|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-420 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 837.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAK 80
Cdd:PRK00402 1 MGMTLAEKILARHSGRD-VSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 81 ILRDFARQQQLTHYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPES 160
Cdd:PRK00402 80 ILREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 161 IKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKG 240
Cdd:PRK00402 159 IKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 241 RARRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:PRK00402 239 RAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:PRK00402 319 APGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLAS 398
|
410 420
....*....|....*....|
gi 1493453643 401 PAVAAASAILGRIAAPQEVL 420
Cdd:PRK00402 399 PAVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-419 |
0e+00 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 772.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGlDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAK 80
Cdd:COG0065 1 MGMTLAEKILARHAG-REVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 81 ILRDFARQQQLThYFEVGRMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPES 160
Cdd:COG0065 80 TLREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 161 IKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKG 240
Cdd:COG0065 159 MRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 241 RARRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:COG0065 239 RPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:COG0065 319 APGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYLAS 398
|
410
....*....|....*....
gi 1493453643 401 PAVAAASAILGRIAAPQEV 419
Cdd:COG0065 399 PATAAASAIAGRITDPREL 417
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
3-419 |
0e+00 |
|
3-isopropylmalate dehydratase, large 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. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 729.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 3 MTITEKILAAHAGLDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKIL 82
Cdd:TIGR02083 1 MTMAEKILAQHAGLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 83 RDFARQQQLTHYFEVGRMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIK 162
Cdd:TIGR02083 81 REFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 163 FVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRA 242
Cdd:TIGR02083 161 FVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 243 RRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQ--QVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:TIGR02083 241 KREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKEEIKidQVVIGSCTNGRLEDLRLAAEILKGKTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:TIGR02083 321 APDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSEVYLAS 400
|
410
....*....|....*....
gi 1493453643 401 PAVAAASAILGRIAAPQEV 419
Cdd:TIGR02083 401 PAVAAASAIKGYIASPEEV 419
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-413 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic 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.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 660.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 31 LVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKILRDFARQQQlTHYFEVGRMGIEHCLLPEQ 110
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFG-INFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 111 GLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDG 190
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 191 ALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRVYQSDPDARYARVYEFDVSKLEP 270
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYDKVVEIDASELEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 271 QVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFID 350
Cdd:cd01583 240 QVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493453643 351 AGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:cd01583 320 AGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-416 |
2.07e-174 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 493.89 E-value: 2.07e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 3 MTITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVPNKDIKSAEQAKIL 82
Cdd:NF040615 1 MTLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 83 RDFARQQQLTHYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIK 162
Cdd:NF040615 79 REFVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 163 FVYYGElQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRA 242
Cdd:NF040615 158 VNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 243 --------RRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARV 314
Cdd:NF040615 237 vseeeiaeLKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 315 LQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPES 394
Cdd:NF040615 317 LKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNINS 396
|
410 420
....*....|....*....|..
gi 1493453643 395 EVYLSNPAVAAASAILGRIAAP 416
Cdd:NF040615 397 YIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-411 |
1.24e-135 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 396.79 E-value: 1.24e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 7 EKILAAHagLDRVEPGQLINVrVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVPN------------KDIK 74
Cdd:pfam00330 1 EKIWDAH--LVEELDGSLLYI-PDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTdlvidhapdaldKNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 75 SA-----EQAKILRDFARQQQLThYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMA 149
Cdd:pfam00330 77 DEisrnkEQYDFLEWNAKKFGIR-FVPPGQ-GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 150 LGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVP 229
Cdd:pfam00330 155 TQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 230 PDEITLDYVK--GRARRP----------YRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQA---------- 287
Cdd:pfam00330 235 PDETTFEYLRatGRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELvpdpfadavk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 288 -------------------GHVEIQQVVIGSCTNGRLEDLRLAARVL-----QGKKVHPDVRLIVIPGTQEVYRTALKEG 343
Cdd:pfam00330 315 rkaaeraleymglgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLkkaveKGLKVAPGVKASVVPGSEVVRAYAEAEG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1493453643 344 LIEIFIDAGAAVSTPTCGPCLGGHmGILAAGERCLATTNRNFVGRMgHPESEVYLSNPAVAAASAILG 411
Cdd:pfam00330 395 LDKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-420 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 837.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAK 80
Cdd:PRK00402 1 MGMTLAEKILARHSGRD-VSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 81 ILRDFARQQQLTHYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPES 160
Cdd:PRK00402 80 ILREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 161 IKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKG 240
Cdd:PRK00402 159 IKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 241 RARRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:PRK00402 239 RAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:PRK00402 319 APGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLAS 398
|
410 420
....*....|....*....|
gi 1493453643 401 PAVAAASAILGRIAAPQEVL 420
Cdd:PRK00402 399 PAVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-419 |
0e+00 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 772.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGlDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAK 80
Cdd:COG0065 1 MGMTLAEKILARHAG-REVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 81 ILRDFARQQQLThYFEVGRMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPES 160
Cdd:COG0065 80 TLREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 161 IKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKG 240
Cdd:COG0065 159 MRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 241 RARRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:COG0065 239 RPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:COG0065 319 APGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYLAS 398
|
410
....*....|....*....
