|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-634 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 1065.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 1 MNLAYKILSTKLKSGELVAGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHNMLQTGFENMDDHEFIR 80
Cdd:PRK07229 3 LTLTEKILYAHLVEGELEPGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYVDHNLLQADFENADDHRFLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 81 SVAKKHGITFSKPGNGVCHQLQLENFAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLV 160
Cdd:PRK07229 83 SVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 161 GKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREED 240
Cdd:PRK07229 163 GKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQGREDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 241 YVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVS 320
Cdd:PRK07229 243 WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 321 LVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKGVSLRTINRNFKGRSGTNDASVYLVSPEVAAL 400
Cdd:PRK07229 323 LVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQAPATGNVSLRTFNRNFPGRSGTKDAQVYLASPETAAA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 401 SAIKGYLTDEFED-DMYLDDIE-NTP--FVKNKNFFIdeYDPQN----EVYMGPNIKPVPRGDKLPDTFKGKVCLKVGDN 472
Cdd:PRK07229 403 SALTGVITDPRTLaLENGEYPKlEEPegFAVDDAGII--APAEDgsdvEVVRGPNIKPLPLLEPLPDLLEGKVLLKVGDN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 473 ISTDHIVPSDSKLLPYRSNVPHLAKFSFCKVDDQFYNRCIENGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIFAISFA 552
Cdd:PRK07229 481 ITTDHIMPAGAKWLPYRSNIPNISEFVFEGVDNTFPERAKEQGGGIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 553 RIHRSNLINNGILPLVI-NQKDYDFFNDQDEYELINLLDSVEnNKDITVINKTNNQTITAKLKLSPREKTMIQYGGLLNA 631
Cdd:PRK07229 561 RIHKANLINFGILPLTFaDPADYDKIEEGDVLEIEDLREFLP-GGPLTVVNVTKDEEIEVRHTLSERQIEILLAGGALNL 639
|
...
gi 1473349579 632 IKE 634
Cdd:PRK07229 640 IKK 642
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
3-634 |
0e+00 |
|
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: 802.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 3 LAYKILSTKLKSGELVAGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHNMLQTGFENMDDHEFIRSV 82
Cdd:TIGR01342 2 LAEKIIDDHLVEGDLEPGEEIAIEIDQTLSQDATGTMCWLEFEALEMDEVKTELAAQYCDHNMLQFDFKNADDHKFLMSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 83 AKKHGITFSKPGNGVCHQLQLENFAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGK 162
Cdd:TIGR01342 82 AGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAFYLEMPEIVGVHLEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 163 KAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREEDYV 242
Cdd:TIGR01342 162 LPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDITEAWLAAFDREDDFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 243 ELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLV 322
Cdd:TIGR01342 242 DLLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREIAGIEVDQVMIGSCTNGAFEDLLPAAKLLEGREVHKDTEFA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 323 IAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKGVSLRTINRNFKGRSGTNDASVYLVSPEVAALSA 402
Cdd:TIGR01342 322 VAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGIGFAPASDGVSLRSFNRNFEGRAGIEDAKVYLASPETATAAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 403 IKGYLTDEFEDDMYLDDIENTPFVKNKNF-------FIDEYDPQ----NEVYMGPNIKPVPRGDKLPDTFKGKVCLKVGD 471
Cdd:TIGR01342 402 IAGEIIDPRDLADDEGDLEAIGFEMGEKFpggydaaDIDIIPKEeredDDIIKGPNIKPLPEFDPLGADIEGETALIMED 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 472 NISTDHIVPSDSKLLPYRSNVPHLAKFSFCKVDDQFYNRCI----ENGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:TIGR01342 482 NITTDHIIPAGADILKFRSNIEAISEFTLHRIDDEFAERAKaadeKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVI 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 548 AISFARIHRSNLINNGILPLVI-NQKDYDFFNDQDEYELIN-LLDSVENNKDITVINKTNNQTITAKLKLSPREKTMIQY 625
Cdd:TIGR01342 562 AKSFARIHHANLFNFGILPLEFdNEEDYAKFELGDDIEIPDdLAAALADGEDEFTINKNDDEEALATLDASEREKEILAA 641
|
....*....
gi 1473349579 626 GGLLNAIKE 634
Cdd:TIGR01342 642 GGKLNLIKN 650
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
28-407 |
0e+00 |
|
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: 662.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 28 DQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHNMLQTGFENMDDHEFIRSVAKKHGITFSKPGNGVCHQLQLENFA 107
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYVDHNTLQTDFENADDHRFLQTVAARYGIYFSRPGNGICHQVHLERFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 108 KPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVN 187
Cdd:cd01585 81 VPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 188 KIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREEDYVELKADVDATYDEEITVDLSKLVPLT 267
Cdd:cd01585 161 KIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVELAADADAEYDEEIEIDLSELEPLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 268 AKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAG 347
Cdd:cd01585 241 ARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 348 ARILECGCGPCIGMGQAPLSKGVSLRTINRNFKGRSGTNDASVYLVSPEVAALSAIKGYL 407
Cdd:cd01585 321 ARILESACGPCIGMGQAPPTGGVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-409 |
2.06e-152 |
|
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: 446.01 E-value: 2.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 1 MNLAYKILSTKLKSgELVAGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHVA-VEKAVAYIDHNMLQTGFENMDDHEFI 79
Cdd:COG0065 3 MTLAEKILARHAGR-EVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWdPDRIVAVFDHNVPTKDPKSAEQVKTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 80 RSVAKKHGITFSKPG-NGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRV 157
Cdd:COG0065 82 REFAKEFGITFFDVGdPGICHVVLPEQgLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 158 NLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLiqQGR 237
Cdd:COG0065 162 EVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYL--KGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 238 E-EDYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVA 316
Cdd:COG0065 240 PfAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 317 THVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSP 395
Cdd:COG0065 320 PGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGeRCASTSNRNFEGRMGSPGSRTYLASP 399
|
410
....*....|....
gi 1473349579 396 EVAALSAIKGYLTD 409
Cdd:COG0065 400 ATAAASAIAGRITD 413
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
31-405 |
5.43e-144 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 426.07 E-value: 5.43e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 31 LTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHN---------MLQTGFENMDD--------HEFIRSVAKKHGITFSKP 93
Cdd:pfam00330 24 LMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLvptdlvidhAPDALDKNIEDeisrnkeqYDFLEWNAKKFGIRFVPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 94 GNGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDV 172
Cdd:pfam00330 104 GQGIVHQVGLEYgLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 173 ILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGRE-----EDYVE---- 243
Cdd:pfam00330 184 ILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTFEYLRATGRPeapkgEAYDKavaw 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 244 --LKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSE-----------------------------LRGMKINQVVI 292
Cdd:pfam00330 264 ktLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfadavkrkaaeraleymglgpgtpLSDGKVDIAFI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 293 GSCTNSSLPDMLKAAKILK-----GRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGmGQAPLS 367
Cdd:pfam00330 344 GSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIG-NSDRLP 422
|
410 420 430
....*....|....*....|....*....|....*....
