NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18414006|ref|NP_567405|]
View 

isopropyl malate isomerase large subunit 1 [Arabidopsis thaliana]

Protein Classification

3-isopropylmalate dehydratase large subunit( domain architecture ID 10000557)

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

CATH:  3.30.499.10|3.30.499.20
EC:  4.2.1.33
Gene Ontology:  GO:0003861|GO:0051539|GO:0009098|GO:0046872

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LeuC COG0065
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ...
 66-507 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: 603.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  66 GMTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFkREFGeKAKVWDPEKIVVIPDHYIFTADKRANRNV 145
Cdd:COG0065   2 GMTLAEKILARHAGRE-VEPGEIVLLYIDLHLVHDVTSPQAFEGL-REAG-GRKVWDPDRIVAVFDHNVPTKDPKSAEQV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 146 DIMREHCREQNIKyFYDITDlgnfkanpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLG 225
Cdd:COG0065  79 KTLREFAKEFGIT-FFDVGD----------PGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 226 TGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIP 305
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 306 PDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:COG0065 228 PDETTFEYLKGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLR 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 386 AAAKLfhAAGRKVK--VPTFLVPATQKVWMdvYALpvpgAGGktCAQIFEEAGCdTPASPSCGACLGGPADtyaRLNEPQ 463
Cdd:COG0065 308 AAAEI--LKGRKVApgVRAIVVPGSQEVYR--QAE----AEG--LDEIFIEAGA-EWREPGCGMCLGMNMG---VLAPGE 373

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 18414006 464 VCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREF 507
Cdd:COG0065 374 RCASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRITDPREL 417
 
Name Accession Description Interval E-value
LeuC COG0065
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ...
 66-507 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: 603.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  66 GMTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFkREFGeKAKVWDPEKIVVIPDHYIFTADKRANRNV 145
Cdd:COG0065   2 GMTLAEKILARHAGRE-VEPGEIVLLYIDLHLVHDVTSPQAFEGL-REAG-GRKVWDPDRIVAVFDHNVPTKDPKSAEQV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 146 DIMREHCREQNIKyFYDITDlgnfkanpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLG 225
Cdd:COG0065  79 KTLREFAKEFGIT-FFDVGD----------PGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 226 TGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIP 305
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 306 PDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:COG0065 228 PDETTFEYLKGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLR 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 386 AAAKLfhAAGRKVK--VPTFLVPATQKVWMdvYALpvpgAGGktCAQIFEEAGCdTPASPSCGACLGGPADtyaRLNEPQ 463
Cdd:COG0065 308 AAAEI--LKGRKVApgVRAIVVPGSQEVYR--QAE----AEG--LDEIFIEAGA-EWREPGCGMCLGMNMG---VLAPGE 373

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 18414006 464 VCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREF 507
Cdd:COG0065 374 RCASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRITDPREL 417
IPMI cd01583
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ...
 95-501 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: 593.78  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  95 VLMTHDVCGPGAFGIFKREFGEKakVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKyFYDItdlgnfkanpD 174
Cdd:cd01583   1 LHLVHDVTSPQAFEGLREAGREK--VWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGIN-FFDV----------G 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 175 YKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDL 254
Cdd:cd01583  68 RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 255 ILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSVPFEPVYSDGNASFV 334
Cdd:cd01583 148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 335 ADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTFLVPATQKVWMD 414
Cdd:cd01583 228 KVVEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQ 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 415 VYAlpvpgaggKTCAQIFEEAGCDTPAsPSCGACLGGPADtyaRLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAA 494
Cdd:cd01583 308 AEK--------EGLIEIFIEAGAEVRP-PGCGACLGGHMG---VLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAA 375


                ....*..
gi 18414006 495 SALTGRV 501
Cdd:cd01583 376 SAITGEI 382
PRK00402 PRK00402
3-isopropylmalate dehydratase large subunit; Reviewed
 66-508 0e+00

3-isopropylmalate dehydratase large subunit; Reviewed


Pssm-ID: 234748  Cd Length: 418  Bit Score: 555.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   66 GMTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREfgEKAKVWDPEKIVVIPDHYIFTADKRANRNV 145
Cdd:PRK00402   2 GMTLAEKILARHSGRD-VSPGDIVEAKVDLVMAHDITGPLAIKEFEKI--GGDKVFDPSKIVIVFDHFVPAKDIKSAEQQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  146 DIMREHCREQNIKYFYDItdlgnfkanpdYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLG 225
Cdd:PRK00402  79 KILREFAKEQGIPNFFDV-----------GEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  226 TGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIP 305
Cdd:PRK00402 148 TGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  306 PDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:PRK00402 228 PDEKTLEYLKERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLR 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  386 AAAKLFhaAGRKVK--VPTFLVPATQKVWMDVYALPVpgaggktcAQIFEEAGCdTPASPSCGACLGGpadTYARLNEPQ 463
Cdd:PRK00402 308 IAAEIL--KGRKVApgVRLIVIPASQKIYLQALKEGL--------IEIFVDAGA-VVSTPTCGPCLGG---HMGVLAPGE 373

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 18414006  464 VCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREFL 508
Cdd:PRK00402 374 VCLSTTNRNFKGRMGSPESEVYLASPAVAAASAVTGKITDPREVL 418
hacA_fam TIGR01343
homoaconitate hydratase family protein; This model represents a subfamily of proteins ...
 68-505 2.21e-157

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: 453.83  E-value: 2.21e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    68 TMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKakVWDPEKIVVIPDHYIFTADKRANRNVDI 147
Cdd:TIGR01343   1 TIAEKILSKKSGKE-VYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDK--VWNPEKIVIVFDHQVPADTIKAAEMQKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   148 MREHCREQNIKYFYDITdlgnfkanpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTG 227
Cdd:TIGR01343  78 AREFVKKQGIKYFYDVG-----------EGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   228 KILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPD 307
Cdd:TIGR01343 147 KTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   308 ATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAA 387
Cdd:TIGR01343 227 EKTIQYLKERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVA 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   388 AKLFHaaGRKVK--VPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAGCdTPASPSCGACLGGpadTYARLNEPQVC 465
Cdd:TIGR01343 307 AKILK--GRKVApdVRLIVIPASRAVYLQ--------ALKEGLIEIFVKAGA-VVSTPGCGPCLGS---HQGVLAPGEVC 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 18414006   466 VSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPR 505
Cdd:TIGR01343 373 ISTSNRNFKGRMGHPNAEIYLASPATAAASAVKGYIADPR 412
HacA_Meth NF040615
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 67-504 1.13e-117

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


Pssm-ID: 468587  Cd Length: 419  Bit Score: 352.91  E-value: 1.13e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   67 MTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKrEFGEKakVWDPEKIVVIPDHYIFTADKRANRNVD 146
Cdd:NF040615   1 MTLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFK-EISDK--VWDNEKIVIVFDHNVPANTVKAANMQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  147 IMREHCREQNIKYFYditdlgnfkanPDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGT 226
Cdd:NF040615  77 ITREFVKEQGIKNFY-----------LGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYAT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  227 GKILLKVPPTMRFILDGEMPsYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPP 306
Cdd:NF040615 146 GKTWIKVPKTIRVNIVGKNE-NISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  307 DATTLNYVENRTSVPFEPVY--------SDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTG 378
Cdd:NF040615 225 DEITYEYLRKEGVSEEEIAElkknritvNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTN 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  379 GKTEDFMAAAKLFHaaGRKV--KVPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAG---CdtpaSPSCGACLGGPA 453
Cdd:NF040615 305 GRLSDLRIAAKYLK--GKKVhkDVRLIVIPASKKVFKQ--------ALKEGLIEIFVKAGamiC----TPGCGPCLGAHQ 370

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18414006  454 DTyarLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADP 504
Cdd:NF040615 371 GV---LGDGEVCLSTTNRNFKGRMGNINSYIYLSSPKIAAKSAVKGYITNE 418
Aconitase pfam00330
Aconitase family (aconitate hydratase);
95-499 4.94e-101

Aconitase family (aconitate hydratase);


Pssm-ID: 459764  Cd Length: 460  Bit Score: 311.28  E-value: 4.94e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    95 VLMtHDVCGPGAFGIFkREFGEKakVWDPEKIVVIPDHYIFT------ADKRANRNVDI-----------MREHCREQNI 157
Cdd:pfam00330  23 VLM-HDVTSPQAFVDL-RAAGRA--VRRPGGTPATIDHLVPTdlvidhAPDALDKNIEDeisrnkeqydfLEWNAKKFGI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   158 KYFyditDLGNfkanpdykGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTM 237
Cdd:pfam00330  99 RFV----PPGQ--------GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQPLEMKKPKVV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   238 RFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE-- 315
Cdd:pfam00330 167 GVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTFEYLRat 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   316 NRTSVP----------FEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNR-------------ALAREC--------- 363
Cdd:pfam00330 247 GRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAvplselvpdpfadAVKRKAaeraleymg 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   364 -------KDVKIDRVYIGSCTGGKTEDFMAAAKLF---HAAGRKVK--VPTFLVPATQKVWMdvYA----Lpvpgaggkt 427
Cdd:pfam00330 327 lgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLkkaVEKGLKVApgVKASVVPGSEVVRA--YAeaegL--------- 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18414006   428 cAQIFEEAGCDTpASPSCGACLGGPadtyARLNEPQVCVSTTNRNFPGRMgHKEGQIYLASPYTAAASALTG 499
Cdd:pfam00330 396 -DKILEEAGFEW-RGPGCSMCIGNS----DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
 
Name Accession Description Interval E-value
LeuC COG0065
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ...
 66-507 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: 603.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  66 GMTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFkREFGeKAKVWDPEKIVVIPDHYIFTADKRANRNV 145
Cdd:COG0065   2 GMTLAEKILARHAGRE-VEPGEIVLLYIDLHLVHDVTSPQAFEGL-REAG-GRKVWDPDRIVAVFDHNVPTKDPKSAEQV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 146 DIMREHCREQNIKyFYDITDlgnfkanpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLG 225
Cdd:COG0065  79 KTLREFAKEFGIT-FFDVGD----------PGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 226 TGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIP 305
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 306 PDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:COG0065 228 PDETTFEYLKGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLR 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 386 AAAKLfhAAGRKVK--VPTFLVPATQKVWMdvYALpvpgAGGktCAQIFEEAGCdTPASPSCGACLGGPADtyaRLNEPQ 463
Cdd:COG0065 308 AAAEI--LKGRKVApgVRAIVVPGSQEVYR--QAE----AEG--LDEIFIEAGA-EWREPGCGMCLGMNMG---VLAPGE 373

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 18414006 464 VCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREF 507
Cdd:COG0065 374 RCASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRITDPREL 417
IPMI cd01583
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ...
 95-501 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: 593.78  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  95 VLMTHDVCGPGAFGIFKREFGEKakVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKyFYDItdlgnfkanpD 174
Cdd:cd01583   1 LHLVHDVTSPQAFEGLREAGREK--VWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGIN-FFDV----------G 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 175 YKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDL 254
Cdd:cd01583  68 RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 255 ILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSVPFEPVYSDGNASFV 334
Cdd:cd01583 148 ILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAYWKELKSDEDAEYD 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 335 ADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTFLVPATQKVWMD 414
Cdd:cd01583 228 KVVEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQ 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 415 VYAlpvpgaggKTCAQIFEEAGCDTPAsPSCGACLGGPADtyaRLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAA 494
Cdd:cd01583 308 AEK--------EGLIEIFIEAGAEVRP-PGCGACLGGHMG---VLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAA 375


                ....*..
gi 18414006 495 SALTGRV 501
Cdd:cd01583 376 SAITGEI 382
PRK00402 PRK00402
3-isopropylmalate dehydratase large subunit; Reviewed
 66-508 0e+00

3-isopropylmalate dehydratase large subunit; Reviewed


Pssm-ID: 234748  Cd Length: 418  Bit Score: 555.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   66 GMTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREfgEKAKVWDPEKIVVIPDHYIFTADKRANRNV 145
Cdd:PRK00402   2 GMTLAEKILARHSGRD-VSPGDIVEAKVDLVMAHDITGPLAIKEFEKI--GGDKVFDPSKIVIVFDHFVPAKDIKSAEQQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  146 DIMREHCREQNIKYFYDItdlgnfkanpdYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLG 225
Cdd:PRK00402  79 KILREFAKEQGIPNFFDV-----------GEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  226 TGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIP 305
Cdd:PRK00402 148 TGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  306 PDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:PRK00402 228 PDEKTLEYLKERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLR 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  386 AAAKLFhaAGRKVK--VPTFLVPATQKVWMDVYALPVpgaggktcAQIFEEAGCdTPASPSCGACLGGpadTYARLNEPQ 463
Cdd:PRK00402 308 IAAEIL--KGRKVApgVRLIVIPASQKIYLQALKEGL--------IEIFVDAGA-VVSTPTCGPCLGG---HMGVLAPGE 373