gi 1493453643 401 PAVAAASAILGRIAAPQEV 419
Cdd:COG0065 399 PATAAASAIAGRITDPREL 417
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
3-419 |
0e+00 |
|
3-isopropylmalate dehydratase, large 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. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 729.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 3 MTITEKILAAHAGLDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKIL 82
Cdd:TIGR02083 1 MTMAEKILAQHAGLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 83 RDFARQQQLTHYFEVGRMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIK 162
Cdd:TIGR02083 81 REFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 163 FVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRA 242
Cdd:TIGR02083 161 FVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 243 RRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQ--QVVIGSCTNGRLEDLRLAARVLQGKKV 320
Cdd:TIGR02083 241 KREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKEEIKidQVVIGSCTNGRLEDLRLAAEILKGKTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 321 HPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSN 400
Cdd:TIGR02083 321 APDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSEVYLAS 400
|
410
....*....|....*....
gi 1493453643 401 PAVAAASAILGRIAAPQEV 419
Cdd:TIGR02083 401 PAVAAASAIKGYIASPEEV 419
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-413 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic 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.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 660.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 31 LVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKILRDFARQQQlTHYFEVGRMGIEHCLLPEQ 110
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFG-INFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 111 GLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDG 190
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 191 ALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRVYQSDPDARYARVYEFDVSKLEP 270
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYDKVVEIDASELEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 271 QVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFID 350
Cdd:cd01583 240 QVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493453643 351 AGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:cd01583 320 AGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-416 |
0e+00 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 636.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 4 TITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKILR 83
Cdd:TIGR01343 1 TIAEKILSKKSGKE-VYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 84 DFARQQQLTHYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKF 163
Cdd:TIGR01343 80 EFVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 164 VYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRAR 243
Cdd:TIGR01343 159 NITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 244 RPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPD 323
Cdd:TIGR01343 239 EPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 324 VRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPAV 403
Cdd:TIGR01343 319 VRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASPAT 398
|
410
....*....|...
gi 1493453643 404 AAASAILGRIAAP 416
Cdd:TIGR01343 399 AAASAVKGYIADP 411
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-418 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 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: 273960 Cd Length: 413 Bit Score: 557.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 3 MTITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKIL 82
Cdd:TIGR02086 1 MTLAEKILSEKVGRP-VCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 83 RDFARQQQLTHyFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIK 162
Cdd:TIGR02086 80 REFAKRHGIKN-FDVGE-GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 163 FVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRA 242
Cdd:TIGR02086 158 VVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 243 RRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHP 322
Cdd:TIGR02086 238 GLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 323 DVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPA 402
Cdd:TIGR02086 318 DVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSPNAEIYLASPA 397
|
410
....*....|....*.
gi 1493453643 403 VAAASAILGRIAAPQE 418
Cdd:TIGR02086 398 TAAASAVEGYITDPED 413
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-416 |
2.07e-174 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 493.89 E-value: 2.07e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 3 MTITEKILAAHAGLDrVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVPNKDIKSAEQAKIL 82
Cdd:NF040615 1 MTLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 83 RDFARQQQLTHYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIK 162
Cdd:NF040615 79 REFVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 163 FVYYGElQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRA 242
Cdd:NF040615 158 VNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 243 --------RRPYRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARV 314
Cdd:NF040615 237 vseeeiaeLKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 315 LQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPES 394
Cdd:NF040615 317 LKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNINS 396
|
410 420
....*....|....*....|..