gi 1473349579 368 KG-VSLRTINRNFKGRSGTNdASVYLVSPEVAALSAIKG 405
Cdd:pfam00330 423 PGeRCVSSSNRNFEGRQGPG-GRTHLASPALVAAAAIAG 460
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-409 |
3.88e-143 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 422.28 E-value: 3.88e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 1 MNLAYKILSTKlkSGELV-AGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHVAV-EKAVAYIDHNmlqtgFENMDD--- 75
Cdd:PRK00402 3 MTLAEKILARH--SGRDVsPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDpSKIVIVFDHF-----VPAKDIksa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 76 --HEFIRSVAKKHGIT-FSKPGNGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQC 151
Cdd:PRK00402 76 eqQKILREFAKEQGIPnFFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 152 PSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEY 231
Cdd:PRK00402 156 PETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 232 LiQQGREEDYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILK 311
Cdd:PRK00402 236 L-KERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 312 GRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASV 390
Cdd:PRK00402 315 GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGeVCLSTTNRNFKGRMGSPESEV 394
|
410
....*....|....*....
gi 1473349579 391 YLVSPEVAALSAIKGYLTD 409
Cdd:PRK00402 395 YLASPAVAAASAVTGKITD 413
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-407 |
6.55e-133 |
|
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: 395.02 E-value: 6.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 31 LTQDSTGTMAYLQLEAMGIEHVAV-EKAVAYIDHNMLQTGFENMDDHEFIRSVAKKHGITFSKPGN-GVCHQLQLEN-FA 107
Cdd:cd01583 3 LVHDVTSPQAFEGLREAGREKVWDpEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRqGICHVILPEKgLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 108 KPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVN 187
Cdd:cd01583 83 LPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 188 KIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLiqQGRE-EDYVELKADVDATYDEEITVDLSKLVPL 266
Cdd:cd01583 163 KAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYL--KGRGkAYWKELKSDEDAEYDKVVEIDASELEPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 267 TAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAA 346
Cdd:cd01583 241 VAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1473349579 347 GARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPEVAALSAIKGYL 407
Cdd:cd01583 321 GAEVRPPGCGACLGGHMGVLAPGeRCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
29-405 |
1.27e-130 |
|
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: 389.55 E-value: 1.27e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 29 QTLTQDSTGTMAYLQLEAMG-IEHVAVEKAVAYIDHNMLQTGFE-NMDDHEFIRSVAKKHGITFSKPGNGVCHQLQLENF 106
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAaLGKVADPSQIACVHDHAVQLEKPvNNEGHKFLSFFAALQGIAFYRPGVGIIHQIMVENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 107 AKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGV 186
Cdd:cd01351 81 ALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 187 NKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGR-------EEDYVELKADVDATYDEEITVD 259
Cdd:cd01351 161 NRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRpllknlwLAFPEELLADEGAEYDQVIEID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 260 LSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGA 339
Cdd:cd01351 241 LSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGY 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1473349579 340 LADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPEVAALSAIKG 405
Cdd:cd01351 321 YEILVDSGARILPPGCGPCMGNGARLVADGeVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAG 387
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
3-409 |
5.37e-128 |
|
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: 383.33 E-value: 5.37e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 3 LAYKILSTKLKSgELVAGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHV-AVEKAVAYIDHNMLQTGFENMDDHEFIRS 81
Cdd:TIGR01343 2 IAEKILSKKSGK-EVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVwNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 82 VAKKHGI-TFSKPGNGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNL 159
Cdd:TIGR01343 81 FVKKQGIkYFYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 160 VGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLiQQGREE 239
Cdd:TIGR01343 161 TGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYL-KERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 240 DYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHV 319
Cdd:TIGR01343 240 PFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 320 SLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPEVA 398
Cdd:TIGR01343 320 RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGeVCISTSNRNFKGRMGHPNAEIYLASPATA 399
|
410
....*....|.
gi 1473349579 399 ALSAIKGYLTD 409
Cdd:TIGR01343 400 AASAVKGYIAD 410
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
1-409 |
5.27e-127 |
|
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: 381.03 E-value: 5.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 1 MNLAYKILSTKlkSGELV-AGQQIGIQIDQTLTQDSTGTMAYLQLEAMGIEHV-AVEKAVAYIDHNMLQTGFENMDDHEF 78
Cdd:TIGR02086 1 MTLAEKILSEK--VGRPVcAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVwDPEKIVIAFDHNVPPPTVEAAEMQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 79 IRSVAKKHGITFSKPGNGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRV 157
Cdd:TIGR02086 79 IREFAKRHGIKNFDVGEGICHQILAEEgYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 158 NLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGR 237
Cdd:TIGR02086 159 VVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 238 EEdYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVAT 317
Cdd:TIGR02086 239 LE-FRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 318 HVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPE 396
Cdd:TIGR02086 318 DVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGeVCLSTTNRNFKGRMGSPNAEIYLASPA 397
|
410
....*....|...
gi 1473349579 397 VAALSAIKGYLTD 409
Cdd:TIGR02086 398 TAAASAVEGYITD 410
|
|
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
1-632 |
2.51e-126 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 390.39 E-value: 2.51e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 1 MNLAYKILSTKLKS-GELVAGQQIG---------IQIDQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVaYIDHNML-QTG 69
Cdd:TIGR01340 20 LTLAEKILYSHLDDpEESLLSQDIGdvrgksylkLRPDRVAMQDASAQMALLQFMTCGLPQVAVPASI-HCDHLIVgQKG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 70 FE---------NMDDHEFIRSVAKKHGITFSKPGNGVCHQLQLENFAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAV 140
Cdd:TIGR01340 99 GDkdlaraiatNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPNAGGLGTIAIGVGGADAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 141 AMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTS 220
Cdd:TIGR01340 179 ALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSCTGMATICNMGAEIGATTS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 221 VFPTDEITKEYLIQQGREE----------DYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRG------ 284
Cdd:TIGR01340 259 IFPFNEAMSRYLKATNRAQiaedaktgqySFFKLKADEGAQYDELIEIDLSKLEPHINGPFTPDLSTPISKFKEtvqkng 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 285 --MKINQVVIGSCTNSSLPDMLKAAKILKGRR---VATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCI 359
Cdd:TIGR01340 339 wpEKLSAGLIGSCTNSSYEDMSRCASIVKDAEqagLKPKSPFYVTPGSEQIRATLERDGILQTFEKFGGIVLANACGPCI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 360 GM--GQAPLSKGVS---LRTINRNFKGRSGTNDASV-YLVSPEVAALSAIKGY-----LTDEFED----DMYL-----DD 419
Cdd:TIGR01340 419 GQwdRKDDVKKGEPntiLTSYNRNFRGRNDGNPATMnFLASPEIVTAMSYAGSltfnpLTDSLTTpdgkEFKFpapkgDE 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 420 IENTPFVKNKNFFIDEYDPQNEvymGPNIKPVPRGDKLP-----DTFKGK------VCLKVGDNISTDHIVPSdSKLLPY 488
Cdd:TIGR01340 499 LPEKGFEAGRDTFQAPPGSPNP---NVEVAVSPSSDRLQllepfEPWNGKdlsglrVLIKVTGKCTTDHISAA-GPWLKY 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 489 RSNVPHLAKFSFCKVD-------DQFYNRCIENGG--------------GFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:TIGR01340 575 KGHLDNISNNTLIGAVnaetgevNKAYDLDGSKGTipelardwkargqpWVVVAEHNYGEGSAREHAALEPRHLGGRIII 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 548 AISFARIHRSNLINNGILPLVI-NQKDYDFFNDQDEYELINLLDSVENN--KDITV-INKTNNQTITAKLK--LSPREKT 621
Cdd:TIGR01340 655 TKSFARIHETNLKKQGVLPLTFaNEADYDKIQPGDEVATLNLYEMLKNGggGEVDLrVTKKNGKVFEIKLKhtVSKDQIG 734
|
730
....*....|.
