|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-461 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 856.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPT----TDRDLPIAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK05478 77 PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VT 310
Cdd:PRK05478 237 ETTFEYLKGRPFAPKgeDWDKAVAYWKTLKSD-EDAvFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDpedfadpVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 311 DKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIF 390
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 391 TDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFY 461
Cdd:PRK05478 396 IEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-460 |
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: 666.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIA-GKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPTAptpvtsvesv 78
Cdd:COG0065 1 MGMTLAEKILARHAGReVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 79 mDQISKLQITTLQKNCRDFGVELADIGDKdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDkniera 317
Cdd:COG0065 228 PDETTFEYLKGRPFAP---------WRTLKSD-EDAvYDKEVEIDASDLEPQVAWPHSPDNVVP-------VSE------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 318 ydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:COG0065 285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226735976 398 RDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:COG0065 354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-460 |
0e+00 |
|
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: 656.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPT----QNRDFNIKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR00170 77 EVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR00170 157 TLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VTD 311
Cdd:TIGR00170 237 ETTFEYCKGRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDpesfadpVDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:TIGR00170 317 ASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-452 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 611.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 7 DKVWDKHVIAGKKGDpqLLYV-DLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAP----TPVTSVESVMDQ 81
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 82 IS--KLQITTLQKNCRDFGVELADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST 159
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 160 QTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINP 239
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 240 DQKTFDYLR--GRERVPK--DFDKAVEyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-----AV 309
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgeAYDKAVA-WKTLASD-PGAeYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 310 TDKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAAEKI 384
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226735976 385 GLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-454 |
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: 551.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 29 LHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPTAptpvtsvesvmDQISKLQITTLQKNCRDFGVELADIGDk 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-----------DIKAAEQVKTLRKFAKEFGINFFDVGR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 dQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01583 69 -QGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvpkdfdkavEYWKQF 267
Cdd:cd01583 148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---------AYWKEL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01583 219 KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVP-------VSE-----------------VEGIKIDQVFIGSCTNGRL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01583 275 EDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNF 354
|
410 420
....*....|....*....|....*...
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGINGHF 454
Cdd:cd01583 355 KGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-453 |
1.78e-80 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 255.45 E-value: 1.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 4 TLFDKVWDKHViaGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPtaPTPVTSVEsvmd 80
Cdd:NF040615 2 TLAEKILSKKL--GKEvyaGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--ANTVKAAN---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 qisklqittLQKNCRDFgVELADIGD---KDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVF 157
Cdd:NF040615 74 ---------MQKITREF-VKEQGIKNfylGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 158 STQTLWQVKPKNLGVHVTGhLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMI 237
Cdd:NF040615 144 ATGKTWIKVPKTIRVNIVG-KNENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 238 NPDQKTFDYLRgRERVPkdfDKAVEYWKQFKTDSPD---AYDWIIELDVSDLAPYVSwgttpsmsvpygakLPAVTDkni 314
Cdd:NF040615 223 EADEITYEYLR-KEGVS---EEEIAELKKNRITVNEkeeNYYKEIEIDITDMEEQVA--------------CPHHPD--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 315 eraydymDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAG 394
Cdd:NF040615 282 -------NVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 395 CEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGH 453
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-461 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 856.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPT----TDRDLPIAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK05478 77 PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VT 310
Cdd:PRK05478 237 ETTFEYLKGRPFAPKgeDWDKAVAYWKTLKSD-EDAvFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDpedfadpVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 311 DKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIF 390
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 391 TDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFY 461
Cdd:PRK05478 396 IEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-464 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 721.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAPTPVTSVEsvmD 80
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGRDRGIT---D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK12466 79 PGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-------AVTD 311
Cdd:PRK12466 239 ETTFDYLRGRPRAPKgaLWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPdpaaeadPARR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:PRK12466 319 AAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFYQGE 464
