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Conserved domains on  [gi|664280233|ref|WP_030810383|]
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MULTISPECIES: 4-hydroxy-tetrahydrodipicolinate reductase [Streptomyces albovinaceus subgroup]

Protein Classification

4-hydroxy-tetrahydrodipicolinate reductase( domain architecture ID 11416656)

4-hydroxy-tetrahydrodipicolinate reductase catalyzes the NAD(P)-dependent conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate in amino acid biosynthesis pathways

CATH:  3.30.360.10|3.40.50.720
EC:  1.17.1.8
Gene Ontology:  GO:0016726|GO:0009089|GO:0050661|GO:0008839|GO:0051287
PubMed:  6094578|7893645
SCOP:  4000095

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 4-247 4.75e-90

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


:

Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 266.60  E-value: 4.75e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRG-----------------DKLEAlADAGAQVAVELTTPASVMGNLD 66
Cdd:COG0289    1 IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPgspgqdagelalgvpvtDDLEE-ALAKADVVIDFTHPEATLENLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  67 FCVRHGIHAVVGTTGWTEERLAQLNgwlDNSPETGVLIAPNFSIGAVLTMKFAEQAARYF---ESVEVLELHHPNKVDAP 143
Cdd:COG0289   80 AALEAGVPVVIGTTGFSEEQLAELE---EAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLgddYDIEIIEAHHRQKVDAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233 144 SGTATRTAQLIAAARAKAGSAPQPDaTTTALDGARgaDVDGVPVHAIRLRGLLAHQEVLLGGEGETLTIRHDSLHHSSFM 223
Cdd:COG0289  157 SGTALKLAEAIAEARGRDLDDVAVY-GREGITGAR--KKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFA 233

                        250       260
                 ....*....|....*....|....*
gi 664280233 224 PGILLGVRRVVT-TPGLtFGLEHFL 247
Cdd:COG0289  234 PGALLAARWLAGkPPGL-YGMEDVL 257
 
Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 4-247 4.75e-90

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 266.60  E-value: 4.75e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRG-----------------DKLEAlADAGAQVAVELTTPASVMGNLD 66
Cdd:COG0289    1 IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPgspgqdagelalgvpvtDDLEE-ALAKADVVIDFTHPEATLENLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  67 FCVRHGIHAVVGTTGWTEERLAQLNgwlDNSPETGVLIAPNFSIGAVLTMKFAEQAARYF---ESVEVLELHHPNKVDAP 143
Cdd:COG0289   80 AALEAGVPVVIGTTGFSEEQLAELE---EAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLgddYDIEIIEAHHRQKVDAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233 144 SGTATRTAQLIAAARAKAGSAPQPDaTTTALDGARgaDVDGVPVHAIRLRGLLAHQEVLLGGEGETLTIRHDSLHHSSFM 223
Cdd:COG0289  157 SGTALKLAEAIAEARGRDLDDVAVY-GREGITGAR--KKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFA 233

                        250       260
                 ....*....|....*....|....*
gi 664280233 224 PGILLGVRRVVT-TPGLtFGLEHFL 247
Cdd:COG0289  234 PGALLAARWLAGkPPGL-YGMEDVL 257
dapB TIGR00036
4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]
 4-248 1.56e-62

4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129147 [Multi-domain]  Cd Length: 266  Bit Score: 196.86  E-value: 1.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233    4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGR------GDKLEALADAG----------------AQVAVELTTPASV 61
Cdd:TIGR00036   2 IKVAVAGAAGRMGRELIKAALAAEGLQLVAAFERhgsslqGTDAGELAGIGkvgvpvtddleavetdPDVLIDFTTPEGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   62 MGNLDFCVRHGIHAVVGTTGWTEERLAQLnGWLDNSPETGVLIAPNFSIGAVLTMKFAEQAARYFESV--EVLELHHPNK 139
Cdd:TIGR00036  82 LNHLKFALEHGVRLVVGTTGFSEEDKQEL-ADLAEKAGIAAVIAPNFSIGVNLMFKLLEKAAKYLGDYdiEIIELHHRHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  140 VDAPSGTATRTAQLIAAARAKAGSAPQPDATTTaLDGARGADVDGVpvHAIRLRGLLAHQEVLLGGEGETLTIRHDSLHH 219
Cdd:TIGR00036 161 KDAPSGTALKTAEMIAEARGERLKNVAVTEREG-LTGERGREEIGI--HAVRGGDVVGEHTVMFAGDGERLEITHRASSR 237

                         250       260
                  ....*....|....*....|....*....
gi 664280233  220 SSFMPGILLGVRRVVTTPGLTFGLEHFLD 248
Cdd:TIGR00036 238 ACFANGAVRAARWLADKEAGVYDMEDVLD 266
DapB_C pfam05173
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 117-247 4.56e-36

Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.


Pssm-ID: 461568  Cd Length: 122  Bit Score: 124.16  E-value: 4.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  117 KFAEQAARYFES---VEVLELHHPNKVDAPSGTATRTAQLIAaarakagsapqpDATTTALDGARGADVDGVPVHAIRLR 193
Cdd:pfam05173   1 KLAKEAAKLLGDaydVEIIESHHNQKKDAPSGTALKLAEAIA------------ELGARKNKWARGAARDGIGIHSVRGG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 664280233  194 GLLAHQEVLLGGEGETLTIRHDSLHHSSFMPGILLGVRRVVTT-PGLtFGLEHFL 247
Cdd:pfam05173  69 GVVGEHTVLFAGDGERIEITHDAHSREIFAPGALLAARWLAGKkPGL-YGMEDVL 122
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 4-118 1.14e-30

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 110.73  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRGDKLEALADAG---------------------AQVAVELTTPASVM 62
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGglagigtgvivsldlelaaadADVVIDFTTPEATL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  63 GNLDFCVRHGIHAVVGTTGWTEERLAQLNGWLDNspeTGVLIAPN----FSIGAVLTMKF 118
Cdd:cd02274   81 ENLEAAAKAGVPLVIGTTGFSEEQLAEIEEAAKK---IPVVIAPNsreiFAPGALLAARW 137
PLN02775 PLN02775
Probable dihydrodipicolinate reductase
 28-147 2.54e-07

Probable dihydrodipicolinate reductase


Pssm-ID: 178374  Cd Length: 286  Bit Score: 50.42  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  28 DLELVAALGRGDKLEALADAGAQV-AVELTTPASVMGNLDFCVRHGIHAVVGTTGWTEERLaqlngwLDNSPETGV--LI 104
Cdd:PLN02775  59 EVRLVGPSEREAVLSSVKAEYPNLiVVDYTLPDAVNDNAELYCKNGLPFVMGTTGGDRDRL------LKDVEESGVyaVI 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 664280233 105 APNF-----SIGAVLTMkFAEQAARYFE--SVEVLELHHPNKVDApSGTA 147
Cdd:PLN02775 133 APQMgkqvvAFQAAMEI-MAEQFPGAFSgyTLEVVESHQATKLDT-SGTA 180
 
Name Accession Description Interval E-value
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 4-247 4.75e-90

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 266.60  E-value: 4.75e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRG-----------------DKLEAlADAGAQVAVELTTPASVMGNLD 66
Cdd:COG0289    1 IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPgspgqdagelalgvpvtDDLEE-ALAKADVVIDFTHPEATLENLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  67 FCVRHGIHAVVGTTGWTEERLAQLNgwlDNSPETGVLIAPNFSIGAVLTMKFAEQAARYF---ESVEVLELHHPNKVDAP 143
Cdd:COG0289   80 AALEAGVPVVIGTTGFSEEQLAELE---EAAKGIPVLIAPNFSLGVNLLFKLAEEAAKYLgddYDIEIIEAHHRQKVDAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233 144 SGTATRTAQLIAAARAKAGSAPQPDaTTTALDGARgaDVDGVPVHAIRLRGLLAHQEVLLGGEGETLTIRHDSLHHSSFM 223
Cdd:COG0289  157 SGTALKLAEAIAEARGRDLDDVAVY-GREGITGAR--KKGEIGIHSVRGGDIVGEHTVIFAGEGERIEIRHDASSRESFA 233

                        250       260
                 ....*....|....*....|....*
gi 664280233 224 PGILLGVRRVVT-TPGLtFGLEHFL 247
Cdd:COG0289  234 PGALLAARWLAGkPPGL-YGMEDVL 257
dapB TIGR00036
4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]
 4-248 1.56e-62

4-hydroxy-tetrahydrodipicolinate reductase; [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129147 [Multi-domain]  Cd Length: 266  Bit Score: 196.86  E-value: 1.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233    4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGR------GDKLEALADAG----------------AQVAVELTTPASV 61
Cdd:TIGR00036   2 IKVAVAGAAGRMGRELIKAALAAEGLQLVAAFERhgsslqGTDAGELAGIGkvgvpvtddleavetdPDVLIDFTTPEGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   62 MGNLDFCVRHGIHAVVGTTGWTEERLAQLnGWLDNSPETGVLIAPNFSIGAVLTMKFAEQAARYFESV--EVLELHHPNK 139
Cdd:TIGR00036  82 LNHLKFALEHGVRLVVGTTGFSEEDKQEL-ADLAEKAGIAAVIAPNFSIGVNLMFKLLEKAAKYLGDYdiEIIELHHRHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  140 VDAPSGTATRTAQLIAAARAKAGSAPQPDATTTaLDGARGADVDGVpvHAIRLRGLLAHQEVLLGGEGETLTIRHDSLHH 219
Cdd:TIGR00036 161 KDAPSGTALKTAEMIAEARGERLKNVAVTEREG-LTGERGREEIGI--HAVRGGDVVGEHTVMFAGDGERLEITHRASSR 237

                         250       260
                  ....*....|....*....|....*....
gi 664280233  220 SSFMPGILLGVRRVVTTPGLTFGLEHFLD 248
Cdd:TIGR00036 238 ACFANGAVRAARWLADKEAGVYDMEDVLD 266
DapB_C pfam05173
Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 117-247 4.56e-36

Dihydrodipicolinate reductase, C-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The C-terminal domain of DapB has been proposed to be the substrate- binding domain.


Pssm-ID: 461568  Cd Length: 122  Bit Score: 124.16  E-value: 4.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  117 KFAEQAARYFES---VEVLELHHPNKVDAPSGTATRTAQLIAaarakagsapqpDATTTALDGARGADVDGVPVHAIRLR 193
Cdd:pfam05173   1 KLAKEAAKLLGDaydVEIIESHHNQKKDAPSGTALKLAEAIA------------ELGARKNKWARGAARDGIGIHSVRGG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 664280233  194 GLLAHQEVLLGGEGETLTIRHDSLHHSSFMPGILLGVRRVVTT-PGLtFGLEHFL 247
Cdd:pfam05173  69 GVVGEHTVLFAGDGERIEITHDAHSREIFAPGALLAARWLAGKkPGL-YGMEDVL 122
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 4-108 5.68e-31

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 111.17  E-value: 5.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233    4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRGDKLEALADAG-------------------AQVAVELTTPASVMGN 64
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGSSLLGSDAGelaplgvpvtddleevladADVLIDFTTPEATLEN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 664280233   65 LDFCVRHGIHAVVGTTGWTEERLAQLNgwlDNSPETGVLIAPNF 108
Cdd:pfam01113  81 LEFALKHGVPLVIGTTGFTEEQLAELK---EAAKKIPIVIAPNF 121
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 4-118 1.14e-30

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 110.73  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAQGRIGSEAVRAVEAAEDLELVAALGRGDKLEALADAG---------------------AQVAVELTTPASVM 62
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGglagigtgvivsldlelaaadADVVIDFTTPEATL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  63 GNLDFCVRHGIHAVVGTTGWTEERLAQLNGWLDNspeTGVLIAPN----FSIGAVLTMKF 118
Cdd:cd02274   81 ENLEAAAKAGVPLVIGTTGFSEEQLAEIEEAAKK---IPVVIAPNsreiFAPGALLAARW 137
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 4-107 3.40e-10

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 55.82  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233   4 LRVAVLGAqGRIGSEAVRAVEAAEDLELVAALGRGDklealadagaqVAVELTTPASVMGNL-DFCVRHGIHAVVGTTGW 82
Cdd:cd05192    1 IRVAINGF-GRIGRIVFRAIADQDDLDVVAINDRRD-----------VVIECTGSFTDDDNAeKHIKAGGKKAVITAPEK 68

                         90       100
                 ....*....|....*....|....*.
gi 664280233  83 TEER-LAQLNGWLDNSPETGVLIAPN 107
Cdd:cd05192   69 GDIPtIVVVLNELAKSAGATVVSNAN 94
PLN02775 PLN02775
Probable dihydrodipicolinate reductase
 28-147 2.54e-07

Probable dihydrodipicolinate reductase


Pssm-ID: 178374  Cd Length: 286  Bit Score: 50.42  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664280233  28 DLELVAALGRGDKLEALADAGAQV-AVELTTPASVMGNLDFCVRHGIHAVVGTTGWTEERLaqlngwLDNSPETGV--LI 104
Cdd:PLN02775  59 EVRLVGPSEREAVLSSVKAEYPNLiVVDYTLPDAVNDNAELYCKNGLPFVMGTTGGDRDRL------LKDVEESGVyaVI 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 664280233 105 APNF-----SIGAVLTMkFAEQAARYFE--SVEVLELHHPNKVDApSGTA 147
Cdd:PLN02775 133 APQMgkqvvAFQAAMEI-MAEQFPGAFSgyTLEVVESHQATKLDT-SGTA 180
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-47 1.21e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.52  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 664280233   1 MTKLRVAVLGAqGRIGSEAVRAVEAAEDLELVAALGR-GDKLEALADA 47
Cdd:COG0673    1 MDKLRVGIIGA-GGIGRAHAPALAALPGVELVAVADRdPERAEAFAEE 47
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 5-81 3.93e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.22  E-value: 3.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664280233   5 RVAVLGAQGRIGSEAVRavEAAEDLELVAALGR-GDKLEALADAGAQVAV-ELTTPASVMGNLDfcvrhGIHAVVGTTG 81
Cdd:cd05243    1 KVLVVGATGKVGRHVVR--ELLDRGYQVRALVRdPSQAEKLEAAGAEVVVgDLTDAESLAAALE-----GIDAVISAAG 72
 
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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