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 18414006  464 VCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREFL 508
Cdd:PRK00402 374 VCLSTTNRNFKGRMGSPESEVYLASPAVAAASAVTGKITDPREVL 418
hacA_fam TIGR01343
homoaconitate hydratase family protein; This model represents a subfamily of proteins ...
 68-505 2.21e-157

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: 453.83  E-value: 2.21e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    68 TMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKakVWDPEKIVVIPDHYIFTADKRANRNVDI 147
Cdd:TIGR01343   1 TIAEKILSKKSGKE-VYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDK--VWNPEKIVIVFDHQVPADTIKAAEMQKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   148 MREHCREQNIKYFYDITdlgnfkanpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTG 227
Cdd:TIGR01343  78 AREFVKKQGIKYFYDVG-----------EGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   228 KILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPD 307
Cdd:TIGR01343 147 KTWFKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   308 ATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAA 387
Cdd:TIGR01343 227 EKTIQYLKERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVA 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   388 AKLFHaaGRKVK--VPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAGCdTPASPSCGACLGGpadTYARLNEPQVC 465
Cdd:TIGR01343 307 AKILK--GRKVApdVRLIVIPASRAVYLQ--------ALKEGLIEIFVKAGA-VVSTPGCGPCLGS---HQGVLAPGEVC 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 18414006   466 VSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPR 505
Cdd:TIGR01343 373 ISTSNRNFKGRMGHPNAEIYLASPATAAASAVKGYIADPR 412
IPMI_arch TIGR02086
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ...
 67-506 5.71e-141

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: 412.23  E-value: 5.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    67 MTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFkREFGEkAKVWDPEKIVVIPDHYIFTADKRANRNVD 146
Cdd:TIGR02086   1 MTLAEKILSEKVGRP-VCAGEIVEVEVDLAMTHDGTGPLAIKAL-RELGV-ARVWDPEKIVIAFDHNVPPPTVEAAEMQK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   147 IMREHCREQNIKyfyditdlgNFKANpdyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGT 226
Cdd:TIGR02086  78 EIREFAKRHGIK---------NFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALAT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   227 GKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPP 306
Cdd:TIGR02086 146 GKTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   307 DATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMA 386
Cdd:TIGR02086 226 DEETYEYLKKRRGLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRI 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   387 AAKLFHAAGRKVKVPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAGCdTPASPSCGACLGGpadTYARLNEPQVCV 466
Cdd:TIGR02086 306 AAEILKGRRVHPDVRLIVIPASRKVYLR--------ALEEGIILTLVRAGA-MICPPGCGPCLGA---HMGVLGDGEVCL 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 18414006   467 STTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPRE 506
Cdd:TIGR02086 374 STTNRNFKGRMGSPNAEIYLASPATAAASAVEGYITDPED 413
LEU2 TIGR02083
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 67-506 8.26e-130

3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 131138  Cd Length: 419  Bit Score: 383.78  E-value: 8.26e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    67 MTMTEKILARASEKSLVVPGDNIWVNVDVLMTHDVCGPGAFGIFKrEFGEKaKVWDPEKIVVIPDHYIFTADKRANRNVD 146
Cdd:TIGR02083   1 MTMAEKILAQHAGLESVEPGELILAKLDIVLGNDITTPLAIKAFK-EYGGK-KVFDPDRVALVPDHFTPNKDIKSAEQCK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   147 IMREHCREQNIKYFYDItdlGNFkanpdykGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGT 226
Cdd:TIGR02083  79 MMREFAREQGIEKFFEI---GNM-------GIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMAT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   227 GKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPP 306
Cdd:TIGR02083 149 GKAWFRVPEAIKFVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   307 DATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALAREC--KDVKIDRVYIGSCTGGKTEDF 384
Cdd:TIGR02083 229 DEITIEYEKGRGKREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAgkEEIKIDQVVIGSCTNGRLEDL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   385 MAAAKLFHaaGRKVK--VPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAGCdTPASPSCGACLGGPADTYArlnEP 462
Cdd:TIGR02083 309 RLAAEILK--GKTVApdVRCIIIPGSQNVYLE--------AMKEGLLEIFIEAGA-VVSTPTCGPCLGGHMGILA---EG 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 18414006   463 QVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPRE 506
Cdd:TIGR02083 375 ERAISTTNRNFVGRMGHPKSEVYLASPAVAAASAIKGYIASPEE 418
HacA_Meth NF040615
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
 67-504 1.13e-117

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


Pssm-ID: 468587  Cd Length: 419  Bit Score: 352.91  E-value: 1.13e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   67 MTMTEKILARASEKSlVVPGDNIWVNVDVLMTHDVCGPGAFGIFKrEFGEKakVWDPEKIVVIPDHYIFTADKRANRNVD 146
Cdd:NF040615   1 MTLAEKILSKKLGKE-VYAGDTVEVDVDLAMTHDGTTPLTYKAFK-EISDK--VWDNEKIVIVFDHNVPANTVKAANMQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  147 IMREHCREQNIKYFYditdlgnfkanPDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGT 226
Cdd:NF040615  77 ITREFVKEQGIKNFY-----------LGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYAT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  227 GKILLKVPPTMRFILDGEMPsYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPP 306
Cdd:NF040615 146 GKTWIKVPKTIRVNIVGKNE-NISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  307 DATTLNYVENRTSVPFEPVY--------SDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTG 378
Cdd:NF040615 225 DEITYEYLRKEGVSEEEIAElkknritvNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTN 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  379 GKTEDFMAAAKLFHaaGRKV--KVPTFLVPATQKVWMDvyalpvpgAGGKTCAQIFEEAG---CdtpaSPSCGACLGGPA 453
Cdd:NF040615 305 GRLSDLRIAAKYLK--GKKVhkDVRLIVIPASKKVFKQ--------ALKEGLIEIFVKAGamiC----TPGCGPCLGAHQ 370

