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Conserved domains on  [gi|226735976|sp|B2GCB8|]
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RecName: Full=3-isopropylmalate dehydratase large subunit; AltName: Full=Alpha-IPM isomerase; Short=IPMI; AltName: Full=Isopropylmalate isomerase

Protein Classification

3-isopropylmalate dehydratase large subunit( domain architecture ID 10012433)

3-isopropylmalate dehydratase large subunit catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate

EC:  4.2.1.33
Gene Symbol:  leuC

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05478 PRK05478
3-isopropylmalate dehydratase large subunit;
1-461 0e+00

3-isopropylmalate dehydratase large subunit;


:

Pssm-ID: 235490  Cd Length: 466  Bit Score: 856.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:PRK05478   1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPT----TDRDLPIAD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK05478  77 PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VT 310
Cdd:PRK05478 237 ETTFEYLKGRPFAPKgeDWDKAVAYWKTLKSD-EDAvFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDpedfadpVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 311 DKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIF 390
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIF 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 391 TDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFY 461
Cdd:PRK05478 396 IEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
 
Name Accession Description Interval E-value
PRK05478 PRK05478
3-isopropylmalate dehydratase large subunit;
1-461 0e+00

3-isopropylmalate dehydratase large subunit;


Pssm-ID: 235490  Cd Length: 466  Bit Score: 856.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:PRK05478   1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPT----TDRDLPIAD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK05478  77 PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VT 310
Cdd:PRK05478 237 ETTFEYLKGRPFAPKgeDWDKAVAYWKTLKSD-EDAvFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDpedfadpVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 311 DKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIF 390
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIF 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 391 TDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFY 461
Cdd:PRK05478 396 IEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
LeuC COG0065
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ...
1-460 0e+00

Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439835  Cd Length: 417  Bit Score: 666.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIA-GKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPTAptpvtsvesv 78
Cdd:COG0065    1 MGMTLAEKILARHAGReVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  79 mDQISKLQITTLQKNCRDFGVELADIGDKdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:COG0065   71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:COG0065  148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDkniera 317
Cdd:COG0065  228 PDETTFEYLKGRPFAP---------WRTLKSD-EDAvYDKEVEIDASDLEPQVAWPHSPDNVVP-------VSE------ 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 318 ydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:COG0065  285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226735976 398 RDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:COG0065  354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
leuC TIGR00170
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ...
1-460 0e+00

3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272940  Cd Length: 465  Bit Score: 656.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:TIGR00170   1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPT----QNRDFNIKD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR00170  77 EVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR00170 157 TLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VTD 311
Cdd:TIGR00170 237 ETTFEYCKGRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDpesfadpVDK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:TIGR00170 317 ASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFI 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226735976  392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
Aconitase pfam00330
Aconitase family (aconitate hydratase);
7-452 0e+00

Aconitase family (aconitate hydratase);


Pssm-ID: 459764  Cd Length: 460  Bit Score: 611.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    7 DKVWDKHVIAGKKGDpqLLYV-DLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAP----TPVTSVESVMDQ 81
Cdd:pfam00330   1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   82 IS--KLQITTLQKNCRDFGVELADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST 159
Cdd:pfam00330  79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  160 QTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINP 239
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  240 DQKTFDYLR--GRERVPK--DFDKAVEyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-----AV 309
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgeAYDKAVA-WKTLASD-PGAeYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  310 TDKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAAEKI 384
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226735976  385 GLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
IPMI cd01583
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ...
29-454 0e+00

3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.


Pssm-ID: 153133  Cd Length: 382  Bit Score: 551.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  29 LHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPTAptpvtsvesvmDQISKLQITTLQKNCRDFGVELADIGDk 107
Cdd:cd01583    1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-----------DIKAAEQVKTLRKFAKEFGINFFDVGR- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 dQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01583   69 -QGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvpkdfdkavEYWKQF 267
Cdd:cd01583  148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---------AYWKEL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01583  219 KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVP-------VSE-----------------VEGIKIDQVFIGSCTNGRL 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01583  275 EDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNF 354
                        410       420
                 ....*....|....*....|....*...
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGINGHF 454
Cdd:cd01583  355 KGRMGsPGARIYLASPATAAASAITGEI 382
HacA_Meth NF040615
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
4-453 1.78e-80

homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens


Pssm-ID: 468587  Cd Length: 419  Bit Score: 255.45  E-value: 1.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   4 TLFDKVWDKHViaGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPtaPTPVTSVEsvmd 80
Cdd:NF040615   2 TLAEKILSKKL--GKEvyaGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--ANTVKAAN---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 qisklqittLQKNCRDFgVELADIGD---KDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVF 157
Cdd:NF040615  74 ---------MQKITREF-VKEQGIKNfylGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 158 STQTLWQVKPKNLGVHVTGhLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMI 237
Cdd:NF040615 144 ATGKTWIKVPKTIRVNIVG-KNENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGII 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 238 NPDQKTFDYLRgRERVPkdfDKAVEYWKQFKTDSPD---AYDWIIELDVSDLAPYVSwgttpsmsvpygakLPAVTDkni 314
Cdd:NF040615 223 EADEITYEYLR-KEGVS---EEEIAELKKNRITVNEkeeNYYKEIEIDITDMEEQVA--------------CPHHPD--- 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 315 eraydymDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAG 394
Cdd:NF040615 282 -------NVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 395 CEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGH 453
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
 
Name Accession Description Interval E-value
PRK05478 PRK05478
3-isopropylmalate dehydratase large subunit;
1-461 0e+00

3-isopropylmalate dehydratase large subunit;


Pssm-ID: 235490  Cd Length: 466  Bit Score: 856.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:PRK05478   1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPT----TDRDLPIAD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK05478  77 PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK05478 157 TLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VT 310
Cdd:PRK05478 237 ETTFEYLKGRPFAPKgeDWDKAVAYWKTLKSD-EDAvFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDpedfadpVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 311 DKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIF 390
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIF 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976 391 TDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFY 461
Cdd:PRK05478 396 IEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
PRK12466 PRK12466
3-isopropylmalate dehydratase large subunit;
1-464 0e+00

3-isopropylmalate dehydratase large subunit;


Pssm-ID: 183543  Cd Length: 471  Bit Score: 721.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAPTPVTSVEsvmD 80
Cdd:PRK12466   2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGRDRGIT---D 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:PRK12466  79 PGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-------AVTD 311
Cdd:PRK12466 239 ETTFDYLRGRPRAPKgaLWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPdpaaeadPARR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:PRK12466 319 AAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFI 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKFYQGE 464
Cdd:PRK12466 399 AAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQAG 471
LeuC COG0065
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ...
1-460 0e+00

Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439835  Cd Length: 417  Bit Score: 666.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHVIA-GKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPTAptpvtsvesv 78
Cdd:COG0065    1 MGMTLAEKILARHAGReVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  79 mDQISKLQITTLQKNCRDFGVELADIGDKdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:COG0065   71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:COG0065  148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDkniera 317
Cdd:COG0065  228 PDETTFEYLKGRPFAP---------WRTLKSD-EDAvYDKEVEIDASDLEPQVAWPHSPDNVVP-------VSE------ 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 318 ydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:COG0065  285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226735976 398 RDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:COG0065  354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
leuC TIGR00170
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ...
1-460 0e+00

3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272940  Cd Length: 465  Bit Score: 656.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    1 MAKTLFDKVWDKHVIAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTaptpVTSVESVMD 80
Cdd:TIGR00170   1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPT----QNRDFNIKD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   81 QISKLQITTLQKNCRDFGVELADIGDKDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR00170  77 EVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR00170 157 TLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  241 QKTFDYLRGRERVPK--DFDKAVEYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLPA-------VTD 311
Cdd:TIGR00170 237 ETTFEYCKGRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDpesfadpVDK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  312 KNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:TIGR00170 317 ASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFI 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226735976  392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
Aconitase pfam00330
Aconitase family (aconitate hydratase);
7-452 0e+00

Aconitase family (aconitate hydratase);


Pssm-ID: 459764  Cd Length: 460  Bit Score: 611.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    7 DKVWDKHVIAGKKGDpqLLYV-DLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAP----TPVTSVESVMDQ 81
Cdd:pfam00330   1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   82 IS--KLQITTLQKNCRDFGVELADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST 159
Cdd:pfam00330  79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  160 QTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINP 239
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  240 DQKTFDYLR--GRERVPK--DFDKAVEyWKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPYGAKLP-----AV 309
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgeAYDKAVA-WKTLASD-PGAeYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  310 TDKNIERAYDYMDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAAEKI 384
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226735976  385 GLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
IPMI cd01583
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ...
29-454 0e+00

3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.