gi 1493453643 395 EVYLSNPAVAAASAILGRIAAP 416
Cdd:NF040615 397 YIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-411 |
1.24e-135 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 396.79 E-value: 1.24e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 7 EKILAAHagLDRVEPGQLINVrVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVPN------------KDIK 74
Cdd:pfam00330 1 EKIWDAH--LVEELDGSLLYI-PDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTdlvidhapdaldKNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 75 SA-----EQAKILRDFARQQQLThYFEVGRmGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMA 149
Cdd:pfam00330 77 DEisrnkEQYDFLEWNAKKFGIR-FVPPGQ-GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 150 LGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVP 229
Cdd:pfam00330 155 TQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 230 PDEITLDYVK--GRARRP----------YRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQA---------- 287
Cdd:pfam00330 235 PDETTFEYLRatGRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELvpdpfadavk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 288 -------------------GHVEIQQVVIGSCTNGRLEDLRLAARVL-----QGKKVHPDVRLIVIPGTQEVYRTALKEG 343
Cdd:pfam00330 315 rkaaeraleymglgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLkkaveKGLKVAPGVKASVVPGSEVVRAYAEAEG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1493453643 344 LIEIFIDAGAAVSTPTCGPCLGGHmGILAAGERCLATTNRNFVGRMgHPESEVYLSNPAVAAASAILG 411
Cdd:pfam00330 395 LDKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-420 |
9.23e-127 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 374.63 E-value: 9.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGLDRVEPGQLInvRVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVPNKDIK------ 74
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLL--YIDRHLLNEYTSPQAFSGLRARG-RTVRRPDLTLAVVDHVVPTRPGRdrgitd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 75 --SAEQAKILRDFARQQQLtHYFEVG--RMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMAL 150
Cdd:PRK12466 79 pgGALQVDYLRENCADFGI-RLFDVDdpRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 151 GEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPP 230
Cdd:PRK12466 158 QTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 231 DEITLDYVKGRARRP-----------YRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVS-------------Q 286
Cdd:PRK12466 238 DETTFDYLRGRPRAPkgalwdaalayWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITgrvpdpaaeadpaR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 287 AGHVE------------------IQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIF 348
Cdd:PRK12466 318 RAAMEraldymgltpgtplagipIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493453643 349 IDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGhPESEVYLSNPAVAAASAILGRIAAPQEVL 420
Cdd:PRK12466 398 IAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQG-PGARTHLMSPAMVAAAAVAGHITDVRSLL 468
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-413 |
9.18e-116 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) 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. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), 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: 153129 [Multi-domain] Cd Length: 389 Bit Score: 343.32 E-value: 9.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 31 LVLGNDITAPVAIKEFRRIGV-EKVFDRERVVLVPDHFVPNKDIKSAEQAKILRDFARQQQLtHYFEVGRmGIEHCLLPE 109
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAAlGKVADPSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGI-AFYRPGV-GIIHQIMVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 110 QGLVgPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVD 189
Cdd:cd01351 79 NLAL-PGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 190 GALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRAR-------RPYRVYQ-SDPDARYARVY 261
Cdd:cd01351 158 GVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRpllknlwLAFPEELlADEGAEYDQVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 262 EFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALK 341
Cdd:cd01351 238 EIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSR 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493453643 342 EGLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:cd01351 318 EGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-418 |
1.13e-114 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 349.06 E-value: 1.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAGLDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVpDHFVPNKDIKSAEQAK 80
Cdd:PRK07229 1 MGLTLTEKILYAHLVEGELEPGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYV-DHNLLQADFENADDHR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 81 ILRDFARQQQLtHYFEVGRmGIEHCLLPEQGLVgPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPES 160
Cdd:PRK07229 80 FLQSVAAKYGI-YFSKPGN-GICHQVHLERFAF-PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 161 IKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVK- 239
Cdd:PRK07229 157 VGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 240 -GRARRPYRVYQsDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGK 318
Cdd:PRK07229 237 qGREDDWVELLA-DPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSCTNSSYEDLMRAASILKGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 319 KVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGghMGIL-AAGERCLATTNRNFVGRMGHPESEVY 397
Cdd:PRK07229 316 KVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIG--MGQApATGNVSLRTFNRNFPGRSGTKDAQVY 393
|
410 420
....*....|....*....|.