gi 1473349579 622 MIQYGGLLNAI 632
Cdd:TIGR01340 735 FFKAGSALNLM 745
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
33-630 |
3.88e-121 |
|
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: 380.99 E-value: 3.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 33 QDSTGTMAYLQLEAMG----------------------IEH-VAVEK---AVAYiDHNMlQTGFE-NMDDHEFIRSVAKK 85
Cdd:COG1048 87 QDFTGVPAVVDLAAMRdavarlggdpkkinplvpvdlvIDHsVQVDYfgtPDAL-EKNL-ELEFErNRERYQFLKWGQQA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 86 -HGITFSKPGNGVCHQLQLENFAKP-------------GKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQC 151
Cdd:COG1048 165 fDNFRVVPPGTGIVHQVNLEYLAFVvwtreedgetvayPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 152 PSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEY 231
Cdd:COG1048 245 PEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDY 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 232 LIQQGREEDYVEL-----KA--------DVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELR--------------- 283
Cdd:COG1048 325 LRLTGRSEEQIELveayaKAqglwrdpdAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKeafraalaapvgeel 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 284 ----GMKINQ---------VV---IGSCTNSSLPDMLKAAKIL------KGRRVATHVSLVIAPGSSSILAMLSKCGALA 341
Cdd:COG1048 405 dkpvRVEVDGeefelghgaVViaaITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLP 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 342 DMVAAGARILECGCGPCIGM-GqaPLSKGVSlRTI-------------NRNFKGRSGTNDASVYLVSPE-VAALsAIKGY 406
Cdd:COG1048 485 YLEALGFNVVGYGCTTCIGNsG--PLPPEIS-EAIeendlvvaavlsgNRNFEGRIHPDVKANFLASPPlVVAY-ALAGT 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 407 LTDEFEDD----------MYLDDI-----ENTPFVK---NKNFFIDEYDpqnEVYMGP---NIKPVPRGD---------- 455
Cdd:COG1048 561 VDIDLTTDplgtdkdgkpVYLKDIwpsgeEIPAAVFkavTPEMFRARYA---DVFDGDerwQALEVPAGElydwdpdsty 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 456 -----------KLPDTFKG----KVCLKVGDNISTDHIVPS-----DSKLLPY-RSNVPHLAKF-SFCK--------VDD 505
Cdd:COG1048 638 irrppffeglqLEPEPFKDikgaRVLAKLGDSITTDHISPAgaikaDSPAGRYlLEHGVEPKDFnSYGSrrgnhevmMRG 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 506 QFYNRCIEN----G--GGF---------------------------IVGGDNYGQGSSREHAALVPNYLKIKAIFAISFA 552
Cdd:COG1048 718 TFANIRIKNllapGteGGYtkhqptgevmsiydaamrykaegtplvVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFE 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 553 RIHRSNLINNGILPLV-INQKDYDFFN-DQDE-YELINLLDSVENNKDITV-INKTNNQTITAKLKL---SPREKTMIQY 625
Cdd:COG1048 798 RIHRSNLVGMGVLPLQfPEGESAESLGlTGDEtFDIEGLDEGLAPGKTVTVtATRADGSTEEFPVLHridTPVEVEYYRA 877
|
....*
gi 1473349579 626 GGLLN 630
Cdd:COG1048 878 GGILQ 882
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
33-407 |
2.55e-97 |
|
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: 304.36 E-value: 2.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 33 QDSTGTMAYLQLEAMGIEHVAVEKAVaYIDHNM-LQTGFE---------NMDDHEFIRSVAKKHGITFSKPGNGVCHQLQ 102
Cdd:cd01584 5 QDATAQMALLQFMSSGLPKVAVPSTI-HCDHLIeAQVGGEkdlkrakdiNKEVYDFLASAGAKYGIGFWKPGSGIIHQIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 103 LENFAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSV 182
Cdd:cd01584 84 LENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 183 KGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREE--------DYVELKADVDATYDE 254
Cdd:cd01584 164 KGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEiadladefKDDLLVADEGAEYDQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 255 EITVDLSKLVPLTAKPHSPDAVVPVSELRG--------MKINQVVIGSCTNSSLPDMLKAAKILK---GRRVATHVSLVI 323
Cdd:cd01584 244 LIEINLSELEPHINGPFTPDLATPVSKFKEvaekngwpLDLRVGLIGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 324 APGSSSILAMLSKCGALADMVAAGARILECGCGPCIGM----GQAPLSKGVSLRTINRNFKGRSGTNDAS-VYLVSPEVA 398
Cdd:cd01584 324 TPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwdrkDIKKGEKNTIVTSYNRNFTGRNDANPAThAFVASPEIV 403
|
....*....
gi 1473349579 399 ALSAIKGYL 407
Cdd:cd01584 404 TAMAIAGTL 412
|
|
| h_aconitase |
TIGR00139 |
homoaconitase; Homoaconitase is known only as a fungal enzyme from two species, where it is ... |
2-569 |
2.75e-83 |
|
homoaconitase; Homoaconitase is known only as a fungal enzyme from two species, where it is part of an unusual lysine biosynthesis pathway. Because this model is based on just two sequences from a narrow taxonomic range, it may not recognize distant orthologs, should any exist. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures, but 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble leuC and leuD over their lengths but are even closer to the respective domains of homoaconitase, and their identity is uncertain. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129245 [Multi-domain] Cd Length: 712 Bit Score: 276.54 E-value: 2.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 2 NLAYKIL---STKLKSGELV-AGQQIGIQIDQTLTQDSTGTMAylqLEAMGIEHVAV---EKAVAYIDHNMLQTGFENMD 74
Cdd:TIGR00139 3 NLTEKIVqkyAVGLPEGKFVhSGDYVSIKPAHCMSHDNSWPCA---LKFMGIGASKIhnpDQIVMTLDHDIQNKSDKNLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 75 DHEFIRSVAKKHGITFSKPGNGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPS 153
Cdd:TIGR00139 80 KYKNIEEFAKKHGIDFYPAGRGIGHQIMIEEgFAFPGNLAVASDSHSNMYGGLGCLGTPIVRTDAAAIWATGKTWWQIPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 154 VVRVNLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTG--EGLKELSLTDRATICNMGAELGATTSVFPTDEITKEY 231
Cdd:TIGR00139 160 VAKVEFKGQLPPGVSGKDIIVALCGLFNKDDVLNHAIEFTGseDSLNALPIDHRLTIANMTTEWGALSGLFPIDKTLIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 232 LIQQGR------------------------EEDY-VELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSEL--RG 284
Cdd:TIGR00139 240 LKGKATlaalgladgpfinpaaerfthpalEEKAeIPLKADKDAHYAKELFIDLASLSHYVSGPNSVKVANPLKDLeaQD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 285 MKINQVVIGSCTNSSLPDMLKAAKIL---------KGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGC 355
Cdd:TIGR00139 320 IKIDKAYLVSCTNSRASDIAAAADVFceaadknggKINKIAPGVEFYIAAASIEEEAAAEGNGAWEKLLEAGAIPLPAGC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 356 GPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPEVAALSAIKG-------YLTDEF--------------ED 413
Cdd:TIGR00139 400 GPCIGLGAGLLEPGeVGISASNRNFKGRMGSKDAKAYLASPAVVAASALLGkisgpaeVLSPEGwteiifgegdgikeED 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 414 DMYLDD---------IENtPFVKNKNFFIDEYDPQNEVYMGP-NIKPvprgdKLPDTFKGKVCLKVGDNISTDHIVPSDs 483
Cdd:TIGR00139 480 RMLTNEealekiigiIDD-LVADEEKNAASEAPAQEESEQGLtEILE-----GFPEEFSGELVFCDADNINTDGIYPGK- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 484 klLPYRSNVP--HLAKFSFCKVDDQFYNRCIEngGGFIVGGDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRSNLIN 561
Cdd:TIGR00139 553 --YTYQDDVPkeKMAQVCMENYDAEFRTKAHE--GDILVSGFNFGCGSSREQAATAILAKGINLVVSGSFGNIFSRNSIN 628
|
....*...
gi 1473349579 562 NGILPLVI 569
Cdd:TIGR00139 629 NALLGLEI 636
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
63-630 |
2.29e-77 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 261.48 E-value: 2.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 63 HNMLQT--GFENMDDHEFIRSVAKKHGITFSKPGNGVCHQLQLENFAKPGKTLVGSDSHTpTCGAMGMIAIGAGGLDVAV 140
Cdd:PRK11413 93 HNSLCAvgGTINEDDHVFGLSAAQKYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 141 AMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGV-NKIIEYTGEGLKELSLTDRATICNMGAELGATT 219
Cdd:PRK11413 172 QLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 220 SVFPTDEITKEYLIQQGREEDYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELR---------------- 283
Cdd:PRK11413 252 SIWQTDEEVHNWLALHGRGQDYCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNqnltdilreveieser 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 284 -----------------GMKINQVVIGSCTNSSLPDMLKAAKILKGRRV-ATHVSLVIAPGSSSILAMLSKCGALADMVA 345
Cdd:PRK11413 332 vahgkaklslldkiengRLKVQQGIIAGCSGGNYENVIAAANALRGQSCgNDTFSLSVYPSSQPVFMDLAKKGVVADLMG 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 346 AGARILECGCGPCIGMGQAPLSKGVSLRTINRNFKGRSGTND-----ASVYLV-SPEVAALSAIKGYLT-------DEFE 412
Cdd:PRK11413 412 AGAIIRTAFCGPCFGAGDTPANNGLSIRHTTRNFPNREGSKPangqmSAVALMdARSIAATAANGGYLTsateldcWDNV 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 413 DDMYLDDienTPFvKNKNFF-IDEYDPQNEVYMGPNIKPVPRGDKLPDTFKGKVCLKVGDNI-STDHIVPSdSKLLPYRS 490
Cdd:PRK11413 492 PEYAFDV---TPY-KNRVYQgFGKGATQQPLIYGPNIKDWPEMGALTDNILLKVCSKILDPVtTTDELIPS-GETSSYRS 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 491 NVPHLAKFSFCKVDDQFYNRC------------------------IENGGGFI--------VGGDNY----GQGSSREHA 534
Cdd:PRK11413 567 NPLGLAEFTLSRRDPGYVGRSkavaelenqrlagnvseltevfarIKQIAGQEhidplqteIGSMVYavkpGDGSAREQA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 535 ALVPNYLKIKAIFAISFA-RIHRSNLINNGILPLVINQkDYDFFNdqDEYELI-NLLDSVENNKD-IT--VINKTNN-QT 608
Cdd:PRK11413 647 ASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAE-EPTFEV--GDYIYIpGIRAALDNPGTtFKgyVIHEDAPvTE 723
|
650 660
....*....|....*....|...
gi 1473349579 609 ITAKLK-LSPREKTMIQYGGLLN 630
Cdd:PRK11413 724 ITLYMEsLTAEEREIIKAGCLIN 746
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
93-629 |
6.53e-73 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 251.97 E-value: 6.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 93 PGNGVCHQLQLENFAK------PGK------TLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLV 160
Cdd:PRK09277 176 PGTGICHQVNLEYLAPvvwtreDGElvaypdTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 161 GKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREED 240
Cdd:PRK09277 256 GKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 241 YVEL-----KA-------DVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRG------------------------ 284
Cdd:PRK09277 336 QVALveayaKAqglwrdpLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEafaksaelgvqgfgldeaeegedy 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 285 -MKINQVVIG---SCTNSSLPDMLKAAKIL------KGRRVATHV--SLviAPGSSSILAMLSKCGALADMVAAGARILE 352
Cdd:PRK09277 416 eLPDGAVVIAaitSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVktSL--APGSKVVTDYLEKAGLLPYLEALGFNLVG 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 353 CGCGPCIGM-GqaPLSKGVSlRTI-------------NRNFKGRSGTNDASVYLVSPE-VAALsAIKGYLTDEFE----- 412
Cdd:PRK09277 494 YGCTTCIGNsG--PLPPEIE-KAIndndlvvtavlsgNRNFEGRIHPLVKANYLASPPlVVAY-ALAGTVDIDLEkdplg 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 413 -----DDMYLDDI-----ENTPFVK---NKNFFIDEYD--------------PQNEVY-----------------MGPNI 448
Cdd:PRK09277 570 tdkdgNPVYLKDIwpsdeEIDAVVAkavKPEMFRKEYAdvfegderwnaievPEGPLYdwdpdstyirnppyfegMLAEP 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 449 KPVprgdklpDTFKG-KVCLKVGDNISTDHIVPS-------------DSKLLPY---------RSNvpHL----AKFSfc 501
Cdd:PRK09277 650 GPV-------RDIKGaRVLALLGDSITTDHISPAgaikadspagkylLEHGVEPkdfnsygsrRGN--HEvmmrGTFA-- 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 502 kvddqfyNRCIEN------GGGF---------------------------IVGGDNYGQGSSREHAALVPNYLKIKAIFA 548
Cdd:PRK09277 719 -------NIRIRNemvpgvEGGYtrhfpegevmsiydaamkykeegtplvVIAGKEYGTGSSRDWAAKGTRLLGVKAVIA 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 549 ISFARIHRSNLINNGILPLVI----NQKDYDFfnDQDEYELINLLDSVENNKDITV-INKTNNQTITAKLKL---SPREK 620
Cdd:PRK09277 792 ESFERIHRSNLVGMGVLPLQFkpgeSRKTLGL--DGTETFDIEGLEDLKPGATVTVvITRADGEVVEFPVLCridTAVEV 869
|
....*....
gi 1473349579 621 TMIQYGGLL 629
Cdd:PRK09277 870 DYYRNGGIL 878
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
31-567 |
3.71e-69 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 241.37 E-value: 3.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 31 LTQDSTGTMAYLQLEAM-------G---------------IEH-VAVEkavAYIDHNMLQtgfENMDdHEFIRSVAKKHG 87
Cdd:PRK12881 87 VMQDFTGVPALVDLAAMrdaaaeaGgdpakinplvpvdlvVDHsVAVD---YFGQKDALD---LNMK-IEFQRNAERYQF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 88 ITFSK----------PGNGVCHQLQLE--------------NFAKPgKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMA 143
Cdd:PRK12881 160 LKWGMqafdnfrvvpPGTGIMHQVNLEylarvvhtkeddgdTVAYP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAVML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 144 TGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFP 223
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 224 TDEITKEYLIQQGREEDYVEL-----KA-------DVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELR-------- 283
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEAQIALveayaKAqglwgdpKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKsafsdlfs 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 284 ------------------GMKINQVVIG---SCTNSSLPDMLKAAKIL------KGRRVATHVSLVIAPGSSSILAMLSK 336
Cdd:PRK12881 399 kpvaengfakkaqtsngvDLPDGAVAIAaitSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLER 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 337 CGALADMVAAGARILECGCGPCIGMG---QAPLSKGVSLRTI--------NRNFKGRSGTNDASVYLVSPEVAALSAIKG 405
Cdd:PRK12881 479 AGLLPYLEKLGFGIVGYGCTTCIGNSgplTPEIEQAITKNDLvaaavlsgNRNFEGRIHPNIKANFLASPPLVVAYALAG 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 406 YLT-DEFED---------DMYLDDI-----ENTPFVKNK---NFFIDEYD--------------PQNEVY---------- 443
Cdd:PRK12881 559 TVRrDLMTEplgkgkdgrPVYLKDIwpssaEIDALVAFAvdpEDFRKNYAevfkgselwaaieaPDGPLYdwdpkstyir 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 444 --------MGPnikpvprGDKLPDTFKGKVCLKVGDNISTDHIVPS-----DS---KLLPYRSNVPH-LAKFSFCKVDDQ 506
Cdd:PRK12881 639 rppffdfsMGP-------AASIATVKGARPLAVLGDSITTDHISPAgaikaDSpagKYLKENGVPKAdFNSYGSRRGNHE 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 507 ------FYNRCIEN------GGGF---------------------------IVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:PRK12881 712 vmmrgtFANVRIKNlmipgkEGGLtlhqpsgevlsiydaamryqaagtplvVIAGEEYGTGSSRDWAAKGTRLLGVKAVI 791
|
730 740
....*....|....*....|
gi 1473349579 548 AISFARIHRSNLINNGILPL 567
Cdd:PRK12881 792 AESFERIHRSNLVGMGVLPL 811
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
93-630 |
1.76e-68 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 239.53 E-value: 1.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 93 PGNGVCHQLQLENFAK----------PgKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGK 162
Cdd:PTZ00092 182 PGSGIVHQVNLEYLARvvfnkdgllyP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 163 KAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREEDYV 242
Cdd:PTZ00092 261 LSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEEKV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 243 E-----LKA-------DVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSEL-----------------------RGMKI 287
Cdd:PTZ00092 341 EliekyLKAnglfrtyAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLkkdftaclsapvgfkgfgipeekHEKKV 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 288 N-------------QVVIG---SCTNSSLPDMLKAAKIL------KGRRVATHVSLVIAPGSSSILAMLSKCGALADMVA 345
Cdd:PTZ00092 421 KftykgkeytlthgSVVIAaitSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 346 AGARILECGCGPCIGmGQAPLSKGVSlRTI-------------NRNFKGRSGTNDASVYLVSPEVAALSAIKGYLTDEFE 412
Cdd:PTZ00092 501 LGFYTAGYGCMTCIG-NSGDLDPEVS-EAItnndlvaaavlsgNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNIDFE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 413 DDMYLDDIENTP-FVKN---KNFFIDEYDPQ-------NEVYmgPNIK---------PVPRGDKL-----------PDTF 461
Cdd:PTZ00092 579 TEPLGSDKTGKPvFLRDiwpSREEIQALEAKyvkpemfKEVY--SNITqgnkqwnelQVPKGKLYewdekstyihnPPFF 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 462 KGK--------------VCLKVGDNISTDHIVPS-----DSKLLPY-----------------RSNVPHLAKFSFCKVdd 505
Cdd:PTZ00092 657 QTMelepppiksienayCLLNLGDSITTDHISPAgniakNSPAAKYlmergverkdfntygarRGNDEVMVRGTFANI-- 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 506 QFYNRCIENGGGF---------------------------IVGGDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRSN 558
Cdd:PTZ00092 735 RLINKLCGKVGPNtvhvptgekmsiydaaekykqegvpliVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSN 814
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1473349579 559 LINNGILPL-VINQKDYDFFN-DQDEYELINLLDS-VENNKDITVINkTNNQTITAKLKL-SPREKTMIQYGGLLN 630
Cdd:PTZ00092 815 LVGMGILPLqFLNGENADSLGlTGKEQFSIDLNSGeLKPGQDVTVKT-DTGKTFDTILRIdTEVEVEYFKHGGILQ 889
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
27-409 |
2.78e-68 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 230.01 E-value: 2.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 27 IDQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHN-----------------MLQTGFENmddhefirsvAKKHGIT 89
Cdd:PRK05478 27 IDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNvpttdrdlpiadpvsriQVETLEKN----------CKEFGIT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 90 FSKPG---NGVCHQLQLEN-FAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAK 165
Cdd:PRK05478 97 LFDLGdprQGIVHVVGPEQgLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 166 WASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLiqQGRE------- 238
Cdd:PRK05478 177 GVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYL--KGRPfapkged 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 239 -EDYVE----LKADVDATYDEEITVDLSKLVPL----TakphSPDAVVPVSE---------------------------- 281
Cdd:PRK05478 255 wDKAVAywktLKSDEDAVFDKVVTLDAADIEPQvtwgT----NPGQVISIDGkvpdpedfadpvkrasaeralaymglkp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 282 ---LRGMKINQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGaLADM-VAAGARILECGCGP 357
Cdd:PRK05478 331 gtpITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEG-LDKIfIEAGFEWREPGCSM 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1473349579 358 CIGMGQAPLSKG---VSlrTINRNFKGRSGtNDASVYLVSPEVAALSAIKGYLTD 409
Cdd:PRK05478 410 CLAMNPDKLPPGercAS--TSNRNFEGRQG-KGGRTHLVSPAMAAAAAITGHFVD 461
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
31-407 |
7.68e-68 |
|
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: 225.57 E-value: 7.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 31 LTQDSTGTMAylqLEAMGIEHVAV---EKAVAYIDHNMLQTGFENMDDHEFIRSVAKKHGITFSKPGNGVCHQLQLEN-F 106
Cdd:cd01582 3 MTHDNSWPVA---LKFMSIGATKIhnpDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIGHQIMIEEgY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 107 AKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVILYILQQLSVKGGV 186
Cdd:cd01582 80 AFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 187 NKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEitkeyliqqgreedyvelkadvdatydEEITVDLSKLVPL 266
Cdd:cd01582 160 NHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA---------------------------KHLILDLSTLSPY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 267 TAKPHSPDAVVPVSEL--RGMKINQVVIGSCTNSSLPDMLKAAKILKGRR-------VATHVSLVIAPGSSSILAMLSKC 337
Cdd:cd01582 213 VSGPNSVKVSTPLKELeaQNIKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKN 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1473349579 338 GALADMVAAGARILECGCGPCIGMGQAPLSKG-VSLRTINRNFKGRSGTNDASVYLVSPEVAALSAIKGYL 407
Cdd:cd01582 293 GDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGeVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
25-409 |
1.66e-66 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 225.17 E-value: 1.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 25 IQIDQTLTQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHN----------MLQTGFENMDDHefIRSVAKKHGITF---S 91
Cdd:PRK12466 26 LYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVvptrpgrdrgITDPGGALQVDY--LRENCADFGIRLfdvD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 92 KPGNGVCHQLQLE-NFAKPGKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAK 170
Cdd:PRK12466 104 DPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 171 DVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLiqQGRE------------ 238
Cdd:PRK12466 184 DLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYL--RGRPrapkgalwdaal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 239 EDYVELKADVDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSE-------------------------------LRGMKI 287
Cdd:PRK12466 262 AYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGrvpdpaaeadparraameraldymgltpgtpLAGIPI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 288 NQVVIGSCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGMGQAPLS 367
Cdd:PRK12466 342 DRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLA 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1473349579 368 KG---VSlrTINRNFKGRSGTnDASVYLVSPEVAALSAIKGYLTD 409
Cdd:PRK12466 422 PGercAS--TTNRNFEGRQGP-GARTHLMSPAMVAAAAVAGHITD 463
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
93-635 |
5.86e-54 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 198.88 E-value: 5.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 93 PGNGVCHQLQLENFAK----------PgKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGK 162
Cdd:PLN00070 214 PGSGIVHQVNLEYLGRvvfntdgilyP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 163 KAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDEITKEYLIQQGREEDYV 242
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 243 E-----LKAD----------VDATYDEEITVDLSKLVPLTAKPHSPDAVVPVSELRG----------------------- 284
Cdd:PLN00070 373 AmieayLRANkmfvdynepqQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKAdwhscldnkvgfkgfavpkeaqs 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 285 -------------MKINQVVIG---SCTNSSLPD-MLKAAKILK-----GRRVATHVSLVIAPGSSSILAMLSKCGALAD 342
Cdd:PLN00070 453 kvakfsfhgqpaeLRHGSVVIAaitSCTNTSNPSvMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKY 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 343 MVAAGARILECGCGPCIGMG---QAPLSKGVSLRTI--------NRNFKGRSGTNDASVYLVSPEVAALSAIKGYLTDEF 411
Cdd:PLN00070 533 LNQQGFHIVGYGCTTCIGNSgelDESVASAITENDIvaaavlsgNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDF 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 412 E----------DDMYLDDI-----ENTPFVKNK---NFFIDEYDPQNEVYMGPNIKPVPRGDKL-----------PDTFK 462
Cdd:PLN00070 613 EkepigtgkdgKDVFFRDIwpsneEVAEVVQSSvlpDMFKSTYEAITKGNPMWNQLSVPSGTLYswdpkstyihePPYFK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 463 GKV-------------C-LKVGDNISTDHIVPSDS--------------------------------------------- 483
Cdd:PLN00070 693 NMTmsppgphgvkdayClLNFGDSITTDHISPAGSihkdspaakylmergvdrkdfnsygsrrgndeimargtfaniriv 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 484 -KLL-----PYRSNVPHLAKFSFCKVDDQFYNrciENGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRS 557
Cdd:PLN00070 773 nKLLkgevgPKTVHIPTGEKLSVFDAAMKYKS---EGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRS 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 558 NLINNGILPLVINQ-KDYDFF--NDQDEY--ELINLLDSVENNKDITVINKtNNQTITAKLKLSPR-EKTMIQYGGLLN- 630
Cdd:PLN00070 850 NLVGMGIIPLCFKSgEDADTLglTGHERYtiDLPSNISEIKPGQDVTVTTD-NGKSFTCTLRFDTEvELAYFDHGGILPy 928
|
....*
gi 1473349579 631 AIKEL 635
Cdd:PLN00070 929 VIRNL 933
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
468-587 |
2.61e-51 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 173.01 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 468 KVGDNISTDHIVPSDSKLLPYRSNVPHLAKFSFCKVDDQFYNRCIENGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:cd01579 1 KVGDNITTDHIMPAGAKVLPLRSNIPAISEFVFHRVDPTFAERAKAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1473349579 548 AISFARIHRSNLINNGILPLVI-NQKDYDFFNDQDEYELIN 587
Cdd:cd01579 81 AKSFARIHRANLINFGILPLTFaDEDDYDRFEQGDQLELPL 121
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
93-405 |
1.47e-49 |
|
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: 177.88 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 93 PGNGVCHQLQLENFAK--------------PgKTLVGSDSHTPTCGAMGMIAIGAGGLDVAVAMATGTYYLQCPSVVRVN 158
Cdd:cd01586 91 PGTGIIHQVNLEYLARvvftseedgdgvayP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 159 LVGKKAKWASAKDVILYILQQLSVKGGVNKIIEYTGEGLKELSLTDRATICNMGAELGATTSVFPTDeitkeyliqqgre 238
Cdd:cd01586 170 LTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 239 edyvelkadvdatyDEEITVDLSKLVPLTAKPHSPDAVVPVSelrgmkiNQVVIG---SCTNSSLPDMLKAAKIL----- 310
Cdd:cd01586 237 --------------TQVVELDLSTVEPSVSGPKRPQDRVPLH-------GSVVIAaitSCTNTSNPSVMLAAGLLakkav 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 311 -KGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGmGQAPLSKGVSlRTI-------------N 376
Cdd:cd01586 296 eLGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG-NSGPLPEEVE-EAIkendlvvaavlsgN 373
|
330 340
....*....|....*....|....*....
gi 1473349579 377 RNFKGRSGTNDASVYLVSPEVAALSAIKG 405
Cdd:cd01586 374 RNFEGRIHPLVRANYLASPPLVVAYALAG 402
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
92-407 |
5.69e-38 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 150.71 E-value: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 92 KPGNGVCHQLqLENFAKPGKTLVGSDSHT--PtcgaMGmIAIGAG-GLdVAVAMATGTYYLQCPSVVRVNLVGKKAKWAS 168
Cdd:PRK09238 462 RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfP----IG-ISFPAGsGL-VAFAAATGVMPLDMPESVLVRFKGEMQPGIT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 169 AKDVI----LYILQQ--LSV--KGGVN----KIIEYtgEGLKELS------LTDrATicnmgAELGATTSVFPTDEIT-K 229
Cdd:PRK09238 535 LRDLVhaipYYAIKQglLTVekKGKKNifsgRILEI--EGLPDLKveqafeLTD-AS-----AERSAAGCTIKLSKEPiI 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 230 EYL------IQQGREEDY--------------------VELKADVDATYDEEITVDLSKLV-PLTAKPHSPDAVVPVSEL 282
Cdd:PRK09238 607 EYLrsnivlLKWMIAEGYgdartlerriaameewlanpELLEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEV 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 283 RGMKINQVVIGSC-TNssLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCigM 361
Cdd:PRK09238 687 AGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLC--M 762
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1473349579 362 G-QAPLSKGVS-LRTINRNFKGRSGtNDASVYLVSPEVAALSAIKGYL 407
Cdd:PRK09238 763 GnQARVADGATvFSTSTRNFPNRLG-KGANVYLGSAELAAVCALLGRI 809
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
32-407 |
9.56e-36 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 139.94 E-value: 9.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 32 TQDSTGTMAYLQLEAMGIEHVAVEKAVAYIDHNMLQTGFENMDDHEFIRSVAKKHGITFSKPGNGVCHQLqLENFAKPGK 111
Cdd:cd01581 30 SQDTTGPMTRDELKELACLGFSADLVMQSFCHTAAYPKPVDVKTHRTLPDFISNRGGVALRPGDGVIHSW-LNRMLLPDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 112 TLVGSDSHTPTcgAMGmIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVI----LYILQQ--LSV--K 183
Cdd:cd01581 109 VGTGGDSHTRF--PIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVnaipYYAIQQglLTVekK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 184 GGVN----KIIEYtgEGLKELSLTDRATICNMGAELGATTSVFPTDEIT-KEYL----------IQQGRE---------- 238
Cdd:cd01581 186 GKKNvfngRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLDKEPvIEYLesnvvlmkimIANGYDdartllrrii 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 239 --EDYVE----LKADVDATYDEEITVDLSKLV-PLTAKPHSPDAVVPVSELRGMKINQVVIGSC-TNssLPDMLKAAKIL 310
Cdd:cd01581 264 amEEWLAnpplLEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 311 KGRRVAThVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGmGQAPLSKGVS-LRTINRNFKGRSGTnDAS 389
Cdd:cd01581 342 RGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMG-NQARVADGATvFSTSTRNFDNRVGK-GAE 418
|
410
....*....|....*...
gi 1473349579 390 VYLVSPEVAALSAIKGYL 407
Cdd:cd01581 419 VYLGSAELAAVCALLGRI 436
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
462-636 |
3.07e-31 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 119.55 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 462 KGKVcLKVGDNISTDHIVPSdsKLLPYrSNVPHLAKFSFCKVDDQFYNRCieNGGGFIVGGDNYGQGSSREHAALVPNYL 541
Cdd:PRK00439 1 KGRV-WKFGDNIDTDVIIPA--RYLNT-SDPQELAKHCMEDLDPEFAKKV--KPGDIIVAGKNFGCGSSREHAPIALKAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 542 KIKAIFAISFARIHRSNLINNGiLPLVINQKDYDFFNDQDEYELinlldSVENNkdiTVINKTNNQTITAK-LKLSPREk 620
Cdd:PRK00439 75 GVSAVIAKSFARIFYRNAINIG-LPVLECDEAVDKIEDGDEVEV-----DLETG---VITNLTTGEEYKFKpIPEFMLE- 144
|
170
....*....|....*.
gi 1473349579 621 tMIQYGGLLNAIKELG 636
Cdd:PRK00439 145 -ILKAGGLIEYLKKKG 159
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
32-423 |
2.46e-26 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 115.02 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 32 TQDSTGTMAYLQLEAMGI-------------EHVAVEKAVAYIDHNMLQTgfenmddheFIRSvakKHGITFsKPGNGVC 98
Cdd:PLN00094 476 SQDTTGPMTRDELKDLAClgfsadlvmqsfcHTAAYPKPVDVVTHHTLPD---------FIRN---RGGVSL-RPGDGVI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 99 HQLqLENFAKPGKTLVGSDSHT--PtcgaMGmIAIGAGGLDVAVAMATGTYYLQCPSVVRVNLVGKKAKWASAKDVI--- 173
Cdd:PLN00094 543 HSW-LNRMLLPDTVGTGGDSHTrfP----IG-ISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVhai 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 174 -LYILQQ--LSV--KGGVN----KIIEYtgEGLKELSLTDRATICNMGAELGATTSVFPTD-EITKEYL----------I 233
Cdd:PLN00094 617 pYTAIQDglLTVekKGKKNvfsgRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDkEPIIEYLnsnvvmlkwmI 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 234 QQG------------REEDYVE----LKADVDATYDEEITVDLSKLV-PLTAKPHSPDAVVPVSELRGMKINQVVIGSCT 296
Cdd:PLN00094 695 AEGygdrrtlerriaRMQQWLAdpelLEADPDAEYAAVIEIDMDEIKePILCAPNDPDDARLLSEVTGDKIDEVFIGSCM 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 297 nSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALADMVAAGARILECGCGPCIGmGQAPLSKGVS-LRTI 375
Cdd:PLN00094 775 -TNIGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTvVSTS 852
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1473349579 376 NRNFKGRSGTNdASVYLVSPEVAALSAIKGYLTDEFEDDMYLDDIENT 423
Cdd:PLN00094 853 TRNFPNRLGKG-ANVYLASAELAAVAAILGRLPTVEEYLSYMEKLDAT 899
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
460-626 |
3.48e-22 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 94.47 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 460 TFKGKVCLKVGDNISTDHIVPSDskllpY--RSNVPHLAKFSFckvDDQFYNRCIE----------NGGGFIVGGDNYGQ 527
Cdd:COG0066 5 TLTGRAVPLDGDNIDTDQIIPAR-----FlkTIDREGLGKHLF---EDWRYDRSPDpdfvlnqpryQGADILVAGRNFGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 528 GSSREHAALVpnyLK---IKAIFAISFARIHRSNLINNGILPLVINQKDYD----FFNDQDEYEL-INLldsvENNkdiT 599
Cdd:COG0066 77 GSSREHAPWA---LKdygFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDalfaAIEANPGDELtVDL----EAG---T 146
|
170 180
....*....|....*....|....*..
gi 1473349579 600 VINKTnnqTITAKLKLSPREKTMIQYG 626
Cdd:COG0066 147 VTNGT---GETYPFEIDPFRRECLLNG 170
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
468-587 |
9.22e-21 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 87.14 E-value: 9.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 468 KVGDNISTDHIVPSdskllpyrsnvphlakfsfckvddqfynrcienGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:cd00404 1 KVAGNITTDHISPA---------------------------------GPGVVIGDENYGTGSSREHAALELRLLGGRAVI 47
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1473349579 548 AISFARIHRSNLINNGILPL-VINQKDYDFFNDQDEYELIN 587
Cdd:cd00404 48 AKSFARIFFRNLVDQGLLPLeFADPEDYLKLHTGDELDIYP 88
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
463-633 |
1.41e-20 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 88.63 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 463 GKVcLKVGDNISTDHIVPSdskllPY--RSNVPHLAKFSFCKVDDQFYNRCIEngGGFIVGGDNYGQGSSREHAALVPNY 540
Cdd:TIGR02087 1 GRV-WKFGDDIDTDEIIPG-----RYlrTTDPDELASHAMEGIDPEFAKKVRP--GDVIVAGKNFGCGSSREQAALALKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 541 LKIKAIFAISFARIHRSNLINNGiLPLVINQKdydffndqdeyELINLLDSVENNKDITVINKTNNQTITAKlKLSPREK 620
Cdd:TIGR02087 73 AGIAAVIAESFARIFYRNAINIG-LPLIEAKT-----------EGIKDGDEVTVDLETGEIRVNGNEEYKGE-PLPDFLL 139
|
170
....*....|...
