|
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: 1118.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 2 ANYFNTLNLRQQLAQLGKCRFMARDEFADGAGYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAIAEKRASWRK 81
Cdd:PRK05225 1 ANYFNTLNLRQQLAQLGKCRFMDRDEFADGASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 82 ATENGFQVGTYEELIPQADLVVNLTPDKQHSDVVRAVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 161
Cdd:PRK05225 81 ATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRAVQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 162 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 241
Cdd:PRK05225 161 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 242 EEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSGMMADWA 321
Cdd:PRK05225 241 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKIRAFELSEQLKEIMAPLFQKHMDDIISGEFSSTMMADWA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 322 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMIAMVKAGVELAFETMVAAGIIEESAYYESLHELPLIANTI 401
Cdd:PRK05225 321 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMVAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 402 ARKRLYEMNVVISDTAEYGNYLFANAAVPLLKEFMTKLQPGDLGKAVEGTAVDNAQLRDVNDAIRSHEIEKVGQKLRGYM 481
Cdd:PRK05225 401 ARKRLYEMNVVISDTAEYGNYLFSHAAVPLLKDFMATLQPGDLGKGLPSNAVDNAQLRDVNEAIRNHPIEQVGKKLRGYM 480
|
....*..
gi 1382576672 482 TDMKRIA 488
Cdd:PRK05225 481 TDMKRIA 487
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
22-353 |
1.77e-165 |
|
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: 470.31 E-value: 1.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 22 FMARDefaDGAGYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRkeaiaEKRASWRKATENGFQVGTYEELIPQADL 101
Cdd:COG0059 5 YYDKD---ADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLR-----EGSKSWKKAEEDGFEVMTVAEAAKRADV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 102 VVNLTPDKQHSDVVR-AVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpe 180
Cdd:COG0059 77 IMILTPDEVQAAVYEeEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVH-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 181 NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWET 260
Cdd:COG0059 155 QDATGKAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 261 ITEALKQGGITLMMDRLSNPAKLRAYALSEQLKT-IMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAF 339
Cdd:COG0059 235 IVDLIYEGGIANMRYSISNTAEYGDYTRGPRVITeEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPI 314
|
330
....*....|....
gi 1382576672 340 ENAPQYEGKISEQE 353
Cdd:COG0059 315 EKVGAELRAMMPWL 328
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
35-369 |
1.24e-162 |
|
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: 462.62 E-value: 1.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 35 LKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAiaekrASWRKATENGFQVGTYEELIPQADLVVNLTPDK-QHSD 113
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGG-----ASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEvQHEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 114 VVRAVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPenDPKGEGMAIAKA 193
Cdd:TIGR00465 76 YEAEIQPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQ--DPTGEAMAIALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLM 273
Cdd:TIGR00465 154 YAKAIGGGRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 274 MDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSgmmaDWANDDkklltwreETGKTAFENAPQYEgkiSEQE 353
Cdd:TIGR00465 234 RDRISNTAEYGALTRRRIIKEELKPEMQKILKEIQNGEFAK----EWALEN--------EAGKPAFNTARKYE---SEHE 298
|
330
....*....|....*.
gi 1382576672 354 YFDKGVLMIAMVKAGV 369
Cdd:TIGR00465 299 IEKVGKELRAMVPAGK 314
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
34-204 |
1.27e-69 |
|
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: 219.34 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 34 YLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEaiaekRASWRKATENGFQVGTYEELIPQADLVVNLTPDKQHSD 113
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREG-----SKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 114 VVRA-VQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAK 192
Cdd:pfam07991 76 VYEEeIAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVH--QDASGKAKDLAL 153
|
170
....*....|..
gi 1382576672 193 AWAAATGGHRAG 204
Cdd:pfam07991 154 AYAKGIGGTRAG 165
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
37-139 |
1.63e-04 |
|
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: 43.98 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVN 104
Cdd:cd00401 195 GKVVVVAGygwVG-----KGCAMRARGLgarvivtevDPICAL--QAAMD-----------GFEVMPMEEAAKIGDIFVT 256
|
90 100 110
....*....|....*....|....*....|....*.
gi 1382576672 105 LTPDKqhsDVVRAVQ-PLMKDGAALGYSHGFNiVEV 139
Cdd:cd00401 257 ATGNK---DVIRGEHfEKMKDGAILCNAGHFD-VEI 288
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
37-135 |
7.25e-04 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.13 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVGCGAQGlnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVNLTP 107
Cdd:smart00997 23 GKNVVVAGYGDVG--KGVAARLRGLgarvivteiDPIRAL--EAAMD-----------GFEVMKMEEAAKRADIFVTATG 87
|
90 100
....*....|....*....|....*....
gi 1382576672 108 DKqhsDVVRAVQPL-MKDGAALGYSHGFN 135
Cdd:smart00997 88 NK---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: 1118.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 2 ANYFNTLNLRQQLAQLGKCRFMARDEFADGAGYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAIAEKRASWRK 81
Cdd:PRK05225 1 ANYFNTLNLRQQLAQLGKCRFMDRDEFADGASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 82 ATENGFQVGTYEELIPQADLVVNLTPDKQHSDVVRAVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 161
Cdd:PRK05225 81 ATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRAVQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 162 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 241
Cdd:PRK05225 161 REEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 242 EEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSGMMADWA 321
Cdd:PRK05225 241 AEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKIRAFELSEQLKEIMAPLFQKHMDDIISGEFSSTMMADWA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 322 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMIAMVKAGVELAFETMVAAGIIEESAYYESLHELPLIANTI 401
Cdd:PRK05225 321 NDDKKLLTWREETGKTAFENAPQYEGKISEQEYFDKGVLMVAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 402 ARKRLYEMNVVISDTAEYGNYLFANAAVPLLKEFMTKLQPGDLGKAVEGTAVDNAQLRDVNDAIRSHEIEKVGQKLRGYM 481
Cdd:PRK05225 401 ARKRLYEMNVVISDTAEYGNYLFSHAAVPLLKDFMATLQPGDLGKGLPSNAVDNAQLRDVNEAIRNHPIEQVGKKLRGYM 480
|
....*..
gi 1382576672 482 TDMKRIA 488
Cdd:PRK05225 481 TDMKRIA 487
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
22-353 |
1.77e-165 |
|
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: 470.31 E-value: 1.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 22 FMARDefaDGAGYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRkeaiaEKRASWRKATENGFQVGTYEELIPQADL 101
Cdd:COG0059 5 YYDKD---ADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLR-----EGSKSWKKAEEDGFEVMTVAEAAKRADV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 102 VVNLTPDKQHSDVVR-AVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpe 180
Cdd:COG0059 77 IMILTPDEVQAAVYEeEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVH-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 181 NDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWET 260
Cdd:COG0059 155 QDATGKAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 261 ITEALKQGGITLMMDRLSNPAKLRAYALSEQLKT-IMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAF 339
Cdd:COG0059 235 IVDLIYEGGIANMRYSISNTAEYGDYTRGPRVITeEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPI 314
|
330
....*....|....
gi 1382576672 340 ENAPQYEGKISEQE 353
Cdd:COG0059 315 EKVGAELRAMMPWL 328
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
35-369 |
1.24e-162 |
|
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: 462.62 E-value: 1.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 35 LKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAiaekrASWRKATENGFQVGTYEELIPQADLVVNLTPDK-QHSD 113
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGG-----ASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEvQHEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 114 VVRAVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPenDPKGEGMAIAKA 193
Cdd:TIGR00465 76 YEAEIQPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQ--DPTGEAMAIALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLM 273
Cdd:TIGR00465 154 YAKAIGGGRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 274 MDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSgmmaDWANDDkklltwreETGKTAFENAPQYEgkiSEQE 353
Cdd:TIGR00465 234 RDRISNTAEYGALTRRRIIKEELKPEMQKILKEIQNGEFAK----EWALEN--------EAGKPAFNTARKYE---SEHE 298
|
330
....*....|....*.
gi 1382576672 354 YFDKGVLMIAMVKAGV 369
Cdd:TIGR00465 299 IEKVGKELRAMVPAGK 314
|
|
| PRK05479 |
PRK05479 |
ketol-acid reductoisomerase; Provisional |
33-481 |
9.98e-70 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 225.35 E-value: 9.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 33 GYLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAiaekrASWRKATENGFQVGTYEELIPQADLVVNLTPDKQHS 112
Cdd:PRK05479 13 SLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGS-----KSWKKAEADGFEVLTVAEAAKWADVIMILLPDEVQA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 113 DVVRA-VQPLMKDGAALGYSHGFNIVEvgEQI--RKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMA 189
Cdd:PRK05479 88 EVYEEeIEPNLKEGAALAFAHGFNIHF--GQIvpPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVH--QDASGNAKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 190 IAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCgmlqagsllcfdklveegtdpayaekliqfgwetitealkqGG 269
Cdd:PRK05479 164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLC-----------------------------------------GG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 270 ITlmmdrlsnpaklrayalseqlktimaplfqkhmddiisgefssgmmadwanddkklltwreetgktafenapqyegki 349
Cdd:PRK05479 203 LT------------------------------------------------------------------------------ 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 350 seqeyfdkgvlmiAMVKAGvelaFETMVAAGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYL----FA 425
Cdd:PRK05479 205 -------------ELIKAG----FETLVEAGYQPEMAYFECLHELKLIVDLIYEGGIANMRYSISNTAEYGDYVsgprVI 267
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1382576672 426 NAAV-PLLKEFMTKLQPGDLGKA-VEGTAVDNAQLRDVNDAIRSHEIEKVGQKLRGYM 481
Cdd:PRK05479 268 TEETkKEMKEVLKDIQSGEFAKEwILENKAGRPTFKALRREEAEHPIEKVGAKLRAMM 325
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
34-204 |
1.27e-69 |
|
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: 219.34 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 34 YLKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEaiaekRASWRKATENGFQVGTYEELIPQADLVVNLTPDKQHSD 113
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREG-----SKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 114 VVRA-VQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAK 192
Cdd:pfam07991 76 VYEEeIAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVH--QDASGKAKDLAL 153
|
170
....*....|..
gi 1382576672 193 AWAAATGGHRAG 204
Cdd:pfam07991 154 AYAKGIGGTRAG 165
|
|
| PRK13403 |
PRK13403 |
ketol-acid reductoisomerase; Provisional |
35-313 |
5.78e-38 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 106361 [Multi-domain] Cd Length: 335 Bit Score: 141.81 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 35 LKGKKVVIVGCGAQGLNQGLNMRDSGLDVSYALRKEAiaekraSWRKATENGFQVGTYEELIPQADLVVNLTPDKQHSDV 114
Cdd:PRK13403 14 LQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGK------SFEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQQAHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 115 VRA-VQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAIAKA 193
Cdd:PRK13403 88 YKAeVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVH--QDATGTALHVALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 194 WAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDP--AYAEKLIQFgwETITEALKQGGIT 271
Cdd:PRK13403 166 YAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPeiAYFECLHEL--KLIVDLMYEGGLT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1382576672 272 LMMDRLSNPAKLRAYALSEQLKTIMAPLFQKH-MDDIISGEFS 313
Cdd:PRK13403 244 NMRHSISDTAEFGDYVTGSRIVTDETKKEMKRvLTEIQQGEFA 286
|
|
| IlvC |
pfam01450 |
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
213-340 |
7.16e-28 |
|
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: 107.94 E-value: 7.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 213 EVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDP--AYAEKLiqfgWET--ITEALKQGGITLMMDRLSNPAKLRAYAL 288
Cdd:pfam01450 3 ETETDLFGEQAVLCGGVTGLVKAGFETLVEAGYQPeaAYFECL----HELklIVDLIYEGGIAGMRYSISDTAEYGDLTR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1382576672 289 SEQLKT-IMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFE 340
Cdd:pfam01450 79 GPRVIYdATKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIE 131
|
|
| IlvC |
pfam01450 |
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
358-478 |
5.32e-20 |
|
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: 85.98 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 358 GVLMiAMVKAGVELAFETMVAAGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYL----FANAAV-PLL 432
Cdd:pfam01450 13 AVLC-GGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTrgprVIYDATkELM 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1382576672 433 KEFMTKLQPGDLGKAV-EGTAVDNAQLRDVNDAIRSHEIEKVGQKLR 478
Cdd:pfam01450 92 KEILDEIQSGEFAKEWiLEYQAGRPELKALRREEAEHPIEKVGKELR 138
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
37-139 |
1.63e-04 |
|
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: 43.98 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVN 104
Cdd:cd00401 195 GKVVVVAGygwVG-----KGCAMRARGLgarvivtevDPICAL--QAAMD-----------GFEVMPMEEAAKIGDIFVT 256
|
90 100 110
....*....|....*....|....*....|....*.
gi 1382576672 105 LTPDKqhsDVVRAVQ-PLMKDGAALGYSHGFNiVEV 139
Cdd:cd00401 257 ATGNK---DVIRGEHfEKMKDGAILCNAGHFD-VEI 288
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
35-128 |
7.17e-04 |
|
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: 40.56 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 35 LKGKKVVIVGCGAQGLN-----QGLNMRDSGLDVSyaLRKEAIAEkraswrkatENGFQVGTYEELIPQADLVVN---LT 106
Cdd:pfam02826 34 LSGKTVGIIGLGRIGRAvakrlKAFGMKVIAYDRY--PKPEEEEE---------ELGARYVSLDELLAESDVVSLhlpLT 102
|
90 100
....*....|....*....|..
gi 1382576672 107 PDKQHSdVVRAVQPLMKDGAAL 128
Cdd:pfam02826 103 PETRHL-INAERLALMKPGAIL 123
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
37-135 |
7.25e-04 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.13 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVGCGAQGlnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVNLTP 107
Cdd:smart00997 23 GKNVVVAGYGDVG--KGVAARLRGLgarvivteiDPIRAL--EAAMD-----------GFEVMKMEEAAKRADIFVTATG 87
|
90 100
....*....|....*....|....*....
gi 1382576672 108 DKqhsDVVRAVQPL-MKDGAALGYSHGFN 135
Cdd:smart00997 88 NK---DVITREHFRaMKDGAILANAGHFD 113
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
35-109 |
2.19e-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: 37.46 E-value: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1382576672 35 LKGKKVVIVGCGAQGLNQGLNMRDSGLDVS-YALRKEAIAEKRASWRKAtengfqvgTYEELIPQADLVVNLTPDK 109
Cdd:pfam13241 5 LRGKRVLVVGGGEVAARKARKLLEAGAKVTvVSPEITPFLEGLLDLIRR--------EFEGDLDGADLVIAATDDP 72
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
37-139 |
4.11e-03 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 39.65 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVN 104
Cdd:COG0499 209 GKTVVVAGygwCG-----KGVAMRARGLgarvivtevDPICAL--EAAMD-----------GFRVMPMEEAAKLGDIFVT 270
|
90 100 110
....*....|....*....|....*....|....*.
gi 1382576672 105 LTPDKqhsDVVRAVQ-PLMKDGAALGYSHGFNiVEV 139
Cdd:COG0499 271 ATGNK---DVITAEHfEAMKDGAILANAGHFD-VEI 302
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
38-126 |
5.77e-03 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 38.57 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 38 KKVVIVGCG------AQGL-NQGLNMRDSGLDVSYALRKEAIAEK---RASWrkatengfqvgTYEELIPQADLVVNLTP 107
Cdd:COG0287 2 MRIAIIGLGliggslALALkRAGLAHEVVGVDRSPETLERALELGvidRAAT-----------DLEEAVADADLVVLAVP 70
|
90
....*....|....*....
gi 1382576672 108 DKQHSDVVRAVQPLMKDGA 126
Cdd:COG0287 71 VGATIEVLAELAPHLKPGA 89
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
37-136 |
6.33e-03 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 38.95 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382576672 37 GKKVVIVG---CGaqglnQGLNMRDSGL---------DVSYALrkEAIAEkraswrkatenGFQVGTYEELIPQADLVVN 104
Cdd:PRK05476 212 GKVVVVAGygdVG-----KGCAQRLRGLgarvivtevDPICAL--QAAMD-----------GFRVMTMEEAAELGDIFVT 273
|
90 100 110
....*....|....*....|....*....|...
gi 1382576672 105 LTPDKqhsDVVRAVQ-PLMKDGAALGYSHGFNI 136
Cdd:PRK05476 274 ATGNK---DVITAEHmEAMKDGAILANIGHFDN 303
|
|
| |