gi 1493453643 398 LSNPAVAAASAILGRIAAPQE 418
Cdd:PRK07229 394 LASPETAAASALTGVITDPRT 414
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-420 |
1.33e-114 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 343.26 E-value: 1.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHagLDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVeKVFDRERVVLVPDHFVPNKDIK------ 74
Cdd:PRK05478 1 MGKTLYDKLWDAH--VVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGR-KVRRPDLTFATMDHNVPTTDRDlpiadp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 75 -SAEQAKILRDFARQQQLTHY-FEVGRMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGE 152
Cdd:PRK05478 78 vSRIQVETLEKNCKEFGITLFdLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 153 IWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDE 232
Cdd:PRK05478 158 LLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 233 ITLDYVKGRARRP-----------YRVYQSDPDARYARVYEFDVSKLEPQV--------------AFPHLPSNVRPVSQA 287
Cdd:PRK05478 238 TTFEYLKGRPFAPkgedwdkavayWKTLKSDEDAVFDKVVTLDAADIEPQVtwgtnpgqvisidgKVPDPEDFADPVKRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 288 GH-----------------VEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFID 350
Cdd:PRK05478 318 SAeralaymglkpgtpitdIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 351 AGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGhPESEVYLSNPAVAAASAILGRIAAPQEVL 420
Cdd:PRK05478 398 AGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQG-KGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-419 |
2.89e-96 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. 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. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 296.38 E-value: 2.89e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 1 MPMTITEKILAAHAgLDRVEPGQLInVRVDLVLGNDITAPVAIKEFRRIGvEKVFDRERVVLVPDHFVP--NKDI-KSAE 77
Cdd:TIGR00170 1 MPRTLYEKLFDAHI-VYEAEGETPL-LYIDRHLIHEVTSPQAFEGLRQAG-RKVRRPQKTFATMDHNIPtqNRDFnIKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 78 QAKI-LRDFARQQQLT--HYFEVG--RMGIEHCLLPEQGLVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGE 152
Cdd:TIGR00170 78 VAKIqVTELEKNCKEFgvRLFDLHsvDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 153 IWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDE 232
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 233 ITLDYVKGRARRP-----------YRVYQSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPVS---------------- 285
Cdd:TIGR00170 238 TTFEYCKGRPHAPkgkefdkavayWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNsevpdpesfadpvdka 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 286 ---QAGH------------VEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFID 350
Cdd:TIGR00170 318 saeRALAymglepgtplkdIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1493453643 351 AGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHpESEVYLSNPAVAAASAILGRIAAPQEV 419
Cdd:TIGR00170 398 AGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
30-413 |
6.67e-95 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic 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 distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 289.73 E-value: 6.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 30 DLVLGNDITAPVAIKEFRRIGVEKVFDRERVVLVpDHFVPNKDIKSAEQAKILRDFArqQQLTHYFEVGRMGIEHCLLPE 109
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYV-DHNTLQTDFENADDHRFLQTVA--ARYGIYFSRPGNGICHQVHLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 110 QGLVgPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVD 189
Cdd:cd01585 78 RFAV-PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 190 GALYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRV-YQSDPDARYARVYEFDVSKL 268
Cdd:cd01585 157 GGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVeLAADADAEYDEEIEIDLSEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 269 EPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIF 348
