|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
14-500 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 872.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDpdIDDSTQakLIYVDRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTPGRNSfkteeyI 93
Cdd:PRK05478 5 LYDKLWDAHVVHE--EEDGPD--LLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLP------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 94 KESASRAQYMALEKNVRRSRIPYFSLWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLA 173
Cdd:PRK05478 75 ADPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 174 TQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVA 253
Cdd:PRK05478 155 TQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 254 PDETTFAYLKGRPMAPpstnvpvawDGEKdiWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGC 333
Cdd:PRK05478 235 PDETTFEYLKGRPFAP---------KGED--WDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 VPDPKAIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:PRK05478 304 VPDPEDFADPVKRASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKG----RKVAPGVRALVVPGS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:PRK05478 380 GLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHF 459
|
....*..
gi 1860672246 494 TDVRTLV 500
Cdd:PRK05478 460 VDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
14-497 |
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: 700.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDpdidDSTQAKLIYVDRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTpGRNSFkteeyI 93
Cdd:TIGR00170 5 LYEKLFDAHIVYE----AEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQ-NRDFN-----I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 94 KESASRAQYMALEKNVRRSRIPYFSLWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLA 173
Cdd:TIGR00170 75 KDEVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 174 TQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVA 253
Cdd:TIGR00170 155 TQTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 254 PDETTFAYLKGRPMAPpstnvpvawDGEKdiWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGC 333
Cdd:TIGR00170 235 PDETTFEYCKGRPHAP---------KGKE--FDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 VPDPKAIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:TIGR00170 304 VPDPESFADPVDKASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKG----RKVADNVKALVVPGS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:TIGR00170 380 GLVKLQAEKEGLDKIFIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHF 459
|
....
gi 1860672246 494 TDVR 497
Cdd:TIGR00170 460 VDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
14-499 |
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: 658.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDPDIDDSTqakLIYVDRHLVHEVSSPQAFDGLWSA-KRSVRRPDCTLATADHNVPTTPgrnsfkteey 92
Cdd:COG0065 5 LAEKILARHAGREVEPGEIV---LLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPTKD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 93 ikeSASRAQYMALEKNVRRSRIPYFSLwdTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVL 172
Cdd:COG0065 72 ---PKSAEQVKTLREFAKEFGITFFDV--GDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 173 ATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMV 252
Cdd:COG0065 147 ATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 253 APDETTFAYLKGRPMAPpstnvpvawdgekdiwdeaveyWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITG 332
Cdd:COG0065 227 APDETTFEYLKGRPFAP----------------------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 333 cvpdpkaiqnqakregvekaleymglvgstrMEDIKIDKVFLGSCTNSRIEDLRIAANILAsvGpeARVAEGVMAMVVPG 412
Cdd:COG0065 285 -------------------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILK--G--RKVAPGVRAIVVPG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 413 SGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQG-TGGRTHLVSPAMAVAAALKG 491
Cdd:COG0065 330 SQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAG 409
|
....*...
gi 1860672246 492 RLTDVRTL 499
Cdd:COG0065 410 RITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
16-491 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 653.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 16 DKIWEKHVVYDPDIDdstqakLIYV-DRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTP----GRNSFKTE 90
Cdd:pfam00330 1 EKIWDAHLVEELDGS------LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 91 EYIKESASRAQYMALEKNVRRSRIPYfslWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEH 170
Cdd:pfam00330 75 IEDEISRNKEQYDFLEWNAKKFGIRF---VPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 171 VLATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAG 250
Cdd:pfam00330 152 VLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 251 MVAPDETTFAYLK--GRPMAPpstnvpvawDGEKdiWDEAVEyWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNV 328
Cdd:pfam00330 232 LFPPDETTFEYLRatGRPEAP---------KGEA--YDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 329 PITGCVPDPkaIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILA-SVGPEARVAEGVMA 407
Cdd:pfam00330 300 PLSELVPDP--FADAVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkAVEKGLKVAPGVKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 408 MVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGlNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAA 487
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAA 456
|
....
gi 1860672246 488 ALKG 491
Cdd:pfam00330 457 AIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
42-493 |
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: 562.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 42 RHLVHEVSSPQAFDGLWSAKRS-VRRPDCTLATADHNVPTtpgrnsfkteeyiKESASRAQYMALEKNVRRSRIPYFSLw 120
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------------PDIKAAEQVKTLRKFAKEFGINFFDV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 121 dTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSK 200
Cdd:cd01583 67 -GRQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 201 DVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLKGRPmappstnvpvawdg 280
Cdd:cd01583 146 DVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRG-------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 281 ekdiwdeaVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGCVPdpkaiqnqakregvekaleymglvg 360
Cdd:cd01583 212 --------KAYWKELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 361 strmedIKIDKVFLGSCTNSRIEDLRIAANILAsvgpEARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAG 440
Cdd:cd01583 259 ------IKIDQVFIGSCTNGRLEDLRAAAEILK----GRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPG 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 441 CSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGG-RTHLVSPAMAVAAALKGRL 493
Cdd:cd01583 329 CGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
561-766 |
1.97e-85 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 269.30 E-value: 1.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPVTKEETDFILNQKPWKEAKIVVsAGKNFGCGSS 640
Cdd:PRK01641 4 FTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILL-AGDNFGCGSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 641 REHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLANYAAT--GEEMEVDLEKQEIRClrrrdlqdsd 718
Cdd:PRK01641 83 REHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEAnpGAELTVDLEAQTVTA---------- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860672246 719 DSMVTPFNVDPVNRDRLLAGLDDIDMTLSVEKEVSKYEEKRRREWRWL 766
Cdd:PRK01641 153 PDKTFPFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
561-766 |
7.23e-83 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 262.42 E-value: 7.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPVTKEetDFILNQKPWKEAKIVVsAGKNFGCGSS 640
Cdd:COG0066 3 FTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDRSPDP--DFVLNQPRYQGADILV-AGRNFGCGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 641 REHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLAN--YAATGEEMEVDLEKQEIRCLrrrdlqdsd 718
Cdd:COG0066 80 REHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAaiEANPGDELTVDLEAGTVTNG--------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860672246 719 DSMVTPFNVDPVNRDRLLAGLDDIDMTLSVEKEVSKYEEKRRrewRWL 766
Cdd:COG0066 151 TGETYPFEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRP---AWL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
561-752 |
3.71e-56 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 190.80 E-value: 3.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFN--RFRWDPVTKEETDFILNQKPWKEAKIVVsAGKNFGCG 638
Cdd:TIGR00171 4 FKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFdwRFLDANGKEPNPDFVLNQPQYQGASILL-ARENFGCG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 639 SSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESIC-ETLANYAATGEEMEVDLEKQEIRclrrrdlqDS 717
Cdd:TIGR00171 83 SSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVkELFGQVENQGLQMTVDLENQLIH--------DS 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1860672246 718 DDSMVTpFNVDPVNRDRLLAGLDDIDMTLSVEKEV 752
Cdd:TIGR00171 155 EGKVYS-FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
560-681 |
1.04e-35 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 131.33 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 560 RFTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPV----TKEETDFILNQKPWKE--AKIVVSAGK 633
Cdd:pfam00694 3 VFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVrylpDGENPDFYDAAMRYKQhgAPIVVIGGK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1860672246 634 NFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSE 681
Cdd:pfam00694 83 NFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
571-701 |
7.42e-34 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 124.62 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 571 LRMENIDTDMLVPAPLLkgltrtglakalfnrfrwdpvtkeetdfilnqkpwkeAKIVVsAGKNFGCGSSREHAVWALKD 650
Cdd:cd01577 1 LFGDNIDTDQIIPARFL-------------------------------------GDIIV-AGKNFGCGSSREHAPWALKD 42
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1860672246 651 FGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLAnyAATGEEMEVDL 701
Cdd:cd01577 43 AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVE--AKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
574-707 |
6.72e-14 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 70.13 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPAPLLKGLTRTGLAKALFNrfrwdpvtKEETDFILNQKpwkEAKIVVsAGKNFGCGSSREHAVWALKDFGI 653
Cdd:NF040625 13 DNIDTDVIIPGRYLRTFNPDDLASHVME--------GERPDFTKNVQ---KGDIIV-AGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1860672246 654 TCVIAPSYGDIFFNNCLQNGVLLVTlsesicetlANYAAT-GEEMEVDLEKQEIR 707
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIGLPVIV---------ADIEADdGDILSIDLEKGIIK 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
14-500 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 872.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDpdIDDSTQakLIYVDRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTPGRNSfkteeyI 93
Cdd:PRK05478 5 LYDKLWDAHVVHE--EEDGPD--LLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLP------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 94 KESASRAQYMALEKNVRRSRIPYFSLWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLA 173
Cdd:PRK05478 75 ADPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 174 TQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVA 253
Cdd:PRK05478 155 TQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 254 PDETTFAYLKGRPMAPpstnvpvawDGEKdiWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGC 333
Cdd:PRK05478 235 PDETTFEYLKGRPFAP---------KGED--WDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 VPDPKAIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:PRK05478 304 VPDPEDFADPVKRASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKG----RKVAPGVRALVVPGS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:PRK05478 380 GLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHF 459
|
....*..
gi 1860672246 494 TDVRTLV 500
Cdd:PRK05478 460 VDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
14-503 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 764.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDPDIDDStqakLIYVDRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTPGRnsfktEEYI 93
Cdd:PRK12466 6 LYDKLWDSHTVARLDDGHV----LLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGR-----DRGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 94 KESASRAQYMALEKNVRRSRIPYFSLWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLA 173
Cdd:PRK12466 77 TDPGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 174 TQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVA 253
Cdd:PRK12466 157 TQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 254 PDETTFAYLKGRPMAPpstnvpvawDGEKdiWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGC 333
Cdd:PRK12466 237 PDETTFDYLRGRPRAP---------KGAL--WDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 VPDPKAIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:PRK12466 306 VPDPAAEADPARRAAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRG----RKVAPGVRAMVVPGS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:PRK12466 382 GAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHI 461
|
490
....*....|
gi 1860672246 494 TDVRTLVKTE 503
Cdd:PRK12466 462 TDVRSLLQAG 471
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
14-497 |
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: 700.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDpdidDSTQAKLIYVDRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTpGRNSFkteeyI 93
Cdd:TIGR00170 5 LYEKLFDAHIVYE----AEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQ-NRDFN-----I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 94 KESASRAQYMALEKNVRRSRIPYFSLWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLA 173
Cdd:TIGR00170 75 KDEVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 174 TQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVA 253
Cdd:TIGR00170 155 TQTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 254 PDETTFAYLKGRPMAPpstnvpvawDGEKdiWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGC 333
Cdd:TIGR00170 235 PDETTFEYCKGRPHAP---------KGKE--FDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 VPDPKAIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:TIGR00170 304 VPDPESFADPVDKASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKG----RKVADNVKALVVPGS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:TIGR00170 380 GLVKLQAEKEGLDKIFIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHF 459
|
....
gi 1860672246 494 TDVR 497
Cdd:TIGR00170 460 VDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
14-499 |
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: 658.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDPDIDDSTqakLIYVDRHLVHEVSSPQAFDGLWSA-KRSVRRPDCTLATADHNVPTTPgrnsfkteey 92
Cdd:COG0065 5 LAEKILARHAGREVEPGEIV---LLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPTKD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 93 ikeSASRAQYMALEKNVRRSRIPYFSLwdTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVL 172
Cdd:COG0065 72 ---PKSAEQVKTLREFAKEFGITFFDV--GDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 173 ATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMV 252
Cdd:COG0065 147 ATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 253 APDETTFAYLKGRPMAPpstnvpvawdgekdiwdeaveyWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITG 332
Cdd:COG0065 227 APDETTFEYLKGRPFAP----------------------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 333 cvpdpkaiqnqakregvekaleymglvgstrMEDIKIDKVFLGSCTNSRIEDLRIAANILAsvGpeARVAEGVMAMVVPG 412
Cdd:COG0065 285 -------------------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILK--G--RKVAPGVRAIVVPG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 413 SGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQG-TGGRTHLVSPAMAVAAALKG 491
Cdd:COG0065 330 SQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAG 409
|
....*...
gi 1860672246 492 RLTDVRTL 499
Cdd:COG0065 410 RITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
16-491 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 653.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 16 DKIWEKHVVYDPDIDdstqakLIYV-DRHLVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTTP----GRNSFKTE 90
Cdd:pfam00330 1 EKIWDAHLVEELDGS------LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 91 EYIKESASRAQYMALEKNVRRSRIPYfslWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEH 170
Cdd:pfam00330 75 IEDEISRNKEQYDFLEWNAKKFGIRF---VPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 171 VLATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAG 250
Cdd:pfam00330 152 VLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 251 MVAPDETTFAYLK--GRPMAPpstnvpvawDGEKdiWDEAVEyWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNV 328
Cdd:pfam00330 232 LFPPDETTFEYLRatGRPEAP---------KGEA--YDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 329 PITGCVPDPkaIQNQAKREGVEKALEYMGLVGSTRMEDIKIDKVFLGSCTNSRIEDLRIAANILA-SVGPEARVAEGVMA 407
Cdd:pfam00330 300 PLSELVPDP--FADAVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkAVEKGLKVAPGVKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 408 MVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGlNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAA 487
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAA 456
|
....
gi 1860672246 488 ALKG 491
Cdd:pfam00330 457 AIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
42-493 |
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: 562.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 42 RHLVHEVSSPQAFDGLWSAKRS-VRRPDCTLATADHNVPTtpgrnsfkteeyiKESASRAQYMALEKNVRRSRIPYFSLw 120
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------------PDIKAAEQVKTLRKFAKEFGINFFDV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 121 dTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSK 200
Cdd:cd01583 67 -GRQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 201 DVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLKGRPmappstnvpvawdg 280
Cdd:cd01583 146 DVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRG-------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 281 ekdiwdeaVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGCVPdpkaiqnqakregvekaleymglvg 360
Cdd:cd01583 212 --------KAYWKELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 361 strmedIKIDKVFLGSCTNSRIEDLRIAANILAsvgpEARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAG 440
Cdd:cd01583 259 ------IKIDQVFIGSCTNGRLEDLRAAAEILK----GRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPG 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 441 CSMCIGLNPDQLGSGERCASTSNRNFRDRQGTGG-RTHLVSPAMAVAAALKGRL 493
Cdd:cd01583 329 CGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
17-500 |
4.32e-119 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 365.27 E-value: 4.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 17 KIWEKHVVYDPDIDDSTQAKliyVDRHLVHEVSSPQAFDGLWSA-KRSVRRPDCTLATADHNVPTtpgrnsfkteeyiKE 95
Cdd:PRK00402 8 KILARHSGRDVSPGDIVEAK---VDLVMAHDITGPLAIKEFEKIgGDKVFDPSKIVIVFDHFVPA-------------KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 96 SASRAQYMALEKNVRRSRIPYFslWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQ 175
Cdd:PRK00402 72 IKSAEQQKILREFAKEQGIPNF--FDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 176 TIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPD 255
Cdd:PRK00402 150 KTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 256 ETTFAYLKGRPMAPPstnvpvawdgekdiwdeaveywKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPeDNVpitgcvp 335
Cdd:PRK00402 230 EKTLEYLKERAGRDY----------------------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLP-DNV------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 336 dpKAIqnqakregvekaleymglvgsTRMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGSGV 415
Cdd:PRK00402 280 --KPV---------------------SEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKG----RKVAPGVRLIVIPASQK 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 416 VKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQG-TGGRTHLVSPAMAVAAALKGRLT 494
Cdd:PRK00402 333 IYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKIT 412
|
....*.
gi 1860672246 495 DVRTLV 500
Cdd:PRK00402 413 DPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
16-497 |
2.51e-97 |
|
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: 308.61 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 16 DKIWEKHVVYDPDIDDSTQAKliyVDRHLVHEVSSPQAFDGLWS-AKRSVRRPDCTLATADHNVPTtpgrNSFKteeyik 94
Cdd:TIGR01343 4 EKILSKKSGKEVYAGDLIEAE---IDLAMVHDITAPLAIKTLEEyGIDKVWNPEKIVIVFDHQVPA----DTIK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 95 esASRAQYMALEKnVRRSRIPYFslWDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLAT 174
Cdd:TIGR01343 71 --AAEMQKLAREF-VKKQGIKYF--YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 175 QTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAP 254
Cdd:TIGR01343 146 GKTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 255 DETTFAYLKgrpmappstnvpvawdgekdiwDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPeDNV-PITGc 333
Cdd:TIGR01343 226 DEKTIQYLK----------------------ERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNV-DNVkPVSE- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 334 vpdpkaiqnqakregvekaleymglvgstrMEDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGS 413
Cdd:TIGR01343 282 ------------------------------VEGTEIDQVFIGSCTNGRLEDLRVAAKILKG----RKVAPDVRLIVIPAS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGT-GGRTHLVSPAMAVAAALKGR 492
Cdd:TIGR01343 328 RAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHpNAEIYLASPATAAASAVKGY 407
|
....*
gi 1860672246 493 LTDVR 497
Cdd:TIGR01343 408 IADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
14-497 |
2.25e-87 |
|
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: 282.42 E-value: 2.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 14 LYDKIWEKHVVYDPDIDDSTQAKliyVDRHLVHEVSSPQAFDGL-WSAKRSVRRPDCTLATADHNVPTtpgrNSFKteey 92
Cdd:TIGR02086 3 LAEKILSEKVGRPVCAGEIVEVE---VDLAMTHDGTGPLAIKALrELGVARVWDPEKIVIAFDHNVPP----PTVE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 93 ikesASRAQYMALEKnVRRSRIPYFslwDTRQGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVL 172
Cdd:TIGR02086 72 ----AAEMQKEIREF-AKRHGIKNF---DVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 173 ATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMV 252
Cdd:TIGR02086 144 ATGKTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGII 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 253 APDETTFAYLKGRPMAPPstnvpvawdgekdiwdeaveywKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPItg 332
Cdd:TIGR02086 224 EPDEETYEYLKKRRGLEF----------------------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPV-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 333 cvpdpkaiqnqakregvekaleymglvgsTRMEDIKIDKVFLGSCTNSRIEDLRIAANILAsvgpEARVAEGVMAMVVPG 412
Cdd:TIGR02086 280 -----------------------------SDVEGTEIDQVFIGSCTNGRLEDLRIAAEILK----GRRVHPDVRLIVIPA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 413 SGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGLNPDQLGSGERCASTSNRNFRDRQGT-GGRTHLVSPAMAVAAALKG 491
Cdd:TIGR02086 327 SRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEG 406
|
....*.
gi 1860672246 492 RLTDVR 497
Cdd:TIGR02086 407 YITDPE 412
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
561-766 |
1.97e-85 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 269.30 E-value: 1.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPVTKEETDFILNQKPWKEAKIVVsAGKNFGCGSS 640
Cdd:PRK01641 4 FTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILL-AGDNFGCGSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 641 REHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLANYAAT--GEEMEVDLEKQEIRClrrrdlqdsd 718
Cdd:PRK01641 83 REHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEAnpGAELTVDLEAQTVTA---------- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860672246 719 DSMVTPFNVDPVNRDRLLAGLDDIDMTLSVEKEVSKYEEKRRREWRWL 766
Cdd:PRK01641 153 PDKTFPFEIDPFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
561-766 |
7.23e-83 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 262.42 E-value: 7.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPVTKEetDFILNQKPWKEAKIVVsAGKNFGCGSS 640
Cdd:COG0066 3 FTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDRSPDP--DFVLNQPRYQGADILV-AGRNFGCGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 641 REHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLAN--YAATGEEMEVDLEKQEIRCLrrrdlqdsd 718
Cdd:COG0066 80 REHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAaiEANPGDELTVDLEAGTVTNG--------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1860672246 719 DSMVTPFNVDPVNRDRLLAGLDDIDMTLSVEKEVSKYEEKRRrewRWL 766
Cdd:COG0066 151 TGETYPFEIDPFRRECLLNGLDDIGLTLKHADAIAAFEAKRP---AWL 195
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
120-493 |
1.31e-63 |
|
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: 218.13 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 120 WDTRQGIVHVIGGEQgFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTS 199
Cdd:cd01351 65 YRPGVGIIHQIMVEN-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 200 KDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLKGRpmappstnvpvawd 279
Cdd:cd01351 144 KDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEAT-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 280 GEKDIWDEAVEYWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPItgcvpdpkaiqnqakregvekaleymglv 359
Cdd:cd01351 210 GRPLLKNLWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV----------------------------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 360 gsTRMEDIKIDKVFLGSCTNSRIEDLRIAANILAsvgpEARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREA 439
Cdd:cd01351 261 --SEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLK----GAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1860672246 440 GCSMCIGLNPDQLGSGERCASTSNRNFRDRQGTG-GRTHLVSPAMAVAAALKGRL 493
Cdd:cd01351 335 GCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYeRHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
125-675 |
1.46e-60 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 216.55 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 125 GIVHVIGGEQgFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVIL 204
Cdd:PRK07229 98 GICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 205 HIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPmappstnvpvawdgek 282
Cdd:PRK07229 177 ELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGRE---------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 283 DIWDEaveywktLKSDEGAKFDKEVVIQAEDISPTVTWGTSPeDNVpitgcVPdpkaiqnqakregVEKaleymglvgst 362
Cdd:PRK07229 241 DDWVE-------LLADPDAEYDEVIEIDLSELEPLIAGPHSP-DNV-----VP-------------VSE----------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 363 rMEDIKIDKVFLGSCTNSRIEDLRIAANILAsvgpEARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCS 442
Cdd:PRK07229 284 -VAGIKVDQVLIGSCTNSSYEDLMRAASILK----GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 443 MCIGLNPDQlGSGERCASTSNRNFRDRQGT-GGRTHLVSPAMAVAAALKGRLTDVRTLVKT----EELKKSTTDAVKKAG 517
Cdd:PRK07229 359 PCIGMGQAP-ATGNVSLRTFNRNFPGRSGTkDAQVYLASPETAAASALTGVITDPRTLALEngeyPKLEEPEGFAVDDAG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 518 SLPDLLFEEQVSV---------PDLPEPKESLkldsssgsedamaarrqsrrftsvrGVAVPLRME-NIDTDMLVPA--- 584
Cdd:PRK07229 438 IIAPAEDGSDVEVvrgpnikplPLLEPLPDLL-------------------------EGKVLLKVGdNITTDHIMPAgak 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 585 --PLLKGLTRtgLAKALFNRFrwDPvtkeetDFilNQKPWKEAKIVVSAGKNFGCGSSREHAVWALKDFGITCVIAPSYG 662
Cdd:PRK07229 493 wlPYRSNIPN--ISEFVFEGV--DN------TF--PERAKEQGGGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFA 560
|
570
....*....|...
gi 1860672246 663 DIFFNNCLQNGVL 675
Cdd:PRK07229 561 RIHKANLINFGIL 573
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
561-752 |
3.71e-56 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 190.80 E-value: 3.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 561 FTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFN--RFRWDPVTKEETDFILNQKPWKEAKIVVsAGKNFGCG 638
Cdd:TIGR00171 4 FKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFdwRFLDANGKEPNPDFVLNQPQYQGASILL-ARENFGCG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 639 SSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESIC-ETLANYAATGEEMEVDLEKQEIRclrrrdlqDS 717
Cdd:TIGR00171 83 SSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVkELFGQVENQGLQMTVDLENQLIH--------DS 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1860672246 718 DDSMVTpFNVDPVNRDRLLAGLDDIDMTLSVEKEV 752
Cdd:TIGR00171 155 EGKVYS-FEIDPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
125-493 |
3.01e-51 |
|
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: 183.80 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 125 GIVHVIGGEQgFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVIL 204
Cdd:cd01585 69 GICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 205 HIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLKgrpmappstnvpvAWDGEKDi 284
Cdd:cd01585 148 ELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLA-------------AQGREDD- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 285 wdeaveyWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPItgcvpdpkaiqnqakREgvekaleymglvgstrM 364
Cdd:cd01585 214 -------WVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPV---------------RE----------------V 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 365 EDIKIDKVFLGSCTNSRIEDLRIAANILASvgpeARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMC 444
Cdd:cd01585 256 AGIKVDQVAIGSCTNSSYEDLMTVAAILKG----RRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPC 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1860672246 445 IGLN--PdqlGSGERCASTSNRNFRDRQGT-GGRTHLVSPAMAVAAALKGRL 493
Cdd:cd01585 332 IGMGqaP---PTGGVSVRTFNRNFEGRSGTkDDLVYLASPEVAAAAALTGVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
560-681 |
1.04e-35 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 131.33 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 560 RFTSVRGVAVPLRMENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPV----TKEETDFILNQKPWKE--AKIVVSAGK 633
Cdd:pfam00694 3 VFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVrylpDGENPDFYDAAMRYKQhgAPIVVIGGK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1860672246 634 NFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSE 681
Cdd:pfam00694 83 NFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
44-493 |
3.00e-35 |
|