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18414006  454 DTyarLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADP 504
Cdd:NF040615 371 GV---LGDGEVCLSTTNRNFKGRMGNINSYIYLSSPKIAAKSAVKGYITNE 418
PRK12466 PRK12466
3-isopropylmalate dehydratase large subunit;
65-509 1.53e-103

3-isopropylmalate dehydratase large subunit;


Pssm-ID: 183543  Cd Length: 471  Bit Score: 318.39  E-value: 1.53e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   65 TGMTMTEKILArasekSLVV---PGDNIWVNVDVLMTHDVCGPGAF-GIfkREFGekAKVWDPEKIVVIPDHYIFTADKR 140
Cdd:PRK12466   2 MPRTLYDKLWD-----SHTVarlDDGHVLLYIDRHLLNEYTSPQAFsGL--RARG--RTVRRPDLTLAVVDHVVPTRPGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  141 --------ANRNVDIMREHCREQNIKYFyDITDlgnfkanPDyKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFA 212
Cdd:PRK12466  73 drgitdpgGALQVDYLRENCADFGIRLF-DVDD-------PR-QGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  213 TGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCN 292
Cdd:PRK12466 144 FGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCN 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  293 MVVEAGGKNGVIPPDATTLNYVENRtsvPFEP--------------VYSDGNASFVADYRFDVSKLEPVVAKPHSPD--- 355
Cdd:PRK12466 224 MAVEAGARGGLIAPDETTFDYLRGR---PRAPkgalwdaalaywrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDqav 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  356 ---------------------NRALA-------RECKDVKIDRVYIGSCTGGKTEDFMAAAKLfhAAGRKVKVPtflvpa 407
Cdd:PRK12466 301 pitgrvpdpaaeadparraamERALDymgltpgTPLAGIPIDRVFIGSCTNGRIEDLRAAAAV--LRGRKVAPG------ 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  408 tqkvwmdVYALPVPGAG-------GKTCAQIFEEAGCDTPAsPSCGACLGGPADTYARlnePQVCVSTTNRNFPGRMGhK 480
Cdd:PRK12466 373 -------VRAMVVPGSGavrrqaeAEGLARIFIAAGFEWRE-PGCSMCLAMNDDVLAP---GERCASTTNRNFEGRQG-P 440

                        490       500
                 ....*....|....*....|....*....
gi 18414006  481 EGQIYLASPYTAAASALTGRVADPREFLQ 509
Cdd:PRK12466 441 GARTHLMSPAMVAAAAVAGHITDVRSLLQ 469
Aconitase pfam00330
Aconitase family (aconitate hydratase);
95-499 4.94e-101

Aconitase family (aconitate hydratase);


Pssm-ID: 459764  Cd Length: 460  Bit Score: 311.28  E-value: 4.94e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    95 VLMtHDVCGPGAFGIFkREFGEKakVWDPEKIVVIPDHYIFT------ADKRANRNVDI-----------MREHCREQNI 157
Cdd:pfam00330  23 VLM-HDVTSPQAFVDL-RAAGRA--VRRPGGTPATIDHLVPTdlvidhAPDALDKNIEDeisrnkeqydfLEWNAKKFGI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   158 KYFyditDLGNfkanpdykGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTM 237
Cdd:pfam00330  99 RFV----PPGQ--------GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQPLEMKKPKVV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   238 RFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE-- 315
Cdd:pfam00330 167 GVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTFEYLRat 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   316 NRTSVP----------FEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNR-------------ALAREC--------- 363
Cdd:pfam00330 247 GRPEAPkgeaydkavaWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAvplselvpdpfadAVKRKAaeraleymg 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   364 -------KDVKIDRVYIGSCTGGKTEDFMAAAKLF---HAAGRKVK--VPTFLVPATQKVWMdvYA----Lpvpgaggkt 427
Cdd:pfam00330 327 lgpgtplSDGKVDIAFIGSCTNSSIEDLRAAAGLLkkaVEKGLKVApgVKASVVPGSEVVRA--YAeaegL--------- 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18414006   428 cAQIFEEAGCDTpASPSCGACLGGPadtyARLNEPQVCVSTTNRNFPGRMgHKEGQIYLASPYTAAASALTG 499
Cdd:pfam00330 396 -DKILEEAGFEW-RGPGCSMCIGNS----DRLPPGERCVSSSNRNFEGRQ-GPGGRTHLASPALVAAAAIAG 460
PRK05478 PRK05478
3-isopropylmalate dehydratase large subunit;
93-508 1.69e-95

3-isopropylmalate dehydratase large subunit;


Pssm-ID: 235490  Cd Length: 466  Bit Score: 297.42  E-value: 1.69e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   93 VDVLMTHDVCGPGAF-GIfkREFGEKakVWDPEKIVVIPDHYIFTADKR-------ANRNVDIMREHCREQNIKyFYDIT 164
Cdd:PRK05478  27 IDRHLVHEVTSPQAFeGL--RLAGRK--VRRPDLTFATMDHNVPTTDRDlpiadpvSRIQVETLEKNCKEFGIT-LFDLG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  165 DlgnfkanpDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGE 244
Cdd:PRK05478 102 D--------PRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGK 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  245 MPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRtsvPFEP 324
Cdd:PRK05478 174 LPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLKGR---PFAP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  325 --------------VYSDGNASFVADYRFDVSKLEPVV-------------------AKPHSPDNRALAREC-------- 363
Cdd:PRK05478 251 kgedwdkavaywktLKSDEDAVFDKVVTLDAADIEPQVtwgtnpgqvisidgkvpdpEDFADPVKRASAERAlaymglkp 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  364 ----KDVKIDRVYIGSCTGGKTEDFMAAAKLfhAAGRKVKvptflvpatqkvwMDVYALPVPGAGG-KTCA------QIF 432
Cdd:PRK05478 331 gtpiTDIKIDKVFIGSCTNSRIEDLRAAAAV--VKGRKVA-------------PGVRALVVPGSGLvKAQAeaegldKIF 395

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414006  433 EEAGCDTpASPSCGACLGGPADtyaRLNEPQVCVSTTNRNFPGRMGhKEGQIYLASPYTAAASALTGRVADPREFL 508
Cdd:PRK05478 396 IEAGFEW-REPGCSMCLAMNPD---KLPPGERCASTSNRNFEGRQG-KGGRTHLVSPAMAAAAAITGHFVDVRELL 466
Aconitase cd01351
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ...
 96-501 2.85e-77

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: 247.80  E-value: 2.85e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  96 LMTHDVCGPGAFGIFKReFGEKAKVWDPEKIVVIPDHYIFTADKRANRNvdimrehcrEQNIKYFYDITDLGNFKANpdy 175
Cdd:cd01351   2 VMLQDATGPMAMKAFEI-LAALGKVADPSQIACVHDHAVQLEKPVNNEG---------HKFLSFFAALQGIAFYRPG--- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 176 KGVCHvALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLI 255
Cdd:cd01351  69 VGIIH-QIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 256 LQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSVP--------FEPVYS 327
Cdd:cd01351 148 LKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLlknlwlafPEELLA 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 328 DGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTFLVPA 407
Cdd:cd01351 228 DEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPG 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 408 TQKVWMDVYALPVpgaggktcAQIFEEAGCDTPAsPSCGACLGGPAdtyARLNEPQVCVSTTNRNFPGRMGHKEGQIYLA 487
Cdd:cd01351 308 SRMVYATLSREGY--------YEILVDSGARILP-PGCGPCMGNGA---RLVADGEVGVSSGNRNFPGRLGTYERHVYLA 375

                       410
                ....*....|....
gi 18414006 488 SPYTAAASALTGRV 501
Cdd:cd01351 376 SPELAAATAIAGKI 389
PRK07229 PRK07229
aconitate hydratase; Validated
 66-507 8.61e-72

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 240.43  E-value: 8.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   66 GMTMTEKILarasEKSLV----VPGDNIWVNVDVLMTHDVCGPGAF------GIfkrefgEKAKVwdpEKIVVIPDHYIF 135
Cdd:PRK07229   2 GLTLTEKIL----YAHLVegelEPGEEIAIRIDQTLTQDATGTMAYlqfeamGL------DRVKT---ELSVQYVDHNLL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  136 TADKRaNRNV-DIMREHCREQNIkYFydiTDLGNfkanpdykGVCH-VALaqEGHCRPGEVLLGTDSHTCTAGAFGQFAT 213
Cdd:PRK07229  69 QADFE-NADDhRFLQSVAAKYGI-YF---SKPGN--------GICHqVHL--ERFAFPGKTLLGSDSHTPTAGGLGMLAI 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  214 GIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNM 293
Cdd:PRK07229 134 GAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNM 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  294 VVEAGGKNGVIPPDATTLNYVE--NRTSVpFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRV 371
Cdd:PRK07229 214 GAELGATTSIFPSDERTREFLKaqGREDD-WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQV 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  372 YIGSCTGGKTEDFMAAAKLfhAAGRKV--KVPTFLVPATQKVWMDVYA----LPVPGAGgktcAQIFEeagcdtpasPSC 445
Cdd:PRK07229 293 LIGSCTNSSYEDLMRAASI--LKGKKVhpKVSLVINPGSRQVLEMLARdgalADLIAAG----ARILE---------NAC 357

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18414006  446 GACLG---GPAdtyarlnEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREF 507
Cdd:PRK07229 358 GPCIGmgqAPA-------TGNVSLRTFNRNFPGRSGTKDAQVYLASPETAAASALTGVITDPRTL 415
acon_putative TIGR01342
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ...
 68-507 5.48e-65

aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]


Pssm-ID: 130409 [Multi-domain]  Cd Length: 658  Bit Score: 222.55  E-value: 5.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006    68 TMTEKILARASEKSLVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKAKVwdpEKIVVIPDHYIFTADkraNRNVDI 147
Cdd:TIGR01342   1 TLAEKIIDDHLVEGDLEPGEEIAIEIDQTLSQDATGTMCWLEFEALEMDEVKT---ELAAQYCDHNMLQFD---FKNADD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   148 MReHCREQNIKYFYDITDLGNfkanpdykGVCHvALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTG 227
Cdd:TIGR01342  75 HK-FLMSAAGKFGAWFSKPGN--------GICH-NVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   228 KILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPD 307
Cdd:TIGR01342 145 AFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   308 ATTLNYV--ENRTSvPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFM 385
Cdd:TIGR01342 225 DITEAWLaaFDRED-DFVDLLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAGIEVDQVMIGSCTNGAFEDLL 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006   386 AAAKLFHaaGRKVKVPTFLV--PATQKvwmdvyALPVPGAGGKTCAqiFEEAGCDTPASpSCGACLG----GPADTyarl 459
Cdd:TIGR01342 304 PAAKLLE--GREVHKDTEFAvaPGSKQ------ALELIAQEGALAE--FLAAGANFLEA-ACGACIGigfaPASDG---- 368

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 18414006   460 nepqVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREF 507
Cdd:TIGR01342 369 ----VSLRSFNRNFEGRAGIEDAKVYLASPETATAAAIAGEIIDPRDL 412
AcnA_Bact cd01585
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ...
 177-499 3.56e-64

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: 213.08  E-value: 3.56e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 177 GVCHvALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLIL 256
Cdd:cd01585  69 GICH-QVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 257 QIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE--NRTSVpFEPVYSDGNASFV 334
Cdd:cd01585 148 ELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGREDD-WVELAADADAEYD 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 335 ADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFhaAGRKVKVPTFLV--PATQKVW 412
Cdd:cd01585 227 EEIEIDLSELEPLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAIL--KGRRVHPHVSMVvaPGSKQVL 304

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 413 MDV----YALPVPGAGgktcAQIFEeagcdtpasPSCGACLG---GPADTyarlnepQVCVSTTNRNFPGRMGHKEGQIY 485
Cdd:cd01585 305 EMLarngALADLLAAG----ARILE---------SACGPCIGmgqAPPTG-------GVSVRTFNRNFEGRSGTKDDLVY 364

                       330
                ....*....|....
gi 18414006 486 LASPYTAAASALTG 499
Cdd:cd01585 365 LASPEVAAAAALTG 378
Homoaconitase cd01582
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ...
 97-501 1.29e-50

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: 177.04  E-value: 1.29e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  97 MTHDVCGPGAFgifkrEFGE--KAKVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKYFyditdlgnfkanPD 174
Cdd:cd01582   3 MTHDNSWPVAL-----KFMSigATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFY------------PA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 175 YKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDL 254
Cdd:cd01582  66 GRGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 255 ILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNyvenrtsvpfepvysdgnasfv 334
Cdd:cd01582 146 IVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI---------------------- 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 335 adyrFDVSKLEPVVAKPHSPD--NRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTflVPATQKVW 412
Cdd:cd01582 204 ----LDLSTLSPYVSGPNSVKvsTPLKELEAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKEKNGKIP--VAPGVEFY 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 413 MDVYALPVPGAGGKTCA-QIFEEAGCdTPASPSCGACLGGPAdtyARLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYT 491
Cdd:cd01582 278 VAAASSEVQAAAEKNGDwQTLLEAGA-TPLPAGCGPCIGLGQ---GLLEPGEVGISATNRNFKGRMGSTEALAYLASPAV 353

                       410
                ....*....|
gi 18414006 492 AAASALTGRV 501
Cdd:cd01582 354 VAASAISGKI 363
AcnA_Mitochondrial cd01584
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ...
 186-500 1.66e-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: 128.71  E-value: 1.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 186 EGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVA 265
Cdd:cd01584  85 ENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVK 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 266 GATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE--NRTSVP-------FEPVYSDGNASFVAD 336
Cdd:cd01584 165 GGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAEIAdladefkDDLLVADEGAEYDQL 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 337 YRFDVSKLEPVVAKPHSPDNRALARECKDV--------KIDRVYIGSCTGGKTEDFMAAAKLFHAA---GRKVKVPTFLV 405
Cdd:cd01584 245 IEINLSELEPHINGPFTPDLATPVSKFKEVaekngwplDLRVGLIGSCTNSSYEDMGRAASIAKQAlahGLKCKSIFTIT 324

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 406 PATQKVwmdVYALPVPGAggktcAQIFEEAGCDTPASpSCGACLGGPADTYARLNEPQVCVSTTNRNFPGRM-GHKEGQI 484
Cdd:cd01584 325 PGSEQI---RATIERDGL-----LQTFRDAGGIVLAN-ACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNdANPATHA 395

                       330
                ....*....|....*.
gi 18414006 485 YLASPYTAAASALTGR 500
Cdd:cd01584 396 FVASPEIVTAMAIAGT 411
PRK09238 PRK09238
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
 191-509 1.27e-25

bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated


Pssm-ID: 236424 [Multi-domain]  Cd Length: 835  Bit Score: 111.04  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  191 PGEVLLGTDSHTctagafgQFATGI----GNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLI----LQII--G 260
Cdd:PRK09238 478 PDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVhaipYYAIkqG 550

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  261 EISVAGATYKTmEFSGTTIE-----SLSMEERMTLCNMVVEAGGKNGVIP-PDATTLNY--------------------- 313
Cdd:PRK09238 551 LLTVEKKGKKN-IFSGRILEieglpDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYlrsnivllkwmiaegygdart 629

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  314 VENRTS---------VPFEPvysDGNASFVADYRFDVSKL-EPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKtED 383
Cdd:PRK09238 630 LERRIAameewlanpELLEA---DADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCMTNI-GH 705

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  384 FMAAAKLFHAAGRKVKVPTFLVPATQkvwMDVYALPVPGAGGktcaqIFEEAGCDTPAsPSCGACLGgpadTYARLNEPQ 463
Cdd:PRK09238 706 FRAAGKLLEGKKGQLPTRLWVAPPTK---MDADQLTEEGYYS-----IFGKAGARIEM-PGCSLCMG----NQARVADGA 772

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 18414006  464 VCVSTTNRNFPGRMGhKEGQIYLASPYTAAASALTGRVADPREFLQ 509
Cdd:PRK09238 773 TVFSTSTRNFPNRLG-KGANVYLGSAELAAVCALLGRIPTVEEYQE 817
AcnB cd01581
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ...
 191-501 1.58e-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: 102.96  E-value: 1.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 191 PGEVLLGTDSHTctagafgQFATGI----GNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLI----LQII--G 260
Cdd:cd01581 106 PDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVnaipYYAIqqG 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 261 EISVAGATYKTMeFSGTTIE-----SLSMEERMTLCNMVVEAGGKNGVIPPD--------------------------AT 309
Cdd:cd01581 179 LLTVEKKGKKNV-FNGRILEieglpDLKVEQAFELTDASAERSAAACTVRLDkepvieylesnvvlmkimiangyddaRT 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 310 TLNYVENRTSVPFEPVY--SDGNASFVADYRFDVSKL-EPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTeDFMA 386
Cdd:cd01581 258 LLRRIIAMEEWLANPPLlePDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLLSEVAGKKIDEVFIGSCMTNIG-HFRA 336

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 387 AAKLFHAAGRKvKVPTFLVPATQKVWMDVYAlpvpgaggKTCAQIFEEAGCDTPAsPSCGACLGgpadTYARLNEPQVCV 466
Cdd:cd01581 337 AAKILRGKEFK-PTRLWVAPPTRMDWAILQE--------EGYYSIFGDAGARTEM-PGCSLCMG----NQARVADGATVF 402

                       330       340       350
                ....*....|....*....|....*....|....*
gi 18414006 467 STTNRNFPGRMGhKEGQIYLASPYTAAASALTGRV 501
Cdd:cd01581 403 STSTRNFDNRVG-KGAEVYLGSAELAAVCALLGRI 436
PLN00094 PLN00094
aconitate hydratase 2; Provisional
 191-509 1.76e-20

aconitate hydratase 2; Provisional


Pssm-ID: 215053 [Multi-domain]  Cd Length: 938  Bit Score: 95.37  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  191 PGEVLLGTDSHTctagafgQFATGI----GNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQI------IG 260
Cdd:PLN00094 552 PDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqDG 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  261 EISVAGATyKTMEFSGTTIE-----SLSMEERMTLCNMVVEAGGKNGVI----PPDATTLN-------------YVENRT 318
Cdd:PLN00094 625 LLTVEKKG-KKNVFSGRILEieglpHLKCEQAFELSDASAERSAAGCTIkldkEPIIEYLNsnvvmlkwmiaegYGDRRT 703

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  319 ------------SVPfEPVYSDGNASFVADYRFDVSKL-EPVVAKPHSPDNRALARECKDVKIDRVYIGSCTgGKTEDFM 385
Cdd:PLN00094 704 lerriarmqqwlADP-ELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCM-TNIGHFR 781