Pssm-ID: 153133  Cd Length: 382  Bit Score: 551.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  29 LHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPTAptpvtsvesvmDQISKLQITTLQKNCRDFGVELADIGDk 107
Cdd:cd01583    1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-----------DIKAAEQVKTLRKFAKEFGINFFDVGR- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 dQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01583   69 -QGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvpkdfdkavEYWKQF 267
Cdd:cd01583  148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK---------AYWKEL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01583  219 KSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVP-------VSE-----------------VEGIKIDQVFIGSCTNGRL 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01583  275 EDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNF 354
                        410       420
                 ....*....|....*....|....*...
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGINGHF 454
Cdd:cd01583  355 KGRMGsPGARIYLASPATAAASAITGEI 382
PRK00402 PRK00402
3-isopropylmalate dehydratase large subunit; Reviewed
1-460 8.27e-125

3-isopropylmalate dehydratase large subunit; Reviewed


Pssm-ID: 234748  Cd Length: 418  Bit Score: 369.12  E-value: 8.27e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   1 MAKTLFDKVWDKHviAGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAG-RKLRRPDKTFATIDHNVPtAPTpvtsve 76
Cdd:PRK00402   1 MGMTLAEKILARH--SGRDvspGDIVEAKVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVP-AKD------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  77 svmdqiskLQITTLQKNCRDFGVELA-----DIGDkdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTS 151
Cdd:PRK00402  72 --------IKSAEQQKILREFAKEQGipnffDVGE---GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGST 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 152 EIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGG 231
Cdd:PRK00402 141 DMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAG 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 232 AKVAMINPDQKTFDYLRGRERVPkdfdkaveyWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTD 311
Cdd:PRK00402 221 AKAGIFAPDEKTLEYLKERAGRD---------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKP-------VSE 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 312 knieraydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFT 391
Cdd:PRK00402 285 -----------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFV 347
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 392 DAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:PRK00402 348 DAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
hacA_fam TIGR01343
homoaconitate hydratase family protein; This model represents a subfamily of proteins ...
4-458 1.87e-102

homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.


Pssm-ID: 273563  Cd Length: 412  Bit Score: 312.07  E-value: 1.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    4 TLFDKVWDKHviAGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPtAPTpvtsVESVM 79
Cdd:TIGR01343   1 TIAEKILSKK--SGKEvyaGDLIEAEIDLAMVHDITAPLAIKTLEEYGIdKVWNPEKIVIVFDHQVP-ADT----IKAAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   80 DQIsklqitTLQKNCRDFGVE-LADIGdkdQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFS 158
Cdd:TIGR01343  74 MQK------LAREFVKKQGIKyFYDVG---EGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  159 TQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMIN 238
Cdd:TIGR01343 145 TGKTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  239 PDQKTFDYLRGRERVPkdfdkaveyWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSmsvpygaklpavtdkNIERAY 318
Cdd:TIGR01343 225 PDEKTIQYLKERRKEP---------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVD---------------NVKPVS 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  319 DymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWR 398
Cdd:TIGR01343 281 E---------VEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVS 351
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226735976  399 DPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVR 458
Cdd:TIGR01343 352 TPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
IPMI_arch TIGR02086
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ...
3-458 2.25e-91

3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.


Pssm-ID: 273960  Cd Length: 413  Bit Score: 283.58  E-value: 2.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976    3 KTLFDKVWDKHV-IAGKKGDPQLLYVDLHLIHEVTSPQPFDGLRQAGR-KLRRPDKTFATIDHNVPtAPTpvtsVESvmd 80
Cdd:TIGR02086   1 MTLAEKILSEKVgRPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVP-PPT----VEA--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   81 qiSKLQiTTLQKNCRDFGVELADIGDkdqGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQ 160
Cdd:TIGR02086  73 --AEMQ-KEIREFAKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  161 TLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPD 240
Cdd:TIGR02086 147 KTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  241 QKTFDYLRGRERvpkdfdkavEYWKQFKTDSPDAYDWIIELDVSDLAPYVSwgttpsmsVPygaklpavtdknierayDY 320
Cdd:TIGR02086 227 EETYEYLKKRRG---------LEFRILVPDPGANYYKEIEIDLSDLEPQVA--------VP-----------------HS 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  321 MD-LEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRD 399
Cdd:TIGR02086 273 VDnVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICP 352
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  400 PGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVR 458
Cdd:TIGR02086 353 PGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITDPE 412
HacA_Meth NF040615
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
4-453 1.78e-80

homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens


Pssm-ID: 468587  Cd Length: 419  Bit Score: 255.45  E-value: 1.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976   4 TLFDKVWDKHViaGKK---GDPQLLYVDLHLIHEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPtaPTPVTSVEsvmd 80
Cdd:NF040615   2 TLAEKILSKKL--GKEvyaGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--ANTVKAAN---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  81 qisklqittLQKNCRDFgVELADIGD---KDQGIVHVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVF 157
Cdd:NF040615  74 ---------MQKITREF-VKEQGIKNfylGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 158 STQTLWQVKPKNLGVHVTGhLAPGIFAKDIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMI 237
Cdd:NF040615 144 ATGKTWIKVPKTIRVNIVG-KNENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGII 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 238 NPDQKTFDYLRgRERVPkdfDKAVEYWKQFKTDSPD---AYDWIIELDVSDLAPYVSwgttpsmsvpygakLPAVTDkni 314
Cdd:NF040615 223 EADEITYEYLR-KEGVS---EEEIAELKKNRITVNEkeeNYYKEIEIDITDMEEQVA--------------CPHHPD--- 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 315 eraydymDLEPEMPVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAG 394
Cdd:NF040615 282 -------NVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 395 CEWRDPGCSACLAMNPDKVPAGMHCASTTNRNFEGRQG-PGTRTHMASPAMVAAAGINGH 453
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
Aconitase cd01351
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ...
108-452 5.20e-65

Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.


Pssm-ID: 153129 [Multi-domain]  Cd Length: 389  Bit Score: 214.28  E-value: 5.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 108 DQGIVHVIGPQLGLtQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDI 187
Cdd:cd01351   68 GVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 188 VMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvPKDFDKAVEYWKQF 267
Cdd:cd01351  147 VLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR-PLLKNLWLAFPEEL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 268 KTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRL 347
Cdd:cd01351  226 LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVS-------VSE-----------------VEGTKIDQVLIGSCTNNRY 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTNRNF 427
Cdd:cd01351  282 SDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNF 361
                        330       340
                 ....*....|....*....|....*.
gi 226735976 428 EGRQG-PGTRTHMASPAMVAAAGING 452
Cdd:cd01351  362 PGRLGtYERHVYLASPELAAATAIAG 387
PRK07229 PRK07229
aconitate hydratase; Validated
110-460 8.47e-53

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 188.05  E-value: 8.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGLTQ---PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQtLWQVK-PKNLGVHVTGHLAPGIFAK 185
Cdd:PRK07229  98 GICH----QVHLERfafPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGG-PYYLKmPKVVGVKLTGKLPPWVSAK 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 186 DIVMALIAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRERVpkdfdkavey 263
Cdd:PRK07229 173 DVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGREDD---------- 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 264 WKQFKTDsPDA-YDWIIELDVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSC 342
Cdd:PRK07229 243 WVELLAD-PDAeYDEVIEIDLSELEPLIAGPHSPDNVVP-------VSE-----------------VAGIKVDQVLIGSC 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 343 TNGRLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMnpDKVPA-GMHCAS 421
Cdd:PRK07229 298 TNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM--GQAPAtGNVSLR 375
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 226735976 422 TTNRNFEGRQG-PGTRTHMASPAMVAAAGINGHFVDVRKF 460
Cdd:PRK07229 376 TFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRTL 415
AcnA_Bact cd01585
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ...
124-454 1.08e-49

Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.


Pssm-ID: 153135  Cd Length: 380  Bit Score: 173.79  E-value: 1.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 124 PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGY 203
Cdd:cd01585   82 PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGK 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 204 ALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRErvpkdfdkavEYWKQFKTDSPDAYDWIIEL 281
Cdd:cd01585  162 IFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE----------DDWVELAADADAEYDEEIEI 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 282 DVSDLAPYVSWGTTPSMSVPygaklpaVTDknieraydymdlepempVQDIPINWVFIGSCTNGRLSDLKEAARVMKGKH 361
Cdd:cd01585  232 DLSELEPLIARPHSPDNVVP-------VRE-----------------VAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRR 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 362 LAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNpDKVPAGMHCASTTNRNFEGRQG-PGTRTHMA 440
Cdd:cd01585  288 VHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG-QAPPTGGVSVRTFNRNFEGRSGtKDDLVYLA 366
                        330
                 ....*....|....
gi 226735976 441 SPAMVAAAGINGHF 454
Cdd:cd01585  367 SPEVAAAAALTGVI 380
Homoaconitase cd01582
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ...
33-452 5.36e-46

Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.


