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Conserved domains on  [gi|6325224|ref|NP_015292|]
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Srl4p [Saccharomyces cerevisiae S288C]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 28-230 1.30e-07

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05339:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 243  Bit Score: 51.47  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSNeLGIELCETFIEDYHTKV---INIDTIDSINGKNARRSEKLYTFI-SCKDFSDIK-CLEESMLYLQNlei 102
Cdd:cd05339   1 IVLITGGGSG-IGRLLALEFAKRGAKVVildINEKGAEETANNVRKAGGKVHYYKcDVSKREEVYeAAKKIKKEVGD--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  103 iPTVLINNMqeGIESTLlkedKFLRLDEEslnEFEKIVRYNLQSVILITKfclsNIFPKVQaeaqEKAKGfYIVNISSVL 182
Cdd:cd05339  77 -VTILINNA--GVVSGK----KLLELPDE---EIEKTFEVNTLAHFWTTK----AFLPDML----ERNHG-HIVTIASVA 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6325224  183 TLKPCKSGTHFITSKCGINSFHDGITSELKLKDSNlNVKTLIaYLPSF 230
Cdd:cd05339 138 GLISPAGLADYCASKAAAVGFHESLRLELKAYGKP-GIKTTL-VCPYF 183
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 28-230 1.30e-07

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 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 have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. 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) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 51.47  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSNeLGIELCETFIEDYHTKV---INIDTIDSINGKNARRSEKLYTFI-SCKDFSDIK-CLEESMLYLQNlei 102
Cdd:cd05339   1 IVLITGGGSG-IGRLLALEFAKRGAKVVildINEKGAEETANNVRKAGGKVHYYKcDVSKREEVYeAAKKIKKEVGD--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  103 iPTVLINNMqeGIESTLlkedKFLRLDEEslnEFEKIVRYNLQSVILITKfclsNIFPKVQaeaqEKAKGfYIVNISSVL 182
Cdd:cd05339  77 -VTILINNA--GVVSGK----KLLELPDE---EIEKTFEVNTLAHFWTTK----AFLPDML----ERNHG-HIVTIASVA 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6325224  183 TLKPCKSGTHFITSKCGINSFHDGITSELKLKDSNlNVKTLIaYLPSF 230
Cdd:cd05339 138 GLISPAGLADYCASKAAAVGFHESLRLELKAYGKP-GIKTTL-VCPYF 183
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 28-212 8.64e-07

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 48.38  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224     28 TVLIIGGSSNeLGIELCETFIEDYHTKVInidtIDSINGKNARRSEKL------YTFISCkDFSDikclEESM--LYLQN 99
Cdd:pfam00106   2 VALVTGASSG-IGRAIAKRLAKEGAKVVL----VDRSEEKLEAVAKELgalggkALFIQG-DVTD----RAQVkaLVEQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    100 LEIIPTV--LINNMqeGIESTLlkedKFLRLDEEslnEFEKIVRYNLQSVILITKFCLsnifpkvqaEAQEKAKGFYIVN 177
Cdd:pfam00106  72 VERLGRLdiLVNNA--GITGLG----PFSELSDE---DWERVIDVNLTGVFNLTRAVL---------PAMIKGSGGRIVN 133

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6325224    178 ISSVLTLKPCKSGTHFITSKCGINSFHDGITSELK 212
Cdd:pfam00106 134 ISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELA 168
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 29-203 2.11e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 44.80  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    29 VLIIGGSSNELGIELCETFIEDYHTKVINidTIDSINGKN---ARRSEKLYTFISCK-DFSDikclEESMlylQNL--EI 102
Cdd:PRK05557   7 VALVTGASRGIGRAIAERLAAQGANVVIN--YASSEAGAEalvAEIGALGGKALAVQgDVSD----AESV---ERAvdEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   103 IPT-----VLINNmqEGIestlLKEDKFLRLDEEslnEFEKIVRYNLQSVILITKFClsnifpkvqAEAQEKAKGFYIVN 177
Cdd:PRK05557  78 KAEfggvdILVNN--AGI----TRDNLLMRMKEE---DWDRVIDTNLTGVFNLTKAV---------ARPMMKQRSGRIIN 139

                        170       180
                 ....*....|....*....|....*.
gi 6325224   178 ISSVLTLKPCKSGTHFITSKCGINSF 203
Cdd:PRK05557 140 ISSVVGLMGNPGQANYAASKAGVIGF 165
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
28-223 3.71e-03

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 37.93  E-value: 3.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSnelGI--ELCETFIEDYHTKVINidtidsingknARRSEKL-------------YTFISCkDFSDIKCLEE 92
Cdd:COG0300   7 TVLITGASS---GIgrALARALAARGARVVLV-----------ARDAERLealaaelraagarVEVVAL-DVTDPDAVAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   93 SMLYLQNLEIIPTVLINN---MQEGiestllkedkflRLDEESLNEFEKIVRYNLQSVILITKFCLsnifpkvqaEAQEK 169
Cdd:COG0300  72 LAEAVLARFGPIDVLVNNagvGGGG------------PFEELDLEDLRRVFEVNVFGPVRLTRALL---------PLMRA 130

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6325224  170 AKGFYIVNISSVLTLKPCKSGTHFITSKCGINSFHDGITSElkLKDSNLNVKTL 223
Cdd:COG0300 131 RGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAE--LAPTGVRVTAV 182
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 28-230 1.30e-07

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 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 have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. 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) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 51.47  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSNeLGIELCETFIEDYHTKV---INIDTIDSINGKNARRSEKLYTFI-SCKDFSDIK-CLEESMLYLQNlei 102
Cdd:cd05339   1 IVLITGGGSG-IGRLLALEFAKRGAKVVildINEKGAEETANNVRKAGGKVHYYKcDVSKREEVYeAAKKIKKEVGD--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  103 iPTVLINNMqeGIESTLlkedKFLRLDEEslnEFEKIVRYNLQSVILITKfclsNIFPKVQaeaqEKAKGfYIVNISSVL 182
Cdd:cd05339  77 -VTILINNA--GVVSGK----KLLELPDE---EIEKTFEVNTLAHFWTTK----AFLPDML----ERNHG-HIVTIASVA 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6325224  183 TLKPCKSGTHFITSKCGINSFHDGITSELKLKDSNlNVKTLIaYLPSF 230
Cdd:cd05339 138 GLISPAGLADYCASKAAAVGFHESLRLELKAYGKP-GIKTTL-VCPYF 183
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 28-212 8.64e-07

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 48.38  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224     28 TVLIIGGSSNeLGIELCETFIEDYHTKVInidtIDSINGKNARRSEKL------YTFISCkDFSDikclEESM--LYLQN 99
Cdd:pfam00106   2 VALVTGASSG-IGRAIAKRLAKEGAKVVL----VDRSEEKLEAVAKELgalggkALFIQG-DVTD----RAQVkaLVEQA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    100 LEIIPTV--LINNMqeGIESTLlkedKFLRLDEEslnEFEKIVRYNLQSVILITKFCLsnifpkvqaEAQEKAKGFYIVN 177
Cdd:pfam00106  72 VERLGRLdiLVNNA--GITGLG----PFSELSDE---DWERVIDVNLTGVFNLTRAVL---------PAMIKGSGGRIVN 133

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6325224    178 ISSVLTLKPCKSGTHFITSKCGINSFHDGITSELK 212
Cdd:pfam00106 134 ISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELA 168
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 96-229 3.06e-06

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. 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 have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. 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) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 47.21  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   96 YLQNLEIipTVLINNMqeGIESTLlkEDKFLRLDEESLNefeKIVRYNLQSVILITKFCLSNIfpkvqaeaQEKAKGFyI 175
Cdd:cd05356  73 ELEGLDI--GILVNNV--GISHSI--PEYFLETPEDELQ---DIINVNVMATLKMTRLILPGM--------VKRKKGA-I 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6325224  176 VNISSVLTLKPCKSGTHFITSKCGINSFHDGITSElkLKDSNLNVKTLIAYLPS 229
Cdd:cd05356 135 VNISSFAGLIPTPLLATYSASKAFLDFFSRALYEE--YKSQGIDVQSLLPYLVA 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 28-241 1.90e-05

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) 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: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 44.60  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSNeLGIELCETFIEDyHTKVInidtidsINGknaRRSEKLYTFISckdfsDIKCLEESMLYLQNLEIIPT-- 105
Cdd:cd05370   7 TVLITGGTSG-IGLALARKFLEA-GNTVI-------ITG---RREERLAEAKK-----ELPNIHTIVLDVGDAESVEAla 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  106 -----------VLINN--MQEGIEstllkedkfLRLDEESLNEFEKIVRYNLQSVILITKfclsNIFP--KVQAEAQeka 170
Cdd:cd05370  70 eallseypnldILINNagIQRPID---------LRDPASDLDKADTEIDTNLIGPIRLIK----AFLPhlKKQPEAT--- 133