Cdd:cd01585 237 EPLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493453643 349 IDAGAAVSTPTCGPCLGghMG-ILAAGERCLATTNRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:cd01585 317 LAAGARILESACGPCIG--MGqAPPTGGVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
32-413 |
2.38e-76 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. 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.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 241.75 E-value: 2.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 32 VLGNDITAPVAIKeFRRIGVEKVFDRERVVLVPDHFVPNKDIKSAEQAKILRDFARQQQLTHYfEVGRmGIEHCLLPEQG 111
Cdd:cd01582 2 CMTHDNSWPVALK-FMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFY-PAGR-GIGHQIMIEEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 112 LVGPGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGA 191
Cdd:cd01582 79 YAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 192 LYQAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDeitldyvkgrarrpyrvyqsdpdaryARVYEFDVSKLEPQ 271
Cdd:cd01582 159 LNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD--------------------------AKHLILDLSTLSPY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 272 VAFPHLPSNVRPVS--QAGHVEIQQVVIGSCTNGRLEDLRLAARVLQGKK-------VHPDVRLIVIPGTQEVYRTALKE 342
Cdd:cd01582 213 VSGPNSVKVSTPLKelEAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKN 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493453643 343 GLIEIFIDAGAAVSTPTCGPCLGGHMGILAAGERCLATTNRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:cd01582 293 GDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
115-413 |
4.12e-47 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic 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. Cis-aconitate is formed as an intermediary product during the course of the reaction. 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: 153134 Cd Length: 412 Bit Score: 166.46 E-value: 4.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 115 PGDVVIGADSHTCTYGALGAFATGVGSTDLAAAMAlGEIW-LKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDGALY 193
Cdd:cd01584 90 PGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 194 QAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARR---------PYRVYQSDPDARYARVYEFD 264
Cdd:cd01584 169 AIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAeiadladefKDDLLVADEGAEYDQLIEIN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 265 VSKLEPQVAFPHLPSNVRPVSQAGHV--------EIQQVVIGSCTNGRLEDLRLAARVLQ---GKKVHPDVRLIVIPGTQ 333
Cdd:cd01584 249 LSELEPHINGPFTPDLATPVSKFKEVaekngwplDLRVGLIGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 334 EVYRTALKEGLIEIFIDAGAAVSTPTCGPCLG--GHMGILAAGERCLATT-NRNFVGRM-GHPESEVYLSNPAVAAASAI 409
Cdd:cd01584 329 QIRATIERDGLLQTFRDAGGIVLANACGPCIGqwDRKDIKKGEKNTIVTSyNRNFTGRNdANPATHAFVASPEIVTAMAI 408
|
....
gi 1493453643 410 LGRI 413
Cdd:cd01584 409 AGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
116-413 |
1.16e-37 |
|
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: 145.63 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 116 GDVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILyTIGQI----GVDG 190
Cdd:COG1048 203 PDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAM-LGQpVSMLIPEVVGVKLTGKLPEGVTATDLVL-TVTEMlrkkGVVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 191 ALyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVK--GRAR------RPYRVYQ------SDPDAR 256
Cdd:COG1048 281 KF---VEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRltGRSEeqielvEAYAKAQglwrdpDAPEPY 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 257 YARVYEFDVSKLEPQVAFPHLPSNVRPVSQA---------------------------------GHVEIqqVVIGSCTNG 303
Cdd:COG1048 358 YSDVLELDLSTVEPSLAGPKRPQDRIPLSDLkeafraalaapvgeeldkpvrvevdgeefelghGAVVI--AAITSCTNT 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 304 RLEDLRLAARVL------QGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGghM-GIL----- 371
Cdd:COG1048 436 SNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIG--NsGPLppeis 513
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1493453643 372 -AAGERCLATT-----NRNFVGRMGHPESEVYLSNPAVAAASAILGRI 413
