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Conserved domains on  [gi|55770836|ref|NP_057086|]
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saccharopine dehydrogenase-like oxidoreductase [Homo sapiens]

Protein Classification

saccharopine dehydrogenase family protein( domain architecture ID 11461686)

saccharopine dehydrogenase family protein contains a Rossmann fold NADP-binding domain, such as vertebrate saccharopine dehydrogenase-like oxidoreductase and mycobacterial trans-acting enoyl reductase

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0016491
PubMed:  30945211|31869345|25704928

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.96e-76

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


:

Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 240.90  E-value: 5.96e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqvdperssRLPWAVAGRSREKLQRVLEKaalkLGRPTLssevGIIICDIA 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAVAAE----LGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  81 NPASLDEMAKQATVVLNCVGPYRFYGEPVIKACIENGASCIDISGEPQFLELMQLKYHEKAADKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 161 LGVIYTRNKMNGtLTAVESFLTIHSGPEGlsihdGTWKSAIYGFGDQSNLRKLRnvsNLKPVPLiGPKLKRRWPISYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNG---RLVRVPY-ALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 241 lKGYSIPFMGSDVSVVRRTQRYLyenleespvQYAAYVTVGGITSVIKLMFAGLFFLFFVRFGIGRQLLIKfpWFFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 321 fskQGPTQKQIDAASFTLTFfgqgysQGTGTDKNkpniKICTQVKGPEaGYVATPIAMVQAAMTLLSDAshlPKAGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWG------EARTAGGR----RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 55770836 401 PGAAFSkTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.96e-76

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 240.90  E-value: 5.96e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqvdperssRLPWAVAGRSREKLQRVLEKaalkLGRPTLssevGIIICDIA 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAVAAE----LGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  81 NPASLDEMAKQATVVLNCVGPYRFYGEPVIKACIENGASCIDISGEPQFLELMQLKYHEKAADKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 161 LGVIYTRNKMNGtLTAVESFLTIHSGPEGlsihdGTWKSAIYGFGDQSNLRKLRnvsNLKPVPLiGPKLKRRWPISYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNG---RLVRVPY-ALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 241 lKGYSIPFMGSDVSVVRRTQRYLyenleespvQYAAYVTVGGITSVIKLMFAGLFFLFFVRFGIGRQLLIKfpWFFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 321 fskQGPTQKQIDAASFTLTFfgqgysQGTGTDKNkpniKICTQVKGPEaGYVATPIAMVQAAMTLLSDAshlPKAGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWG------EARTAGGR----RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 55770836 401 PGAAFSkTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-149 5.34e-25

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 98.82  E-value: 5.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836    10 LVVFGAsGFTGQFVTEEVAREQVDPErssrlpWAVAGRSREKLQRVLEKAALKlgrptlssEVGIIICDIANPAS-LDEM 88
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHFDVDR------ITVADRTLEKAQALAAKLGGV--------RFIAVAVDADNYEAvLAAL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770836    89 AKQATVVLNCVGPYrfYGEPVIKACIENGASCIDISgepqFLELMQLKYHEKAADKGVYII 149
Cdd:pfam03435  66 LKEGDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 12-119 4.45e-04

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 41.93  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  12 VFGASGFTGQfvteEVAREQVDPERSSRLpwavAGRSREKLQRVlekaalklgrptlsSEVGIIICDIANPASLDEMAKQ 91
Cdd:cd05229   4 VLGASGPIGR----EVARELRRRGWDVRL----VSRSGSKLAWL--------------PGVEIVAADAMDASSVIAAARG 61

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 55770836  92 ATVVLNCVGP-YRFYG-------EPVIKACIENGAS 119
Cdd:cd05229  62 ADVIYHCANPaYTRWEelfpplmENVVAAAEANGAK 97
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.96e-76

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 240.90  E-value: 5.96e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqvdperssRLPWAVAGRSREKLQRVLEKaalkLGRPTLssevGIIICDIA 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAVAAE----LGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  81 NPASLDEMAKQATVVLNCVGPYRFYGEPVIKACIENGASCIDISGEPQFLELMQLKYHEKAADKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 161 LGVIYTRNKMNGtLTAVESFLTIHSGPEGlsihdGTWKSAIYGFGDQSNLRKLRnvsNLKPVPLiGPKLKRRWPISYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNG---RLVRVPY-ALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 241 lKGYSIPFMGSDVSVVRRTQRYLyenleespvQYAAYVTVGGITSVIKLMFAGLFFLFFVRFGIGRQLLIKfpWFFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836 321 fskQGPTQKQIDAASFTLTFfgqgysQGTGTDKNkpniKICTQVKGPEaGYVATPIAMVQAAMTLLSDAshlPKAGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWG------EARTAGGR----RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 55770836 401 PGAAFSkTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-149 5.34e-25

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 98.82  E-value: 5.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836    10 LVVFGAsGFTGQFVTEEVAREQVDPErssrlpWAVAGRSREKLQRVLEKAALKlgrptlssEVGIIICDIANPAS-LDEM 88
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHFDVDR------ITVADRTLEKAQALAAKLGGV--------RFIAVAVDADNYEAvLAAL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770836    89 AKQATVVLNCVGPYrfYGEPVIKACIENGASCIDISgepqFLELMQLKYHEKAADKGVYII 149
Cdd:pfam03435  66 LKEGDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 44-155 2.32e-15

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 76.80  E-value: 2.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  44 VAGRSREKLQRVLEKaalklgrptlSSEVGIIICDIANPASLDEMAKQATVVLNCVGPYRfyGEPVIKACIENGASCIDI 123
Cdd:COG1748   5 LADRSLEKAEALAAS----------GPKVEAAQLDASDPEALAALIAGADLVINALPPYL--NLTVAEACIEAGVHYVDL 72

                        90       100       110
                ....*....|....*....|....*....|..
gi 55770836 124 SGEPQFLElMQLKYHEKAADKGVYIIGSSGFD 155
Cdd:COG1748  73 SEDEPETE-AKLALDELAKEAGVTAIPGCGLA 103
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 11-117 2.57e-06

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 47.92  E-value: 2.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  11 VVFGASGFTGQFVTEEVAREQVDPerssrlpwAVAGRSREKLQRVLEKaalklgrptlssEVGIIICDIANPASLDEMAK 90
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPV--------RALVRDPEKAAALAAA------------GVEVVQGDLDDPESLAAALA 62

                        90       100       110
                ....*....|....*....|....*....|....*
gi 55770836  91 QATVVLNCVGP--------YRFYGEPVIKACIENG 117
Cdd:COG0702  63 GVDAVFLLVPSgpggdfavDVEGARNLADAAKAAG 97
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
9-101 3.59e-05

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 44.46  E-value: 3.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836   9 HLVVFGASGFTGQFVTEE-VAR-EQVDperssrlpwAVAgRSREKLqrvlekaalklgrPTLSSEVGIIICDIANPASLD 86
Cdd:COG2910   1 KIAVIGATGRVGSLIVREaLARgHEVT---------ALV-RNPEKL-------------PDEHPGLTVVVGDVLDPAAVA 57

                        90
                ....*....|....*
gi 55770836  87 EMAKQATVVLNCVGP 101
Cdd:COG2910  58 EALAGADAVVSALGA 72
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 12-119 4.45e-04

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 41.93  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  12 VFGASGFTGQfvteEVAREQVDPERSSRLpwavAGRSREKLQRVlekaalklgrptlsSEVGIIICDIANPASLDEMAKQ 91
Cdd:cd05229   4 VLGASGPIGR----EVARELRRRGWDVRL----VSRSGSKLAWL--------------PGVEIVAADAMDASSVIAAARG 61

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 55770836  92 ATVVLNCVGP-YRFYG-------EPVIKACIENGAS 119
Cdd:cd05229  62 ADVIYHCANPaYTRWEelfpplmENVVAAAEANGAK 97
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 12-118 4.87e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 40.85  E-value: 4.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  12 VFGASGFTGQfvteEVAREqvdperSSRLPWAVAGRSREklqrvlEKAALKLGRPTLSSEVGiiicDIANPASLDEMAKQ 91
Cdd:cd05226   3 ILGATGFIGR----ALARE------LLEQGHEVTLLVRN------TKRLSKEDQEPVAVVEG----DLRDLDSLSDAVQG 62

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 55770836  92 ATVVLNCVGPYRFYGEP----------VIKACIENGA 118
Cdd:cd05226  63 VDVVIHLAGAPRDTRDFcevdvegtrnVLEAAKEAGV 99
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 9-100 1.22e-03

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 40.31  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836   9 HLVVFGASGFTGQFVTEEVARE--QVdperssrlpwAVAGRSREKLQRVleKAALKLGRPTLSSEVGIIICDIANPASLD 86
Cdd:cd08939   3 HVLITGGSSGIGKALAKELVKEgaNV----------IIVARSESKLEEA--VEEIEAEANASGQKVSYISADLSDYEEVE 70

                        90       100
                ....*....|....*....|.
gi 55770836  87 EMAKQA-------TVVLNCVG 100
Cdd:cd08939  71 QAFAQAvekggppDLVVNCAG 91
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 11-118 1.29e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 40.31  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  11 VVFGASGFTGQFVTEEVARE--QVdperssrlpwAVAGRSREKLQRVLekaalklgrptLSSEVGIII---CDIANPASL 85
Cdd:cd05271   4 TVFGATGFIGRYVVNRLAKRgsQV----------IVPYRCEAYARRLL-----------VMGDLGQVLfveFDLRDDESI 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 55770836  86 DEMAKQATVVLNCVG------PYRFYG------EPVIKACIENGA 118
Cdd:cd05271  63 RKALEGSDVVINLVGrlyetkNFSFEDvhvegpERLAKAAKEAGV 107
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 11-100 4.13e-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: 38.37  E-value: 4.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770836  11 VVFGASGFTGQFVTEEVAREQVDPerssrlpwaVAG-RSREKLQRVLEkaalklgrptlsSEVGIIICDIANPASLDEMA 89
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGYQV---------RALvRDPSQAEKLEA------------AGAEVVVGDLTDAESLAAAL 61

                        90
                ....*....|.
gi 55770836  90 KQATVVLNCVG 100
Cdd:cd05243  62 EGIDAVISAAG 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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