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6325224  171 kgfyIVNISSVLTLKPCKSGTHFITSKCGINSFHDGITSELKlkdsNLNVKTLIAYLPSFESEAHWKRLSP 241
Cdd:cd05370 134 ----IVNVSSGLAFVPMAANPVYCATKAALHSYTLALRHQLK----DTGVEVVEIVPPAVDTELHEERRNP 196
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 29-203 2.11e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 44.80  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    29 VLIIGGSSNELGIELCETFIEDYHTKVINidTIDSINGKN---ARRSEKLYTFISCK-DFSDikclEESMlylQNL--EI 102
Cdd:PRK05557   7 VALVTGASRGIGRAIAERLAAQGANVVIN--YASSEAGAEalvAEIGALGGKALAVQgDVSD----AESV---ERAvdEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   103 IPT-----VLINNmqEGIestlLKEDKFLRLDEEslnEFEKIVRYNLQSVILITKFClsnifpkvqAEAQEKAKGFYIVN 177
Cdd:PRK05557  78 KAEfggvdILVNN--AGI----TRDNLLMRMKEE---DWDRVIDTNLTGVFNLTKAV---------ARPMMKQRSGRIIN 139

                        170       180
                 ....*....|....*....|....*.
gi 6325224   178 ISSVLTLKPCKSGTHFITSKCGINSF 203
Cdd:PRK05557 140 ISSVVGLMGNPGQANYAASKAGVIGF 165
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 29-211 3.21e-05

classical (c) 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, 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: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 44.20  E-value: 3.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   29 VLIIGGSSNeLGIELCETFIEDYHTKVINidtidSINGKNARRSEKLY------TFISCkDFSDIKCLEESMLYLQNLEI 102
Cdd:cd05233   1 ALVTGASSG-IGRAIARRLAREGAKVVLA-----DRNEEALAELAAIEalggnaVAVQA-DVSDEEDVEALVEEALEEFG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  103 IPTVLINNmqEGIEStllkedkFLRLDEESLNEFEKIVRYNLQSVILITKFCLSNIFpkvqaeaqeKAKGFYIVNISSVL 182
Cdd:cd05233  74 RLDILVNN--AGIAR-------PGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMK---------KQGGGRIVNISSVA 135

                       170       180
                ....*....|....*....|....*....
gi 6325224  183 TLKPCKSGTHFITSKCGINSFHDGITSEL 211
Cdd:cd05233 136 GLRPLPGQAAYAASKAALEGLTRSLALEL 164
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-203 4.03e-05

classical (c) SDR, subgroup 11; 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: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 43.94  E-value: 4.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   27 DTVLIIGGSSNELGIELCETFIEDyHTKVinidtidSINGKNARRSEKlytfisckdfSDIKCLEESMLYLQNLEIIPTV 106
Cdd:cd05364   3 GKVAIITGSSSGIGAGTAILFARL-GARL-------ALTGRDAERLEE----------TRQSCLQAGVSEKKILLVVADL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  107 LINNMQEGIESTLLKedKFLRLD---------------EESLNEFEKIVRYNLQSVILITKFCLSNIFpkvqaeaqeKAK 171
Cdd:cd05364  65 TEEEGQDRIISTTLA--KFGRLDilvnnagilakgggeDQDIEEYDKVMNLNLRAVIYLTKLAVPHLI---------KTK 133

                       170       180       190
                ....*....|....*....|....*....|..
gi 6325224  172 GfYIVNISSVLTLKPCKSGTHFITSKCGINSF 203
Cdd:cd05364 134 G-EIVNVSSVAGGRSFPGVLYYCISKAALDQF 164
PRK06398 PRK06398
aldose dehydrogenase; Validated
 27-197 5.26e-05

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 43.67  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    27 DTVLIIGGSSNELGIELCETFIeDYHTKVINIDTIDSingknarrSEKLYTFISCkDFSDIKCLEESMLYLQNLEIIPTV 106
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLK-EEGSNVINFDIKEP--------SYNDVDYFKV-DVSNKEQVIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   107 LINNmqEGIEStllkedkFLRLDEESLNEFEKIVRYNLQSVILITKFCLSNIFpkvqaeaqeKAKGFYIVNISSVLTLKP 186
Cdd:PRK06398  76 LVNN--AGIES-------YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYML---------KQDKGVIINIASVQSFAV 137

                        170
                 ....*....|.
gi 6325224   187 CKSGTHFITSK 197
Cdd:PRK06398 138 TRNAAAYVTSK 148
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-228 2.88e-04

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.21  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    30 LIIGGSSNELGIELCETFIEDyHTKVINID-TIDSINGKNARRSEKLYTFISCkDFSDIKCLE---ESMLYLQNLEIIPT 105
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEK-GTHVISISrTENKELTKLAEQYNSNLTFHSL-DLQDVHELEtnfNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   106 V-LINN--MQEGIEstllkedkflRLDEESLNEFEKIVRYNLQSVILitkfcLSNIFPKVQAEAQEKAKgfyIVNISSVL 182
Cdd:PRK06924  82 IhLINNagMVAPIK----------PIEKAESEELITNVHLNLLAPMI-----LTSTFMKHTKDWKVDKR---VINISSGA 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6325224   183 TLKPCKSGTHFITSKCGINSFHDGITSELKLKDSNLNVktlIAYLP 228
Cdd:PRK06924 144 AKNPYFGWSAYCSSKAGLDMFTQTVATEQEEEEYPVKI---VAFSP 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
 24-211 1.63e-03

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 39.83  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    24 PSHDTVLIIGGSSNeLGIELCETFIEDYHTKVInidtIDSingkNARRSEKLYTFIS------CKDFSDIKCLEESMLYL 97
Cdd:PRK06484 267 ESPRVVAITGGARG-IGRAVADRFAAAGDRLLI----IDR----DAEGAKKLAEALGdehlsvQADITDEAAVESAFAQI 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224    98 QNLEIIPTVLINNmqEGIEstllkeDKFLRLDEESLNEFEKIVRYNlqsvilitkfcLSNIFPKVQAEAQEKAKGFYIVN 177
Cdd:PRK06484 338 QARWGRLDVLVNN--AGIA------EVFKPSLEQSAEDFTRVYDVN-----------LSGAFACARAAARLMSQGGVIVN 398

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6325224   178 ISSVLTLKPCKSGTHFITSKCGINSFHDGITSEL 211
Cdd:PRK06484 399 LGSIASLLALPPRNAYCASKAAVTMLSRSLACEW 432
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
28-223 3.71e-03

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 37.93  E-value: 3.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   28 TVLIIGGSSnelGI--ELCETFIEDYHTKVINidtidsingknARRSEKL-------------YTFISCkDFSDIKCLEE 92
Cdd:COG0300   7 TVLITGASS---GIgrALARALAARGARVVLV-----------ARDAERLealaaelraagarVEVVAL-DVTDPDAVAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   93 SMLYLQNLEIIPTVLINN---MQEGiestllkedkflRLDEESLNEFEKIVRYNLQSVILITKFCLsnifpkvqaEAQEK 169
Cdd:COG0300  72 LAEAVLARFGPIDVLVNNagvGGGG------------PFEELDLEDLRRVFEVNVFGPVRLTRALL---------PLMRA 130

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6325224  170 AKGFYIVNISSVLTLKPCKSGTHFITSKCGINSFHDGITSElkLKDSNLNVKTL 223
Cdd:COG0300 131 RGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAE--LAPTGVRVTAV 182
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 106-203 5.00e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 37.51  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   106 VLINNmqEGIESTLLKEDkflrldeESLNEFEKIVRYNLQSVILITKFCLsNIFpkvqaeaqEKAKGFYIVNISSV--LT 183
Cdd:PRK05565  86 ILVNN--AGISNFGLVTD-------MTDEEWDRVIDVNLTGVMLLTRYAL-PYM--------IKRKSGVIVNISSIwgLI 147

                         90       100
                 ....*....|....*....|
gi 6325224   184 LKPCksGTHFITSKCGINSF 203
Cdd:PRK05565 148 GASC--EVLYSASKGAVNAF 165
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 29-212 5.74e-03

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. 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: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 37.27  E-value: 5.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224   29 VLIIGGSSNELGIELCETFIE-DYHTKVINIDTIDSIN--GKNARRSEKLYTFISCkDFSDI---KCLEESMLYLqNLEI 102
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKrGSPSVVVLLARSEEPLqeLKEELRPGLRVTTVKA-DLSDAagvEQLLEAIRKL-DGER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325224  103 IptVLINNmqegiESTLlkeDKFLRLDEESLNEFEKIVRYNLQSVILITKfCLSNIFPKvqaEAQEKAkgfyIVNISSVL 182
Cdd:cd05367  79 D--LLINN-----AGSL---GPVSKIEFIDLDELQKYFDLNLTSPVCLTS-TLLRAFKK---RGLKKT----VVNVSSGA 140

                       170       180       190
                ....*....|....*....|....*....|
gi 6325224  183 TLKPCKSGTHFITSKCGINSFHDGITSELK 212
Cdd:cd05367 141 AVNPFKGWGLYCSSKAARDMFFRVLAAEEP 170
 
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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