Cdd:PRK12466 399 AAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQAG 471
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-460 |
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: 666.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIA-GKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPTAptpvtsvesv 78
Cdd:COG0065 1 MGMTLAEKILARHAGReVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 79 mDQISKLQITTLQKNCRDFGVELADIGDKdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDkniera 317
Cdd:COG0065 228 PDETTFEYLKGRPFAP---------WRTLKSD-EDAvYDKEVEIDASDLEPQVAWPHSPDNVVP-------VSE------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 318 ydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:COG0065 285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226735976 398 RDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:COG0065 354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-460 |
0e+00 |
|
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: 656.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPT----QNRDFNIKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR00170 77 EVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR00170 157 TLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VTD 311
Cdd:TIGR00170 237 ETTFEYCKGRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDpesfadpVDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:TIGR00170 317 ASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-452 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 611.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 7 DKVWDKHVIAGKKGDpqLLYV-DLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAP----TPVTSVESVMDQ 81
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 82 IS--KLQITTLQKNCRDFGVELADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST 159
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 160 QTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINP 239
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 240 DQKTFDYLR--GRERVPK--DFDKAVEyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-----AV 309
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgeAYDKAVA-WKTLASD-PGAeYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 310 TDKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAAEKI 384
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226735976 385 GLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-454 |
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: 551.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 29 LHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPTAptpvtsvesvmDQISKLQITTLQKNCRDFGVELADIGDk 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-----------DIKAAEQVKTLRKFAKEFGINFFDVGR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 dQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01583 69 -QGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvpkdfdkavEYWKQF 267
Cdd:cd01583 148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---------AYWKEL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01583 219 KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVP-------VSE-----------------VEGIKIDQVFIGSCTNGRL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01583 275 EDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNF 354
|
410 420
....*....|....*....|....*...
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGINGHF 454
Cdd:cd01583 355 KGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-460 |
8.27e-125 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 369.12 E-value: 8.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 1 MAKTLFDKVWDKHviAGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPtAPTpvtsve 76
Cdd:PRK00402 1 MGMTLAEKILARH--SGRDvspGDIVEAKVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVP-AKD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 77 svmdqiskLQITTLQKNCRDFGVELA-----DIGDkdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTS 151
Cdd:PRK00402 72 --------IKSAEQQKILREFAKEQGipnffDVGE---GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGST 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 152 EIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGG 231
Cdd:PRK00402 141 DMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 232 AKVAMINPDQKTFDYLRGRERVPkdfdkaveyWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTD 311
Cdd:PRK00402 221 AKAGIFAPDEKTLEYLKERAGRD---------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKP-------VSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 knieraydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:PRK00402 285 -----------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFV 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:PRK00402 348 DAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-458 |
1.87e-102 |
|
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: 312.07 E-value: 1.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 4 TLFDKVWDKHviAGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPtAPTpvtsVESVM 79
Cdd:TIGR01343 1 TIAEKILSKK--SGKEvyaGDLIEAEIDLAMVHDITAPLAIKTLEEYGIdKVWNPEKIVIVFDHQVP-ADT----IKAAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 80 DQIsklqitTLQKNCRDFGVE-LADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:TIGR01343 74 MQK------LAREFVKKQGIKyFYDVG---EGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:TIGR01343 145 TGKTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSmsvpygaklpavtdkNIERAY 318
Cdd:TIGR01343 225 PDEKTIQYLKERRKEP---------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVD---------------NVKPVS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 319 DymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWR 398
Cdd:TIGR01343 281 E---------VEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVS 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 399 DPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVR 458
Cdd:TIGR01343 352 TPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-458 |
2.25e-91 |
|
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: 283.58 E-value: 2.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 3 KTLFDKVWDKHV-IAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPtAPTpvtsVESvmd 80
Cdd:TIGR02086 1 MTLAEKILSEKVgRPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVP-PPT----VEA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 qiSKLQiTTLQKNCRDFGVELADIGDkdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR02086 73 --AEMQ-KEIREFAKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR02086 147 KTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERvpkdfdkavEYWKQFKTDSPDAYDWIIELDVSDLAPYVSwgttpsmsVPygaklpavtdknierayDY 320