Cdd:COG1048 514 eAIEENDLVVAavlsgNRNFEGRIHPDVKANFLASPPLVVAYALAGTV 561
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
7-413 |
2.62e-36 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 138.02 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 7 EKILAAHAGLDRVEPGQLINVRVDLVLGNDITAPVAIKEFRRIGVeKVFDRERVVLVPDHFVPNKDIKSAEQAKILRDFA 86
Cdd:cd01581 3 QKIVGRACGVKGVRPGTYCEPKMTTVGSQDTTGPMTRDELKELAC-LGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 87 RQQQLTHYFEVGrmGIEHCLLPEQGLvgPGDVVIGADSHT-----CTYGAlgafatgvGSTDLAAAMALGEIWLKVPESI 161
Cdd:cd01581 82 SNRGGVALRPGD--GVIHSWLNRMLL--PDTVGTGGDSHTrfpigISFPA--------GSGLVAFAAATGVMPLDMPESV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 162 KFVYYGELQPWVGGKDLI----LYTIGQigvdGALYQAME-----FTGPAIE-----TLSMDGRLTMANMAVEAGAKNGI 227
Cdd:cd01581 150 LVRFKGKMQPGITLRDLVnaipYYAIQQ----GLLTVEKKgkknvFNGRILEieglpDLKVEQAFELTDASAERSAAACT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 228 VPPDEITL-DYVK--------------GRARRPYR-------------VYQSDPDARYARVYEFDVSKL-EPQVAFPHLP 278
Cdd:cd01581 226 VRLDKEPViEYLEsnvvlmkimiangyDDARTLLRriiameewlanppLLEPDADAEYAAVIEIDLDDIkEPILACPNDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 279 SNVRPVSQAGHVEIQQVVIGSC-TNgrLEDLRLAARVLQGKKVHPdVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVST 357
Cdd:cd01581 306 DDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEM 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1493453643 358 PTCGPCLGGHMGIlAAGERCLATTNRNFVGRMGHpESEVYLSNPAVAAASAILGRI 413
Cdd:cd01581 383 PGCSLCMGNQARV-ADGATVFSTSTRNFDNRVGK-GAEVYLGSAELAAVCALLGRI 436
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
115-418 |
1.20e-35 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 139.54 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 115 PGDVVIGADSHTctygalgAFATGV----GSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDLI----LYTIGQi 186
Cdd:PRK09238 478 PDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVhaipYYAIKQ- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 187 gvdGALYQAME-----FTGPAIE-----TLSMDGRLTMANMAVEAGAKNGIVP-PDEITLDYVK--------------GR 241
Cdd:PRK09238 550 ---GLLTVEKKgkkniFSGRILEieglpDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLRsnivllkwmiaegyGD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 242 ARRPYR-------------VYQSDPDARYARVYEFDVSKL-EPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSC-TNgrLE 306
Cdd:PRK09238 627 ARTLERriaameewlanpeLLEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCmTN--IG 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 307 DLRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGIlAAGERCLATTNRNFV 386
Cdd:PRK09238 705 HFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARV-ADGATVFSTSTRNFP 783
|
330 340 350
....*....|....*....|....*....|..
gi 1493453643 387 GRMGhPESEVYLSNPAVAAASAILGRIAAPQE 418
Cdd:PRK09238 784 NRLG-KGANVYLGSAELAAVCALLGRIPTVEE 814
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
112-418 |
1.34e-31 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 127.43 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 112 LVGPGDVVIGADSHTcTYGALGAFATGVGSTDLAAAMaLGEIW-LKVPESIKFVYYGELQPWVGGKDLILYTIGQIGVDG 190
Cdd:PRK11413 138 MAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQL-LNDTYdIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 191 ALY-QAMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRP-YRVYQSDPDARYARVYEFDVSKL 268
Cdd:PRK11413 216 YVKnKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQdYCELNPQPMAYYDGCISVDLSAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 269 EPQVAFPHLPSNVRPVSQA---------------------------------GHVEIQQVVIGSCTNGRLEDLRLAARVL 315
Cdd:PRK11413 296 KPMIALPFHPSNVYEIDELnqnltdilreveieservahgkaklslldkienGRLKVQQGIIAGCSGGNYENVIAAANAL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 316 QGKKVHPDV-RLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGhmG-ILAAGERCLATTNRNFVGRMGHPE 393
Cdd:PRK11413 376 RGQSCGNDTfSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGA--GdTPANNGLSIRHTTRNFPNREGSKP 453
|
330 340 350
....*....|....*....|....*....|..
gi 1493453643 394 SEVYLSnpAVA-------AASAILGRIAAPQE 418
Cdd:PRK11413 454 ANGQMS--AVAlmdarsiAATAANGGYLTSAT 483
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
104-413 |
1.87e-31 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 127.05 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 104 HCLLPEQGLVGPgDVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILyT 182
Cdd:PTZ00092 197 RVVFNKDGLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVM-LGQpISMVLPEVVGFKLTGKLSEHVTATDLVL-T 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 183 IGQI----GVDGALyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVK--GR-------------AR 243
Cdd:PTZ00092 274 VTSMlrkrGVVGKF---VEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRseekveliekylkAN 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 244 RPYRVYQSDPdaRYARVYEFDVSKLEPQVAFPHLP------SNVR---------PVSQAGH----------VEIQ----- 293
Cdd:PTZ00092 351 GLFRTYAEQI--EYSDVLELDLSTVVPSVAGPKRPhdrvplSDLKkdftaclsaPVGFKGFgipeekhekkVKFTykgke 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 294 ------QVVIG---SCTNGRLEDLRLAARVL------QGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTP 358
Cdd:PTZ00092 429 ytlthgSVVIAaitSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFYTAGY 508
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493453643 359 TCGPCLGGHMGILAAGERCLA----------TTNRNFVGRMgHPESEV-YLSNPAVAAASAILGRI 413
Cdd:PTZ00092 509 GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGRV 573
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
109-413 |
4.58e-28 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. 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.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 114.32 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 109 EQGLVGPgDVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILYT---IG 184
Cdd:cd01586 115 GDGVAYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVM-LGQpISMLLPEVVGVKLTGKLRPGVTATDLVLTVtqmLR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 185 QIGVDGALyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDeitldyvkgrarrpyrvyqsdpdaryARVYEFD 264
Cdd:cd01586 193 KVGVVGKF---VEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD--------------------------TQVVELD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 265 VSKLEPQVAFPHLPSNVRPVsqagHVEIQQVVIGSCTNGRLEDLRLAARVL------QGKKVHPDVRLIVIPGTQEVYRT 338
Cdd:cd01586 244 LSTVEPSVSGPKRPQDRVPL----HGSVVIAAITSCTNTSNPSVMLAAGLLakkaveLGLKVKPYVKTSLAPGSRVVTKY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 339 ALKEGLIEIFIDAGAAVSTPTCGPCLG--GHM-----------GILAAGercLATTNRNFVGRMgHPESE-VYLSNPAVA 404
Cdd:cd01586 320 LEASGLLPYLEKLGFHVVGYGCTTCIGnsGPLpeeveeaikenDLVVAA---VLSGNRNFEGRI-HPLVRaNYLASPPLV 395
|
....*....
gi 1493453643 405 AASAILGRI 413
Cdd:cd01586 396 VAYALAGTV 404
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
117-414 |
1.08e-26 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 112.72 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 117 DVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILyTIGQ----IGVDGA 191
Cdd:PRK12881 206 DTLVGTDSHTTMINGIGVLGWGVGGIEAEAVM-LGQpVYMLIPDVVGVELTGKLREGVTATDLVL-TVTEmlrkEGVVGK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 192 LyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRVYQ-----------SDPDA--RYA 258
Cdd:PRK12881 284 F---VEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEAQIALveayakaqglwGDPKAepRYT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 259 RVYEFDVSKLEPQVAFPHLP------SNV---------RPVSQAGHVEIQQ-----------VVIG---SCTNGRLEDLR 309
Cdd:PRK12881 361 RTLELDLSTVAPSLAGPKRPqdrialGNVksafsdlfsKPVAENGFAKKAQtsngvdlpdgaVAIAaitSCTNTSNPSVL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 310 LAARVL------QGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLgGHMGIL------AAGERC 377
Cdd:PRK12881 441 IAAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCI-GNSGPLtpeieqAITKND 519
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1493453643 378 LATT-----NRNFVGRMgHPESEV-YLSNPAVAAASAILGRIA 414
Cdd:PRK12881 520 LVAAavlsgNRNFEGRI-HPNIKAnFLASPPLVVAYALAGTVR 561
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
117-413 |
5.80e-25 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 107.52 E-value: 5.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 117 DVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILyTIGQI----GVDGA 191
Cdd:PRK09277 206 DTLVGTDSHTTMINGLGVLGWGVGGIEAEAAM-LGQpSSMLIPEVVGVKLTGKLPEGVTATDLVL-TVTEMlrkkGVVGK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 192 LyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRV-------------YQSDPDARYA 258
Cdd:PRK09277 284 F---VEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEEQValveayakaqglwRDPLEEPVYT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 259 RVYEFDVSKLEPQVAFPHLPSNVRPVSQA-----------------------GHVEIQQ--VVIG---SCTN-------- 302
Cdd:PRK09277 361 DVLELDLSTVEPSLAGPKRPQDRIPLSDVkeafaksaelgvqgfgldeaeegEDYELPDgaVVIAaitSCTNtsnpsvmi 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 303 --GrledlrLAAR--VLQGKKVHPDVRLIVIPGTQEV--YrtaLKE-GLIEiFIDA-GAAVSTPTCGPCLGghM-GIL-- 371
Cdd:PRK09277 441 aaG------LLAKkaVEKGLKVKPWVKTSLAPGSKVVtdY---LEKaGLLP-YLEAlGFNLVGYGCTTCIG--NsGPLpp 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1493453643 372 ----AAGERCLATT-----NRNFVGRMgHPE-SEVYLSNPAVAAASAILGRI 413
Cdd:PRK09277 509 eiekAINDNDLVVTavlsgNRNFEGRI-HPLvKANYLASPPLVVAYALAGTV 559
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
115-420 |
2.42e-23 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 102.69 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 115 PGDVVIGADSHTctygalgAFATGV----GSTDLAAAMALGEIWLKVPESIKFVYYGELQPWVGGKDL---ILYTIGQig 187
Cdd:PLN00094 552 PDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLvhaIPYTAIQ-- 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 188 vDGALYQAME-----FTGPAIET-----LSMDGRLTMANMAVEAGAKNGIVPPDE-----------------ITLDYVKG 240
Cdd:PLN00094 623 -DGLLTVEKKgkknvFSGRILEIeglphLKCEQAFELSDASAERSAAGCTIKLDKepiieylnsnvvmlkwmIAEGYGDR 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 241 RA--RRPYRVYQ---------SDPDARYARVYEFDVSKL-EPQVAFPHLPSNVRPVSQAGHVEIQQVVIGSC-TNgrLED 307
Cdd:PLN00094 702 RTleRRIARMQQwladpelleADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCmTN--IGH 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 308 LRLAARVLQGKKVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCLGGHMGIlAAGERCLATTNRNFVG 387
Cdd:PLN00094 780 FRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARV-AEKSTVVSTSTRNFPN 858
|
330 340 350
....*....|....*....|....*....|...
gi 1493453643 388 RMGHpESEVYLSNPAVAAASAILGRIAAPQEVL 420
Cdd:PLN00094 859 RLGK-GANVYLASAELAAVAAILGRLPTVEEYL 890
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
111-413 |
1.70e-20 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 94.10 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 111 GLVGPgDVVIGADSHTCTYGALGAFATGVGSTDLAAAMaLGE-IWLKVPESIKFVYYGELQPWVGGKDLILyTIGQI--- 186
Cdd:PLN00070 236 GILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAM-LGQpMSMVLPGVVGFKLSGKLRDGVTATDLVL-TVTQMlrk 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 187 -GVDGALyqaMEFTGPAIETLSMDGRLTMANMAVEAGAKNGIVPPDEITLDYVKGRARRPYRVY---------------- 249
Cdd:PLN00070 313 hGVVGKF---VEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAmieaylrankmfvdyn 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 250 QSDPDARYARVYEFDVSKLEPQVAFPHLPSNVRPV---------------------------------------SQAGHV 290
Cdd:PLN00070 390 EPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLkemkadwhscldnkvgfkgfavpkeaqskvakfsfhgqpAELRHG 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493453643 291 EIQQVVIGSCTNGRLEDLRLAARVLQGK------KVHPDVRLIVIPGTQEVYRTALKEGLIEIFIDAGAAVSTPTCGPCL 364
Cdd:PLN00070 470 SVVIAAITSCTNTSNPSVMLGAGLVAKKacelglEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCI 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493453643 365 G--GHM-----------GILAAGercLATTNRNFVGRMgHPESEV-YLSNPAVAAASAILGRI 413
Cdd:PLN00070 550 GnsGELdesvasaitenDIVAAA---VLSGNRNFEGRV-HPLTRAnYLASPPLVVAYALAGTV 608
|
|
| |
