|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
10-961 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1346.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 10 FEYLIETLNDSSRKKFFDVSKLG-TKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDWK-TKQSNVEVPFFPARVLL 87
Cdd:PTZ00092 16 FEKVLKTLKDGGSYKYYSLNELHdPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEeNSKKQIEIPFKPARVLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 88 QDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKcaiqnapnpgggdlqkagklsplkvqpkklp 167
Cdd:PTZ00092 96 QDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSR------------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 168 crgqttcrgscdsgelgrnsgtfssqientpilcpfhlqpvpEPETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPP 247
Cdd:PTZ00092 145 ------------------------------------------SPDALELNQEIEFERNLERFEFLKWGSKAFKNLLIVPP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 248 GTGMAHQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSN 327
Cdd:PTZ00092 183 GSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 328 PFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLES 407
Cdd:PTZ00092 263 EHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSEEKVEL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 408 METYLKAVKLFRNDQNssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDI 487
Cdd:PTZ00092 343 IEKYLKANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSAPVGFKGFGIPEEKHEKK 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 488 VSIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLS 567
Cdd:PTZ00092 420 VKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLE 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 568 KLGFEIVGYGCSTCVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQT 647
Cdd:PTZ00092 500 KLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGRVNIDFET 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 648 EPLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKL 727
Cdd:PTZ00092 580 EPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGKLYEWDEKSTYIHNPPFFQTM 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 728 TKEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNK 807
Cdd:PTZ00092 660 ELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGARRGNDEVMVRGTFANIRLINK 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 808 FIGKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIG 887
Cdd:PTZ00092 740 LCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMG 819
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114658342 888 IAPLQFLPGENADSLGLSGRETFSLTFPE-ELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARK 961
Cdd:PTZ00092 820 ILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEVEYFKHGGILQYVLRK 894
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
24-962 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1259.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 24 KFFDVSKL----GTKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDW-KTKQSNVEVPFFPARVLLQDFTGIPAMVD 98
Cdd:PRK09277 21 DYYSLRALeakgLGDISRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWlPKAKPDREIPFRPARVVMQDFTGVPAVVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 99 FAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFskcaiqnapnpgGGDlqkagklsplkvqpkklpcrgqttcrgsc 178
Cdd:PRK09277 101 LAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDY------------FGT----------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 179 dsgelgrnsgtfssqientpilcpfhlqpvpePETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLE 258
Cdd:PRK09277 140 --------------------------------PDAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVPPGTGICHQVNLE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 259 YLSRVVFEEKD---LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDV 335
Cdd:PRK09277 188 YLAPVVWTREDgelVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 336 VLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYLKAV 415
Cdd:PRK09277 268 VLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEEQVALVEAYAKAQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 416 KLFRNDqnsSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQAclNEKVGFKGFQIAAEKqkdivsihyEGS 495
Cdd:PRK09277 348 GLWRDP---LEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAK--SAELGVQGFGLDEAE---------EGE 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 496 EYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVG 575
Cdd:PRK09277 414 DYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFNLVG 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 576 YGCSTCVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDPT 655
Cdd:PRK09277 494 YGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVVAYALAGTVDIDLEKDPLGTDKD 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 656 GKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPIALQ 735
Cdd:PRK09277 574 GNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDPDSTYIRNPPYFEGMLAEPGPVR 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 736 AIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GKPAP 814
Cdd:PRK09277 654 DIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVpGVEGG 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 815 KTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFL 894
Cdd:PRK09277 734 YTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFK 813
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 114658342 895 PGENADSLGLSGRETFSLTFPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNFVARKF 962
Cdd:PRK09277 814 PGESRKTLGLDGTETFDIEGLEDLKPGatVTVVITRADGEVveFPVLCRIDTAVEVDYYRNGGILQYVLRDL 885
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
16-962 |
0e+00 |
|
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: 1246.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 16 TLNDSSRK-KFFDVSKL---GTKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDW-KTKQSNVEVPFFPARVLLQDF 90
Cdd:COG1048 10 TLTVGGKPyTYYSLPALeeaGGDISRLPYSLKILLENLLRNEDGETVTEEDIKALANWlPKARGDDEIPFRPARVLMQDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 91 TGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSkcaiqnapnpgggdlqkagklsplkvqpkklpcrg 170
Cdd:COG1048 90 TGVPAVVDLAAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYF----------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 171 qttcrGSCDSGElgrnsgtfssqientpilcpfhlqpvpepetvlKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTG 250
Cdd:COG1048 135 -----GTPDALE---------------------------------KNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 251 MAHQINLEYLSRVVFEEKD----LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSS 326
Cdd:COG1048 177 IVHQVNLEYLAFVVWTREEdgetVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 327 NPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLE 406
Cdd:COG1048 257 PEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEEQIE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 407 SMETYLKAVKLFRNDqnSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGfkgfqiaaEKQKD 486
Cdd:COG1048 337 LVEAYAKAQGLWRDP--DAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG--------EELDK 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 487 IVSIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYL 566
Cdd:COG1048 407 PVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYL 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 567 SKLGFEIVGYGCSTCVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQ 646
Cdd:COG1048 487 EALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALAGTVDIDLT 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 647 TEPLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDK 726
Cdd:COG1048 567 TDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYIRRPPFFEG 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 727 LTKEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFN 806
Cdd:COG1048 647 LQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGTFANIRIKN 726
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 807 KFI-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIG 885
Cdd:COG1048 727 LLApGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVG 806
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 886 IGIAPLQFLPGENADSLGLSGRETFSLT-FPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNFVAR 960
Cdd:COG1048 807 MGVLPLQFPEGESAESLGLTGDETFDIEgLDEGLAPGktVTVTATRADGSTeeFPVLHRIDTPVEVEYYRAGGILQYVLR 886
|
..
gi 114658342 961 KF 962
Cdd:COG1048 887 QL 888
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
30-962 |
0e+00 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 1133.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 30 KLGTKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDWKTKQ-SNVEVPFFPARVLLQDFTGIPAMVDFAAMREAVKT 108
Cdd:TIGR01341 13 ESGGKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEvADTEIAFKPARVVMQDFTGVPAVVDLAAMREAMKN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 109 LGGDPEKVHPACPTDLTVDHSLQIDfskcaiqnapnpgggdlqKAGklsplkvqpkklpcrgqttcrgscdsgelgrnsg 188
Cdd:TIGR01341 93 LGGDPKKINPLVPVDLVIDHSVQVD------------------YYG---------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 189 tfssqientpilcpfhlqpvpEPETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLEYLSRVVFEE- 267
Cdd:TIGR01341 121 ---------------------TEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGIIHQVNLEYLATVVFKAe 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 268 ---KDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLR 344
Cdd:TIGR01341 180 vdgELTAYPDSLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPYYMNVPEVIGVKLTGKLQEGVTATDLVLTVTQMLR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 345 QVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYLKAVKLFRNDqns 424
Cdd:TIGR01341 260 KKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTGRDGDHVELVEKYARAQGLFYDD--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 425 SGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVsihyEGSEYKLSHGSV 504
Cdd:TIGR01341 337 SEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTLRKEPLKKKV----NGQNKQLEDGAV 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 505 VIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTCVGN 584
Cdd:TIGR01341 413 VIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAESGLLPYLEELGFNLVGYGCTTCIGN 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 585 TAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDPTGKNIYLHDI 664
Cdd:TIGR01341 493 SGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAGNIDINLYTEPIGTDKDGKPVYLRDI 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 665 WPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIENAHVLL 744
Cdd:TIGR01341 573 WPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIRLPPFFEEMKQDPEEVEDIKGARILL 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 745 YLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GKPAPKTIHFPSGQ 823
Cdd:TIGR01341 653 LLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTFANIRIKNLMVkGKEGGYTVHFPDGK 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 824 TLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLG 903
Cdd:TIGR01341 733 VASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERIHRSNLVGMGVIPLQFPQGEDAETLG 812
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114658342 904 LSGRETFSLTFPEELSPGITLNIQTSTGK----VFSVIASFEDDVEITLYKHGGLLNFVARKF 962
Cdd:TIGR01341 813 LTGDETIDIDGIKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHGGILQYVLRKF 875
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
24-963 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1121.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 24 KFFDVSKLG-TKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDW-KTKQSNVEVPFFPARVLLQDFTGIPAMVDFAA 101
Cdd:PLN00070 62 KYYSLPALNdPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWeNTSPKQVEIPFKPARVLLQDFTGVPAVVDLAC 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 102 MREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKCAiqNApnpgggdlqkagklsplkvqpkklpcrgqttcrgscdsg 181
Cdd:PLN00070 142 MRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSE--NA--------------------------------------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 182 elgrnsgtfssqientpilcpfhlqpvpepetVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLEYLS 261
Cdd:PLN00070 181 --------------------------------VQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 262 RVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 341
Cdd:PLN00070 229 RVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 342 HLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYLKAVKLFRND 421
Cdd:PLN00070 309 MLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 422 QNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVSIHYEGSEYKLSH 501
Cdd:PLN00070 389 NEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVGFKGFAVPKEAQSKVAKFSFHGQPAELRH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 502 GSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTC 581
Cdd:PLN00070 469 GSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTC 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 582 VGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDPTGKNIYL 661
Cdd:PLN00070 549 IGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFF 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 662 HDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIENAH 741
Cdd:PLN00070 629 RDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVPSGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAY 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 742 VLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GKPAPKTIHFP 820
Cdd:PLN00070 709 CLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLLkGEVGPKTVHIP 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 821 SGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENAD 900
Cdd:PLN00070 789 TGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDAD 868
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114658342 901 SLGLSGRETFSLTFP---EELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARKFS 963
Cdd:PLN00070 869 TLGLTGHERYTIDLPsniSEIKPGQDVTVTTDNGKSFTCTLRFDTEVELAYFDHGGILPYVIRNLI 934
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
13-962 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1104.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 13 LIETLNDSSRKKFFDV----SKLGTKYDVLPYSIRVLLEAAVRNCDGFLMTKEDVMNILDWK-TKQSNVEVPFFPARVLL 87
Cdd:PRK12881 9 LKEFDVGGKTYKFYSLpalgKELGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLpERKSDDEIPFVPARVVM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 88 QDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFskcaiqnapnpgGGDlqkagklsplkvqpkklp 167
Cdd:PRK12881 89 QDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDY------------FGQ------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 168 crgqttcrgscdsgelgrnsgtfssqientpilcpfhlqpvpePETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPP 247
Cdd:PRK12881 139 -------------------------------------------KDALDLNMKIEFQRNAERYQFLKWGMQAFDNFRVVPP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 248 GTGMAHQINLEYLSRVVFEEKD----LLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELT 323
Cdd:PRK12881 176 GTGIMHQVNLEYLARVVHTKEDdgdtVAYPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 324 GSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKA 403
Cdd:PRK12881 256 GKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 404 KLESMETYLKAVKLFRNDQNssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEk 483
Cdd:PRK12881 336 QIALVEAYAKAQGLWGDPKA---EPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKAQ- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 484 qkdivsihyEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVL 563
Cdd:PRK12881 412 ---------TSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLL 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 564 PYLSKLGFEIVGYGCSTCVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNI 643
Cdd:PRK12881 483 PYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANFLASPPLVVAYALAGTVRR 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 644 DFQTEPLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSF 723
Cdd:PRK12881 563 DLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPDGPLYDWDPKSTYIRRPPF 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 724 FDKLTKEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIK 803
Cdd:PRK12881 643 FDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYGSRRGNHEVMMRGTFANVR 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 804 LFNKFI-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDH 882
Cdd:PRK12881 723 IKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSN 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 883 LIGIGIAPLQFLPGENADSLGLSGRETFSLT-FPEELSPG--ITLNIQTSTGKV--FSVIASFEDDVEITLYKHGGLLNF 957
Cdd:PRK12881 803 LVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRqdVTLVIHRADGSTerVPVLCRIDTPIEVDYYKAGGILPY 882
|
....*
gi 114658342 958 VARKF 962
Cdd:PRK12881 883 VLRQL 887
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
84-641 |
0e+00 |
|
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: 711.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 84 RVLLQDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKCaiqnapnpgggdlqkagklsplkvqp 163
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGT-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 164 kklpcrgqttcrgscdsgelgrnsgtfssqientpilcpfhlqpvpePETVLKNQEVEFGRNRERLQFFKWSSRVFKNVA 243
Cdd:cd01586 55 -----------------------------------------------ADALAKNMKLEFERNRERYEFLKWGQKAFKNLR 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 244 VIPPGTGMAHQINLEYLSRVVF----EEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVG 319
Cdd:cd01586 88 VVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 320 CELTGSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDnvtlkhlehtg 399
Cdd:cd01586 168 VKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD----------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 400 fskaklesmetylkavklfrndqnssgepeySQVIQINLNSIVPSVSGPKRPQDRVAVtdmksdfqaclnekvgfkgfqi 479
Cdd:cd01586 237 -------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL---------------------- 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 480 aaekqkdivsihyegseyklsHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSS 559
Cdd:cd01586 264 ---------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVKTSLAPGSRVVTKYLEA 322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 560 SGVLPYLSKLGFEIVGYGCSTCVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAG 639
Cdd:cd01586 323 SGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVRANYLASPPLVVAYALAG 402
|
..
gi 114658342 640 TV 641
Cdd:cd01586 403 TV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
77-639 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 551.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 77 EVPFFPARVLLQDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSlqidfskcaiqnapnpgggdlqkagkl 156
Cdd:pfam00330 15 SLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 157 splkvqpkklpcrgqttcrgscdsgelgrnsgtfssqientpilcpfhlqpvpePETVLKNQEVEFGRNRERLQFFKWSS 236
Cdd:pfam00330 68 ------------------------------------------------------PDALDKNIEDEISRNKEQYDFLEWNA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 237 RVFkNVAVIPPGTGMAHQINLEYLsrvvfeekdLLFPD-SVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLP 315
Cdd:pfam00330 94 KKF-GIRFVPPGQGIVHQVGLEYG---------LALPGmTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQPLEMKKP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 316 EVVGCELTGSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHL 395
Cdd:pfam00330 164 KVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDETTFEYL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 396 EHTGFSKAKLEsmETYLKAVKLFRNDqnSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSD-FQACLNEKVGF 474
Cdd:pfam00330 244 RATGRPEAPKG--EAYDKAVAWKTLA--SDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDpFADAVKRKAAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 475 KGfqiaaekqkdiVSIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLaKKAVEAGLRVKPYIRTSLSPGSGMVT 554
Cdd:pfam00330 320 RA-----------LEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLL-KKAVEKGLKVAPGVKASVVPGSEVVR 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 555 HYLSSSGVLPYLSKLGFEIVGYGCSTCVGNTAPLSDavlnavkqGDlvtCGILSGNKNFEGRLCDCVRAnYLASPPLVVA 634
Cdd:pfam00330 388 AYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GE---RCVSSSNRNFEGRQGPGGRT-HLASPALVAA 455
|
....*
gi 114658342 635 YAIAG 639
Cdd:pfam00330 456 AAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
84-641 |
2.71e-140 |
|
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: 424.22 E-value: 2.71e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 84 RVLLQDFTGIPAMVDFAAMREAVKtlggdpekVHPACPTDLTVDHSLQIDFskcaiqnapnpgggdlqkagklsplkvqp 163
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQLEK----------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 164 kklpcrgqttcrgscdsgelgrnsgtfssqientpilcpfhlqpvpepetvlknqevefGRNRERLQFFKWSSRVFKnVA 243
Cdd:cd01351 44 -----------------------------------------------------------PVNNEGHKFLSFFAALQG-IA 63
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 244 VIPPGTGMAHQINLEYLsrvvfeekdLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELT 323
Cdd:cd01351 64 FYRPGVGIIHQIMVENL---------ALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLT 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 324 GSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKA 403
Cdd:cd01351 135 GKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLL 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 404 KLesmetylkAVKLFRNDQNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSdfqaclnekvgfkgfqiaaek 483
Cdd:cd01351 215 KN--------LWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------------------- 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 484 qkdivsihyegseyklshGSVVIAAVISCTNNCnPSVMLAAGLLAKKAVeaglrVKPYIRTSLSPGSGMVTHYLSSSGVL 563
Cdd:cd01351 266 ------------------TKIDQVLIGSCTNNR-YSDMLAAAKLLKGAK-----VAPGVRLIVTPGSRMVYATLSREGYY 321
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114658342 564 PYLSKLGFEIVGYGCSTCVGNTAPLsdavlnavkqGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 641
Cdd:cd01351 322 EILVDSGARILPPGCGPCMGNGARL----------VADGEVGVSSGNRNFPGRLGTYERHVYLASPELAAATAIAGKI 389
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
745-913 |
1.49e-108 |
|
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: 332.70 E-value: 1.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 745 YLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKPAPKTIHFPS-GQ 823
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGTTHHPPtGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 824 TLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLG 903
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
170
....*....|
gi 114658342 904 LSGRETFSLT 913
Cdd:cd01580 161 LTGEETYDII 170
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
246-961 |
1.34e-66 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 235.81 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 246 PPGTGMAHQINLEYLSrvvfeekdllFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTG 324
Cdd:PRK07229 94 KPGNGICHQVHLERFA----------FPgKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 325 SSNPFVTSIDVVLgitKHLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDnvtlkhlehtgfs 401
Cdd:PRK07229 164 KLPPWVSAKDVIL---ELLRRLTVKGgvgKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSD------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 402 kaklESMETYLKA-------VKLFRNDqnssgEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKsdfqaclnekvgf 474
Cdd:PRK07229 228 ----ERTREFLKAqgreddwVELLADP-----DAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA------------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 475 kgfqiaaekqkdivsihyegseyklshGSVVIAAVI-SCTnncNPS---VMLAAGLLAKKaveaglRVKPyiRTSL--SP 548
Cdd:PRK07229 286 ---------------------------GIKVDQVLIgSCT---NSSyedLMRAASILKGK------KVHP--KVSLviNP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 549 GSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTCVGNT-APLSDAVlnavkqgdlvtcgIL-SGNKNFEGR---LCDCVra 623
Cdd:PRK07229 328 GSRQVLEMLARDGALADLIAAGARILENACGPCIGMGqAPATGNV-------------SLrTFNRNFPGRsgtKDAQV-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 624 nYLASPPLVVAYAIAGTVnidfqteplgTDPTGkniyLHDIWPSREEVHRVEEEHVILSMF-----KALKDKIEMGnkrw 698
Cdd:PRK07229 393 -YLASPETAAASALTGVI----------TDPRT----LALENGEYPKLEEPEGFAVDDAGIiapaeDGSDVEVVRG---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 699 nsleaPDSVLFPwdlkstyircpsffdklTKEPiaLQAIENAHVLLYLGDSVTTDHISPAGsiarnsaaAKYLTNRGltp 778
Cdd:PRK07229 454 -----PNIKPLP-----------------LLEP--LPDLLEGKVLLKVGDNITTDHIMPAG--------AKWLPYRS--- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 779 refnsygarrgndavmtrgtfaNIklfnkfigkpaPKTIHFpsgqtldVFEAA--ELYQ--KEGIPLIILAGKKYGSGNS 854
Cdd:PRK07229 499 ----------------------NI-----------PNISEF-------VFEGVdnTFPEraKEQGGGIVVGGENYGQGSS 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 855 RDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLGLSgrETFSLTFPEELSPGITLNIQTST-GKV 933
Cdd:PRK07229 539 REHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEG--DVLEIEDLREFLPGGPLTVVNVTkDEE 616
|
730 740
....*....|....*....|....*...
gi 114658342 934 FSVIASFEDDvEITLYKHGGLLNFVARK 961
Cdd:PRK07229 617 IEVRHTLSER-QIEILLAGGALNLIKKK 643
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
247-641 |
1.63e-45 |
|
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: 168.40 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 247 PGTGMAHQINLEylsRVVFEEKDLLfpdsvvGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSS 326
Cdd:cd01585 66 PGNGICHQVHLE---RFAVPGKTLL------GSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGEL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 327 NPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLE 406
Cdd:cd01585 137 PPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 407 smetyLKAvklfrnDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDmksdfqaclnekvgfkgfqiaAEKQKd 486
Cdd:cd01585 217 -----LAA------DADA----EYDEEIEIDLSELEPLIARPHSPDNVVPVRE---------------------VAGIK- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 487 ivsihyegseyklshgsVVIAAVISCTNNCNPSVMLAAGLLakkaveAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYL 566
Cdd:cd01585 260 -----------------VDQVAIGSCTNSSYEDLMTVAAIL------KGRRVHPHVSMVVAPGSKQVLEMLARNGALADL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 114658342 567 SKLGFEIVGYGCSTCVG-NTAPLSDAVlnavkqgdlvtcGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 641
Cdd:cd01585 317 LAAGARILESACGPCIGmGQAPPTGGV------------SVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
246-640 |
2.60e-42 |
|
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: 159.91 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 246 PPGTGMAHQINLEYLSrvvfeekdllFPDS-VVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTG 324
Cdd:cd01584 73 KPGSGIIHQIVLENYA----------FPGLlMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 325 SSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAK 404
Cdd:cd01584 143 KLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 405 LESMETylkAVKLFRNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQA---CLNEKVGFKGfqiaa 481
Cdd:cd01584 223 DLADEF---KDDLLVADEGA----EYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKngwPLDLRVGLIG----- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 482 ekqkdivsihyegseyklshgsvviaaviSCTNNCNPSVMLAAGlLAKKAVEAGLRVKpyIRTSLSPGSGMVTHYLSSSG 561
Cdd:cd01584 291 -----------------------------SCTNSSYEDMGRAAS-IAKQALAHGLKCK--SIFTITPGSEQIRATIERDG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 562 VLPYLSKLGFEIVGYGCSTCVGNTAPlsdavlNAVKQGDLVTCgILSGNKNFEGRlCDCVRA--NYLASPPLVVAYAIAG 639
Cdd:cd01584 339 LLQTFRDAGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGR-NDANPAthAFVASPEIVTAMAIAG 410
|
.