gi 1473349579 621 TMIQYGGLLNAIK 633
Cdd:TIGR02087 140 EILREGGLLEYLK 152
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
519-571 |
3.69e-20 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 86.65 E-value: 3.69e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1473349579 519 IVGGDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRSNLINNGILPLVINQ 571
Cdd:pfam00694 78 VIGGKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPE 130
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
468-588 |
4.42e-19 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 82.25 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 468 KVGDNISTDHIVPSdskllpyrsnvphlakfsfckvddQFYnrciengGGFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:cd01577 1 LFGDNIDTDQIIPA------------------------RFL-------GDIIVAGKNFGCGSSREHAPWALKDAGIRAVI 49
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1473349579 548 AISFARIHRSNLINNGILPLVINQKDYD--FFNDQDEYElINL 588
Cdd:cd01577 50 AESFARIFFRNAINNGLLPVTLADEDVEevEAKPGDEVE-VDL 91
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
513-590 |
3.46e-17 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 78.66 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 513 ENGGGFIVGGD-NYGQGSSREHAALVPNYLKIKAIFAISFARIHRSNLINNGILPLVI-NQKDYDFFNDQDEYELINLLD 590
Cdd:cd01578 66 AHGIKWVVIGDeNYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFaDPADYDKIHPDDKVDILGLTD 145
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
468-585 |
1.02e-16 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 77.92 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 468 KVGDNISTDHIVPSdsKLLPYRSNVPHLAKFSFCKVDDQFYNRCieNGGGFIVGGDNYGQGSSREHAALVPNYLKIKAIF 547
Cdd:PRK14023 6 KFGDNINTDDILPG--KYAPFMVGEDRFHNYAFAHLRPEFASTV--RPGDILVAGRNFGLGSSREYAPEALKMLGIGAII 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1473349579 548 AISFARIHRSNLINNGIlPLVINQKDYDFFNDQDEYEL 585
Cdd:PRK14023 82 AKSYARIFYRNLVNLGI-PPFESEEVVDALEDGDEVEL 118
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
468-567 |
3.68e-15 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 73.46 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 468 KVGDNISTDHIVPS-----DSKLLPY-----------------RSNVPHLAKFSFCKVddQFYNRCIENGGG-------- 517
Cdd:cd01580 1 LLGDSVTTDHISPAgsiakDSPAGKYlaergvkprdfnsygsrRGNDEVMMRGTFANI--RLRNKLVPGTEGgtthhppt 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 518 --------------------FIVGGDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRSNLINNGILPL 567
Cdd:cd01580 79 gevmsiydaamrykeegvplVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPL 148
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
454-567 |
2.86e-14 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 72.97 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 454 GDKLPDTFKGKvCLKVGDNISTDHIVPSDskllpYRSNVP-------HLAKFSFCKVDDQFYNRCIENGG-----GFIVG 521
Cdd:PLN00072 62 ESTSSTTFHGL-CFVVGDNIDTDQIIPAE-----YLTLVPskpdeyeKLGSYALIGLPAFYKTRFVEPGEmktkySIIIG 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1473349579 522 GDNYGQGSSREHAALVPNYLKIKAIFAISFARIHRSNLINNG-ILPL 567
Cdd:PLN00072 136 GENFGCGSSREHAPVALGAAGAKAVVAESYARIFFRNSVATGeVYPL 182
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
460-611 |
2.47e-12 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 66.30 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 460 TFKGKVCLKVGDNISTDHIVP-----------------SDSKLLPYRSNVPHlakFSFckvddqfyNRCIENGGGFIVGG 522
Cdd:PRK01641 6 THTGLAVPLDRANVDTDQIIPkqflkritrtgfgkglfDDWRYLDDGQPNPD---FVL--------NQPRYQGASILLAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 523 DNYGQGSSREHA--ALVpNYlKIKAIFAISFARIHRSNLINNGILPLVINQKDYDFfndqdeyelinLLDSVENNKDITV 600
Cdd:PRK01641 75 DNFGCGSSREHApwALA-DY-GFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDE-----------LFKLVEANPGAEL 141
|
170
....*....|.
gi 1473349579 601 INKTNNQTITA 611
Cdd:PRK01641 142 TVDLEAQTVTA 152
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
471-572 |
3.16e-08 |
|
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238837 [Multi-domain] Cd Length: 129 Bit Score: 52.68 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 471 DNISTDHIVPSDsklLPYRSNVP--HLAKFSFCKVDDQFYNRCIEngGGFIVGGDNYGQGSSREHAALVPNYLKIKAIFA 548
Cdd:cd01674 4 DNLNTDGIYPGK---YTYQDDITpeKMAEVCMENYDSEFSTKTKQ--GDILVSGFNFGTGSSREQAATALLAKGIPLVVS 78
|
90 100
....*....|....*....|....
gi 1473349579 549 ISFARIHRSNLINNGILPLVINQK 572
Cdd:cd01674 79 GSFGNIFSRNSINNALLSIELPFL 102
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
528-568 |
3.23e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 40.86 E-value: 3.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1473349579 528 GSSREHAALVPNYLKIKAIFAISFARIHRSNLINNGILPLV 568
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIV 43
|
|
| AcnX |
cd01355 |
Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted ... |
212-370 |
3.48e-03 |
|
Putative Aconitase X catalytic domain; Putative Aconitase X catalytic domain. It is predicted by comparative genomic analysis. The proteins are mainly found in archaea and proteobacteria. They are distantly related to Aconitase family of proteins by sequence similarity and seconary structure prediction. The functions have not yet been experimentally characterized. Thus, the prediction should be treated with caution.
Pssm-ID: 153130 Cd Length: 389 Bit Score: 40.04 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 212 GAELGATTSV--FPTDEITKEYLIQQGREEDYVEL-KADVDATYDEeitvdlsklvpLTAKPHSPDAVVpvselrgmkin 288
Cdd:cd01355 226 GAAMATSGSVamFHIVGVTPEAPTLGLDAAETVELtRADLDEAREN-----------LNADGSEPDLVV----------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1473349579 289 qvvIGsCTNSSLPDMLKAAKILKGRRVATHVSLVIAPGSSSILAMLSKCGALAdmvAAGARILECGCgPCIGMGQAPLSK 368
Cdd:cd01355 284 ---LG-CPHASLEELRKLADLLAGRRVAPSVPLYVTTSRAVYAKRMGYVDVIE---KLGARVLTDTC-MVVSPVNEPNGY 355
|
..
gi 1473349579 369 GV 370
Cdd:cd01355 356 KN 357
|
|
| |
