|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05479 |
PRK05479 |
ketol-acid reductoisomerase; Provisional |
1-329 |
0e+00 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 648.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 1 MTKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMIL 79
Cdd:PRK05479 1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 80 LPDELQPEVYEAEIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGV 159
Cdd:PRK05479 81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 160 ATEKALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMY 239
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 240 EGGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRK 319
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320
|
330
....*....|
gi 872689662 320 LREMMPFVQP 329
Cdd:PRK05479 321 LRAMMPWIKK 330
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
1-327 |
0e+00 |
|
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: 625.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 1 MTKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMIL 79
Cdd:COG0059 1 MAKIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEEDGFEVMTVAEAAKRADVIMIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 80 LPDELQPEVYEAEIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGV 159
Cdd:COG0059 81 TPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 160 ATEKALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMY 239
Cdd:COG0059 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 240 EGGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRK 319
Cdd:COG0059 241 EGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAE 320
|
....*...
gi 872689662 320 LREMMPFV 327
Cdd:COG0059 321 LRAMMPWL 328
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
15-328 |
1.85e-166 |
|
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: 466.08 E-value: 1.85e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQPEVYEAEI 93
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGgASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 94 APNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGVATEKALSYADGIGA 173
Cdd:TIGR00465 81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 174 TRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYEGGLENMRYSVSDT 253
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872689662 254 AQWGDFVSGpRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRKLREMMPFVQ 328
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
14-177 |
6.68e-111 |
|
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: 319.49 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 14 VLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQPEVYEAE 92
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 93 IAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGVATEKALSYADGIG 172
Cdd:pfam07991 81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160
|
....*
gi 872689662 173 ATRAG 177
Cdd:pfam07991 161 GTRAG 165
|
|
| formate_dh_like |
cd05198 |
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
15-81 |
3.84e-04 |
|
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 41.46 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDkAKEDGFSVYTVAEAAEKADVVMILLP 81
Cdd:cd05198 138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEP-EEDLGFRVVSLDELLAQSDVVVLHLP 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05479 |
PRK05479 |
ketol-acid reductoisomerase; Provisional |
1-329 |
0e+00 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 648.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 1 MTKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMIL 79
Cdd:PRK05479 1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 80 LPDELQPEVYEAEIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGV 159
Cdd:PRK05479 81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 160 ATEKALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMY 239
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 240 EGGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRK 319
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320
|
330
....*....|
gi 872689662 320 LREMMPFVQP 329
Cdd:PRK05479 321 LRAMMPWIKK 330
|
|
| IlvC |
COG0059 |
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
1-327 |
0e+00 |
|
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: 625.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 1 MTKVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMIL 79
Cdd:COG0059 1 MAKIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEEDGFEVMTVAEAAKRADVIMIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 80 LPDELQPEVYEAEIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGV 159
Cdd:COG0059 81 TPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 160 ATEKALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMY 239
Cdd:COG0059 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 240 EGGLENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRK 319
Cdd:COG0059 241 EGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAE 320
|
....*...
gi 872689662 320 LREMMPFV 327
Cdd:COG0059 321 LRAMMPWL 328
|
|
| ilvC |
TIGR00465 |
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
15-328 |
1.85e-166 |
|
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: 466.08 E-value: 1.85e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQPEVYEAEI 93
Cdd:TIGR00465 1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGgASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 94 APNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGVATEKALSYADGIGA 173
Cdd:TIGR00465 81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 174 TRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYEGGLENMRYSVSDT 253
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872689662 254 AQWGDFVSGpRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRKLREMMPFVQ 328
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
|
|
| PRK13403 |
PRK13403 |
ketol-acid reductoisomerase; Provisional |
3-328 |
3.92e-151 |
|
ketol-acid reductoisomerase; Provisional
Pssm-ID: 106361 [Multi-domain] Cd Length: 335 Bit Score: 428.01 E-value: 3.92e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 3 KVYYEKDVTVNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDGFSVYTVAEAAEKADVVMILLPD 82
Cdd:PRK13403 2 KTYYEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFEVMSVSEAVRTAQVVQMLLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 83 ELQPEVYEAEIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGVATE 162
Cdd:PRK13403 82 EQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 163 KALSYADGIGATRAGVLETTFKEETETDLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYEGG 242
Cdd:PRK13403 162 VALAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 243 LENMRYSVSDTAQWGDFVSGPRVVTEDTKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRKLRE 322
Cdd:PRK13403 242 LTNMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELRE 321
|
....*.
gi 872689662 323 MMPFVQ 328
Cdd:PRK13403 322 MMSWIH 327
|
|
| IlvN |
pfam07991 |
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
14-177 |
6.68e-111 |
|
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: 319.49 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 14 VLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG-KSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQPEVYEAE 92
Cdd:pfam07991 1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 93 IAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVYQDATGVATEKALSYADGIG 172
Cdd:pfam07991 81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160
|
....*
gi 872689662 173 ATRAG 177
Cdd:pfam07991 161 GTRAG 165
|
|
| IlvC |
pfam01450 |
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
190-321 |
2.06e-78 |
|
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: 235.83 E-value: 2.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 190 DLFGEQAVLCGGVTALVKAGFETLVDAGYQPELAYFECLHELKLIVDLMYEGGLENMRYSVSDTAQWGDFVSGPRVVTED 269
Cdd:pfam01450 7 DLFGEQAVLCGGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTRGPRVIYDA 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 872689662 270 TKKAMGAVLAEIQDGTFARGWIAEHKAGKPNFHATNEKENEHEIEVVGRKLR 321
Cdd:pfam01450 87 TKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIEKVGKELR 138
|
|
| PRK05225 |
PRK05225 |
ketol-acid reductoisomerase; Validated |
12-324 |
1.22e-40 |
|
ketol-acid reductoisomerase; Validated
Pssm-ID: 235368 [Multi-domain] Cd Length: 487 Bit Score: 148.18 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 12 VNVLKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKG------KSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQ 85
Cdd:PRK05225 31 ASYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEaiaekrASWRKATENGFKVGTYEELIPQADLVINLTPDKQH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 86 PEVYEAeIAPNLKAGNSLVFAHGFNVHFDQVKPPANVDVFLVAPKGPGHLVRRTFAEGGAVPALFAVY--QDATGVATEK 163
Cdd:PRK05225 111 SDVVRA-VQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHpeNDPKGEGMAI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 164 ALSYADGIGATRAGVLETTFKEETETDLFGEQAVLC-----------------------------------------GGV 202
Cdd:PRK05225 190 AKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCgmlqagsllcfdklvaegtdpayaekliqfgwetitealkqGGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 203 T------------------------------------------------------------------------------- 203
Cdd:PRK05225 270 Tlmmdrlsnpakirafelseqlkeimaplfqkhmddiisgefsstmmadwanddkklltwreetgktafenapqyegkis 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 204 ------------ALVKAG----FETLVDAGYQPELAYFECLHELKLIVDLMYEGGLENMRYSVSDTAQWG----DFVSGP 263
Cdd:PRK05225 350 eqeyfdkgvlmvAMVKAGvelaFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGnylfSHAAVP 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872689662 264 RVvtedtKKAMGAVLAEIQDGTFARGWIAEHKagkpnFHATNEKENEHEIEVVGRKLREMM 324
Cdd:PRK05225 430 LL-----KDFMATLQPGDLGKGLPSNAVDNAQ-----LRDVNEAIRNHPIEQVGKKLRGYM 480
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
19-100 |
4.56e-08 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 51.70 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 19 KVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDGFSV-YTVAEAAEKADVVMILLPDElQP--EVYEAE-IA 94
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAaASPAEFVAGLDVVITMVPAG-AAvdAVIFGEgLL 79
|
....*.
gi 872689662 95 PNLKAG 100
Cdd:pfam03446 80 PGLKPG 85
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
18-100 |
8.45e-07 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 49.73 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 18 KKVAIIGYGSQGHAHAQNLRDNGFDVVV-GLRKGKSwDKAKEDGFSVY-TVAEAAEKADVVMILLPDElqPEVYEA---- 91
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAGHEVTVwNRTPAKA-EALVAAGARVAaSPAEAAAAADVVITMLPDD--AAVEEVllge 78
|
90
....*....|
gi 872689662 92 -EIAPNLKAG 100
Cdd:COG2084 79 dGLLAALRPG 88
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
18-105 |
1.61e-06 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 49.22 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 18 KKVAIIG-YGSQGHAHAQNLRDNGFDVVVGLRKGKSWDK-AKEDGFSVYT-VAEAAEKADVVMILLPDELQPEVYEaEIA 94
Cdd:PRK08655 1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEvAKELGVEYANdNIDAAKDADIVIISVPINVTEDVIK-EVA 79
|
90
....*....|.
gi 872689662 95 PNLKAGnSLVF 105
Cdd:PRK08655 80 PHVKEG-SLLM 89
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
15-81 |
2.88e-05 |
|
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: 44.02 E-value: 2.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDGFSVYTVAEAAEKADVVMILLP 81
Cdd:pfam02826 34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSLHLP 100
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
19-100 |
5.25e-05 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 44.14 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 19 KVAIIGYGSQGHAHAQNLRDN-GFDVV--VGLRKGKSWDKAKEDGFSVYT-VAE--AAEKADVVMILLPDELQPEVyeAE 92
Cdd:COG0673 5 RVGIIGAGGIGRAHAPALAALpGVELVavADRDPERAEAFAEEYGVRVYTdYEEllADPDIDAVVIATPNHLHAEL--AI 82
|
....*...
gi 872689662 93 IApnLKAG 100
Cdd:COG0673 83 AA--LEAG 88
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
20-114 |
5.39e-05 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 43.62 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 20 VAIIGYGSQGHAHAQNLRDNGFDVVVGLR---KGKSWDKAKEDGFSVYTVAEAAEKADVVMILLPDELQPEVYEAeIAPN 96
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVIGSRdpeKAAALAAELGPGARAGTNAEAAAAADVVVLAVPYEAVPDVLES-LGDA 79
|
90 100
....*....|....*....|....
gi 872689662 97 LK------AGNSLVFAHGFNVHFD 114
Cdd:COG2085 80 LAgkividATNPLPERDGFILDPP 103
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
17-96 |
2.45e-04 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 42.35 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 17 EKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDKAKEDG-FSVYTVAEAAEKADVVMILLPDelQPEVYEAEIAP 95
Cdd:PRK11559 2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGaETASTAKAVAEQCDVIITMLPN--SPHVKEVALGE 79
|
.
gi 872689662 96 N 96
Cdd:PRK11559 80 N 80
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
18-100 |
2.57e-04 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 42.26 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 18 KKVAIIGYGSQGHAHAQNLRDNGF--DVVVGLRKGKSWDKAKEDGFS---VYTVAEAAEKADVVMILLPDELQPEVyEAE 92
Cdd:PRK07502 7 DRVALIGIGLIGSSLARAIRRLGLagEIVGADRSAETRARARELGLGdrvTTSAAEAVKGADLVILCVPVGASGAV-AAE 85
|
....*...
gi 872689662 93 IAPNLKAG 100
Cdd:PRK07502 86 IAPHLKPG 93
|
|
| formate_dh_like |
cd05198 |
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
15-81 |
3.84e-04 |
|
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 41.46 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRDNGFDVVVGLRKGKSWDkAKEDGFSVYTVAEAAEKADVVMILLP 81
Cdd:cd05198 138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEP-EEDLGFRVVSLDELLAQSDVVVLHLP 203
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
18-76 |
1.92e-03 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 39.72 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872689662 18 KKVAIIGYGSQGHAHAQNLRDNGFDVVVglrkgksWD-------KAKEDGFSVYTVAEAAEKADVV 76
Cdd:PRK05476 213 KVVVVAGYGDVGKGCAQRLRGLGARVIV-------TEvdpicalQAAMDGFRVMTMEEAAELGDIF 271
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
21-98 |
3.74e-03 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 36.06 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 21 AIIGYGSQGHAHAQNLRDNG-FDVVVGLR----KGKSWDKAKEDGFSVYTVAEAAEKADVVMILLPdelqPEVYE---AE 92
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGpHEVVVANSrnpeKAEELAEEYGVGATAVDNEEAAEEADVVFLAVK----PEDAPdvlSE 76
|
....*.
gi 872689662 93 IAPNLK 98
Cdd:pfam03807 77 LSDLLK 82
|
|
| 2-Hacid_dh_6 |
cd12165 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
15-81 |
4.96e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 38.38 E-value: 4.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872689662 15 LKEKKVAIIGYGSQGHAHAQNLRdnGFDV-VVGLRKGKswdKAKEDGFSVYTVA---EAAEKADVVMILLP 81
Cdd:cd12165 135 LRGKTVGILGYGHIGREIARLLK--AFGMrVIGVSRSP---KEDEGADFVGTLSdldEALEQADVVVVALP 200
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
16-98 |
7.93e-03 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 396961 [Multi-domain] Cd Length: 97 Bit Score: 35.26 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872689662 16 KEKKVAIIGYGSQGHA----HAQNLRDNGFDVVVGLRKGKSWDKAkeDGFSVY-TVAEAAEK--ADVVMILLPDELQPEV 88
Cdd:pfam02629 2 KDTKVIVIGAGGLGIQglnyHFIQMLGYGIKMVFGVNPGKGGTEI--LGIPVYnSVDELEEKtgVDVAVITVPAPFAQEA 79
|
90
....*....|
gi 872689662 89 YEAEIAPNLK 98
Cdd:pfam02629 80 IDELVDAGIK 89
|
|
| |
