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Conserved domains on  [gi|53933212|ref|NP_001005574|]
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saccharopine dehydrogenase b [Danio rerio]

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];
8-425 5.71e-73

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


:

Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 233.20  E-value: 5.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212   8 SKRPYHLIVLGASGFTGQFVVEEVARiieEGpggtLQWAVAGRSRHRLEktlsQAADALSKPELksvEVIVADVAEAESL 87
Cdd:COG3268   2 TEREFDIVVYGATGYTGRLVAEYLAR---RG----LRPALAGRNAAKLE----AVAAELGAADL---PLRVADLDDPASL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  88 AIMCKQAVIVLNCVGPYRFYGEPVVKACIENGAHCIDICGEPQFLEGIQLMYHSKAEENGVYVIGSCGFDSIPADMGIIY 167
Cdd:COG3268  68 AALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 168 TRNHFQGtLTAVESFLTISTGPEGGcahdaTWQSAIFGFADSGNLRRIRK----KFGHKPLPAVGARIKKRGAVffskei 243
Cdd:COG3268 148 LQERLPE-ADRLTLAVRAKGGFSGG-----TAASMLEALAAGGADRRNGRlvrvPYALRTREDFPDGGPQQGAW------ 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 244 eqyAIPFMGSDPSVVRRTQRFMheeqkhspvQYMAYVGIGGLFSVVKTLFAGIMFWLMVKFSLGRGLLTQFPEFFSfglf 323
Cdd:COG3268 216 ---TAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKRVLPKPG---- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 324 skSGPSKKQMDGTSFSMRFWGEGySSGQdpsqgkpdsTISTEVTGPEpGYIATPIAMVQAAITLLNEPhclPNKGGVFTP 403
Cdd:COG3268 280 --EGPSEEERERGRFVVWGEART-AGGR---------RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLTP 343

                       410       420
                ....*....|....*....|...
gi 53933212 404 GSVFArSTLIERLNKH-GIQFSI 425
Cdd:COG3268 344 ATAFG-AALVLRLLAVaGLTFEV 365
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
8-425 5.71e-73

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


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 233.20  E-value: 5.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212   8 SKRPYHLIVLGASGFTGQFVVEEVARiieEGpggtLQWAVAGRSRHRLEktlsQAADALSKPELksvEVIVADVAEAESL 87
Cdd:COG3268   2 TEREFDIVVYGATGYTGRLVAEYLAR---RG----LRPALAGRNAAKLE----AVAAELGAADL---PLRVADLDDPASL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  88 AIMCKQAVIVLNCVGPYRFYGEPVVKACIENGAHCIDICGEPQFLEGIQLMYHSKAEENGVYVIGSCGFDSIPADMGIIY 167
Cdd:COG3268  68 AALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 168 TRNHFQGtLTAVESFLTISTGPEGGcahdaTWQSAIFGFADSGNLRRIRK----KFGHKPLPAVGARIKKRGAVffskei 243
Cdd:COG3268 148 LQERLPE-ADRLTLAVRAKGGFSGG-----TAASMLEALAAGGADRRNGRlvrvPYALRTREDFPDGGPQQGAW------ 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 244 eqyAIPFMGSDPSVVRRTQRFMheeqkhspvQYMAYVGIGGLFSVVKTLFAGIMFWLMVKFSLGRGLLTQFPEFFSfglf 323
Cdd:COG3268 216 ---TAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKRVLPKPG---- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 324 skSGPSKKQMDGTSFSMRFWGEGySSGQdpsqgkpdsTISTEVTGPEpGYIATPIAMVQAAITLLNEPhclPNKGGVFTP 403
Cdd:COG3268 280 --EGPSEEERERGRFVVWGEART-AGGR---------RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLTP 343

                       410       420
                ....*....|....*....|...
gi 53933212 404 GSVFArSTLIERLNKH-GIQFSI 425
Cdd:COG3268 344 ATAFG-AALVLRLLAVaGLTFEV 365
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 14-151 2.41e-23

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: 94.19  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212    14 LIVLGAsGFTGQFVVEEVARIIEEgpggtLQWAVAGRSRHRLEKtlsqAADALSKPELKSVEVIVADVAEaeSLAIMCKQ 93
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHFDV-----DRITVADRTLEKAQA----LAAKLGGVRFIAVAVDADNYEA--VLAALLKE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 53933212    94 AVIVLNCVGPYrfYGEPVVKACIENGAHCIDICgepqFLEGIQLMYHSKAEENGVYVI 151
Cdd:pfam03435  69 GDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 15-120 5.30e-07

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: 49.32  E-value: 5.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  15 IVLGASGFTGQFVVEEvarIIEEGpggtlqWAVAGRSRHrlektlsqaADALSKPELKSVEVIVADVAEAESLAIMCKQA 94
Cdd:cd05226   2 LILGATGFIGRALARE---LLEQG------HEVTLLVRN---------TKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGV 63

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 53933212  95 VIVLNCVGPYRFYGEP----------VVKACIENGA 120
Cdd:cd05226  64 DVVIHLAGAPRDTRDFcevdvegtrnVLEAAKEAGV 99
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
8-425 5.71e-73

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


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 233.20  E-value: 5.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212   8 SKRPYHLIVLGASGFTGQFVVEEVARiieEGpggtLQWAVAGRSRHRLEktlsQAADALSKPELksvEVIVADVAEAESL 87
Cdd:COG3268   2 TEREFDIVVYGATGYTGRLVAEYLAR---RG----LRPALAGRNAAKLE----AVAAELGAADL---PLRVADLDDPASL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  88 AIMCKQAVIVLNCVGPYRFYGEPVVKACIENGAHCIDICGEPQFLEGIQLMYHSKAEENGVYVIGSCGFDSIPADMGIIY 167
Cdd:COG3268  68 AALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSDLGAAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 168 TRNHFQGtLTAVESFLTISTGPEGGcahdaTWQSAIFGFADSGNLRRIRK----KFGHKPLPAVGARIKKRGAVffskei 243
Cdd:COG3268 148 LQERLPE-ADRLTLAVRAKGGFSGG-----TAASMLEALAAGGADRRNGRlvrvPYALRTREDFPDGGPQQGAW------ 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 244 eqyAIPFMGSDPSVVRRTQRFMheeqkhspvQYMAYVGIGGLFSVVKTLFAGIMFWLMVKFSLGRGLLTQFPEFFSfglf 323
Cdd:COG3268 216 ---TAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKRVLPKPG---- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212 324 skSGPSKKQMDGTSFSMRFWGEGySSGQdpsqgkpdsTISTEVTGPEpGYIATPIAMVQAAITLLNEPhclPNKGGVFTP 403
Cdd:COG3268 280 --EGPSEEERERGRFVVWGEART-AGGR---------RVRARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLTP 343

                       410       420
                ....*....|....*....|...
gi 53933212 404 GSVFArSTLIERLNKH-GIQFSI 425
Cdd:COG3268 344 ATAFG-AALVLRLLAVaGLTFEV 365
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 14-151 2.41e-23

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: 94.19  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212    14 LIVLGAsGFTGQFVVEEVARIIEEgpggtLQWAVAGRSRHRLEKtlsqAADALSKPELKSVEVIVADVAEaeSLAIMCKQ 93
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHFDV-----DRITVADRTLEKAQA----LAAKLGGVRFIAVAVDADNYEA--VLAALLKE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 53933212    94 AVIVLNCVGPYrfYGEPVVKACIENGAHCIDICgepqFLEGIQLMYHSKAEENGVYVI 151
Cdd:pfam03435  69 GDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 47-157 1.04e-14

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: 74.87  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  47 VAGRSRHRLEKTLSQAADalskpelksVEVIVADVAEAESLAIMCKQAVIVLNCVGPYRfyGEPVVKACIENGAHCIDIC 126
Cdd:COG1748   5 LADRSLEKAEALAASGPK---------VEAAQLDASDPEALAALIAGADLVINALPPYL--NLTVAEACIEAGVHYVDLS 73

                        90       100       110
                ....*....|....*....|....*....|.
gi 53933212 127 GEPQFLEgIQLMYHSKAEENGVYVIGSCGFD 157
Cdd:COG1748  74 EDEPETE-AKLALDELAKEAGVTAIPGCGLA 103
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 15-120 5.30e-07

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: 49.32  E-value: 5.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  15 IVLGASGFTGQFVVEEvarIIEEGpggtlqWAVAGRSRHrlektlsqaADALSKPELKSVEVIVADVAEAESLAIMCKQA 94
Cdd:cd05226   2 LILGATGFIGRALARE---LLEQG------HEVTLLVRN---------TKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGV 63

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 53933212  95 VIVLNCVGPYRFYGEP----------VVKACIENGA 120
Cdd:cd05226  64 DVVIHLAGAPRDTRDFcevdvegtrnVLEAAKEAGV 99
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 15-121 1.41e-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: 43.47  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  15 IVLGASGFTGQfvveEVARIIEEGpggTLQWAVAGRSRHRLEKtlsqaadalskpeLKSVEVIVADVAEAESLAIMCKQA 94
Cdd:cd05229   3 HVLGASGPIGR----EVARELRRR---GWDVRLVSRSGSKLAW-------------LPGVEIVAADAMDASSVIAAARGA 62

                        90       100       110
                ....*....|....*....|....*....|....*
gi 53933212  95 VIVLNCVGP-YRFYG-------EPVVKACIENGAH 121
Cdd:cd05229  63 DVIYHCANPaYTRWEelfpplmENVVAAAEANGAK 97
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 16-119 1.09e-03

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: 40.21  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  16 VLGASGFTGQFVVEevaRIIEEGpggtlqWAVAGRSRHrlektlsqaADALSKPELKSVEVIVADVAEAESLAIMCKQAV 95
Cdd:COG0702   4 VTGATGFIGRRVVR---ALLARG------HPVRALVRD---------PEKAAALAAAGVEVVQGDLDDPESLAAALAGVD 65

                        90       100       110
                ....*....|....*....|....*....|..
gi 53933212  96 IVLNCVGP--------YRFYGEPVVKACIENG 119
Cdd:COG0702  66 AVFLLVPSgpggdfavDVEGARNLADAAKAAG 97
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
15-119 1.94e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 39.96  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  15 IVLGASGFTGQFVVEevaRIIEEGpggtlqWAVAGRSRhrlektLSQAADALskPELKSVEVIVADVAEAESLAIMCKQA 94
Cdd:COG0451   3 LVTGGAGFIGSHLAR---RLLARG------HEVVGLDR------SPPGAANL--AALPGVEFVRGDLRDPEALAAALAGV 65

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 53933212  95 VIVLNCVGPYRFYGEP--------------VVKACIENG 119
Cdd:COG0451  66 DAVVHLAAPAGVGEEDpdetlevnvegtlnLLEAARAAG 104
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
13-103 2.00e-03

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


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 39.45  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  13 HLIVLGASGFTGQFVVEE-VARiieegpgG---TlqwAVAgRSRHRLEKTLSQaadalskpelksVEVIVADVAEAESLA 88
Cdd:COG2910   1 KIAVIGATGRVGSLIVREaLAR-------GhevT---ALV-RNPEKLPDEHPG------------LTVVVGDVLDPAAVA 57

                        90
                ....*....|....*....
gi 53933212  89 imckQAV----IVLNCVGP 103
Cdd:COG2910  58 ----EALagadAVVSALGA 72
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 16-120 2.07e-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: 39.92  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  16 VLGASGFTGQFVVEEVARIieegpgGTlQWAVAGRSRHrlektlsQAADALSKPELKSVEVIVADVAEAESLAIMCKQAV 95
Cdd:cd05271   5 VFGATGFIGRYVVNRLAKR------GS-QVIVPYRCEA-------YARRLLVMGDLGQVLFVEFDLRDDESIRKALEGSD 70

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 53933212  96 IVLNCVG------PYRFYG------EPVVKACIENGA 120
Cdd:cd05271  71 VVINLVGrlyetkNFSFEDvhvegpERLAKAAKEAGV 107
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 16-96 2.21e-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: 39.14  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  16 VLGASGFTGQFVVEEvarIIEEGpggtlqWAVAGRSRHRlektlSQAADAlskpELKSVEVIVADVAEAESLAIMCK--Q 93
Cdd:cd05243   4 VVGATGKVGRHVVRE---LLDRG------YQVRALVRDP-----SQAEKL----EAAGAEVVVGDLTDAESLAAALEgiD 65


                ...
gi 53933212  94 AVI 96
Cdd:cd05243  66 AVI 68
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 30-153 2.54e-03

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, 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). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 38.29  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53933212  30 EVARIIEEGPGGTLQwAVAGRSRHRLEKTLSQAAdalskPELKSVEVIVADVAEAESLaimcKQAVIVLNCVGPYRFYGE 109
Cdd:cd24146  14 GIARYLLEKPGLEIV-GAVDRDPAKVGKDLGELG-----GGAPLGVKVTDDLDAVLAA----TKPDVVVHATTSFLADVA 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 53933212 110 PVVKACIENGAHCIDICGE--------PQFLEgiqlMYHSKAEENGVYVIGS 153
Cdd:cd24146  84 PQIERLLEAGLNVITTCEElfypwardPELAE----ELDALAKENGVTVLGT 131
 
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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