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  386 AAAKLFHAAGRKVKVPTFLVPATQkvwMDVYALPVPGAGGktcaqIFEEAGCDTPAsPSCGACLGgpadTYARLNEPQVC 465
Cdd:PLN00094 782 AAGKLLNDNLSQLPTRLWVAPPTK---MDEAQLKAEGYYS-----TFGTVGARTEM-PGCSLCMG----NQARVAEKSTV 848

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 18414006  466 VSTTNRNFPGRMGhKEGQIYLASPYTAAASALTGRVADPREFLQ 509
Cdd:PLN00094 849 VSTSTRNFPNRLG-KGANVYLASAELAAVAAILGRLPTVEEYLS 891
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 195-501 2.15e-20

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 95.08  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  195 LLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEF 274
Cdd:PTZ00092 211 VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEF 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  275 SGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVeNRTSVPFEPV-----Y---------SDGNASFVADYRFD 340
Cdd:PTZ00092 291 YGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYL-KQTGRSEEKVeliekYlkanglfrtYAEQIEYSDVLELD 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  341 VSKLEPVVAKPHSP-DNRALA------REC------------------KDVKI---DRVY-----------IGSCTGGKT 381
Cdd:PTZ00092 370 LSTVVPSVAGPKRPhDRVPLSdlkkdfTAClsapvgfkgfgipeekheKKVKFtykGKEYtlthgsvviaaITSCTNTSN 449

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  382 EDFMAAAKLF--HAAGRKVKVP----TFLVPatqkvwmdvyalpvpgaGGKTCAQIFEEAGCDTP--------ASPSCGA 447
Cdd:PTZ00092 450 PSVMLAAGLLakKAVEKGLKVPpyikTSLSP-----------------GSKVVTKYLEASGLLKYleklgfytAGYGCMT 512

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18414006  448 CLG--GPAD---TYARLNEPQVCVS--TTNRNFPGRMGHKEGQIYLASPYTAAASALTGRV 501
Cdd:PTZ00092 513 CIGnsGDLDpevSEAITNNDLVAAAvlSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRV 573
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 195-501 3.54e-19

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: 91.32  E-value: 3.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 195 LLGTDSHTCTAGAFGQFATGIGNTDAGFV-LGtgkillkVPPTMR------FILDGEMPSYLQAKDLILQIIGEISVAGA 267
Cdd:COG1048 206 LVGTDSHTTMINGLGVLGWGVGGIEAEAAmLG-------QPVSMLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKGV 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 268 TYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNY-------------VEN--------RTSVPFEPVY 326
Cdd:COG1048 279 VGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYlrltgrseeqielVEAyakaqglwRDPDAPEPYY 358

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 327 SDgnasfvaDYRFDVSKLEPVVAKPHSPDNR------------ALARECKDVKIDRVY-------------------IGS 375
Cdd:COG1048 359 SD-------VLELDLSTVEPSLAGPKRPQDRiplsdlkeafraALAAPVGEELDKPVRvevdgeefelghgavviaaITS 431

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 376 CTGGKTEDFMAAAKLF----HAAGRKVK--VPTFLVPatqkvwmdvyalpvpgaGGKTCAQIFEEAGCDTP--------- 440
Cdd:COG1048 432 CTNTSNPSVMIAAGLLakkaVEKGLKVKpwVKTSLAP-----------------GSKVVTDYLERAGLLPYlealgfnvv 494

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414006 441 --AspsCGACLG--GPadtyarLNEP---------QVCVSTT--NRNFPGRMGHKEGQIYLASPYTAAASALTGRV 501
Cdd:COG1048 495 gyG---CTTCIGnsGP------LPPEiseaieendLVVAAVLsgNRNFEGRIHPDVKANFLASPPLVVAYALAGTV 561
AcnA_IRP cd01586
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ...
 122-501 1.05e-18

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: 88.13  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 122 DPEKI-VVIP-----DH-----YIFTADKRANrNVDIMREHCREQNIKYFYDITDLGNFKANPDYKGVCH-VALA----- 184
Cdd:cd01586  29 DPEKInPLIPvdlviDHsvqvdFYGTADALAK-NMKLEFERNRERYEFLKWGQKAFKNLRVVPPGTGIIHqVNLEylarv 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 185 -------QEGHCRPgEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQ 257
Cdd:cd01586 108 vftseedGDGVAYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLT 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 258 IIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLnyvenrtsvpfepvysdgnasfvady 337
Cdd:cd01586 187 VTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQVV-------------------------- 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 338 RFDVSKLEPVVAKPHSPDNRALARecKDVKIdrVYIGSCTGGKTEDFMAAAKLFH----AAGRKVK--VPTFLVPATQKV 411
Cdd:cd01586 241 ELDLSTVEPSVSGPKRPQDRVPLH--GSVVI--AAITSCTNTSNPSVMLAAGLLAkkavELGLKVKpyVKTSLAPGSRVV 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006 412 wmdVYALPVPGaggktCAQIFEEAGCDTpASPSCGACLG--GPAD--TYARLNEPQVCVSTT---NRNFPGRMGHKEGQI 484
Cdd:cd01586 317 ---TKYLEASG-----LLPYLEKLGFHV-VGYGCTTCIGnsGPLPeeVEEAIKENDLVVAAVlsgNRNFEGRIHPLVRAN 387

                       410
                ....*....|....*..
gi 18414006 485 YLASPYTAAASALTGRV 501
Cdd:cd01586 388 YLASPPLVVAYALAGTV 404
acnA PRK12881
aconitate hydratase AcnA;
168-502 1.11e-16

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 83.44  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  168 NFKANPDYKGVCH---------VALAQEGHCRPGEV---LLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPP 235
Cdd:PRK12881 169 NFRVVPPGTGIMHqvnleylarVVHTKEDDGDTVAYpdtLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPD 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  236 TMRFILDGEMPSYLQAKDLIL---QIIGEISVAGatyKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLN 312
Cdd:PRK12881 249 VVGVELTGKLREGVTATDLVLtvtEMLRKEGVVG---KFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLD 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  313 Y-------------VEN---RTSVPF----EPVYSDGnasfvadYRFDVSKLEPVVAKPHSPDNR--------------- 357
Cdd:PRK12881 326 YlrltgrteaqialVEAyakAQGLWGdpkaEPRYTRT-------LELDLSTVAPSLAGPKRPQDRialgnvksafsdlfs 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  358 ---------ALARECKDVKIDR-----VYIGSCTggKTED---FMAA---AKLFHAAGRKVK--VPTFLVPatqkvwmdv 415
Cdd:PRK12881 399 kpvaengfaKKAQTSNGVDLPDgavaiAAITSCT--NTSNpsvLIAAgllAKKAVERGLTVKpwVKTSLAP--------- 467

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  416 yalpvpgaGGKTCAQIFEEAGCdTP---------ASPSCGACLGGPADTYARLNEPQ-------VCVSTTNRNFPGRMGH 479
Cdd:PRK12881 468 --------GSKVVTEYLERAGL-LPyleklgfgiVGYGCTTCIGNSGPLTPEIEQAItkndlvaAAVLSGNRNFEGRIHP 538

                        410       420
                 ....*....|....*....|...
gi 18414006  480 KEGQIYLASPYTAAASALTGRVA 502
Cdd:PRK12881 539 NIKANFLASPPLVVAYALAGTVR 561
PRK11413 PRK11413
putative hydratase; Provisional
 180-484 2.87e-13

putative hydratase; Provisional


Pssm-ID: 183125 [Multi-domain]  Cd Length: 751  Bit Score: 72.35  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  180 HVAL----AQEGHCRPGEVLLGTDSHTcTAGAFGQFATGIGNTDagFVlgtgKILL------KVPPTMRFILDGEMPSYL 249
Cdd:PRK11413 126 HIAVihqyMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGE--LV----KQLLndtydiDYPGVVAVYLTGKPAPGV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  250 QAKDLILQIIGEISVAGATY-KTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE--NRtsvpfEPVY 326
Cdd:PRK11413 199 GPQDVALAIIGAVFKNGYVKnKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGR-----GQDY 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  327 SDGNASFVADY----RFDVSKLEPVVAKPHSPDN--------------------RALARECKDVKI---DRVY------- 372
Cdd:PRK11413 274 CELNPQPMAYYdgciSVDLSAIKPMIALPFHPSNvyeidelnqnltdilreveiESERVAHGKAKLsllDKIEngrlkvq 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  373 ---IGSCTGGKTEDFMAAAKLFHaaGRKVKVPTF---LVPATQKVWMD------VYALPVPGAGGKTCaqiFeeagcdtp 440
Cdd:PRK11413 354 qgiIAGCSGGNYENVIAAANALR--GQSCGNDTFslsVYPSSQPVFMDlakkgvVADLMGAGAIIRTA---F-------- 420

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 18414006  441 aspsCGACLGGpADTYArlNEpQVCVSTTNRNFPGRMGHK--EGQI 484
Cdd:PRK11413 421 ----CGPCFGA-GDTPA--NN-GLSIRHTTRNFPNREGSKpaNGQM 458
PLN00070 PLN00070
aconitate hydratase
 195-501 6.35e-12

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 68.29  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  195 LLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEF 274
Cdd:PLN00070 243 VVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEF 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  275 SGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVE----NRTSVPFEPVYSDGNASFVaDY------------- 337
Cdd:PLN00070 323 YGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltgrSDETVAMIEAYLRANKMFV-DYnepqqervyssyl 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  338 RFDVSKLEPVVAKPHSPDNRALARE-------CKDVKI------------DRVY--------------------IGSCTG 378
Cdd:PLN00070 402 ELDLEDVEPCISGPKRPHDRVPLKEmkadwhsCLDNKVgfkgfavpkeaqSKVAkfsfhgqpaelrhgsvviaaITSCTN 481

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  379 GKTEDFMAAAKLFHAA----GRKVK--VPTFLVPATQKV-----------WMDVYALPVPGAGGKTCaqifeeAGCDTPA 441
Cdd:PLN00070 482 TSNPSVMLGAGLVAKKacelGLEVKpwIKTSLAPGSGVVtkyllksglqkYLNQQGFHIVGYGCTTC------IGNSGEL 555

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  442 SPSCGACLGGpADTYArlnepqVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRV 501
Cdd:PLN00070 556 DESVASAITE-NDIVA------AAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTV 608
PRK09277 PRK09277
aconitate hydratase AcnA;
122-501 1.38e-09

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 60.91  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  122 DPEKI-VVIP-----DHYI---FTADKRA-NRNVDI--MREHCREQNIKY----FyditdlGNFKANPDYKGVCH----- 180
Cdd:PRK09277 114 DPAKInPLVPvdlviDHSVqvdYFGTPDAfEKNVELefERNEERYQFLKWgqkaF------DNFRVVPPGTGICHqvnle 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  181 -----VALAQEGhcrpGEV-----LLGTDSHTCTAGAFGQFATGIGNTDAGFV-LGTgkillkvPPTMR------FILDG 243
Cdd:PRK09277 188 ylapvVWTREDG----ELVaypdtLVGTDSHTTMINGLGVLGWGVGGIEAEAAmLGQ-------PSSMLipevvgVKLTG 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  244 EMPSYLQAKDLIL---QIIGEISVAGatyKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNY------- 313
Cdd:PRK09277 257 KLPEGVTATDLVLtvtEMLRKKGVVG---KFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYlrltgrd 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  314 ------VEN--------RTSVPfEPVYSDGnasfvadYRFDVSKLEPVVAKPHSPDNR---------------------- 357
Cdd:PRK09277 334 eeqvalVEAyakaqglwRDPLE-EPVYTDV-------LELDLSTVEPSLAGPKRPQDRiplsdvkeafaksaelgvqgfg 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  358 -ALARECKDVKI---DRVY--IGSCTggKTED---FMAA---AKLFHAAGRKVK--VPTFLVPatqkvwmdvyalpvpga 423
Cdd:PRK09277 406 lDEAEEGEDYELpdgAVVIaaITSCT--NTSNpsvMIAAgllAKKAVEKGLKVKpwVKTSLAP----------------- 466

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414006  424 GGKTCAQIFEEAG----------------CDTpaspscgaCLG--GPadtyarLNEPqvcVSTT--------------NR 471
Cdd:PRK09277 467 GSKVVTDYLEKAGllpylealgfnlvgygCTT--------CIGnsGP------LPPE---IEKAindndlvvtavlsgNR 529

                        490       500       510
                 ....*....|....*....|....*....|
gi 18414006  472 NFPGRMGHKEGQIYLASPYTAAASALTGRV 501
Cdd:PRK09277 530 NFEGRIHPLVKANYLASPPLVVAYALAGTV 559
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH