|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05225 |
PRK05225 |
ketol-acid reductoisomerase; Validated |
2-488 |
0e+00 |
|
ketol-acid reductoisomerase; Validated
Pssm-ID: 235368 [Multi-domain] Cd Length: 487 Bit Score: 1113.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 2 ANYFNTLNLRQQLAQLGKCRFMARDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 81
Cdd:PRK05225 1 ANYFNTLNLRQQLAQLGKCRFMDRDEFADGASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 82 ATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 161
Cdd:PRK05225 81 ATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRAVQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 162 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 241
Cdd:PRK05225 161 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 242 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWA 321
Cdd:PRK05225 241 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKIRAFELSEQLKEIMAPLFQKHMDDIISGEFSSTMMADWA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 322 NDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVASGIIEESAYYESLHELPLIANTI 401
Cdd:PRK05225 321 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMVAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 402 ARKRLYEMNVVISDTAEYGNYLFSYACVPLLKEFMTTLQTGDLGTAIAEGAVDNAQLRDVNEAIRSHAIEQVGKKLRGYM 481
Cdd:PRK05225 401 ARKRLYEMNVVISDTAEYGNYLFSHAAVPLLKDFMATLQPGDLGKGLPSNAVDNAQLRDVNEAIRNHPIEQVGKKLRGYM 480
|
....*..
gi 488972257 482 TDMKRIA 488
Cdd:PRK05225 481 TDMKRIA 487
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
35-369 |
2.48e-164 |
|
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 466.86 E-value: 2.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAiaekrASWRKATENGFKVGTYEELIPQADLVVNLTPDK-QHSD 113
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGG-----ASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEvQHEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 114 VVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPenDPKGEGMAIAKA 193
Cdd:TIGR00465 76 YEAEIQPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQ--DPTGEAMAIALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLM 273
Cdd:TIGR00465 154 YAKAIGGGRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 274 MDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSgmmaDWANDDkklltwreETGKTAFETAPQYEgkiGEQE 353
Cdd:TIGR00465 234 RDRISNTAEYGALTRRRIIKEELKPEMQKILKEIQNGEFAK----EWALEN--------EAGKPAFNTARKYE---SEHE 298
|
330
....*....|....*.
gi 488972257 354 YFDKGVLMIAMVKAGV 369
Cdd:TIGR00465 299 IEKVGKELRAMVPAGK 314
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
22-353 |
3.61e-164 |
|
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 466.84 E-value: 3.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 22 FMARDefaDGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRkeaiaEKRASWRKATENGFKVGTYEELIPQADL 101
Cdd:COG0059 5 YYDKD---ADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLR-----EGSKSWKKAEEDGFEVMTVAEAAKRADV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 102 VVNLTPDKQHSDVVR-SVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpe 180
Cdd:COG0059 77 IMILTPDEVQAAVYEeEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVH-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 181 NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWET 260
Cdd:COG0059 155 QDATGKAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 261 ITEALKQGGITLMMDRLSNPAKLRAYALSEQLK-EIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAF 339
Cdd:COG0059 235 IVDLIYEGGIANMRYSISNTAEYGDYTRGPRVItEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPI 314
|
330
....*....|....
gi 488972257 340 ETAPQYEGKIGEQE 353
Cdd:COG0059 315 EKVGAELRAMMPWL 328
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
34-204 |
8.15e-70 |
|
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.
Pssm-ID: 285265 Cd Length: 165 Bit Score: 219.72 E-value: 8.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 34 YLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEaiaekRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSD 113
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREG-----SKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 114 VVR-SVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAK 192
Cdd:pfam07991 76 VYEeEIAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVH--QDASGKAKDLAL 153
|
170
....*....|..
gi 488972257 193 AWAAATGGHRAG 204
Cdd:pfam07991 154 AYAKGIGGTRAG 165
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
37-139 |
1.07e-03 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 41.29 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DISYALrkEAIAEkraswrkatenGFKVGTYEELIPQADLVVN 104
Cdd:cd00401 195 GKVVVVAGygwVG-----KGCAMRARGLgarvivtevDPICAL--QAAMD-----------GFEVMPMEEAAKIGDIFVT 256
|
90 100 110
....*....|....*....|....*....|....*.
gi 488972257 105 LTPDKqhsDVVRSVQ-PLMKDGAALGYSHGFNiVEV 139
Cdd:cd00401 257 ATGNK---DVIRGEHfEKMKDGAILCNAGHFD-VEI 288
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
35-135 |
3.95e-03 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 38.20 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGlnQGLNMRDSGLDIsyalrKEAIAEK---RASwrKATENGFKVGTYEELIPQADLVVNLTPDKqh 111
Cdd:smart00997 21 LAGKNVVVAGYGDVG--KGVAARLRGLGA-----RVIVTEIdpiRAL--EAAMDGFEVMKMEEAAKRADIFVTATGNK-- 89
|
90 100
....*....|....*....|....*
gi 488972257 112 sDVVRSVQPL-MKDGAALGYSHGFN 135
Cdd:smart00997 90 -DVITREHFRaMKDGAILANAGHFD 113
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05225 |
PRK05225 |
ketol-acid reductoisomerase; Validated |
2-488 |
0e+00 |
|
ketol-acid reductoisomerase; Validated
Pssm-ID: 235368 [Multi-domain] Cd Length: 487 Bit Score: 1113.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 2 ANYFNTLNLRQQLAQLGKCRFMARDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 81
Cdd:PRK05225 1 ANYFNTLNLRQQLAQLGKCRFMDRDEFADGASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 82 ATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 161
Cdd:PRK05225 81 ATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRAVQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 162 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 241
Cdd:PRK05225 161 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 242 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWA 321
Cdd:PRK05225 241 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKIRAFELSEQLKEIMAPLFQKHMDDIISGEFSSTMMADWA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 322 NDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVASGIIEESAYYESLHELPLIANTI 401
Cdd:PRK05225 321 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMVAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 402 ARKRLYEMNVVISDTAEYGNYLFSYACVPLLKEFMTTLQTGDLGTAIAEGAVDNAQLRDVNEAIRSHAIEQVGKKLRGYM 481
Cdd:PRK05225 401 ARKRLYEMNVVISDTAEYGNYLFSHAAVPLLKDFMATLQPGDLGKGLPSNAVDNAQLRDVNEAIRNHPIEQVGKKLRGYM 480
|
....*..
gi 488972257 482 TDMKRIA 488
Cdd:PRK05225 481 TDMKRIA 487
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
35-369 |
2.48e-164 |
|
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 466.86 E-value: 2.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAiaekrASWRKATENGFKVGTYEELIPQADLVVNLTPDK-QHSD 113
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGG-----ASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEvQHEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 114 VVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPenDPKGEGMAIAKA 193
Cdd:TIGR00465 76 YEAEIQPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQ--DPTGEAMAIALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWETITEALKQGGITLM 273
Cdd:TIGR00465 154 YAKAIGGGRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 274 MDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSgmmaDWANDDkklltwreETGKTAFETAPQYEgkiGEQE 353
Cdd:TIGR00465 234 RDRISNTAEYGALTRRRIIKEELKPEMQKILKEIQNGEFAK----EWALEN--------EAGKPAFNTARKYE---SEHE 298
|
330
....*....|....*.
gi 488972257 354 YFDKGVLMIAMVKAGV 369
Cdd:TIGR00465 299 IEKVGKELRAMVPAGK 314
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
22-353 |
3.61e-164 |
|
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 466.84 E-value: 3.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 22 FMARDefaDGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRkeaiaEKRASWRKATENGFKVGTYEELIPQADL 101
Cdd:COG0059 5 YYDKD---ADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLR-----EGSKSWKKAEEDGFEVMTVAEAAKRADV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 102 VVNLTPDKQHSDVVR-SVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpe 180
Cdd:COG0059 77 IMILTPDEVQAAVYEeEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVH-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 181 NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDPAYAEKLIQFGWET 260
Cdd:COG0059 155 QDATGKAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 261 ITEALKQGGITLMMDRLSNPAKLRAYALSEQLK-EIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAF 339
Cdd:COG0059 235 IVDLIYEGGIANMRYSISNTAEYGDYTRGPRVItEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPI 314
|
330
....*....|....
gi 488972257 340 ETAPQYEGKIGEQE 353
Cdd:COG0059 315 EKVGAELRAMMPWL 328
|
|
| PRK05479 |
PRK05479 |
ketol-acid reductoisomerase; Provisional |
33-481 |
1.97e-70 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 227.28 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 33 SYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAiaekrASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHS 112
Cdd:PRK05479 13 SLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGS-----KSWKKAEADGFEVLTVAEAAKWADVIMILLPDEVQA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 113 DVVR-SVQPLMKDGAALGYSHGFNIVEvgEQI--RKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMA 189
Cdd:PRK05479 88 EVYEeEIEPNLKEGAALAFAHGFNIHF--GQIvpPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVH--QDASGNAKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 190 IAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCgmlqagsllcfdklvaegtdpayaekliqfgwetitealkqGG 269
Cdd:PRK05479 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLC-----------------------------------------GG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 270 ITlmmdrlsnpaklrayalseqlkeimaplfqkhmddiisgefssgmmadwanddkklltwreetgktafetapqyegki 349
Cdd:PRK05479 203 LT------------------------------------------------------------------------------ 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 350 geqeyfdkgvlmiAMVKAGvelaFETMVASGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACV 429
Cdd:PRK05479 205 -------------ELIKAG----FETLVEAGYQPEMAYFECLHELKLIVDLIYEGGIANMRYSISNTAEYGDYVSGPRVI 267
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 430 -PLLKEFM----TTLQTGDLgtA---IAEGAVDNAQLRDVNEAIRSHAIEQVGKKLRGYM 481
Cdd:PRK05479 268 tEETKKEMkevlKDIQSGEF--AkewILENKAGRPTFKALRREEAEHPIEKVGAKLRAMM 325
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
34-204 |
8.15e-70 |
|
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.
Pssm-ID: 285265 Cd Length: 165 Bit Score: 219.72 E-value: 8.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 34 YLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEaiaekRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSD 113
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREG-----SKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 114 VVR-SVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAK 192
Cdd:pfam07991 76 VYEeEIAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVH--QDASGKAKDLAL 153
|
170
....*....|..
gi 488972257 193 AWAAATGGHRAG 204
Cdd:pfam07991 154 AYAKGIGGTRAG 165
|
|
| PRK13403 |
PRK13403 |
ketol-acid reductoisomerase; Provisional |
35-313 |
1.80e-36 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 106361 [Multi-domain] Cd Length: 335 Bit Score: 137.57 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAiaekraSWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDV 114
Cdd:PRK13403 14 LQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGK------SFEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQQAHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 115 VRS-VQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAKA 193
Cdd:PRK13403 88 YKAeVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVH--QDATGTALHVALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDP--AYAEKLIQFgwETITEALKQGGIT 271
Cdd:PRK13403 166 YAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPeiAYFECLHEL--KLIVDLMYEGGLT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488972257 272 LMMDRLSNPAKLRAYA-----LSEQLKEIMaplfQKHMDDIISGEFS 313
Cdd:PRK13403 244 NMRHSISDTAEFGDYVtgsriVTDETKKEM----KRVLTEIQQGEFA 286
|
|
| IlvC |
pfam01450 |
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
213-342 |
1.48e-27 |
|
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.
Pssm-ID: 460215 [Multi-domain] Cd Length: 138 Bit Score: 107.17 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 213 EVKSDLMGEQTILCGMLQAGSLLCFDKLVAEGTDP--AYAEKLiqfgWET--ITEALKQGGITLMMDRLSNPAKLRAYAL 288
Cdd:pfam01450 3 ETETDLFGEQAVLCGGVTGLVKAGFETLVEAGYQPeaAYFECL----HELklIVDLIYEGGIAGMRYSISDTAEYGDLTR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488972257 289 SEQL-KEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETA 342
Cdd:pfam01450 79 GPRViYDATKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIEKV 133
|
|
| IlvC |
pfam01450 |
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
349-478 |
4.72e-21 |
|
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.
Pssm-ID: 460215 [Multi-domain] Cd Length: 138 Bit Score: 89.06 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 349 IGEQeyfdkGVLMiAMVKAGVELAFETMVASGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYL----F 424
Cdd:pfam01450 9 FGEQ-----AVLC-GGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTrgprV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488972257 425 SYACV-PLLKEFMTTLQTGD-LGTAIAEGAVDNAQLRDVNEAIRSHAIEQVGKKLR 478
Cdd:pfam01450 83 IYDATkELMKEILDEIQSGEfAKEWILEYQAGRPELKALRREEAEHPIEKVGKELR 138
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
35-128 |
1.02e-03 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 40.17 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGLN-----QGLNMRDSGLDISyaLRKEAIAEkraswrkatENGFKVGTYEELIPQADLVVN---LT 106
Cdd:pfam02826 34 LSGKTVGIIGLGRIGRAvakrlKAFGMKVIAYDRY--PKPEEEEE---------ELGARYVSLDELLAESDVVSLhlpLT 102
|
90 100
....*....|....*....|....*
gi 488972257 107 PDKQH---SDVVRsvqpLMKDGAAL 128
Cdd:pfam02826 103 PETRHlinAERLA----LMKPGAIL 123
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
37-139 |
1.07e-03 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 41.29 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DISYALrkEAIAEkraswrkatenGFKVGTYEELIPQADLVVN 104
Cdd:cd00401 195 GKVVVVAGygwVG-----KGCAMRARGLgarvivtevDPICAL--QAAMD-----------GFEVMPMEEAAKIGDIFVT 256
|
90 100 110
....*....|....*....|....*....|....*.
gi 488972257 105 LTPDKqhsDVVRSVQ-PLMKDGAALGYSHGFNiVEV 139
Cdd:cd00401 257 ATGNK---DVIRGEHfEKMKDGAILCNAGHFD-VEI 288
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
35-135 |
3.95e-03 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 38.20 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972257 35 LQGKKVVIVGCGAQGlnQGLNMRDSGLDIsyalrKEAIAEK---RASwrKATENGFKVGTYEELIPQADLVVNLTPDKqh 111
Cdd:smart00997 21 LAGKNVVVAGYGDVG--KGVAARLRGLGA-----RVIVTEIdpiRAL--EAAMDGFEVMKMEEAAKRADIFVTATGNK-- 89
|
90 100
....*....|....*....|....*
gi 488972257 112 sDVVRSVQPL-MKDGAALGYSHGFN 135
Cdd:smart00997 90 -DVITREHFRaMKDGAILANAGHFD 113
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
35-109 |
5.00e-03 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 36.69 E-value: 5.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488972257 35 LQGKKVVIVGCGAQGLNQGLNMRDSGLDIS-YALRKEAIAEKRASWRKAtengfkvgTYEELIPQADLVVNLTPDK 109
Cdd:pfam13241 5 LRGKRVLVVGGGEVAARKARKLLEAGAKVTvVSPEITPFLEGLLDLIRR--------EFEGDLDGADLVIAATDDP 72
|
|
| |