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: 137.75 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 44 LVHEVSSPQAFDGLWSAKRSVRRPDCTLATADHNVPTtpgrnsfkteeyiKESASRAQYMALEKNVRRSRIPYFSlwdTR 123
Cdd:cd01582 3 MTHDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQN-------------KSEKNLKKYKNIESFAKKHGIDFYP---AG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 124 QGIVHVIGGEQGFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVI 203
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 204 LHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDEttfaylkgrpmappstnvpvawdgekd 283
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA--------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 284 iwdeaveywktlksdegakfdKEVVIQAEDISPTVTwgtSPednvpitgcvpdpkaiqNQAKREGVEKALEymglvgstr 363
Cdd:cd01582 200 ---------------------KHLILDLSTLSPYVS---GP-----------------NSVKVSTPLKELE--------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 364 MEDIKIDKVFLGSCTNSRIEDLRIAANIL---ASVGPEARVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAG 440
Cdd:cd01582 230 AQNIKINKAYLVSCTNSRASDIAAAADVVkgkKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAG 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 441 CSMCIGLNPDQLGSGERCASTSNRNFRDRQG-TGGRTHLVSPAMAVAAALKGRL 493
Cdd:cd01582 310 CGPCIGLGQGLLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAISGKI 363
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
571-701 |
7.42e-34 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 124.62 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 571 LRMENIDTDMLVPAPLLkgltrtglakalfnrfrwdpvtkeetdfilnqkpwkeAKIVVsAGKNFGCGSSREHAVWALKD 650
Cdd:cd01577 1 LFGDNIDTDQIIPARFL-------------------------------------GDIIV-AGKNFGCGSSREHAPWALKD 42
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1860672246 651 FGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLAnyAATGEEMEVDL 701
Cdd:cd01577 43 AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVE--AKPGDEVEVDL 91
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
120-493 |
2.23e-32 |
|
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: 130.25 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 120 WDTRQGIVHVIGGEQgFILPGVVAVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTS 199
Cdd:cd01584 72 WKPGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 200 KDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLKGrpmappstnvpvawD 279
Cdd:cd01584 151 KDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKA--------------T 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 280 GEKDIWDEAVEY-WKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITgcvpdpkAIQNQAKREGVEKALEyMGL 358
Cdd:cd01584 217 GRAEIADLADEFkDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVS-------KFKEVAEKNGWPLDLR-VGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 359 VgstrmedikidkvflGSCTNSRIEDLRIAANILasvgpEARVAEGVMA----MVVPGSGVVKRQAEEEGLDVLFKRAGF 434
Cdd:cd01584 289 I---------------GSCTNSSYEDMGRAASIA-----KQALAHGLKCksifTITPGSEQIRATIERDGLLQTFRDAGG 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 435 DWREAGCSMCIGL-NPDQLGSGERCA--STSNRNFRDRQGTGGRTH--LVSPAMAVAAALKGRL 493
Cdd:cd01584 349 IVLANACGPCIGQwDRKDIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGTL 412
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
125-707 |
6.57e-27 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 117.42 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 125 GIVH---------VIGGEQGFILPGVVaVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGL 195
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 196 GVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPMappstn 273
Cdd:PTZ00092 264 HVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRSE------ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 274 vpvawdgekdiwdEAVE----YWKTLK----SDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPI-------TGCVPDP- 337
Cdd:PTZ00092 338 -------------EKVEliekYLKANGlfrtYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLsdlkkdfTACLSAPv 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 338 -------KAIQNQAKREGVEKALEYMGLVGSTRMEDIKidkvflgSCTNSRIEDLRIAANILASVGPEA--RVAEGVMAM 408
Cdd:PTZ00092 405 gfkgfgiPEEKHEKKVKFTYKGKEYTLTHGSVVIAAIT-------SCTNTSNPSVMLAAGLLAKKAVEKglKVPPYIKTS 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 409 VVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGlnpdqlGSGER--------------CAS--TSNRNFRdrqgt 472
Cdd:PTZ00092 478 LSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIG------NSGDLdpevseaitnndlvAAAvlSGNRNFE----- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 473 gGRTH-------LVSPAMAVAAALKGRLT-DVRT-----------------LVKTEELKKSTTDAVKkagslPDLLFEEQ 527
Cdd:PTZ00092 547 -GRVHpltranyLASPPLVVAYALAGRVNiDFETeplgsdktgkpvflrdiWPSREEIQALEAKYVK-----PEMFKEVY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 528 VSVPDLPEPKESLKLDSSSGSE--------------DAMAArrQSRRFTSVRGVAVPLRM-ENIDTDMLVPA-------P 585
Cdd:PTZ00092 621 SNITQGNKQWNELQVPKGKLYEwdekstyihnppffQTMEL--EPPPIKSIENAYCLLNLgDSITTDHISPAgniaknsP 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 586 LLKGLTRTGLAKALFNRF----------------------RWDPVTKEETDFI-LNQK--------PWKEAKI--VVSAG 632
Cdd:PTZ00092 699 AAKYLMERGVERKDFNTYgarrgndevmvrgtfanirlinKLCGKVGPNTVHVpTGEKmsiydaaeKYKQEGVplIVLAG 778
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860672246 633 KNFGCGSSREhavWALKD---FGITCVIAPSYGDIFFNNCLQNGVLLVTLSESicETLANYAATG-EEMEVDLEKQEIR 707
Cdd:PTZ00092 779 KEYGSGSSRD---WAAKGpylQGVKAVIAESFERIHRSNLVGMGILPLQFLNG--ENADSLGLTGkEQFSIDLNSGELK 852
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
574-707 |
6.57e-26 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 104.52 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPAPLLKGLTRTGLAKALFNRFrwDPvtkeetDFILNQKPwkeAKIVVsAGKNFGCGSSREHAVWALKDFGI 653
Cdd:PRK00439 9 DNIDTDVIIPARYLNTSDPQELAKHCMEDL--DP------EFAKKVKP---GDIIV-AGKNFGCGSSREHAPIALKAAGV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 654 TCVIAPSYGDIFFNNCLQNGVLLVTlsesiCETLANYAATGEEMEVDLEKQEIR 707
Cdd:PRK00439 77 SAVIAKSFARIFYRNAINIGLPVLE-----CDEAVDKIEDGDEVEVDLETGVIT 125
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
147-494 |
2.10e-23 |
|
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: 106.34 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 147 DSHTSTLGAFGALAFGIGTSEVEHVLATQTIrlrkskSMRI--LV----NGTLGLGVTSKDVILHIIRTIGTAGGTGYVI 220
Cdd:COG1048 210 DSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLIpeVVgvklTGKLPEGVTATDLVLTVTEMLRKKGVVGKFV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 221 EYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPmappstnvpvawdgekdiwDEAVE----Y--- 291
Cdd:COG1048 284 EFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRltGRS-------------------EEQIElveaYaka 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 292 ---WKTLKSDEgAKFDKEVVIQAEDISPTVTWGTSPEDNVPITgcvpdpkaiqnQAKrEGVEKALEYMGLVGSTRMEDIK 368
Cdd:COG1048 345 qglWRDPDAPE-PYYSDVLELDLSTVEPSLAGPKRPQDRIPLS-----------DLK-EAFRAALAAPVGEELDKPVRVE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 369 ID--KVFLG----------SCTNSRIEDLRIAANILA--SVGPEARVAEGVMAMVVPGSGVVKRQAEEEGL-DVL----F 429
Cdd:COG1048 412 VDgeEFELGhgavviaaitSCTNTSNPSVMIAAGLLAkkAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLlPYLealgF 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 430 KRAGFdwreaGCSMCIG----LNP---DQLGSGE-RCAS-TS-NRNFRdrqgtgGRTH-------LVSPAMAVAAALKGR 492
Cdd:COG1048 492 NVVGY-----GCTTCIGnsgpLPPeisEAIEENDlVVAAvLSgNRNFE------GRIHpdvkanfLASPPLVVAYALAGT 560
|
..
gi 1860672246 493 LT 494
Cdd:COG1048 561 VD 562
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
137-493 |
8.43e-23 |
|
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: 102.19 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 137 ILPGVVAVCGDSHTS-TLGafgaLAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVI----LHIIR--- 208
Cdd:cd01581 104 LLPDTVGTGGDSHTRfPIG----ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVnaipYYAIQqgl 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 209 -TIGTAGG----TGYVIEYAGdvVRGLSMEARMTICNMSIESGARAGMV-APDETTFAYLKgrpmappSTNVPVAWDGEK 282
Cdd:cd01581 180 lTVEKKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLE-------SNVVLMKIMIAN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 283 DIWD--------EAVEYW----KTLKSDEGAKFDKEVVIQAEDIsptvtwgtspedNVPITGCVPDPKAIqnqakregve 350
Cdd:cd01581 251 GYDDartllrriIAMEEWlanpPLLEPDADAEYAAVIEIDLDDI------------KEPILACPNDPDDV---------- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 351 KALEYMglvgstrmEDIKIDKVFLGSC-TNsrIEDLRIAANILASVGPEArvaegVMAMVVPGSGVVKRQAEEEGLDVLF 429
Cdd:cd01581 309 KLLSEV--------AGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-----TRLWVAPPTRMDWAILQEEGYYSIF 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 430 KRAGFDWREAGCSMCIGlNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:cd01581 374 GDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
574-710 |
1.74e-22 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 94.47 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPAPLLKGLTRTGLAKALFNRFRWDPVTKEetdfilnqkpwKEAKIVVsAGKNFGCGSSREHAVWALKDFGI 653
Cdd:TIGR02084 8 DNVDTDVIIPARYLNTSDPKELAKHCMEDLDKDFVKKV-----------KEGDIIV-AGENFGCGSSREHAPIAIKASGI 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860672246 654 TCVIAPSYGDIFFNNCLQNGVLLVTLSESicetlANYAATGEEMEVDLEKQEIRCLR 710
Cdd:TIGR02084 76 SCVIAKSFARIFYRNAINIGLPIVESEEA-----VDEIEEGDEVEVDLEKGIIKNLT 127
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
125-491 |
1.21e-21 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 100.65 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 125 GIVH---------VIGGEQGFILPGVVaVCGDSHTSTLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGL 195
Cdd:PLN00070 217 GIVHqvnleylgrVVFNTDGILYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 196 GVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRpmappstn 273
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGR-------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 274 vpvawDGEKDIWDEA--------VEYWKTLKSDegaKFDKEVVIQAEDISPTVTWGTSPEDNVPITGCVPDPKA-IQNQA 344
Cdd:PLN00070 368 -----SDETVAMIEAylrankmfVDYNEPQQER---VYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHScLDNKV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 345 -------KREGVEKALE--YMGLVGSTRMEDIKIDKVflGSCTNSRIEDLRIAANILASVGPE--ARVAEGVMAMVVPGS 413
Cdd:PLN00070 440 gfkgfavPKEAQSKVAKfsFHGQPAELRHGSVVIAAI--TSCTNTSNPSVMLGAGLVAKKACElgLEVKPWIKTSLAPGS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 414 GVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIGlNPDQLgsGERCAS-------------TSNRNFRdrqgtgGRTH--- 477
Cdd:PLN00070 518 GVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG-NSGEL--DESVASaitendivaaavlSGNRNFE------GRVHplt 588
|
410
....*....|....*...
gi 1860672246 478 ----LVSPAMAVAAALKG 491
Cdd:PLN00070 589 ranyLASPPLVVAYALAG 606
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
574-707 |
2.25e-21 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 91.33 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPAPLLKGLTRTGLAKALFNRFrwDPvtkeetDFilnQKPWKEAKIVVsAGKNFGCGSSREHAVWALKDFGI 653
Cdd:TIGR02087 8 DDIDTDEIIPGRYLRTTDPDELASHAMEGI--DP------EF---AKKVRPGDVIV-AGKNFGCGSSREQAALALKAAGI 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1860672246 654 TCVIAPSYGDIFFNNCLQNGVLLVTL-SESICEtlanyaatGEEMEVDLEKQEIR 707
Cdd:TIGR02087 76 AAVIAESFARIFYRNAINIGLPLIEAkTEGIKD--------GDEVTVDLETGEIR 122
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
104-713 |
5.44e-21 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 98.47 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 104 ALEKNV----RRSRIPY-FSLWDTRQ-----------GIVHVIGGEQ-------------GFILPGVVaVCGDSHTSTLG 154
Cdd:PRK12881 141 ALDLNMkiefQRNAERYqFLKWGMQAfdnfrvvppgtGIMHQVNLEYlarvvhtkeddgdTVAYPDTL-VGTDSHTTMIN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 155 AFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVIL---HIIRTIGTAGGtgYViEYAGDVVRGLS 231
Cdd:PRK12881 220 GIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLtvtEMLRKEGVVGK--FV-EFFGEGVASLT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 232 MEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPmappstnvpvawdgEKDIwdEAVE-YWKTLK----SDEGAKFD 304
Cdd:PRK12881 297 LGDRATIANMAPEYGATMGFFPVDEQTLDYLRltGRT--------------EAQI--ALVEaYAKAQGlwgdPKAEPRYT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 305 KEVVIQAEDISPTVTWGTSPEDNVPITGCvpdPKAIQNQAKREGVEKALEYMGLVGST-RMEDIKIDKVFLGSCTNSRIE 383
Cdd:PRK12881 361 RTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFSKPVAENGFAKKAQTSNGvDLPDGAVAIAAITSCTNTSNP 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 384 DLRIAANILASVGPEA--RVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIG--------LNPDQLG 453
Cdd:PRK12881 438 SVLIAAGLLAKKAVERglTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGnsgpltpeIEQAITK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 454 SGERCAS--TSNRNFRdrqgtgGRTH-------LVSPAMAVAAALKGrltDVRTLVKTEELKK----------------S 508
Cdd:PRK12881 518 NDLVAAAvlSGNRNFE------GRIHpnikanfLASPPLVVAYALAG---TVRRDLMTEPLGKgkdgrpvylkdiwpssA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 509 TTDAVKKAGSLPDlLFE---EQVSVPD-----LPEPK--------ESLKL------DSSSGSEDAMAARRQSRrftsvrg 566
Cdd:PRK12881 589 EIDALVAFAVDPE-DFRknyAEVFKGSelwaaIEAPDgplydwdpKSTYIrrppffDFSMGPAASIATVKGAR------- 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 567 vavPLRM--ENIDTDMLVPA-------PLLKGLTRTGLAKALFNRF---RWDPVTKEETDF----ILNQ-KPWKE----- 624
Cdd:PRK12881 661 ---PLAVlgDSITTDHISPAgaikadsPAGKYLKENGVPKADFNSYgsrRGNHEVMMRGTFanvrIKNLmIPGKEggltl 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 625 ---------------------AKIVVSAGKNFGCGSSREhavWALKD---FGITCVIAPSYGDIFFNNCLQNGVLLVTLS 680
Cdd:PRK12881 738 hqpsgevlsiydaamryqaagTPLVVIAGEEYGTGSSRD---WAAKGtrlLGVKAVIAESFERIHRSNLVGMGVLPLQFK 814
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1860672246 681 ESicETLANYAATGEE-MEVDLEKQEI--RC-----LRRRD 713
Cdd:PRK12881 815 GG--DSRQSLGLTGGEtFDIEGLPGEIkpRQdvtlvIHRAD 853
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
638-764 |
1.69e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 87.47 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 638 GSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLANYAATgEEMEVDLEKQEIrclrrrdlqds 717
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPREVREKLAQLKPT-DQVTVDLEQQKI----------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1860672246 718 ddsmVTP-----FNVDPVNRDRLLAGLDDIDMTLSVEKEVSKYEEKRRREWR 764
Cdd:PRK14812 71 ----ISPveeftFEIDSEWKHKLLNSLDDIGITLQYEELIAAYEKQRPAYWQ 118
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
104-492 |
6.87e-20 |
|
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: 92.75 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 104 ALEKNVR----RSRIPYFSLWDTRQ------------GIVHVI-------------GGEQGFILPGVVaVCGDSHTSTLG 154
Cdd:cd01586 57 ALAKNMKlefeRNRERYEFLKWGQKafknlrvvppgtGIIHQVnleylarvvftseEDGDGVAYPDSV-VGTDSHTTMIN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 155 AFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIIRTIGTAGGTGYVIEYAGDVVRGLSMEA 234
Cdd:cd01586 136 GLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVAD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 235 RMTICNMSIESGARAGMVAPDETTfaylkgrpmappstnvpvawdgekdiwdeaveywktlksdegakfdkeVVIQAEDI 314
Cdd:cd01586 216 RATIANMAPEYGATCGFFPVDTQV------------------------------------------------VELDLSTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 315 SPTVTWGTSPEDNVPITGCVpdpkaiqnqakregVEKALEymglvgstrmedikidkvflgSCTNSRIEDLRIAANILAS 394
Cdd:cd01586 248 EPSVSGPKRPQDRVPLHGSV--------------VIAAIT---------------------SCTNTSNPSVMLAAGLLAK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 395 VGPEA--RVAEGVMAMVVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCIG----LNPD-----QLGSGERCASTS- 462
Cdd:cd01586 293 KAVELglKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgpLPEEveeaiKENDLVVAAVLSg 372
|
410 420 430
....*....|....*....|....*....|....*..
gi 1860672246 463 NRNFRdrqgtgGRTH-------LVSPAMAVAAALKGR 492
Cdd:cd01586 373 NRNFE------GRIHplvranyLASPPLVVAYALAGT 403
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
574-707 |
3.39e-16 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 76.77 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVP---APLLKGLtrtglakalfNRFRWDPVTKEETDFILNQKPwkeAKIVVsAGKNFGCGSSREHAVWALKD 650
Cdd:PRK14023 9 DNINTDDILPgkyAPFMVGE----------DRFHNYAFAHLRPEFASTVRP---GDILV-AGRNFGLGSSREYAPEALKM 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860672246 651 FGITCVIAPSYGDIFFNNCLQNGVLLVTlSESICETLANyaatGEEMEVDLEKQEIR 707
Cdd:PRK14023 75 LGIGAIIAKSYARIFYRNLVNLGIPPFE-SEEVVDALED----GDEVELDLETGVLT 126
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
125-493 |
4.34e-16 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 82.92 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 125 GIVHVIGGEqgFILPGVVAVCGDSHTST-LG-AFGAlafGIGTseVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDV 202
Cdd:PRK09238 466 GVIHSWLNR--MLLPDTVGTGGDSHTRFpIGiSFPA---GSGL--VAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 203 IlHII---------RTIGTAGG----TGYVIEYAGdvVRGLSMEARMTICNMSIESGARAGMVA-PDETTFAYLKgrpma 268
Cdd:PRK09238 539 V-HAIpyyaikqglLTVEKKGKknifSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLR----- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 269 ppSTNVPVAWDGEKDIWD--------EAVEYW----KTLKSDEGAKFDKEVVIQAEDIsptvtwgtspedNVPITGCVPD 336
Cdd:PRK09238 611 --SNIVLLKWMIAEGYGDartlerriAAMEEWlanpELLEADADAEYAAVIEIDLAEI------------KEPILACPND 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 337 PKAIqnqakregveKALEYmglVGSTrmediKIDKVFLGSC-TNsrIEDLRIAANILASVGPEArvaeGVMAMVVPGSGV 415
Cdd:PRK09238 677 PDDV----------RLLSE---VAGT-----KIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQL----PTRLWVAPPTKM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860672246 416 VKRQAEEEGLDVLFKRAGFDWREAGCSMCIGlNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRL 493
Cdd:PRK09238 733 DADQLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRI 809
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
613-700 |
1.41e-14 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 69.80 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 613 TDFILNQKPWkeakiVVSAGKNFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESIcetLANYAA 692
Cdd:cd00404 8 TDHISPAGPG-----VVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE---DYLKLH 79
|
....*...
gi 1860672246 693 TGEEMEVD 700
Cdd:cd00404 80 TGDELDIY 87
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
539-703 |
1.87e-14 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 73.74 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 539 SLKLDSSSGSEDAMAARRQSRRFTSVRGVAVPLRmENIDTDMLVPAPLL-----KGLTRTGLAKALFNRFrwdPVTkEET 613
Cdd:PLN00072 44 KPLTTSSGTSSPTISDSAESTSSTTFHGLCFVVG-DNIDTDQIIPAEYLtlvpsKPDEYEKLGSYALIGL---PAF-YKT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 614 DFILNQKPWKEAKIVVsAGKNFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSES-ICETLanyaA 692
Cdd:PLN00072 119 RFVEPGEMKTKYSIII-GGENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGEVYPLESEVrICEEC----K 193
|
170
....*....|.
gi 1860672246 693 TGEEMEVDLEK 703
Cdd:PLN00072 194 TGDVVTVELGN 204
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
574-707 |
6.72e-14 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 70.13 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPAPLLKGLTRTGLAKALFNrfrwdpvtKEETDFILNQKpwkEAKIVVsAGKNFGCGSSREHAVWALKDFGI 653
Cdd:NF040625 13 DNIDTDVIIPGRYLRTFNPDDLASHVME--------GERPDFTKNVQ---KGDIIV-AGWNFGCGSSREQAPVAIKHAGV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1860672246 654 TCVIAPSYGDIFFNNCLQNGVLLVTlsesicetlANYAAT-GEEMEVDLEKQEIR 707
Cdd:NF040625 81 SAIIAKSFARIFYRNAINIGLPVIV---------ADIEADdGDILSIDLEKGIIK 126
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
147-494 |
1.80e-13 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 74.39 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 147 DSHTSTLGAFGALAFGIGTSEVEHVLATQTIrlrkskSMRI-------LVnGTLGLGVTSKDVILHI---IRTIGTAGGt 216
Cdd:PRK09277 212 DSHTTMINGLGVLGWGVGGIEAEAAMLGQPS------SMLIpevvgvkLT-GKLPEGVTATDLVLTVtemLRKKGVVGK- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 217 gYViEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPmappstnvpvawdgEKDIwdEAVE-YWK 293
Cdd:PRK09277 284 -FV-EFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRD--------------EEQV--ALVEaYAK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 294 T----LKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGCvpdPKAIQNQAKREGVEKALEYMGLVGSTRMEDiki 369
Cdd:PRK09277 346 AqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDV---KEAFAKSAELGVQGFGLDEAEEGEDYELPD--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 370 dkvflG--------SCTNSRIEDLRIAANILASVGPEA--RVAEGVMAMVVPGSGVVKRQAEEEG----LDVL-FKRAGF 434
Cdd:PRK09277 420 -----GavviaaitSCTNTSNPSVMIAAGLLAKKAVEKglKVKPWVKTSLAPGSKVVTDYLEKAGllpyLEALgFNLVGY 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 435 dwreaGCSMCIG----LNPD--------------QLgSGercastsNRNFRdrqgtgGRTH-------LVSPAMAVAAAL 489
Cdd:PRK09277 495 -----GCTTCIGnsgpLPPEiekaindndlvvtaVL-SG-------NRNFE------GRIHplvkanyLASPPLVVAYAL 555
|
....*
gi 1860672246 490 KGRLT 494
Cdd:PRK09277 556 AGTVD 560
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
137-511 |
1.06e-12 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 71.88 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 137 ILPGVVAVCGDSHTS-TLGafgaLAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHI--------I 207
Cdd:PLN00094 550 LLPDTVGTGGDSHTRfPIG----ISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqdgL 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 208 RTIGTAGGT----GYVIEYAGdvVRGLSMEARMTICNMSIESGARAGMVAPDETTFA-YLKgrpmappSTNVPVAWDGEK 282
Cdd:PLN00094 626 LTVEKKGKKnvfsGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIeYLN-------SNVVMLKWMIAE 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 283 DIWDE--------AVEYW----KTLKSDEGAKFDKEVVIQAEDISPTVTwgTSPEDnvpitgcvPDPKAIQNQakregve 350
Cdd:PLN00094 697 GYGDRrtlerriaRMQQWladpELLEADPDAEYAAVIEIDMDEIKEPIL--CAPND--------PDDARLLSE------- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 351 kaleymgLVGStrmediKIDKVFLGSC-TNsrIEDLRIAANILASVGPEARVAegvmAMVVPGSGVVKRQAEEEGLDVLF 429
Cdd:PLN00094 760 -------VTGD------KIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTR----LWVAPPTKMDEAQLKAEGYYSTF 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 430 KRAGFDWREAGCSMCIGlNPDQLGSGERCASTSNRNFRDRQGTGGRTHLVSPAMAVAAALKGRLTDVRTLVK-TEELKKS 508
Cdd:PLN00094 821 GTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEYLSyMEKLDAT 899
|
...
gi 1860672246 509 TTD 511
Cdd:PLN00094 900 ASD 902
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
623-697 |
3.13e-09 |
|
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238837 [Multi-domain] Cd Length: 129 Bit Score: 55.76 E-value: 3.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860672246 623 KEAKIVVSaGKNFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESICETLANYAATGEEM 697
Cdd:cd01674 44 KQGDILVS-GFNFGTGSSREQAATALLAKGIPLVVSGSFGNIFSRNSINNALLSIELPFLVQKLREAFANESKEL 117
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
574-701 |
5.76e-08 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 51.67 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 574 ENIDTDMLVPA-----PLLKGLTRtgLAKALFNRFrwDPVTKEETdfilnqkpwKEAKI-VVSAGKNFGCGSSREHAVWA 647
Cdd:cd01579 4 DNITTDHIMPAgakvlPLRSNIPA--ISEFVFHRV--DPTFAERA---------KAAGPgFIVGGENYGQGSSREHAALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1860672246 648 LKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSEsicETLANYAATGEEMEVDL 701
Cdd:cd01579 71 PMYLGVRAVLAKSFARIHRANLINFGILPLTFAD---EDDYDRFEQGDQLELPL 121
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
143-494 |
2.62e-07 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 54.25 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 143 AVCG------DSHTStLGAFGALAFGIGTSEVEHVLATQTIRLRKSKSMRILVNGTLGLGVTSKDVILHIirtIGTAGGT 216
Cdd:PRK11413 139 AGGGkmilgsDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAI---IGAVFKN 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 217 GY----VIEYAGDVVRGLSMEARMTICNMSIESGARAGMVAPDETTFAYLK--GRPmappstnvpvawdgekdiwdeavE 290
Cdd:PRK11413 215 GYvknkVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRG-----------------------Q 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 291 YWKTLKSDEGAKFDKEVVIQAEDISPTVTWGTSPEDNVPITGCVPDPKAIQNQAKREGVEKALEYMGLVGSTRMED--IK 368
Cdd:PRK11413 272 DYCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLDKIENgrLK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 369 IDKVFLGSCTNSRIEDLRIAANIL--ASVGPEArvaegvMAM-VVPGSGVVKRQAEEEGLDVLFKRAGFDWREAGCSMCI 445
Cdd:PRK11413 352 VQQGIIAGCSGGNYENVIAAANALrgQSCGNDT------FSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCF 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860672246 446 GLNpDQLGSGERCASTSNRNFRDRQGTG-GRTHLVSPAM------AVAAALKGRLT 494
Cdd:PRK11413 426 GAG-DTPANNGLSIRHTTRNFPNREGSKpANGQMSAVALmdarsiAATAANGGYLT 480
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
605-701 |
6.85e-04 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 40.91 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860672246 605 WDPVTKEETDFILNQKPWkeakiVVSAGKNFGCGSSREHAVWALKDFGITCVIAPSYGDIFFNNCLQNGVLLVTLSESic 684
Cdd:cd01578 54 YGPVPDTARDYKAHGIKW-----VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP-- 126
|
90
....*....|....*..
gi 1860672246 685 etlANYAATGEEMEVDL 701
Cdd:cd01578 127 ---ADYDKIHPDDKVDI 140
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
622-675 |
7.45e-04 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 41.11 E-value: 7.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860672246 622 WKEAKI--VVSAGKNFGCGSSREhavWALKD---FGITCVIAPSYGDIFFNNCLQNGVL 675
Cdd:cd01580 91 YKEEGVplVILAGKEYGSGSSRD---WAAKGpflLGVKAVIAESFERIHRSNLVGMGIL 146
|
|
| |
