENFGCGSSREHA 95
Cdd:TIGR02084 9 NVDTDVIIPA-------------------RYLNTSDPKElaKHCMEDLDKDFV---KKVKEGDIIVAGENFGCGSSREHA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598316 96 PWALDEYGFRTVIAPSYADIFFNNSFKNGlLPIILPEAEVDELfrqveaNEGYQLSIDL 154
Cdd:TIGR02084 67 PIAIKASGISCVIAKSFARIFYRNAINIG-LPIVESEEAVDEI------EEGDEVEVDL 118
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
18-135 |
1.77e-20 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 86.07 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 18 NVDTDQIIPKQFLKSIkrtgfgPNLFDEWR----YLDVGQPGQDNSKrplnpdFVL---NQPRYqgaSVLLARENFGCGS 90
Cdd:PLN00072 79 NIDTDQIIPAEYLTLV------PSKPDEYEklgsYALIGLPAFYKTR------FVEpgeMKTKY---SIIIGGENFGCGS 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15598316 91 SREHAPWALDEYGFRTVIAPSYADIFFNNSFKNG-LLPIilpEAEV 135
Cdd:PLN00072 144 SREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPL---ESEV 186
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
17-161 |
3.47e-16 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 72.91 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 17 ANVDTDQIIPKQFlksikrtgfGPNLFDEWRYldvgqpgQDNSKRPLNPDFVlnqPRYQGASVLLARENFGCGSSREHAP 96
Cdd:PRK14023 9 DNINTDDILPGKY---------APFMVGEDRF-------HNYAFAHLRPEFA---STVRPGDILVAGRNFGLGSSREYAP 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598316 97 WALDEYGFRTVIAPSYADIFFNNSFKNGLLPIilpeaEVDELFRQVEanEGYQLSIDLAAQTVTR 161
Cdd:PRK14023 70 EALKMLGIGAIIAKSYARIFYRNLVNLGIPPF-----ESEEVVDALE--DGDEVELDLETGVLTR 127
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
76-153 |
2.35e-14 |
|
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: 65.95 E-value: 2.35e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598316 76 GASVLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIilpeaEVDELFRQVEANEGYQLSID 153
Cdd:cd00404 15 GPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPL-----EFADPEDYLKLHTGDELDIY 87
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
76-154 |
2.19e-09 |
|
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: 53.60 E-value: 2.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598316 76 GASVLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPEAEVDELFRQveaneGYQLSIDL 154
Cdd:cd01579 48 GPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQ-----GDQLELPL 121
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
79-171 |
2.02e-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: 51.13 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 79 VLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPIILPeAEVDELfRQVEANEGYQLsidlaaqt 158
Cdd:cd01674 48 ILVSGFNFGTGSSREQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIELP-FLVQKL-REAFANESKEL-------- 117
|
90
....*....|...
gi 15598316 159 vTRPDGKVLGFEV 171
Cdd:cd01674 118 -TRRTGWKLKWDV 129
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
75-129 |
3.87e-08 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 52.84 E-value: 3.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598316 75 QGASVLLARENFGCGSSREHA---PWALdeyGFRTVIAPSYADIFFNNSFKNGLLPII 129
Cdd:PRK07229 522 QGGGIVVGGENYGQGSSREHAalaPRYL---GVKAVLAKSFARIHKANLINFGILPLT 576
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
78-128 |
1.35e-06 |
|
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: 46.31 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15598316 78 SVLLARENFGCGSSREHAPWALDEYGFRTVIAPSYADIFFNNSFKNGLLPI 128
Cdd:cd01578 71 WVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 121
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
73-171 |
2.85e-04 |
|
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: 41.24 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 73 RYQGA---SVLLARENFGCGSSREHA---PWALdeyGFRTVIAPSYADIFFNNSFKNGLLPIILPEAE--------VDEL 138
Cdd:COG1048 754 RYKAEgtpLVVLAGKEYGTGSSRDWAakgTRLL---GVKAVIAESFERIHRSNLVGMGVLPLQFPEGEsaeslgltGDET 830
|
90 100 110
....*....|....*....|....*....|....*...
gi 15598316 139 FrQVEAnegyqLSIDLAAQ-----TVTRPDGKVLGFEV 171
Cdd:COG1048 831 F-DIEG-----LDEGLAPGktvtvTATRADGSTEEFPV 862
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
73-171 |
5.97e-03 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 37.22 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598316 73 RYQGAS---VLLARENFGCGSSREhapWA------LdeyGFRTVIAPSYADIFFNNSFKNGLLPIILPEAE-VDELfrQV 142
Cdd:PRK12881 753 RYQAAGtplVVIAGEEYGTGSSRD---WAakgtrlL---GVKAVIAESFERIHRSNLVGMGVLPLQFKGGDsRQSL--GL 824
|
90 100 110
....*....|....*....|....*....|....*..
gi 15598316 143 EANEGYQ---LSIDLAAQ-----TVTRPDGKVLGFEV 171
Cdd:PRK12881 825 TGGETFDiegLPGEIKPRqdvtlVIHRADGSTERVPV 861
|
|
| |