Pssm-ID: 153132 [Multi-domain]  Cd Length: 363  Bit Score: 163.55  E-value: 5.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  33 HEVTSPQPFDGLRQAGRKLRRPDKTFATIDHNVPTAPtpvtsvESVMDQISKLQittlqKNCRDFGVELADIGdkdQGIV 112
Cdd:cd01582    5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKS------EKNLKKYKNIE-----SFAKKHGIDFYPAG---RGIG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 113 HVIGPQLGLTQPGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFST-QTLWQVkPKNLGVHVTGHLAPGIFAKDIVMAL 191
Cdd:cd01582   71 HQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQI-PPVAKVELKGQLPKGVTGKDVIVAL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 192 IAKYGTNFAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMinpdqktfdylrgrervpkdfdkaveywkqFKTDS 271
Cdd:cd01582  150 CGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGL------------------------------FPTDA 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 272 PDaydwiIELDVSDLAPYVSWGTTPSMSVPYGaklpavtdknieraydymdlepEMPVQDIPINWVFIGSCTNGRLSDLK 351
Cdd:cd01582  200 KH-----LILDLSTLSPYVSGPNSVKVSTPLK----------------------ELEAQNIKINKAYLVSCTNSRASDIA 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 352 EAARVMKGK-------HLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNPDKVPAGMHCASTTN 424
Cdd:cd01582  253 AAADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATN 332
                        410       420
                 ....*....|....*....|....*....
gi 226735976 425 RNFEGRQG-PGTRTHMASPAMVAAAGING 452
Cdd:cd01582  333 RNFKGRMGsTEALAYLASPAVVAASAISG 361
AcnA_Mitochondrial cd01584
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ...
110-452 2.07e-38

Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 153134  Cd Length: 412  Bit Score: 144.12  E-value: 2.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGLTQ---PGKLIVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTlWQVK-PKNLGVHVTGHLAPGIFAK 185
Cdd:cd01584   77 GIIH----QIVLENyafPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELKcPKVIGVKLTGKLSGWTSPK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 186 DIVMA----LIAKYGTnfaeGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRERVPKDFDK 259
Cdd:cd01584  152 DVILKvagiLTVKGGT----GAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAEIADLADE 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 260 AveYWKQFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVPYgAKLPAVTDKNieraydymdlepEMPVQdipINWVFI 339
Cdd:cd01584  228 F--KDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPV-SKFKEVAEKN------------GWPLD---LRVGLI 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 340 GSCTNGRLSDLKEAARVMK---GKHLAPGVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAM-NPDKVPA 415
Cdd:cd01584  290 GSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwDRKDIKK 369
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 226735976 416 GMHCASTT--NRNFEGRQ--GPGTRTHMASPAMVAAAGING 452
Cdd:cd01584  370 GEKNTIVTsyNRNFTGRNdaNPATHAFVASPEIVTAMAIAG 410
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
110-452 4.59e-29

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 120.89  E-value: 4.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVH---------VIGPQLGLTQPGKLiVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAP 180
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSE 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 181 GIFAKDIVMALiakygTNFAE-----GYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERVPK 255
Cdd:PTZ00092 264 HVTATDLVLTV-----TSMLRkrgvvGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEE 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 256 DFDKAVEYWKQ---FKTDSPD-AYDWIIELDVSDLAPYVSWGTTP---------------SMSVPYGAKLPAVTDKNIER 316
Cdd:PTZ00092 339 KVELIEKYLKAnglFRTYAEQiEYSDVLELDLSTVVPSVAGPKRPhdrvplsdlkkdftaCLSAPVGFKGFGIPEEKHEK 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 317 --AYDYMDLEPEMPVQDIPInwVFIGSCTNGRLSDLKEAA------RVMKGKHLAPGVQAWVVPGSRGVQKAAEKIGLDK 388
Cdd:PTZ00092 419 kvKFTYKGKEYTLTHGSVVI--AAITSCTNTSNPSVMLAAgllakkAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLK 496
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 389 I-----FTDAGCewrdpGCSACLAMNPDKVPAGMHCAS----------TTNRNFEGRQGPGTR-THMASPAMVAAAGING 452
Cdd:PTZ00092 497 YleklgFYTAGY-----GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAG 571
acnA PRK12881
aconitate hydratase AcnA;
132-458 9.59e-29

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 120.04  E-value: 9.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 132 DSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALiakygTNF--AEGYA---LE 206
Cdd:PRK12881 212 DSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTV-----TEMlrKEGVVgkfVE 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 207 YYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLRGRERvPKDFDKAVE-YWKQ----FKTDSPDAYDWIIEL 281
Cdd:PRK12881 287 FFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGR-TEAQIALVEaYAKAqglwGDPKAEPRYTRTLEL 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 282 DVSDLAPYVSWGTTPSMSVPYGAKLPAVTDKNIERAYDYMDLEP-------EMPVQDIPInwVFIGSCTNgrLSD--LKE 352
Cdd:PRK12881 366 DLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKaqtsngvDLPDGAVAI--AAITSCTN--TSNpsVLI 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 353 AARVMKGKHLAPG--VQAWV----VPGSRGVQKAAEKIG----LDKI-FTDAGCewrdpGCSACLAMNPDKVPA------ 415
Cdd:PRK12881 442 AAGLLAKKAVERGltVKPWVktslAPGSKVVTEYLERAGllpyLEKLgFGIVGY-----GCTTCIGNSGPLTPEieqait 516
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 226735976 416 --GMHCAS--TTNRNFEGRQGPGTRTH-MASPAMVAAAGINGhfvDVR 458
Cdd:PRK12881 517 knDLVAAAvlSGNRNFEGRIHPNIKANfLASPPLVVAYALAG---TVR 561
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
110-449 1.40e-26

Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 113.28  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHvigpQLGL----------TQPGKLIVCG------DSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVH 173
Cdd:COG1048  176 GIVH----QVNLeylafvvwtrEEDGETVAYPdtlvgtDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVK 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 174 VTGHLAPGIFAKDIVMA----LIAKYGTnfaeGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR- 248
Cdd:COG1048  252 LTGKLPEGVTATDLVLTvtemLRKKGVV----GKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRl 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 249 -GRE----RVPKDFDKAVEYWKQFKTDSPDaYDWIIELDVSDLAPYVSWGTTPSMSVPYG-------AKLPAVTDKNIER 316
Cdd:COG1048  328 tGRSeeqiELVEAYAKAQGLWRDPDAPEPY-YSDVLELDLSTVEPSLAGPKRPQDRIPLSdlkeafrAALAAPVGEELDK 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 317 AYDYMDLEPEMPVQDipiNWVF---IGSCTN------GRLSDLkeAAR--VMKGKhlapGVQAWV----VPGSRGVQKAA 381
Cdd:COG1048  407 PVRVEVDGEEFELGH---GAVViaaITSCTNtsnpsvMIAAGL--LAKkaVEKGL----KVKPWVktslAPGSKVVTDYL 477
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 382 EKIGL----DKI-FTDAGCewrdpGCSACL--------AMNPDKVPAGMHCASTT--NRNFEGRQGPGTRT-HMASPAMV 445
Cdd:COG1048  478 ERAGLlpylEALgFNVVGY-----GCTTCIgnsgplppEISEAIEENDLVVAAVLsgNRNFEGRIHPDVKAnFLASPPLV 552

                 ....*..
gi 226735976 446 AA---AG 449
Cdd:COG1048  553 VAyalAG 559
AcnB cd01581
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ...
110-453 6.85e-24

Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.


Pssm-ID: 153131  Cd Length: 436  Bit Score: 103.73  E-value: 6.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVHVIGPQLGLtqPGKLIVCGDSHTSTHGGLgalSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVM 189
Cdd:cd01581   94 GVIHSWLNRMLL--PDTVGTGGDSHTRFPIGI---SFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVN 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 190 ALIA------------KYGTNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTF-DYLRG-----RE 251
Cdd:cd01581  169 AIPYyaiqqglltvekKGKKNVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLESnvvlmKI 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 252 RVPKDFD---------KAVEYW----KQFKTDSPDAYDWIIELDVSDLapyvswgttpsmsvpygaKLPAVTDKNieray 318
Cdd:cd01581  247 MIANGYDdartllrriIAMEEWlanpPLLEPDADAEYAAVIEIDLDDI------------------KEPILACPN----- 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 319 DYMDLEPEMPVQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPgVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEW 397
Cdd:cd01581  304 DPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGART 380
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226735976 398 RDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:cd01581  381 EMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGR 435
PRK09277 PRK09277
aconitate hydratase AcnA;
132-452 1.06e-23

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 104.44  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 132 DSHTsTH-GGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALiakygTNF--AEGYA---L 205
Cdd:PRK09277 212 DSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTV-----TEMlrKKGVVgkfV 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 206 EYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GR--ERVpkdfdKAVE-YWKQ---FKTDSPDA-YD 276
Cdd:PRK09277 286 EFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRdeEQV-----ALVEaYAKAqglWRDPLEEPvYT 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 277 WIIELDVSDLapyvswgtTPSMS--------VPYG------AKLPAVTDKNIERAYDYMDLEPEMPVQDIPInwVFIGSC 342
Cdd:PRK09277 361 DVLELDLSTV--------EPSLAgpkrpqdrIPLSdvkeafAKSAELGVQGFGLDEAEEGEDYELPDGAVVI--AAITSC 430
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 343 TN----------GRLsdlkeaAR--VMKGkhLApgVQAWV----VPGSRGVQKAAEKIG----LDKI-FTDAGCewrdpG 401
Cdd:PRK09277 431 TNtsnpsvmiaaGLL------AKkaVEKG--LK--VKPWVktslAPGSKVVTDYLEKAGllpyLEALgFNLVGY-----G 495
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226735976 402 CSACLAMN---PDKVPA-----GMHCAS--TTNRNFEGRQGPGTRT-HMASPAMVAAAGING 452
Cdd:PRK09277 496 CTTCIGNSgplPPEIEKaindnDLVVTAvlSGNRNFEGRIHPLVKAnYLASPPLVVAYALAG 557
PLN00070 PLN00070
aconitate hydratase
110-452 2.83e-22

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 100.26  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 110 GIVH---------VIGPQLGLTQPGKLiVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAP 180
Cdd:PLN00070 217 GIVHqvnleylgrVVFNTDGILYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 181 GIFAKDIVMA---LIAKYGTnfaEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRE---- 251
Cdd:PLN00070 296 GVTATDLVLTvtqMLRKHGV---VGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRSdetv 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 252 -------RVPKDFdkaVEYwkqFKTDSPDAYDWIIELDVSDLAPYVSWGTTPSMSVP---------------YGAKLPAV 309
Cdd:PLN00070 373 amieaylRANKMF---VDY---NEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPlkemkadwhscldnkVGFKGFAV 446
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 310 TDKNIERA--YDYMDLEPEMPVQDIPInwVFIGSCTN-GRLSDLKEAARVMK-----GKHLAPGVQAWVVPGSRGVQKAA 381
Cdd:PLN00070 447 PKEAQSKVakFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYL 524
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 382 EKIGLDKIFTDAGCEWRDPGCSACLA-------------MNPDKVPAGMhcaSTTNRNFEGRQGPGTR-THMASPAMVAA 447
Cdd:PLN00070 525 LKSGLQKYLNQQGFHIVGYGCTTCIGnsgeldesvasaiTENDIVAAAV---LSGNRNFEGRVHPLTRaNYLASPPLVVA 601

                 ....*
gi 226735976 448 AGING 452
Cdd:PLN00070 602 YALAG 606
AcnA_IRP cd01586
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ...
128-452 3.78e-19

Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.


Pssm-ID: 153136  Cd Length: 404  Bit Score: 89.29  E-value: 3.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 128 IVCGDSHTSTHGGLGALSFGIGTSEIEHVFSTQTLWQVKPKNLGVHVTGHLAPGIFAKDIVMALIAKYGTNFAEGYALEY 207
Cdd:cd01586  124 VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEF 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 208 YGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTfdylrgrervpkdfdkaveywkqfktdspdaydwiIELDVSDLA 287
Cdd:cd01586  204 FGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV-----------------------------------VELDLSTVE 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 288 PYVSwgttpsmsvpyGAKLPavtdknieraYDYMDLEpempvQDIPInwVFIGSCTNGRLSDLKEAARVMKGKHLAPG-- 365
Cdd:cd01586  249 PSVS-----------GPKRP----------QDRVPLH-----GSVVI--AAITSCTNTSNPSVMLAAGLLAKKAVELGlk 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 366 VQAWV----VPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMN---PDKVPA-----GMHCAS--TTNRNFEGRQ 431
Cdd:cd01586  301 VKPYVktslAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSgplPEEVEEaikenDLVVAAvlSGNRNFEGRI 380
                        330       340
                 ....*....|....*....|..
gi 226735976 432 GPGTR-THMASPAMVAAAGING 452
Cdd:cd01586  381 HPLVRaNYLASPPLVVAYALAG 402
PRK11413 PRK11413
putative hydratase; Provisional
121-452 6.38e-14

putative hydratase; Provisional


Pssm-ID: 183125 [Multi-domain]  Cd Length: 751  Bit Score: 74.28  E-value: 6.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 121 LTQPGKLIVCGDSHTStHGGLGALSFGIGTSEIEHVFSTQTlWQVK-PKNLGVHVTGHLAPGIFAKDIVMALI-AKYGTN 198
Cdd:PRK11413 138 MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDT-YDIDyPGVVAVYLTGKPAPGVGPQDVALAIIgAVFKNG 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 199 FAEGYALEYYGPTIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTFDYLR--GRErvpkdfdkavEYWKQFKTDSPDAYD 276
Cdd:PRK11413 216 YVKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRG----------QDYCELNPQPMAYYD 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 277 WIIELDVSDLAPYVSWGTTPSMSVP---YGAKLPAVTDKNIERAYDYMDLEPEMPVQDIPIN---WV---FIGSCTNGRL 347
Cdd:PRK11413 286 GCISVDLSAIKPMIALPFHPSNVYEideLNQNLTDILREVEIESERVAHGKAKLSLLDKIENgrlKVqqgIIAGCSGGNY 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 348 SDLKEAARVMKGKHLAPGVQAW-VVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAMNpdKVPA--GMHCASTTn 424
Cdd:PRK11413 366 ENVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAG--DTPAnnGLSIRHTT- 442
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 226735976 425 RNFEGRQG--PGtRTHMASPAM-----VAAAGING 452
Cdd:PRK11413 443 RNFPNREGskPA-NGQMSAVALmdarsIAATAANG 476
PLN00094 PLN00094
aconitate hydratase 2; Provisional
131-452 4.74e-13

aconitate hydratase 2; Provisional


Pssm-ID: 215053 [Multi-domain]  Cd Length: 938  Bit Score: 71.49  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 131 GDSHT------STHGGLGALSFGIGTSEIEHVFstqtlwqvkPKNLGVHVTGHLAPGIFAKDIVMAL-----------IA 193
Cdd:PLN00094 559 GDSHTrfpigiSFPAGSGLVAFGAATGVIPLDM---------PESVLVRFTGTMQPGITLRDLVHAIpytaiqdglltVE 629
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 194 KYG-TNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKTF-DYLR--------------GRERVPKDF 257
Cdd:PLN00094 630 KKGkKNVFSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEPIiEYLNsnvvmlkwmiaegyGDRRTLERR 707
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 258 DKAVEYW----KQFKTDSPDAYDWIIELDVSDLapyvswgTTPSMSVPygaklpavTDKNIERAYDymdlepemPVQDIP 333
Cdd:PLN00094 708 IARMQQWladpELLEADPDAEYAAVIEIDMDEI-------KEPILCAP--------NDPDDARLLS--------EVTGDK 764
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 334 INWVFIGSC-TNgrLSDLKEAARVMKgKHLAP-GVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLAmNPD 411
Cdd:PLN00094 765 IDEVFIGSCmTN--IGHFRAAGKLLN-DNLSQlPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQA 840
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 226735976 412 KVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGING 452
Cdd:PLN00094 841 RVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILG 881
PRK09238 PRK09238
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
98-453 7.62e-13

bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated


Pssm-ID: 236424 [Multi-domain]  Cd Length: 835  Bit Score: 70.98  E-value: 7.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976  98 GVELADiGDkdqGIVHVIGPQLGLtqPGKLIVCGDSHTSTHGGLgalSF--GIGTSEIEHVFSTQTLwqVKPKNLGVHVT 175
Cdd:PRK09238 458 GVSLRP-GD---GVIHSWLNRMLL--PDTVGTGGDSHTRFPIGI---SFpaGSGLVAFAAATGVMPL--DMPESVLVRFK 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 176 GHLAPGIFAKDIVMALIA------------KYGTNFAEGYALEYYGptIDEMPIENRMTLTNMIIEGGAKVAMINPDQKT 243
Cdd:PRK09238 527 GEMQPGITLRDLVHAIPYyaikqglltvekKGKKNIFSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEP 604
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 244 F-DYLRG-----RERVPKDFD---------KAVEYWKQFKTD-SPDA---YDWIIELDVSDLapyvswgttpsmsvpyga 304
Cdd:PRK09238 605 IiEYLRSnivllKWMIAEGYGdartlerriAAMEEWLANPELlEADAdaeYAAVIEIDLAEI------------------ 666
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 305 KLPAVTDKNierayDYMDLEPEMPVQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPGVQAWVVPGSRGVQKAAEK 383
Cdd:PRK09238 667 KEPILACPN-----DPDDVRLLSEVAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTE 739
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 384 IGLDKIFTDAGCEWRDPGCSACLAmNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:PRK09238 740 EGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 808
AcnB COG1049
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ...
329-453 4.31e-11

Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440670 [Multi-domain]  Cd Length: 852  Bit Score: 65.26  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 329 VQDIPINWVFIGSC-TNgrLSDLKEAARVMKGKHLAPgVQAWVVPGSRGVQKAAEKIGLDKIFTDAGCEWRDPGCSACLA 407
Cdd:COG1049  686 VAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG 762
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226735976 408 mNPDKVPAGMHCASTTNRNFEGRQGPGTRTHMASPAMVAAAGINGH 453
Cdd:COG1049  763 -NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 807
PRK02603 PRK02603
photosystem I assembly protein Ycf3; Provisional
189-275 2.00e-03

photosystem I assembly protein Ycf3; Provisional


Pssm-ID: 179448 [Multi-domain]  Cd Length: 172  Bit Score: 38.88  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735976 189 MALIakYGTNFAEGYALEYYGPTIDEMPienRM--TLTNM--IIEGGAKVAMINPDQKTFDYLrgrervpkdFDKAVEYW 264
Cdd:PRK02603  78 MGII--YASNGEHDKALEYYHQALELNP---KQpsALNNIavIYHKRGEKAEEAGDQDEAEAL---------FDKAAEYW 143
                         90
                 ....*....|.
gi 226735976 265 KQFKTDSPDAY 275
Cdd:PRK02603 144 KQAIRLAPNNY 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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