Cdd:TIGR02086 227 EETYEYLKKRRG---------LEFRILVPDPGANYYKEIEIDLSDLEPQVA--------VP-----------------HS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 321 MD-LEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRD 399
Cdd:TIGR02086 273 VDnVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICP 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 400 PGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVR 458
Cdd:TIGR02086 353 PGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITDPE 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-453 |
1.78e-80 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 255.45 E-value: 1.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 4 TLFDKVWDKHViaGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPtaPTPVTSVEsvmd 80
Cdd:NF040615 2 TLAEKILSKKL--GKEvyaGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--ANTVKAAN---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 81 qisklqittLQKNCRDFgVELADIGD---KDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVF 157
Cdd:NF040615 74 ---------MQKITREF-VKEQGIKNfylGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 158 STQTLWQVKPKNLGVHVTGhLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMI 237
Cdd:NF040615 144 ATGKTWIKVPKTIRVNIVG-KNENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 238 NPDQKTFDYLRgRERVPkdfDKAVEYWKQFKTDSPD---AYDWIIELDVSDLAPYVSwgttpsmsvpygakLPAVTDkni 314
Cdd:NF040615 223 EADEITYEYLR-KEGVS---EEEIAELKKNRITVNEkeeNYYKEIEIDITDMEEQVA--------------CPHHPD--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 315 eraydymDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAG 394
Cdd:NF040615 282 -------NVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 395 CEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGH 453
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
108-452 |
5.20e-65 |
|
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: 214.28 E-value: 5.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 DQGIVHVIGPQLGLtQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01351 68 GVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvPKDFDKAVEYWKQF 267
Cdd:cd01351 147 VLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR-PLLKNLWLAFPEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01351 226 LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVS-------VSE-----------------VEGTKIDQVLIGSCTNNRY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01351 282 SDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNF 361
|
330 340
....*....|....*....|....*.
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGING 452
Cdd:cd01351 362 PGRLGtYERHVYLASPELAAATAIAG 387
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
110-460 |
8.47e-53 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 188.05 E-value: 8.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGLTQ---PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQtLWQVK-PKNLGVHVTGHLAPGIFAK 185
Cdd:PRK07229 98 GICH----QVHLERfafPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGG-PYYLKmPKVVGVKLTGKLPPWVSAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 186 DIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRERVpkdfdkavey 263
Cdd:PRK07229 173 DVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGREDD---------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 264 WKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSC 342
Cdd:PRK07229 243 WVELLAD-PDAeYDEVIEIDLSELEPLIAGPHSPDNVVP-------VSE-----------------VAGIKVDQVLIGSC 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 343 TNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMnpDKVPA-GMHCAS 421
Cdd:PRK07229 298 TNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM--GQAPAtGNVSLR 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 226735976 422 TTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:PRK07229 376 TFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRTL 415
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
124-454 |
1.08e-49 |
|
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: 173.79 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 124 PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGY 203
Cdd:cd01585 82 PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 204 ALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRErvpkdfdkavEYWKQFKTDSPDAYDWIIEL 281
Cdd:cd01585 162 IFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE----------DDWVELAADADAEYDEEIEI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 282 DVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKH 361
Cdd:cd01585 232 DLSELEPLIARPHSPDNVVP-------VRE-----------------VAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 362 LAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNpDKVPAGMHCASTTNRNFEGRQG-PGTRTHMA 440
Cdd:cd01585 288 VHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG-QAPPTGGVSVRTFNRNFEGRSGtKDDLVYLA 366
|
330
....*....|....
gi 226735976 441 SPAMVAAAGINGHF 454
Cdd:cd01585 367 SPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
33-452 |
5.36e-46 |
|
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: 163.55 E-value: 5.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 33 HEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAPtpvtsvESVMDQISKLQittlqKNCRDFGVELADIGdkdQGIV 112
Cdd:cd01582 5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKS------EKNLKKYKNIE-----SFAKKHGIDFYPAG---RGIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 113 HVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST-QTLWQVkPKNLGVHVTGHLAPGIFAKDIVMAL 191
Cdd:cd01582 71 HQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQI-PPVAKVELKGQLPKGVTGKDVIVAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 192 IAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMinpdqktfdylrgrervpkdfdkaveywkqFKTDS 271
Cdd:cd01582 150 CGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGL------------------------------FPTDA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 272 PDaydwiIELDVSDLAPYVSWGTTPSMSVPYGaklpavtdknieraydymdlepEMPVQDIPINWVFIGSCTNGRLSDLK 351
Cdd:cd01582 200 KH-----LILDLSTLSPYVSGPNSVKVSTPLK----------------------ELEAQNIKINKAYLVSCTNSRASDIA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 352 EAARVMKGK-------HLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTN 424
Cdd:cd01582 253 AAADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATN 332
|
410 420
....*....|....*....|....*....
gi 226735976 425 RNFEGRQG-PGTRTHMASPAMVAAAGING 452
Cdd:cd01582 333 RNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
110-452 |
2.07e-38 |
|
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: 144.12 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGLTQ---PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTlWQVK-PKNLGVHVTGHLAPGIFAK 185
Cdd:cd01584 77 GIIH----QIVLENyafPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELKcPKVIGVKLTGKLSGWTSPK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 186 DIVMA----LIAKYGTnfaeGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRERVPKDFDK 259
Cdd:cd01584 152 DVILKvagiLTVKGGT----GAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAEIADLADE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 260 AveYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYgAKLPAVTDKNieraydymdlepEMPVQdipINWVFI 339
Cdd:cd01584 228 F--KDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPV-SKFKEVAEKN------------GWPLD---LRVGLI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 340 GSCTNGRLSDLKEAARVMK---GKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAM-NPDKVPA 415
Cdd:cd01584 290 GSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwDRKDIKK 369
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 226735976 416 GMHCASTT--NRNFEGRQ--GPGTRTHMASPAMVAAAGING 452
Cdd:cd01584 370 GEKNTIVTsyNRNFTGRNdaNPATHAFVASPEIVTAMAIAG 410
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
110-452 |
4.59e-29 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 120.89 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVH---------VIGPQLGLTQPGKLiVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAP 180
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 181 GIFAKDIVMALiakygTNFAE-----GYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERVPK 255
Cdd:PTZ00092 264 HVTATDLVLTV-----TSMLRkrgvvGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 256 DFDKAVEYWKQ---FKTDSPD-AYDWIIELDVSDLAPYVSWGTTP---------------SMSVPYGAKLPAVTDKNIER 316
Cdd:PTZ00092 339 KVELIEKYLKAnglFRTYAEQiEYSDVLELDLSTVVPSVAGPKRPhdrvplsdlkkdftaCLSAPVGFKGFGIPEEKHEK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 317 --AYDYMDLEPEMPVQDIPInwVFIGSCTNGRLSDLKEAA------RVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDK 388
Cdd:PTZ00092 419 kvKFTYKGKEYTLTHGSVVI--AAITSCTNTSNPSVMLAAgllakkAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 389 I-----FTDAGCewrdpGCSACLAMNPDKVPAGMHCAS----------TTNRNFEGRQGPGTR-THMASPAMVAAAGING 452
Cdd:PTZ00092 497 YleklgFYTAGY-----GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAG 571
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
132-458 |
9.59e-29 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 120.04 E-value: 9.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 132 DSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALiakygTNF--AEGYA---LE 206
Cdd:PRK12881 212 DSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTV-----TEMlrKEGVVgkfVE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 207 YYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvPKDFDKAVE-YWKQ----FKTDSPDAYDWIIEL 281
Cdd:PRK12881 287 FFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGR-TEAQIALVEaYAKAqglwGDPKAEPRYTRTLEL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 282 DVSDLAPYVSWGTTPSMSVPYGAKLPAVTDKNIERAYDYMDLEP-------EMPVQDIPInwVFIGSCTNgrLSD--LKE 352
Cdd:PRK12881 366 DLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKaqtsngvDLPDGAVAI--AAITSCTN--TSNpsVLI 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 353 AARVMKGKHLAPG--VQAWV----VPGSRGVQKAAEKIG----LDKI-FTDAGCewrdpGCSACLAMNPDKVPA------ 415
Cdd:PRK12881 442 AAGLLAKKAVERGltVKPWVktslAPGSKVVTEYLERAGllpyLEKLgFGIVGY-----GCTTCIGNSGPLTPEieqait 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 226735976 416 --GMHCAS--TTNRNFEGRQGPGTRTH-MASPAMVAAAGINGhfvDVR 458
Cdd:PRK12881 517 knDLVAAAvlSGNRNFEGRIHPNIKANfLASPPLVVAYALAG---TVR 561
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
110-449 |
1.40e-26 |
|
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: 113.28 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGL----------TQPGKLIVCG------DSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVH 173
Cdd:COG1048 176 GIVH----QVNLeylafvvwtrEEDGETVAYPdtlvgtDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 174 VTGHLAPGIFAKDIVMA----LIAKYGTnfaeGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR- 248
Cdd:COG1048 252 LTGKLPEGVTATDLVLTvtemLRKKGVV----GKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRl 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 249 -GRE----RVPKDFDKAVEYWKQFKTDSPDaYDWIIELDVSDLAPYVSWGTTPSMSVPYG-------AKLPAVTDKNIER 316
Cdd:COG1048 328 tGRSeeqiELVEAYAKAQGLWRDPDAPEPY-YSDVLELDLSTVEPSLAGPKRPQDRIPLSdlkeafrAALAAPVGEELDK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 317 AYDYMDLEPEMPVQDipiNWVF---IGSCTN------GRLSDLkeAAR--VMKGKhlapGVQAWV----VPGSRGVQKAA 381
Cdd:COG1048 407 PVRVEVDGEEFELGH---GAVViaaITSCTNtsnpsvMIAAGL--LAKkaVEKGL----KVKPWVktslAPGSKVVTDYL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 382 EKIGL----DKI-FTDAGCewrdpGCSACL--------AMNPDKVPAGMHCASTT--NRNFEGRQGPGTRT-HMASPAMV 445
Cdd:COG1048 478 ERAGLlpylEALgFNVVGY-----GCTTCIgnsgplppEISEAIEENDLVVAAVLsgNRNFEGRIHPDVKAnFLASPPLV 552
|
....*..
gi 226735976 446 AA---AG 449
Cdd:COG1048 553 VAyalAG 559
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
110-453 |
6.85e-24 |
|
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: 103.73 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHVIGPQLGLtqPGKLIVCGDSHTSTHGGLgalSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVM 189
Cdd:cd01581 94 GVIHSWLNRMLL--PDTVGTGGDSHTRFPIGI---SFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 190 ALIA------------KYGTNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTF-DYLRG-----RE 251
Cdd:cd01581 169 AIPYyaiqqglltvekKGKKNVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLESnvvlmKI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 252 RVPKDFD---------KAVEYW----KQFKTDSPDAYDWIIELDVSDLapyvswgttpsmsvpygaKLPAVTDKNieray 318
Cdd:cd01581 247 MIANGYDdartllrriIAMEEWlanpPLLEPDADAEYAAVIEIDLDDI------------------KEPILACPN----- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 319 DYMDLEPEMPVQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPgVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:cd01581 304 DPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGART 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 226735976 398 RDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:cd01581 381 EMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGR 435
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
132-452 |
1.06e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 104.44 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 132 DSHTsTH-GGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALiakygTNF--AEGYA---L 205
Cdd:PRK09277 212 DSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTV-----TEMlrKKGVVgkfV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 206 EYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GR--ERVpkdfdKAVE-YWKQ---FKTDSPDA-YD 276
Cdd:PRK09277 286 EFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRdeEQV-----ALVEaYAKAqglWRDPLEEPvYT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 277 WIIELDVSDLapyvswgtTPSMS--------VPYG------AKLPAVTDKNIERAYDYMDLEPEMPVQDIPInwVFIGSC 342
Cdd:PRK09277 361 DVLELDLSTV--------EPSLAgpkrpqdrIPLSdvkeafAKSAELGVQGFGLDEAEEGEDYELPDGAVVI--AAITSC 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 343 TN----------GRLsdlkeaAR--VMKGkhLApgVQAWV----VPGSRGVQKAAEKIG----LDKI-FTDAGCewrdpG 401
Cdd:PRK09277 431 TNtsnpsvmiaaGLL------AKkaVEKG--LK--VKPWVktslAPGSKVVTDYLEKAGllpyLEALgFNLVGY-----G 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226735976 402 CSACLAMN---PDKVPA-----GMHCAS--TTNRNFEGRQGPGTRT-HMASPAMVAAAGING 452
Cdd:PRK09277 496 CTTCIGNSgplPPEIEKaindnDLVVTAvlSGNRNFEGRIHPLVKAnYLASPPLVVAYALAG 557
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
110-452 |
2.83e-22 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 100.26 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVH---------VIGPQLGLTQPGKLiVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAP 180
Cdd:PLN00070 217 GIVHqvnleylgrVVFNTDGILYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 181 GIFAKDIVMA---LIAKYGTnfaEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRE---- 251
Cdd:PLN00070 296 GVTATDLVLTvtqMLRKHGV---VGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRSdetv 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 252 -------RVPKDFdkaVEYwkqFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVP---------------YGAKLPAV 309
Cdd:PLN00070 373 amieaylRANKMF---VDY---NEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPlkemkadwhscldnkVGFKGFAV 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 310 TDKNIERA--YDYMDLEPEMPVQDIPInwVFIGSCTN-GRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAA 381
Cdd:PLN00070 447 PKEAQSKVakFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 382 EKIGLDKIFTDAGCEWRDPGCSACLA-------------MNPDKVPAGMhcaSTTNRNFEGRQGPGTR-THMASPAMVAA 447
Cdd:PLN00070 525 LKSGLQKYLNQQGFHIVGYGCTTCIGnsgeldesvasaiTENDIVAAAV---LSGNRNFEGRVHPLTRaNYLASPPLVVA 601
|
....*
gi 226735976 448 AGING 452
Cdd:PLN00070 602 YALAG 606
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
128-452 |
3.78e-19 |
|
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: 89.29 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 128 IVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEY 207
Cdd:cd01586 124 VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 208 YGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTfdylrgrervpkdfdkaveywkqfktdspdaydwiIELDVSDLA 287
Cdd:cd01586 204 FGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV-----------------------------------VELDLSTVE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 288 PYVSwgttpsmsvpyGAKLPavtdknieraYDYMDLEpempvQDIPInwVFIGSCTNGRLSDLKEAARVMKGKHLAPG-- 365
Cdd:cd01586 249 PSVS-----------GPKRP----------QDRVPLH-----GSVVI--AAITSCTNTSNPSVMLAAGLLAKKAVELGlk 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 366 VQAWV----VPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMN---PDKVPA-----GMHCAS--TTNRNFEGRQ 431
Cdd:cd01586 301 VKPYVktslAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSgplPEEVEEaikenDLVVAAvlSGNRNFEGRI 380
|
330 340
....*....|....*....|..
gi 226735976 432 GPGTR-THMASPAMVAAAGING 452
Cdd:cd01586 381 HPLVRaNYLASPPLVVAYALAG 402
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
121-452 |
6.38e-14 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 74.28 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 121 LTQPGKLIVCGDSHTStHGGLGALSFGIGTSEIEHVFSTQTlWQVK-PKNLGVHVTGHLAPGIFAKDIVMALI-AKYGTN 198
Cdd:PRK11413 138 MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDT-YDIDyPGVVAVYLTGKPAPGVGPQDVALAIIgAVFKNG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 199 FAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRErvpkdfdkavEYWKQFKTDSPDAYD 276
Cdd:PRK11413 216 YVKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRG----------QDYCELNPQPMAYYD 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 277 WIIELDVSDLAPYVSWGTTPSMSVP---YGAKLPAVTDKNIERAYDYMDLEPEMPVQDIPIN---WV---FIGSCTNGRL 347
Cdd:PRK11413 286 GCISVDLSAIKPMIALPFHPSNVYEideLNQNLTDILREVEIESERVAHGKAKLSLLDKIENgrlKVqqgIIAGCSGGNY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAW-VVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNpdKVPA--GMHCASTTn 424
Cdd:PRK11413 366 ENVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAG--DTPAnnGLSIRHTT- 442
|
330 340 350
....*....|....*....|....*....|....*
gi 226735976 425 RNFEGRQG--PGtRTHMASPAM-----VAAAGING 452
Cdd:PRK11413 443 RNFPNREGskPA-NGQMSAVALmdarsIAATAANG 476
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
131-452 |
4.74e-13 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 71.49 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 131 GDSHT------STHGGLGALSFGIGTSEIEHVFstqtlwqvkPKNLGVHVTGHLAPGIFAKDIVMAL-----------IA 193
Cdd:PLN00094 559 GDSHTrfpigiSFPAGSGLVAFGAATGVIPLDM---------PESVLVRFTGTMQPGITLRDLVHAIpytaiqdglltVE 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 194 KYG-TNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTF-DYLR--------------GRERVPKDF 257
Cdd:PLN00094 630 KKGkKNVFSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEPIiEYLNsnvvmlkwmiaegyGDRRTLERR 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 258 DKAVEYW----KQFKTDSPDAYDWIIELDVSDLapyvswgTTPSMSVPygaklpavTDKNIERAYDymdlepemPVQDIP 333
Cdd:PLN00094 708 IARMQQWladpELLEADPDAEYAAVIEIDMDEI-------KEPILCAP--------NDPDDARLLS--------EVTGDK 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 334 INWVFIGSC-TNgrLSDLKEAARVMKgKHLAP-GVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAmNPD 411
Cdd:PLN00094 765 IDEVFIGSCmTN--IGHFRAAGKLLN-DNLSQlPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQA 840
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 226735976 412 KVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:PLN00094 841 RVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILG 881
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
98-453 |
7.62e-13 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 70.98 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 98 GVELADiGDkdqGIVHVIGPQLGLtqPGKLIVCGDSHTSTHGGLgalSF--GIGTSEIEHVFSTQTLwqVKPKNLGVHVT 175
Cdd:PRK09238 458 GVSLRP-GD---GVIHSWLNRMLL--PDTVGTGGDSHTRFPIGI---SFpaGSGLVAFAAATGVMPL--DMPESVLVRFK 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 176 GHLAPGIFAKDIVMALIA------------KYGTNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKT 243
Cdd:PRK09238 527 GEMQPGITLRDLVHAIPYyaikqglltvekKGKKNIFSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEP 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 244 F-DYLRG-----RERVPKDFD---------KAVEYWKQFKTD-SPDA---YDWIIELDVSDLapyvswgttpsmsvpyga 304
Cdd:PRK09238 605 IiEYLRSnivllKWMIAEGYGdartlerriAAMEEWLANPELlEADAdaeYAAVIEIDLAEI------------------ 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 305 KLPAVTDKNierayDYMDLEPEMPVQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEK 383
Cdd:PRK09238 667 KEPILACPN-----DPDDVRLLSEVAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTE 739
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 384 IGLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:PRK09238 740 EGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 808
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
329-453 |
4.31e-11 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 65.26 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 329 VQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPgVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLA 407
Cdd:COG1049 686 VAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG 762
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 226735976 408 mNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:COG1049 763 -NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 807
|
|
| PRK02603 |
PRK02603 |
photosystem I assembly protein Ycf3; Provisional |
189-275 |
2.00e-03 |
|
photosystem I assembly protein Ycf3; Provisional
Pssm-ID: 179448 [Multi-domain] Cd Length: 172 Bit Score: 38.88 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 189 MALIakYGTNFAEGYALEYYGPTIDEMPienRM--TLTNM--IIEGGAKVAMINPDQKTFDYLrgrervpkdFDKAVEYW 264
Cdd:PRK02603 78 MGII--YASNGEHDKALEYYHQALELNP---KQpsALNNIavIYHKRGEKAEEAGDQDEAEAL---------FDKAAEYW 143
|
90
....*....|.
gi 226735976 265 KQFKTDSPDAY 275
Cdd:PRK02603 144 KQAIRLAPNNY 154
|
|
|