gi 114658342 640 T 640
Cdd:cd01584 411 T 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
767-896 |
2.50e-40 |
|
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: 144.82 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 767 AAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFI-GKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILA 845
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 114658342 846 GKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPG 896
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
263-641 |
3.82e-37 |
|
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: 144.25 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 263 VVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 341
Cdd:cd01583 74 VILPEKGLTLPgMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 342 HLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFskaklesmetylKAVKLFRND 421
Cdd:cd01583 154 KIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK------------AYWKELKSD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 422 QNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDmksdfqaclnekvgfkgfqiaAEKQK-DIVSIhyeGseykls 500
Cdd:cd01583 222 EDA----EYDKVVEIDASELEPQVAWPHSPDNVVPVSE---------------------VEGIKiDQVFI---G------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 501 hgsvviaaviSCTNNCNPSVMLAAGLLAKKaveaglRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCST 580
Cdd:cd01583 268 ----------SCTNGRLEDLRAAAEILKGR------KVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGA 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 114658342 581 CVGntapLSDAVLNAvkqGDLVtcgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 641
Cdd:cd01583 332 CLG----GHMGVLAP---GERC---VSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
263-641 |
7.17e-35 |
|
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: 138.24 E-value: 7.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 263 VVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGItk 341
Cdd:COG0065 103 VVLPEQGLVLPgMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAI-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 342 hLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKaklesmetylkaVKLF 418
Cdd:COG0065 181 -IGKIGADGatgKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKGRPFAP------------WRTL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 419 RNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSdfqaclnekvgfkgfqiaaekqkdiVSIHYegseyk 498
Cdd:COG0065 248 KSDEDA----VYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEG-------------------------IKIDQ------ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 499 lshgsvviaAVI-SCTNNcnpsvML-----AAGLLakkaveAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFE 572
Cdd:COG0065 293 ---------VFIgSCTNG-----RIedlraAAEIL------KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAE 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 573 IVGYGCSTCVG-NTAPLSDavlnavkqGDLVtcgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 641
Cdd:COG0065 353 WREPGCGMCLGmNMGVLAP--------GERC---ASTSNRNFEGRMGSPGSRTYLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
248-639 |
5.02e-27 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 114.89 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 248 GTGMAHQinleylsrvVFEEKDLLFP-DSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSS 326
Cdd:PRK00402 97 GEGICHQ---------VLPEKGLVRPgDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETIKVVLEGKL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 327 NPFVTSIDVVLGItkhLRQVGVAG---KFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEhtgfska 403
Cdd:PRK00402 168 PPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLK------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 404 klesmETYLKAVKLFRNDQNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKsdfqaclNEKVgfkgfqiaaek 483
Cdd:PRK00402 238 -----ERAGRDYKPWKSDEDA----EYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVE-------GTKV----------- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 484 qkDIVSIhyeGseyklshgsvviaaviSCTNNCNPSVMLAAGLLAKKaveaglRVKPYIRTSLSPGSGMVTHYLSSSGVL 563
Cdd:PRK00402 291 --DQVFI---G----------------SCTNGRLEDLRIAAEILKGR------KVAPGVRLIVIPASQKIYLQALKEGLI 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114658342 564 PYLSKLGFeIVGY-GCSTCVGNtaplSDAVLnavkqGDLVTCgILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAG 639
Cdd:PRK00402 344 EIFVDAGA-VVSTpTCGPCLGG----HMGVL-----APGEVC-LSTTNRNFKGRMGSPESEVYLASPAVAAASAVTG 409
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
263-639 |
2.19e-24 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 107.68 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 263 VVFEEKDLLFPDSVVGT-DSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITK 341
Cdd:PRK12466 112 VVAPELGLTLPGMVIVCgDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 342 HLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKlESMETYLKAVKLFRND 421
Cdd:PRK12466 192 RIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKG-ALWDAALAYWRTLRSD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 422 QNSsgepEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQAclnekvgfkgfQIAAEKQKDIV-SIHYEGSEYKLS 500
Cdd:PRK12466 271 ADA----VFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAA-----------EADPARRAAMErALDYMGLTPGTP 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 501 HGSVVIAAVI--SCTNncnpsvmlaaG----LLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIV 574
Cdd:PRK12466 336 LAGIPIDRVFigSCTN----------GriedLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWR 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114658342 575 GYGCSTCVGntaplsdavLNavkqGDLVTCG---ILSGNKNFEGRLCDCVRAnYLASPPLVVAYAIAG 639
Cdd:PRK12466 406 EPGCSMCLA---------MN----DDVLAPGercASTTNRNFEGRQGPGART-HLMSPAMVAAAAVAG 459
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
246-641 |
2.13e-21 |
|
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: 97.30 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 246 PPGTGMAHQINLEylsrvvfeeKDLLFPDSV-VGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTG 324
Cdd:cd01582 64 PAGRGIGHQIMIE---------EGYAFPGTLaVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 325 SSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNvtlKHLehtgfskak 404
Cdd:cd01582 135 QLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA---KHL--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 405 lesmetylkavklfrndqnssgepeysqviQINLNSIVPSVSGPkrpqDRVAVTDMKSDFQaclnekvgfkgfqiaaekQ 484
Cdd:cd01582 203 ------------------------------ILDLSTLSPYVSGP----NSVKVSTPLKELE------------------A 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 485 KDIvsihyegseyklshgSVVIAAVISCTNNCNPSVMLAAGLL-AKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVL 563
Cdd:cd01582 231 QNI---------------KINKAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDW 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114658342 564 PYLSKLGFEIVGYGCSTCVGNTAPLsdavlnaVKQGDLvtcGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTV 641
Cdd:cd01582 296 QTLLEAGATPLPAGCGPCIGLGQGL-------LEPGEV---GISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
840-902 |
5.78e-17 |
|
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: 76.74 E-value: 5.78e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114658342 840 PLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSL 902
Cdd:cd00404 16 PGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKL 78
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
746-893 |
4.91e-16 |
|
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: 75.17 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 746 LGDSVTTDHISPAGsiarnsaaAKYLTNRgltprefnsygarrgndavmtrgtfANIKLFNKFIGKPAPKTIHfpsgqtl 825
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEFVFHRVDPTFA------- 41
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114658342 826 dvfEAAelyqKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQF 893
Cdd:cd01579 42 ---ERA----KAAGPGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
276-451 |
4.98e-08 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 56.94 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 276 VVGTDSHiTMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLRQVG-VAGKFVE 354
Cdd:PRK11413 145 ILGSDSH-TRYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGyVKNKVME 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 355 FFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLEsmetyLKAvklfrndqnssGEPE-YSQV 433
Cdd:PRK11413 224 FVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQDYCE-----LNP-----------QPMAyYDGC 287
|
170
....*....|....*...
gi 114658342 434 IQINLNSIVPSVSGPKRP 451
Cdd:PRK11413 288 ISVDLSAIKPMIALPFHP 305
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
247-639 |
5.15e-08 |
|
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: 56.35 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 247 PGTGMAHQinleYLSRvvfeekdLLFPDSV-VGTDSHITMVNGLGiLGWGVGGIETEAVMLGLPvsLTLPEVVGCELTGS 325
Cdd:cd01581 91 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHTRFPIGIS-FPAGSGLVAFAAATGVMP--LDMPESVLVRFKGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 326 SNPFVTSIDVV-----LGITKHLRQVGVAGKFVEFFG-----SGVSQLSIVDRTTIANMCPEYGA-----ILSFFPV--- 387
Cdd:cd01581 157 MQPGITLRDLVnaipyYAIQQGLLTVEKKGKKNVFNGrileiEGLPDLKVEQAFELTDASAERSAaactvRLDKEPViey 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 388 --DNVTL-KHLEHTGFSKA-----KLESMETYLKAVKLFRNDQNSsgepEYSQVIQINLNSIV-PSVSGPKRPQDRVAVT 458
Cdd:cd01581 237 leSNVVLmKIMIANGYDDArtllrRIIAMEEWLANPPLLEPDADA----EYAAVIEIDLDDIKePILACPNDPDDVKLLS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 459 dmksdfqACLNEKV--GFKGfqiaaekqkdivsihyegseyklshgsvviaaviSCtnncnpsvMLAAGLLakKAVEAGL 536
Cdd:cd01581 313 -------EVAGKKIdeVFIG----------------------------------SC--------MTNIGHF--RAAAKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 537 RVKPYIRTSL--SPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTCVGNTAPLSDavlnavkqGDLVtcgILSGNKNFE 614
Cdd:cd01581 342 RGKEFKPTRLwvAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARVAD--------GATV---FSTSTRNFD 410
|
410 420
....*....|....*....|....*
gi 114658342 615 GRLCDCVRAnYLASPPLVVAYAIAG 639
Cdd:cd01581 411 NRVGKGAEV-YLGSAELAAVCALLG 434
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
842-891 |
2.66e-07 |
|
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: 49.12 E-value: 2.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 114658342 842 IILAGKKYGSGNSR---DWAAKGpylLGVKAVLAESYEKIHKDHLIGIGIAPL 891
Cdd:cd01577 20 IIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPV 69
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
247-639 |
1.33e-05 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 49.15 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 247 PGTGMAHQinleYLSRvvfeekdLLFPDSV-VGTDSH------ITMVNGLGILGWGVG-GIeteavmlglpVSLTLPEVV 318
Cdd:PLN00094 537 PGDGVIHS----WLNR-------MLLPDTVgTGGDSHtrfpigISFPAGSGLVAFGAAtGV----------IPLDMPESV 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 319 GCELTGSSNPFVTSIDVVLGITKHLRQVGV-----AGKFVEFFG-----SGVSQLSIVDRTTIANMCPEYGA-------- 380
Cdd:PLN00094 596 LVRFTGTMQPGITLRDLVHAIPYTAIQDGLltvekKGKKNVFSGrileiEGLPHLKCEQAFELSDASAERSAagctikld 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 381 ---ILSFFPVDNVTLKHLEHTGFSKAK-LE----SMETYLKAVKLFRNDQNSsgepEYSQVIQINLNSIV-PSVSGPKRP 451
Cdd:PLN00094 676 kepIIEYLNSNVVMLKWMIAEGYGDRRtLErriaRMQQWLADPELLEADPDA----EYAAVIEIDMDEIKePILCAPNDP 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 452 QDrvavtdmksdfQACLNEKVGFKgfqiaaekqKDIVSIHyegseyklshgsvviaaviSCTNNCNPsvMLAAGLLAKKa 531
Cdd:PLN00094 752 DD-----------ARLLSEVTGDK---------IDEVFIG-------------------SCMTNIGH--FRAAGKLLND- 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 532 VEAGLRVKPYIrtslSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTCVGNTAPLSDAvlnavkqgdlvtCGILS-GN 610
Cdd:PLN00094 790 NLSQLPTRLWV----APPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARVAEK------------STVVStST 853
|
410 420 430
....*....|....*....|....*....|
gi 114658342 611 KNFEGRLCDcvRAN-YLASPPLVVAYAIAG 639
Cdd:PLN00094 854 RNFPNRLGK--GANvYLASAELAAVAAILG 881
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
842-902 |
2.45e-05 |
|
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: 46.32 E-value: 2.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114658342 842 IILAGKKYGSGNSRD---WAAKGpylLGVKAVLAESYEKIHKDHLIGIGIAPLQfLPGENADSL 902
Cdd:COG0066 67 ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDAL 126
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
706-878 |
3.41e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 43.31 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 706 SVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIenaHVLLY-LGDSVTTDHISPAGsiarnsaaakYLTNRGLTPREFNSY 784
Cdd:PLN00072 38 SSIFPFKPLTTSSGTSSPTISDSAESTSSTTF---HGLCFvVGDNIDTDQIIPAE----------YLTLVPSKPDEYEKL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 785 GArrgndavmtrgtFAniklfnkFIGKPAPKTIHFpsgqtldvFEAAELYQKEGIpliILAGKKYGSGNSRDWAakgPYL 864
Cdd:PLN00072 105 GS------------YA-------LIGLPAFYKTRF--------VEPGEMKTKYSI---IIGGENFGCGSSREHA---PVA 151
|
170
....*....|....*..
gi 114658342 865 LG---VKAVLAESYEKI 878
Cdd:PLN00072 152 LGaagAKAVVAESYARI 168
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
842-961 |
4.81e-04 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 41.74 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114658342 842 IILAGKKYGSGNSRD---WAAKGpylLGVKAVLAESYEKIHKDHLIGIGIaPLqFLPGENADSLGlSGREtfsLTFpeEL 918
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGL-PV-LECDEAVDKIE-DGDE---VEV--DL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 114658342 919 SPGITLNIqtSTGKVFSVIASFEDDVEItlYKHGGLLNFVARK 961
Cdd:PRK00439 120 ETGVITNL--TTGEEYKFKPIPEFMLEI--LKAGGLIEYLKKK 158
|
|
| |
