NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18409781|ref|NP_565014|]
View 

6-phosphogluconate dehydrogenase family protein [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 47-311 1.22e-83

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 253.88  E-value: 1.22e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVD 126
Cdd:COG2084  14 APMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLAALRPGAVVVD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQSCKIG 205
Cdd:COG2084  94 MSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGkRIVHVGDAGAGQAAKLA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 206 NQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAMPG-- 283
Cdd:COG2084 174 NNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGLALEAARAAgv 253

                       250       260       270
                ....*....|....*....|....*....|..
gi 18409781 284 ----AALSKQLFTGMVANGDGKLGIQGVVSVI 311
Cdd:COG2084 254 plplAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 47-311 1.22e-83

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 253.88  E-value: 1.22e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVD 126
Cdd:COG2084  14 APMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLAALRPGAVVVD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQSCKIG 205
Cdd:COG2084  94 MSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGkRIVHVGDAGAGQAAKLA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 206 NQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAMPG-- 283
Cdd:COG2084 174 NNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGLALEAARAAgv 253

                       250       260       270
                ....*....|....*....|....*....|..
gi 18409781 284 ----AALSKQLFTGMVANGDGKLGIQGVVSVI 311
Cdd:COG2084 254 plplAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 42-273 1.17e-53

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 177.55  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   42 IGIMGSAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPG 121
Cdd:PRK11559  10 LGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIEGAKPG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  122 GVTVDMTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGT-VTYMGEAGSGQ 200
Cdd:PRK11559  90 TVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGsVVHTGDIGAGN 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18409781  201 SCKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDL 273
Cdd:PRK11559 170 VTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 43-316 1.12e-50

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: 169.68  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    43 GIMGSAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGG 122
Cdd:TIGR01505   8 GIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIEGAKPGK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   123 VTVDMTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQS 201
Cdd:TIGR01505  88 TLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGkNIVLVGGNGDGQT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   202 CKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAM 281
Cdd:TIGR01505 168 CKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLNLALDSAK 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 18409781   282 P------GAALSKQLFTGMVANGDGKLGIQGVVSVIRRLNG 316
Cdd:TIGR01505 248 AvganlpNTATVQELFNTLRANGGGQLDHSALVQALELLAN 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 47-194 1.03e-47

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: 157.63  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDdGVLSGLTPGGVTVD 126
Cdd:pfam03446  12 SPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLPGLKPGDIIID 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18409781   127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMG 194
Cdd:pfam03446  91 GSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGaCVTYIG 159
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 47-311 1.22e-83

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 253.88  E-value: 1.22e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVD 126
Cdd:COG2084  14 APMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLAALRPGAVVVD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQSCKIG 205
Cdd:COG2084  94 MSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGkRIVHVGDAGAGQAAKLA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781 206 NQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAMPG-- 283
Cdd:COG2084 174 NNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLGLALEAARAAgv 253

                       250       260       270
                ....*....|....*....|....*....|..
gi 18409781 284 ----AALSKQLFTGMVANGDGKLGIQGVVSVI 311
Cdd:COG2084 254 plplAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 42-273 1.17e-53

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 177.55  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   42 IGIMGSAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPG 121
Cdd:PRK11559  10 LGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIEGAKPG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  122 GVTVDMTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGT-VTYMGEAGSGQ 200
Cdd:PRK11559  90 TVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGsVVHTGDIGAGN 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18409781  201 SCKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDL 273
Cdd:PRK11559 170 VTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 43-316 1.12e-50

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: 169.68  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    43 GIMGSAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGG 122
Cdd:TIGR01505   8 GIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIEGAKPGK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   123 VTVDMTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQS 201
Cdd:TIGR01505  88 TLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGkNIVLVGGNGDGQT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   202 CKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAM 281
Cdd:TIGR01505 168 CKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLNLALDSAK 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 18409781   282 P------GAALSKQLFTGMVANGDGKLGIQGVVSVIRRLNG 316
Cdd:TIGR01505 248 AvganlpNTATVQELFNTLRANGGGQLDHSALVQALELLAN 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 47-194 1.03e-47

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: 157.63  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDdGVLSGLTPGGVTVD 126
Cdd:pfam03446  12 SPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLPGLKPGDIIID 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18409781   127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMG 194
Cdd:pfam03446  91 GSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGaCVTYIG 159
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
72-311 4.05e-35

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 128.99  E-value: 4.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   72 DLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVDMTSSKPGLAREIHAEARRRNCWAVD 151
Cdd:PRK15059  37 ELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  152 APVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIG-TVTYMGEAGSGQSCKIGNQIAGASNLVGLAEGIVFAEKAGLD 230
Cdd:PRK15059 117 APVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGkNITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGAD 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  231 TVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLGMAAEAAMP------GAALSKQLFTGMVANGDGKLGI 304
Cdd:PRK15059 197 PVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLNLALQSAKAlalnlpNTATCQELFNTCAANGGSQLDH 276


                 ....*..
gi 18409781  305 QGVVSVI 311
Cdd:PRK15059 277 SALVQAL 283
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 49-312 6.31e-34

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 125.68  E-value: 6.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    49 MVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVDMT 128
Cdd:TIGR01692  11 MAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKVAKGSLLIDCS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   129 SSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGTVT-YMGEAGSGQSCKIGNQ 207
Cdd:TIGR01692  91 TIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIvHCGDHGAGQAAKICNN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   208 IAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLF----GEM---IVKRDYrATGFA-EYMVKDLGMAAEA 279
Cdd:TIGR01692 171 MLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYnpvpGVMpqaPASNGY-QGGFGtALMLKDLGLAQDA 249

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 18409781   280 AMPGAA------LSKQLFTGMVANGDGKLGIQGVVSVIR 312
Cdd:TIGR01692 250 AKSAGAptplgaLARQLYSLFDDKGHGGKDFSSVIQLLR 288
PLN02858 PLN02858
fructose-bisphosphate aldolase
 49-317 1.43e-30

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 121.88  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    49 MVSHIIAAGYSVT---VYARDLRKTKDLqtkGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTV 125
Cdd:PLN02858  339 MASHLLKSNFSVCgydVYKPTLVRFENA---GGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVSALPAGASIV 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   126 DMTSSKPGLAREIHA--EARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGTVTYM--GEAGSGQS 201
Cdd:PLN02858  416 LSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYVikGGCGAGSG 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   202 CKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDgAAGSAVMrlFGEMI---VKRDYRATGFAEYMVKDLGMAAE 278
Cdd:PLN02858  496 VKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISN-AGGTSWM--FENRVphmLDNDYTPYSALDIFVKDLGIVSR 572

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 18409781   279 AAMPG------AALSKQLFTGMVANGDGKLGIQGVVSVIRRLNGI 317
Cdd:PLN02858  573 EGSSRkiplhlSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGV 617
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
47-275 5.46e-22

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 93.77  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   47 SAMVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVD 126
Cdd:PRK15461  14 SPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCEGLSRDALVID 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  127 MTSSKPGLAREIHAEARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGT-VTYMGEAGSGQSCKIG 205
Cdd:PRK15461  94 MSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNeLINAGGPGMGIRVKLI 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18409781  206 NQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRL-FGEMIVKRDYRATGFAEYMVKDLGM 275
Cdd:PRK15461 174 NNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTtWPNKVLKGDLSPAFMIDLAHKDLGI 244
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 197-274 1.27e-16

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: 74.48  E-value: 1.27e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18409781   197 GSGQSCKIGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVM-RLFGEMIVKRDYRATGFAEYMVKDLG 274
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALeNKFPQRVLSRDFDPGFALDLMLKDLG 79
PLN02858 PLN02858
fructose-bisphosphate aldolase
 49-274 1.64e-15

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 77.20  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781    49 MVSHIIAAGYSVTVY-ARDLRKTKDLQTKGARIAnSPKELAEMSDVVFTIVGNFNDVRSLLLGDDGVLSGLTPGGVTVDM 127
Cdd:PLN02858   19 LASSLLRSGFKVQAFeISTPLMEKFCELGGHRCD-SPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAAKGLQKGAVILIR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   128 TSSKPGLAREIHAE--ARRRNCWAVDAPVSGGDAGAREGTLGIFAGGDSEIVEWLSPVMKNIGTVTYM--GEAGSGQSCK 203
Cdd:PLN02858   98 STILPLQLQKLEKKltERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYTfeGEIGAGSKVK 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18409781   204 IGNQIAGASNLVGLAEGIVFAEKAGLDTVKWLEAVKDGAAGSAVMRLFGEMIVKRDYRATGFAEYMVKDLG 274
Cdd:PLN02858  178 MVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQNLG 248
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
49-199 1.20e-08

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 55.14  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781   49 MVSHIIAAGYSVTVYARDLRKTKDLQTKGARIANSPKELAEMSD---VVFTIVGNFNDVRSLLlgdDGVLSGLTPGGVTV 125
Cdd:PRK09599  15 MARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI---DELAPLLSPGDIVI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409781  126 DMTSS--KPGLAReiHAEARRRNCWAVDAPVSGGDAGAREGtLGIFAGGDSEIVEWLSPVMKNIGTVT-----YMGEAGS 198
Cdd:PRK09599  92 DGGNSyyKDDIRR--AELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKALAPRAedgylHAGPVGA 168


                 .
gi 18409781  199 G 199
Cdd:PRK09599 169 G 169
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
154-199 3.01e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 38.95  E-value: 3.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18409781  154 VSGGDAGAREGTlGIFAGGDSEIVEWLSPVMKNI------GT--VTYMGEAGSG 199
Cdd:PRK09287 115 VSGGEEGALHGP-SIMPGGQKEAYELVAPILEKIaakvedGEpcVTYIGPDGAG 167
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 154-199 7.58e-03

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: 37.75  E-value: 7.58e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 18409781 154 VSGGDAGAREGTlGIFAGGDSEIVEWLSPVMKNI-----GT--VTYMGEAGSG 199
Cdd:COG0362 127 VSGGEEGALHGP-SIMPGGSKEAYELVKPILEAIaakvdGEpcVTYIGPDGAG 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH