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Conserved domains on  [gi|516234154|ref|WP_017638117|]
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MULTISPECIES: ketol-acid reductoisomerase [Staphylococcus]

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

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List of domain hits

 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: 633.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   1 MTKVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVL 79
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  80 IPDEIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGH 159
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 160 ARDIALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMY 239
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 240 EGGMDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRD 319
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320

                        330
                 ....*....|
gi 516234154 320 LRDMMPFIKS 329
Cdd:PRK05479 321 LRAMMPWIKK 330
 
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: 633.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   1 MTKVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVL 79
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  80 IPDEIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGH 159
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 160 ARDIALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMY 239
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 240 EGGMDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRD 319
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320

                        330
                 ....*....|
gi 516234154 320 LRDMMPFIKS 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: 615.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   1 MTKVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGR-SFDKAKENGFEVLPVDEATKQADVVMVL 79
Cdd:COG0059    1 MAKIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSkSWKKAEEDGFEVMTVAEAAKRADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  80 IPDEIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGH 159
Cdd:COG0059   81 TPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 160 ARDIALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMY 239
Cdd:COG0059  161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 240 EGGMDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRD 319
Cdd:COG0059  241 EGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAE 320


                 ....*...
gi 516234154 320 LRDMMPFI 327
Cdd:COG0059  321 LRAMMPWL 328
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 15-328 1.24e-154

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: 436.04  E-value: 1.24e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVLIPDEIQGDVYKNEI 93
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGgASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   94 SPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGHARDIALSYAKGIGS 173
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  174 TRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMDNVRYSISNT 253
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516234154  254 AEYGDYVSGpRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRDLRDMMPFIK 328
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 14-177 1.31e-106

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: 308.32  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   14 ALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVLIPDEIQGDVYKNE 92
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   93 ISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGHARDIALSYAKGIG 172
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
gi 516234154  173 STRAG 177
Cdd:pfam07991 161 GTRAG 165
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 15-76 5.06e-05

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: 44.75  E-value: 5.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFdKAKENGFEVLPVDEATKQADVV 76
Cdd:cd00401  193 IAGKVVVVAGYGWVGKGCAMRARGLGARVIVTeVDPICAL-QAAMDGFEVMPMEEAAKIGDIF 254
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
15-76 1.80e-04

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 41.28  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154    15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDV-VIGIRPGRSFdKAKENGFEVLPVDEATKQADVV 76
Cdd:smart00997  21 LAGKNVVVAGYGDVGKGVAARLRGLGARViVTEIDPIRAL-EAAMDGFEVMKMEEAAKRADIF 82
 
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: 633.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   1 MTKVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVL 79
Cdd:PRK05479   1 MMKVYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  80 IPDEIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGH 159
Cdd:PRK05479  81 LPDEVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 160 ARDIALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMY 239
Cdd:PRK05479 161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 240 EGGMDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRD 319
Cdd:PRK05479 241 EGGIANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAK 320

                        330
                 ....*....|
gi 516234154 320 LRDMMPFIKS 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: 615.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   1 MTKVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGR-SFDKAKENGFEVLPVDEATKQADVVMVL 79
Cdd:COG0059    1 MAKIYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSkSWKKAEEDGFEVMTVAEAAKRADVIMIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  80 IPDEIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGH 159
Cdd:COG0059   81 TPDEVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 160 ARDIALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMY 239
Cdd:COG0059  161 AKDLALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 240 EGGMDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRD 319
Cdd:COG0059  241 EGGIANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAE 320


                 ....*...
gi 516234154 320 LRDMMPFI 327
Cdd:COG0059  321 LRAMMPWL 328
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 15-328 1.24e-154

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: 436.04  E-value: 1.24e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVLIPDEIQGDVYKNEI 93
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGgASWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   94 SPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGHARDIALSYAKGIGS 173
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  174 TRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMDNVRYSISNT 253
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516234154  254 AEYGDYVSGpRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRDLRDMMPFIK 328
Cdd:TIGR00465 241 AEYGALTRR-RIIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 3-331 1.75e-141

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 403.36  E-value: 1.75e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   3 KVYYDETVKTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGRSFDKAKENGFEVLPVDEATKQADVVMVLIPD 82
Cdd:PRK13403   2 KTYYEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFEVMSVSEAVRTAQVVQMLLPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  83 EIQGDVYKNEISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGHARD 162
Cdd:PRK13403  82 EQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 163 IALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGG 242
Cdd:PRK13403 162 VALAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 243 MDNVRYSISNTAEYGDYVSGPRVITPDVKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRDLRD 322
Cdd:PRK13403 242 LTNMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELRE 321


                 ....*....
gi 516234154 323 MMPFIKSKR 331
Cdd:PRK13403 322 MMSWIHAPK 330
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 14-177 1.31e-106

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: 308.32  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   14 ALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG-RSFDKAKENGFEVLPVDEATKQADVVMVLIPDEIQGDVYKNE 92
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   93 ISPNLESGNALAFAHGFNIHFGVIQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGVQQDATGHARDIALSYAKGIG 172
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
gi 516234154  173 STRAG 177
Cdd:pfam07991 161 GTRAG 165
IlvC pfam01450
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ...
 190-321 6.50e-82

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: 244.68  E-value: 6.50e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  190 DLFGEQAVLCGGVHKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMDNVRYSISNTAEYGDYVSGPRVITPD 269
Cdd:pfam01450   7 DLFGEQAVLCGGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTRGPRVIYDA 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 516234154  270 VKENMKAVLTDIQNGKFANSFVEDNKNGFKEFYRMREEQAGHPIEKVGRDLR 321
Cdd:pfam01450  87 TKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIEKVGKELR 138
PRK05225 PRK05225
ketol-acid reductoisomerase; Validated
 13-329 8.38e-46

ketol-acid reductoisomerase; Validated


Pssm-ID: 235368 [Multi-domain]  Cd Length: 487  Bit Score: 162.05  E-value: 8.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  13 DALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPG------RSFDKAKENGFEVLPVDEATKQADVVMVLIPDEIQG 86
Cdd:PRK05225  32 SYLKGKKIVIVGCGAQGLNQGLNMRDSGLDISYALRKEaiaekrASWRKATENGFKVGTYEELIPQADLVINLTPDKQHS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  87 DVYkNEISPNLESGNALAFAHGFNI-HFGViQPPEDVDVFLVAPKGPGHLVRRTFEEGSAVPSLFGV--QQDATGHARDI 163
Cdd:PRK05225 112 DVV-RAVQPLMKQGAALGYSHGFNIvEVGE-QIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVhpENDPKGEGMAI 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 164 ALSYAKGIGSTRAGVIETTFKEETETDLFGEQAVLCG----------------GVH-----KLIQSG------------- 209
Cdd:PRK05225 190 AKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGmlqagsllcfdklvaeGTDpayaeKLIQFGwetitealkqggi 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154     --------------------------------------------------------------------------------
Cdd:PRK05225 270 tlmmdrlsnpakirafelseqlkeimaplfqkhmddiisgefsstmmadwanddkklltwreetgktafenapqyegkis 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154 210 ----------------------FETLVEAGYQPELAYFEVLHEMKLIVDL-----MYEggMDNVrysISNTAEYGDYVSG 262
Cdd:PRK05225 350 eqeyfdkgvlmvamvkagvelaFETMVDSGIIEESAYYESLHELPLIANTiarkrLYE--MNVV---ISDTAEYGNYLFS 424

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154 263 pRVITPDVKENMKAVLTDIQNGKFANSFVeDNkngfKEFYRMREEQAGHPIEKVGRDLRDMMPFIKS 329
Cdd:PRK05225 425 -HAAVPLLKDFMATLQPGDLGKGLPSNAV-DN----AQLRDVNEAIRNHPIEQVGKKLRGYMTDMKR 485
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
20-81 2.90e-07

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 50.17  E-value: 2.90e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516234154  20 IAVIGYGSQGHAHAQNLKDNGYDVVIGIR-PGRSFDKAKENGFEVLPVD--EATKQADVVMVLIP 81
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRdPEKAAALAAELGPGARAGTnaEAAAAADVVVLAVP 65
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 19-100 4.43e-06

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: 45.92  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   19 KIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGRSFDKAKENGFEVLP-VDEATKQADVVMVLIPDEIQGD-VYKNE-ISP 95
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAsPAEFVAGLDVVITMVPAGAAVDaVIFGEgLLP 80


                  ....*
gi 516234154   96 NLESG 100
Cdd:pfam03446  81 GLKPG 85
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 15-81 1.17e-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: 45.18  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516234154   15 LAGKKIAVIGYGSQGHAHAQNLKdnGYDV-VIGIRP-GRSFDKAKENGFEVLPVDEATKQADVVMVLIP 81
Cdd:pfam02826  34 LSGKTVGIIGLGRIGRAVAKRLK--AFGMkVIAYDRyPKPEEEEEELGARYVSLDELLAESDVVSLHLP 100
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 15-76 5.06e-05

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: 44.75  E-value: 5.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFdKAKENGFEVLPVDEATKQADVV 76
Cdd:cd00401  193 IAGKVVVVAGYGWVGKGCAMRARGLGARVIVTeVDPICAL-QAAMDGFEVMPMEEAAKIGDIF 254
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 11-75 6.77e-05

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 43.35  E-value: 6.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154  11 KTDALAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKENGFEVLPVDEATKQ-ADV 75
Cdd:cd01075   22 GTDSLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVAdINEEAVARAAELFGATVVAPEEIYSVdADV 88
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 18-103 7.08e-05

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 44.21  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  18 KKIAVIG-YGSQGHAHAQNLKDNGYDVVIGirpGRSFDK----AKENGFEVLP-VDEATKQADVVMVLIPDEIQGDVYKn 91
Cdd:PRK08655   1 MKISIIGgTGGLGKWFARFLKEKGFEVIVT---GRDPKKgkevAKELGVEYANdNIDAAKDADIVIISVPINVTEDVIK- 76

                         90
                 ....*....|..
gi 516234154  92 EISPNLESGNAL 103
Cdd:PRK08655  77 EVAPHVKEGSLL 88
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 15-81 8.29e-05

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 43.63  E-value: 8.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKdnGYDV-VIGIRPGRSFDKAKENGFEVLPVDEATKQADVVMVLIP 81
Cdd:cd12172  140 LYGKTLGIIGLGRIGKAVARRLS--GFGMkVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISLHLP 205
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 15-76 1.32e-04

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: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 43.21  E-value: 1.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGrsfdkAKENGFEVLPVDEATKQADVV 76
Cdd:cd12162  145 LAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKG-----APPLREGYVSLDELLAQSDVI 201
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 15-76 1.49e-04

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 43.19  E-value: 1.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADVV 76
Cdd:PRK05476 210 IAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTeVDPICALQAAMD-GFRVMTMEEAAELGDIF 271
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
15-76 1.80e-04

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 41.28  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154    15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDV-VIGIRPGRSFdKAKENGFEVLPVDEATKQADVV 76
Cdd:smart00997  21 LAGKNVVVAGYGDVGKGVAARLRGLGARViVTEIDPIRAL-EAAMDGFEVMKMEEAAKRADIF 82
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 8-81 4.90e-04

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: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 41.42  E-value: 4.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154   8 ETVKTDALAGKKIAVIGYGSQGHAHAQNLKdnGYDVVIgIRPGRSfdkAKEnGFEVLPVDEATK---QADVVMVLIP 81
Cdd:cd12166  123 EPRRTPSLADRRVLIVGYGSIGRAIERRLA--PFEVRV-TRVART---ARP-GEQVHGIDELPAllpEADVVVLIVP 192
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
12-76 5.94e-04

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 40.03  E-value: 5.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154   12 TDAL-AGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADVV 76
Cdd:pfam00670  17 TDVMiAGKVAVVCGYGDVGKGCAASLKGQGARVIVTeIDPICALQAAME-GFQVVTLEEVVDKADIF 82
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 18-82 1.08e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.05  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516234154  18 KKIAVIGYGSQGHAHAQNLKDNGYDV-VIGIRPGRsFDKAKENGFEVL---PVDEAT------KQADVVMVLIPD 82
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVvVIDKDPER-VERLAEEDVLVIvgdATDEEVleeagiEDADAVIAATGD 169
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 6-81 1.08e-03

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, 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. 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: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 40.26  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154   6 YDETVKTDALAGKKIAVIGYGSQGHAHAQNLKdnGYDV-VIGI-RPGRS---FDK--AKENGFEVLpvdeatKQADVVMV 78
Cdd:cd12155  124 WKMDSSLLELYGKTILFLGTGSIGQEIAKRLK--AFGMkVIGVnTSGRDveyFDKcyPLEELDEVL------KEADIVVN 195


                 ...
gi 516234154  79 LIP 81
Cdd:cd12155  196 VLP 198
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
12-76 1.41e-03

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 40.22  E-value: 1.41e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154    12 TDAL-AGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADVV 76
Cdd:smart00996 201 TDVMiAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTeIDPICALQAAMD-GFEVVTMEEVAPQADIF 266
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 15-81 1.43e-03

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: 39.92  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIRPGRSfDKAKENGFEVLPVDEATKQADVVMVLIP 81
Cdd:cd05198  138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKP-EPEEDLGFRVVSLDELLAQSDVVVLHLP 203
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
15-76 1.81e-03

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 39.65  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADVV 76
Cdd:COG0499  207 IAGKTVVVAGYGWCGKGVAMRARGLGARVIVTeVDPICALEAAMD-GFRVMPMEEAAKLGDIF 268
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 7-81 2.42e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 39.09  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154   7 DETVKTDALAGKKIAVIGYGSQGHAHAQNLKdnGYDV-VIGIRP-GRSFDKAKENGFEVLPVDEATKQADVVMVLIP 81
Cdd:cd12175  132 PEGRPSRELSGKTVGIVGLGNIGRAVARRLR--GFGVeVIYYDRfRDPEAEEKDLGVRYVELDELLAESDVVSLHVP 206
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 15-76 2.98e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 39.01  E-value: 2.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIGIrpGRSFDK----AKENGFEVLPVDE---ATKQADVV 76
Cdd:PRK00045 180 LSGKKVLVIGAGEMGELVAKHLAEKGVRKITVA--NRTLERaeelAEEFGGEAIPLDElpeALAEADIV 246
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 18-80 3.03e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.59  E-value: 3.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516234154  18 KKIAVIGYGSQGHAHAQNLKDNGYD----VVIGIRPGRSFDKAKENGFEVLP-VDEATKQADVVMVLI 80
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASGVPakdiIVSDPSPEKRAALAEEYGVRAATdNQEAAQEADVVVLAV 70
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
21-81 3.11e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 36.44  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516234154   21 AVIGYGSQGHAHA-QNLKDNGYDVVIGIRPG--RSFDKAKENGFEVLPVD--EATKQADVVMVLIP 81
Cdd:pfam03807   1 GFIGAGNMGEALArGLVAAGPHEVVVANSRNpeKAEELAEEYGVGATAVDneEAAEEADVVFLAVK 66
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 18-82 3.16e-03

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 38.56  E-value: 3.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516234154  18 KKIAVIGYGSQGHAHAQNLKDNGYDVVI-GIRPGRSfDKAKENGFEVLP-VDEATKQADVVMVLIPD 82
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVwNRTPAKA-EALVAAGARVAAsPAEAAAAADVVITMLPD 67
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 15-75 4.30e-03

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 38.87  E-value: 4.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADV 75
Cdd:PTZ00075 252 IAGKTVVVCGYGDVGKGCAQALRGFGARVVVTeIDPICALQAAME-GYQVVTLEDVVETADI 312
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 15-94 5.24e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 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: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 38.04  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKdnGYDVVI---GIRPGRSFDKAKENGFEVLpvdeaTKQADVVMVLIP--DEIQGDVY 89
Cdd:cd12179  136 LMGKTVGIIGYGNMGKAFAKRLS--GFGCKViayDKYKNFGDAYAEQVSLETL-----FKEADILSLHIPltPETRGMVN 208


                 ....*
gi 516234154  90 KNEIS 94
Cdd:cd12179  209 KEFIS 213
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 19-82 6.78e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 37.87  E-value: 6.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516234154  19 KIAVIGYGSQGHAHAQNLKDNGYDVViGIRpGRSFDKAKE-----NGFEVLPVDEATKQADVVMVLIPD 82
Cdd:COG5495    5 KIGIIGAGRVGTALAAALRAAGHEVV-GVY-SRSPASAERaaallGAVPALDLEELAAEADLVLLAVPD 71
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
12-78 6.86e-03

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 38.19  E-value: 6.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516234154   12 TDAL-AGKKIAVIGYGSQGHAHAQNLKDNGYDVVIG-IRPGRSFDKAKEnGFEVLPVDEATKQADVVMV 78
Cdd:pfam05221 204 TDVMiAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTeIDPICALQAAME-GYEVVTMEDVVGEADIFIT 271
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 15-86 8.40e-03

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 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. 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 a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 37.59  E-value: 8.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516234154  15 LAGKKIAVIGYGSQGHAHAQNLKDNGYDVVI-GIRPGRSFDKAKENGFEVLPVDEATKQADVVM--VLIPDEIQG 86
Cdd:cd12154  158 VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLItDINVEALEQLEELGGKNVEELEEALAEADVIVttTLLPGKRAG 232
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 15-81 9.32e-03

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. 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.


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 37.25  E-value: 9.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516234154  15 LAGKKIAVIGYGSQGH-----AHAQNLKDNGYDVVigirPGRSFdkAKENGFEVLPVDEATKQADVVMVLIP 81
Cdd:cd12187  137 LAGKTLGVVGTGRIGRrvariARGFGMKVLAYDVV----PDEEL--AERLGFRYVSLEELLQESDIISLHVP 202
 
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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