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Conserved domains on  [gi|740843305|ref|WP_038628558|]
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MULTISPECIES: ketol-acid reductoisomerase [Corynebacterium]

Protein Classification

NADP-dependent ketol-acid reductoisomerase( domain architecture ID 11481043)

NADP-dependent ketol-acid reductoisomerase catalyzes the conversion of 2-(S)-acetolactate (2SAL) into (R)-dihydroxyisovalerate (RDHIV), the second step in the biosynthesis of the branched-chain amino acids (BCAAs) valine, leucine and isoleucine

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0004455|GO:0050661|GO:0009099|GO:0000287|GO:0009097
PubMed:  25849365

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 2-330 0e+00

ketol-acid reductoisomerase; Provisional


:

Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 623.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   2 AIELLYDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVL 81
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  82 VPDTTQAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGE 161
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 162 GRDLALSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMF 241
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 242 EGGIANMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSK 321
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320


                 ....*....
gi 740843305 322 LRDLMSWVK 330
Cdd:PRK05479 321 LRAMMPWIK 329
 
Name Accession Description Interval E-value
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 2-330 0e+00

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 623.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   2 AIELLYDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVL 81
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  82 VPDTTQAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGE 161
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 162 GRDLALSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMF 241
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 242 EGGIANMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSK 321
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320


                 ....*....
gi 740843305 322 LRDLMSWVK 330
Cdd:PRK05479 321 LRAMMPWIK 329
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 1-329 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: 587.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   1 MAiELLYDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMV 80
Cdd:COG0059    1 MA-KIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEEDGFEVMTVAEAAKRADVIMI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  81 LVPDTTQAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKG 160
Cdd:COG0059   80 LTPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 161 EGRDLALSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLM 240
Cdd:COG0059  160 KAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 241 FEGGIANMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGS 320
Cdd:COG0059  240 YEGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGA 319


                 ....*....
gi 740843305 321 KLRDLMSWV 329
Cdd:COG0059  320 ELRAMMPWL 328
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 16-330 7.01e-141

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: 401.37  E-value: 7.01e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   16 IQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQAKVYSEDI 95
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGGASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   96 EPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGEGRDLALSYAAAIGG 175
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  176 ARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMFEGGIANMNYSVSDT 255
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843305  256 AEFGGYLSGpRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSKLRDLMSWVK 330
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 15-169 1.78e-96

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: 282.90  E-value: 1.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   15 IIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQAKVYSED 94
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGSKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843305   95 IEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGEGRDLALSY 169
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAY 155
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
15-78 1.92e-04

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 41.28  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740843305    15 IIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREgsksAVKAQEA---GFEVKSNADAAAWADVI 78
Cdd:smart00997  20 LLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEID----PIRALEAamdGFEVMKMEEAAKRADIF 82
 
Name Accession Description Interval E-value
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 2-330 0e+00

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 623.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   2 AIELLYDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVL 81
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  82 VPDTTQAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGE 161
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 162 GRDLALSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMF 241
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 242 EGGIANMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSK 321
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320


                 ....*....
gi 740843305 322 LRDLMSWVK 330
Cdd:PRK05479 321 LRAMMPWIK 329
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 1-329 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: 587.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   1 MAiELLYDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMV 80
Cdd:COG0059    1 MA-KIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKKAEEDGFEVMTVAEAAKRADVIMI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  81 LVPDTTQAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKG 160
Cdd:COG0059   80 LTPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 161 EGRDLALSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLM 240
Cdd:COG0059  160 KAKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 241 FEGGIANMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGS 320
Cdd:COG0059  240 YEGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGA 319


                 ....*....
gi 740843305 321 KLRDLMSWV 329
Cdd:COG0059  320 ELRAMMPWL 328
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 16-330 7.01e-141

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: 401.37  E-value: 7.01e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   16 IQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQAKVYSEDI 95
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGGASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   96 EPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGEGRDLALSYAAAIGG 175
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  176 ARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMFEGGIANMNYSVSDT 255
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843305  256 AEFGGYLSGpRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSKLRDLMSWVK 330
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 7-330 2.41e-128

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 370.23  E-value: 2.41e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   7 YDDDADLSIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGsKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTT 86
Cdd:PRK13403   5 YEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPG-KSFEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  87 QAKVYSEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGEGRDLA 166
Cdd:PRK13403  84 QAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 167 LSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMFEGGIA 246
Cdd:PRK13403 164 LAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGGLT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 247 NMNYSVSDTAEFGGYLSGPRVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSKLRDLM 326
Cdd:PRK13403 244 NMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELREMM 323


                 ....
gi 740843305 327 SWVK 330
Cdd:PRK13403 324 SWIH 327
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 15-169 1.78e-96

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: 282.90  E-value: 1.78e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   15 IIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQAKVYSED 94
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGSKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843305   95 IEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPKGEGRDLALSY 169
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAY 155
IlvC pfam01450
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ...
 186-323 3.69e-77

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: 232.74  E-value: 3.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  186 EAETVTDLFGEQAVLCGGTEELVKVGFEVLVEAGYEPEMAYFECLHELKLIVDLMFEGGIANMNYSVSDTAEFGGYLSGP 265
Cdd:pfam01450   1 KEETETDLFGEQAVLCGGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTRGP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 740843305  266 RVITADTKQHMREILSDIQDGTFTKRLIANVEGGNKELEDLRASYNNHQIEEVGSKLR 323
Cdd:pfam01450  81 RVIYDATKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIEKVGKELR 138
PRK05225 PRK05225
ketol-acid reductoisomerase; Validated
 14-330 3.12e-44

ketol-acid reductoisomerase; Validated


Pssm-ID: 235368 [Multi-domain]  Cd Length: 487  Bit Score: 158.20  E-value: 3.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  14 SIIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREGS-----KSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQA 88
Cdd:PRK05225  32 SYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEAiaekrASWRKATENGFKVGTYEELIPQADLVINLTPDKQHS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  89 KVYsEDIEPNLKDGDALFFGHGLNIHFDLIKPADNITVGMVAPKGPGHLVRRQFVDGKGVPCLIAV--DQDPKGEGRDLA 166
Cdd:PRK05225 112 DVV-RAVQPLMKQGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVhpENDPKGEGMAIA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 167 LSYAAAIGGARAGVIPTTFEAETVTDLFGEQAVLCG----------------GT-------------------------- 204
Cdd:PRK05225 191 KAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGmlqagsllcfdklvaeGTdpayaekliqfgwetitealkqggit 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 205 ------------------EEL----------------------------------------------------------- 207
Cdd:PRK05225 271 lmmdrlsnpakirafelsEQLkeimaplfqkhmddiisgefsstmmadwanddkklltwreetgktafenapqyegkise 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 208 -------------VKVG----FEVLVEAGYEPEMAYFECLHELKLIVDLMFEGGIANMNYSVSDTAEFGGYLSGPRVITA 270
Cdd:PRK05225 351 qeyfdkgvlmvamVKAGvelaFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSHAAVPL 430

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305 271 dtkqhMREILSDIQDGTFTKRLIANvEGGNKELEDLRASYNNHQIEEVGSKLRDLMSWVK 330
Cdd:PRK05225 431 -----LKDFMATLQPGDLGKGLPSN-AVDNAQLRDVNEAIRNHPIEQVGKKLRGYMTDMK 484
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
21-83 1.29e-07

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 51.32  E-value: 1.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843305  21 VAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVK--SNADAAAWADVIMVLVP 83
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGARagTNAEAAAAADVVVLAVP 65
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
22-83 4.37e-05

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 41.45  E-value: 4.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740843305   22 AILGYGSQGHAHAQNLRESGV-EVVIGLREGSKSAVK-AQEAGFEVK--SNADAAAWADVIMVLVP 83
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPhEVVVANSRNPEKAEElAEEYGVGATavDNEEAAEEADVVFLAVK 66
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 20-105 7.61e-05

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: 42.46  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305   20 KVAILGYGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKSNADAAAWADVIMVLVPDTTQAK-VYSED-IEP 97
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDaVIFGEgLLP 80


                  ....*...
gi 740843305   98 NLKDGDAL 105
Cdd:pfam03446  81 GLKPGDII 88
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
15-78 1.92e-04

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 41.28  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740843305    15 IIQGRKVAILGYGSQGHAHAQNLRESGVEVVIGLREgsksAVKAQEA---GFEVKSNADAAAWADVI 78
Cdd:smart00997  20 LLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEID----PIRALEAamdGFEVMKMEEAAKRADIF 82
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 20-106 1.70e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 39.97  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  20 KVAILG-YGSQGHAHAQNLRESGVEVVIGLREGSKSAVKAQEAGFEVKS-NADAAAWADVIMVLVPDTTQAKVYSEdIEP 97
Cdd:PRK08655   2 KISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANdNIDAAKDADIVIISVPINVTEDVIKE-VAP 80


                 ....*....
gi 740843305  98 NLKDGDALF 106
Cdd:PRK08655  81 HVKEGSLLM 89
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 20-102 7.83e-03

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 37.40  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843305  20 KVAILGYGSQGHAHAQNLRESGVEVVIGLRegSKSAVKA-QEAGFEV-KSNADAAAWADVIMVLVPDTTQAK-VYSED-- 94
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNR--TPAKAEAlVAAGARVaASPAEAAAAADVVITMLPDDAAVEeVLLGEdg 80


                 ....*...
gi 740843305  95 IEPNLKDG 102
Cdd:COG2084   81 LLAALRPG 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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