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Conserved domains on  [gi|79313434|ref|NP_001030765|]
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glyoxylate reductase 1 [Arabidopsis thaliana]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11449905)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

CATH:  3.40.50.720
EC:  1.1.-.-
Gene Ontology:  GO:0050661|GO:0051287|GO:0016491
PubMed:  8749365
SCOP:  4000072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-273 7.34e-105

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 306.27  E-value: 7.34e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG-- 78
Cdd:COG2084   2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDgl 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  79 ---------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:COG2084  82 laalrpgavVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434 150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 79313434 230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAV 273
Cdd:COG2084 242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-273 7.34e-105

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 306.27  E-value: 7.34e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG-- 78
Cdd:COG2084   2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDgl 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  79 ---------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:COG2084  82 laalrpgavVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434 150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 79313434 230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAV 273
Cdd:COG2084 242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-274 1.65e-49

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 165.06  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDP------------CA 69
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSpqveevafgengII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    70 ALSIcEGKGYIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:TIGR01505  81 EGAK-PGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:TIGR01505 160 GGNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 79313434   230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVK 274
Cdd:TIGR01505 240 NLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-270 2.70e-48

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 162.14  E-value: 2.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG-- 78
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENgi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   79 ---------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:PRK11559  83 iegakpgtvVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 79313434  230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVI 270
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALA 283
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-150 3.93e-46

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: 152.24  E-value: 3.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG--- 78
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGllp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79313434    79 -------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYLG 150
Cdd:pfam03446  81 glkpgdiIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-32 5.18e-04

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 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: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 40.94  E-value: 5.18e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRT 32
Cdd:cd12164 133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRS 164
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-273 7.34e-105

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 306.27  E-value: 7.34e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG-- 78
Cdd:COG2084   2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDgl 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  79 ---------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:COG2084  82 laalrpgavVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434 150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 79313434 230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAV 273
Cdd:COG2084 242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-274 1.65e-49

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 165.06  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDP------------CA 69
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSpqveevafgengII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    70 ALSIcEGKGYIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:TIGR01505  81 EGAK-PGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:TIGR01505 160 GGNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 79313434   230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVK 274
Cdd:TIGR01505 240 NLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-270 2.70e-48

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 162.14  E-value: 2.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG-- 78
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENgi 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   79 ---------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:PRK11559  83 iegakpgtvVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  150 GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKDM 229
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 79313434  230 RLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVI 270
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALA 283
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-150 3.93e-46

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: 152.24  E-value: 3.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDPCAALSICEGKG--- 78
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGllp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79313434    79 -------YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYLG 150
Cdd:pfam03446  81 glkpgdiIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
3-276 4.37e-38

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 135.75  E-value: 4.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    3 VGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLsdPCAAL---------SI 73
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITML--PNGDLvrsvlfgenGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   74 CEGKG----YIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:PRK15461  82 CEGLSrdalVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  150 GQVGNGAKMKLIvNMIMGSMMNAFS-EGLVLADKSGLSSDTLLDILD-----LGAMT----NPMFKGkgpsmnksSYPPA 219
Cdd:PRK15461 162 GGPGMGIRVKLI-NNYMSIALNALSaEAAVLCEALGLSFDVALKVMSgtaagKGHFTttwpNKVLKG--------DLSPA 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 79313434  220 FPLKHQQKDMRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVKFS 276
Cdd:PRK15461 233 FMIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVS 289
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-275 5.93e-37

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 132.45  E-value: 5.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVwNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDP------------C 68
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTpqveevlfgengC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   69 AALSIcEGKGYIDMSTVDAETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFY 148
Cdd:PRK15059  80 TKASL-KGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434  149 LGQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKD 228
Cdd:PRK15059 159 VGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKD 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 79313434  229 MRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAVKF 275
Cdd:PRK15059 239 LNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALEL 285
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 153-273 1.16e-27

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 103.37  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   153 GNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGP-SMNKSSYPPAFPLKHQQKDMRL 231
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 79313434   232 ALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIEAV 273
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-271 2.36e-24

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 102.62  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     3 VGFLGLGIMGKAMSMNLLKNGFKVT---VWNRTLSKCDELvehGASVCESPAEVIKKCKYTIAMLS-----------DPC 68
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSVCgydVYKPTLVRFENA---GGLAGNSPAEVAKDVDVLVIMVAnevqaenvlfgDLG 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    69 AALSICEGKGYIDMSTVDAETSLKINEAI--TGKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRS 146
Cdd:PLN02858  404 AVSALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKL 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   147 FYL-GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQ 225
Cdd:PLN02858  484 YVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIF 563

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 79313434   226 QKDMRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVIE 271
Cdd:PLN02858  564 VKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVK 609
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-270 2.36e-23

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 99.54  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434     3 VGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKCKYTIAMLSDP-----------CAAL 71
Cdd:PLN02858    7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPdqvddvffgdeGAAK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    72 SICEGKGYIDMSTVDAETSLKINEAIT--GKGGRFVEGPVSGSKKPAEDGQLIILAAGDKALFEESIPAFDVLGKRSFYL 149
Cdd:PLN02858   87 GLQKGAVILIRSTILPLQLQKLEKKLTerKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYTF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   150 -GQVGNGAKMKLIVNMIMGSMMNAFSEGLVLADKSGLSSDTLLDILDLGAMTNPMFKGKGPSMNKSSYPPAFPLKHQQKD 228
Cdd:PLN02858  167 eGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQN 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 79313434   229 MRLALALGDENAVSMPVAAAANEAFKKARSLGLGDLDFSAVI 270
Cdd:PLN02858  247 LGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLA 288
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-188 6.57e-11

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 61.69  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434    1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVEHGASVCESPAEVIKKckytiamLSDPCAA-LSICEGKgy 79
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAK-------LPAPRVVwLMVPAGE-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313434   80 IDMSTVDA-------------------ETSLKINEAITGKGGRFVEGPVSGSKKPAEDGQ-LIIlaAGDKALFEESIPAF 139
Cdd:PRK09599  72 ITDATIDElapllspgdividggnsyyKDDIRRAELLAEKGIHFVDVGTSGGVWGLERGYcLMI--GGDKEAVERLEPIF 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 79313434  140 DVL---GKRSF-YLGQVGNG--AKMklIVNMIMGSMMNAFSEGLVLADKSGLSSD 188
Cdd:PRK09599 150 KALaprAEDGYlHAGPVGAGhfVKM--VHNGIEYGMMQAYAEGFELLEASRFDLD 202
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 1-44 1.67e-08

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 54.69  E-value: 1.67e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELV-EHGA 44
Cdd:COG0362   3 ADIGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLaEHGK 47
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 2-41 4.91e-08

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 53.64  E-value: 4.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 79313434    2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVE 41
Cdd:PTZ00142   3 DIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVK 42
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-57 2.97e-06

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 47.37  E-value: 2.97e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFK---VTVWNRTLSKCDELVE-HGASVCESPAEVIKKC 57
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQA 63
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-41 3.63e-06

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 47.79  E-value: 3.63e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 79313434    2 EVGFLGLGIMGKAMSMNLLKNGFKVTVWNRTLSKCDELVE 41
Cdd:PLN02350   8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVE 47
PRK07680 PRK07680
late competence protein ComER; Validated
 1-59 1.60e-04

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 42.27  E-value: 1.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79313434    1 MEVGFLGLGIMGKAMSMNLLKNGF----KVTVWNRTLSKCDELVEH--GASVCESPAEVIKKCKY 59
Cdd:PRK07680   1 MNIGFIGTGNMGTILIEAFLESGAvkpsQLTITNRTPAKAYHIKERypGIHVAKTIEEVISQSDL 65
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-32 5.18e-04

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 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: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 40.94  E-value: 5.18e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 79313434   1 MEVGFLGLGIMGKAMSMNLLKNGFKVTVWNRT 32
Cdd:cd12164 133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRS 164
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
11-41 8.23e-04

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 40.49  E-value: 8.23e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 79313434   11 MGKAMSMNLLKNGFKVTVWNRTLSKCDELVE 41
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLA 31
 
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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