|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
5-312 |
1.41e-113 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 330.85 E-value: 1.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNiRASEQFALIGVTTRLEELTRE 84
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGE-APDAVLARIRVTDSLADAVAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:PRK06129 83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 165 AVERTRDLMLSLGQRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLETAHLNAPG 244
Cdd:PRK06129 163 TLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDLNAPG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129993 245 GVADYFQRFGGEISAVSATYGEtpNTQEDRETLAEIARQCEQLVSLEKLDERRAVRDEFLIQLAKLKK 312
Cdd:PRK06129 243 GVADYAQRYGPMYRRMAAERGQ--PVPWDGELVARVEAERRAALPLDQLAARQAWRDRRLMALAAHRR 308
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
4-240 |
8.34e-70 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 218.06 E-value: 8.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 4 QKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNiRASEQFALIGVTTRLEELtR 83
Cdd:COG1250 3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEE-EADAALARITPTTDLAAL-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 84 EAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSP 163
Cdd:COG1250 81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129993 164 SAVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRyalLGSLETAHL 240
Cdd:COG1250 161 ETVATAVAFARRLGKTPVVVK-DTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFP---MGPFELADL 233
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
5-184 |
3.25e-53 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 172.34 E-value: 3.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRAsEQFALIGVTTRLEELtRE 84
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-AALARISFTTDLAAA-VD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:pfam02737 79 ADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPE 158
|
170 180
....*....|....*....|
gi 20129993 165 AVERTRDLMLSLGQRPVTLK 184
Cdd:pfam02737 159 TVATTVELAKKIGKTPVVVK 178
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
6-220 |
6.07e-09 |
|
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).
Pssm-ID: 131494 [Multi-domain] Cd Length: 737 Bit Score: 57.15 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 6 IGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRASeqfALIGVTTRLE-ELTRE 84
Cdd:TIGR02441 338 LAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDS---ILSNLTPTLDySGFKN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 20129993 165 AVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGIlSVADVDRV 220
Cdd:TIGR02441 495 TLASAVAVGLKQGKVVIVVK-DGPGFYTTRCLGPMLAEVIRLLQEGV-DPKKLDKL 548
|
|
| SDR_c9 |
cd08931 |
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ... |
10-47 |
5.11e-04 |
|
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and 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: 187636 [Multi-domain] Cd Length: 227 Bit Score: 40.90 E-value: 5.11e-04
10 20 30
....*....|....*....|....*....|....*...
gi 20129993 10 GSGlIGRAWAMLFAAAGYRVQLYDILESQLATALQELD 47
Cdd:cd08931 9 ASG-IGRETALLFARNGWFVGLYDIDEDGLAALAAELG 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
5-312 |
1.41e-113 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 330.85 E-value: 1.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNiRASEQFALIGVTTRLEELTRE 84
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGE-APDAVLARIRVTDSLADAVAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:PRK06129 83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 165 AVERTRDLMLSLGQRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLETAHLNAPG 244
Cdd:PRK06129 163 TLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDLNAPG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129993 245 GVADYFQRFGGEISAVSATYGEtpNTQEDRETLAEIARQCEQLVSLEKLDERRAVRDEFLIQLAKLKK 312
Cdd:PRK06129 243 GVADYAQRYGPMYRRMAAERGQ--PVPWDGELVARVEAERRAALPLDQLAARQAWRDRRLMALAAHRR 308
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
4-240 |
8.34e-70 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 218.06 E-value: 8.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 4 QKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNiRASEQFALIGVTTRLEELtR 83
Cdd:COG1250 3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEE-EADAALARITPTTDLAAL-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 84 EAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSP 163
Cdd:COG1250 81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129993 164 SAVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRyalLGSLETAHL 240
Cdd:COG1250 161 ETVATAVAFARRLGKTPVVVK-DTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFP---MGPFELADL 233
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
5-184 |
3.25e-53 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 172.34 E-value: 3.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRAsEQFALIGVTTRLEELtRE 84
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-AALARISFTTDLAAA-VD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:pfam02737 79 ADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPE 158
|
170 180
....*....|....*....|
gi 20129993 165 AVERTRDLMLSLGQRPVTLK 184
Cdd:pfam02737 159 TVATTVELAKKIGKTPVVVK 178
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
4-241 |
2.22e-48 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 164.18 E-value: 2.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 4 QKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLhrleeqSALRGNIRASEQFALIGVTTRLEELTR 83
Cdd:PRK06130 5 QNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERAL------GVYAPLGIASAGMGRIRMEAGLAAAVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 84 EAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSP 163
Cdd:PRK06130 79 GADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129993 164 SAVERTRDLMLSLGQRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLETAHLN 241
Cdd:PRK06130 159 QTVATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMN 236
|
|
| PRK07531 |
PRK07531 |
carnitine 3-dehydrogenase; |
5-237 |
5.28e-45 |
|
carnitine 3-dehydrogenase;
Pssm-ID: 236044 [Multi-domain] Cd Length: 495 Bit Score: 159.52 E-value: 5.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAAAGYRVQLYD-------ILESQLATAlqelDKDLHRLEeQSAL--RGNIRASEQfaligvt 75
Cdd:PRK07531 6 KAACIGGGVIGGGWAARFLLAGIDVAVFDphpeaerIIGEVLANA----ERAYAMLT-DAPLppEGRLTFCAS------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 76 trLEELTREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEI 155
Cdd:PRK07531 74 --LAEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 156 VPAPWTSPSAVERTRDLMLSLGQRPVTLKREIQGFATNRiqyaILNEVWR----LVGSGILSVADVDRVLSQGLGLRYAL 231
Cdd:PRK07531 152 VGGGKTSPETIRRAKEILREIGMKPVHIAKEIDAFVGDR----LLEALWRealwLVKDGIATTEEIDDVIRYSFGLRWAQ 227
|
....*.
gi 20129993 232 LGSLET 237
Cdd:PRK07531 228 MGLFET 233
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
14-236 |
9.80e-38 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 136.34 E-value: 9.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 14 IGRAWAMLFAAAGYRVQLYDI-------LESQLATALQELDKDLHRLeeqSALrGNIRASEQFALIG---VTTR--LEEL 81
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFkprdaagWRALDAEARAEIERTLAAL---VAL-GRIDAAQADAVLAriaVVARdgAADA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 82 TREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWT 161
Cdd:PRK08269 77 LADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDAT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129993 162 SPSAVERTRDLMLSLGQRPVTLkREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLE 236
Cdd:PRK08269 157 DPAVVDRLAALLERIGKVPVVC-GPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLGLLE 230
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
9-254 |
3.42e-34 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 127.26 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 9 VGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRASEQFaligVTTrLEELTREAVHI 88
Cdd:PRK07066 13 IGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPARLRF----VAT-IEACVADADFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 89 QECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPSAVER 168
Cdd:PRK07066 88 QESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERTAPEAVDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 169 TRDLMLSLGQRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLETAHL-NAPGGVA 247
Cdd:PRK07066 168 AMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLaGGDAGMR 247
|
....*..
gi 20129993 248 DYFQRFG 254
Cdd:PRK07066 248 HFMQQFG 254
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
4-240 |
2.91e-32 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 121.05 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 4 QKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKdlhrLEEQSALRGNIRASEQ---FALIGVTTRLEE 80
Cdd:PRK09260 2 EKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIAS----IFEQGVARGKLTEAARqaaLARLSYSLDLKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 81 LTREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPW 160
Cdd:PRK09260 78 AVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 161 TSPSAVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSqgLGLRYAlLGSLETAHL 240
Cdd:PRK09260 158 TSDETVQVAKEVAEQMGKETVVVN-EFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIR--LGLNFP-MGPLELGDL 233
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
1-238 |
2.45e-30 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 116.37 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSS-QKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIrASEQFALIGVTTRLE 79
Cdd:PLN02545 1 MAEiKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEE-ADATLGRIRCTTNLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 80 ELtREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAP 159
Cdd:PLN02545 80 EL-RDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129993 160 WTSPSAVERTRDLMLSLGQRPVTlKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRyalLGSLETA 238
Cdd:PLN02545 159 DTSDEVFDATKALAERFGKTVVC-SQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHP---MGPLHLA 233
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-224 |
1.03e-29 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 114.29 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEqsalRGNIRASEQ---FALIGVTTR 77
Cdd:PRK05808 1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVK----KGKMTEADKeaaLARITGTTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 78 LEELtREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVP 157
Cdd:PRK05808 77 LDDL-KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129993 158 APWTSPSAVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQG 224
Cdd:PRK05808 156 GLATSDATHEAVEALAKKIGKTPVEVK-NAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLG 221
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
1-219 |
2.71e-29 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 113.11 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRASEQFALIGVTTRLEE 80
Cdd:PRK08293 1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEAALNRITLTTDLAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 81 LTREAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPW 160
Cdd:PRK08293 81 AVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129993 161 TSPSAVERTRDLMLSLGQRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDR 219
Cdd:PRK08293 161 TDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDK 219
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
1-236 |
1.14e-27 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 112.25 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEqsalRGNIRASEQFALIG---VTTR 77
Cdd:PRK08268 5 PSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVE----KGKLTAEQADAALArlrPVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 78 LEELTREAVHIqECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVP 157
Cdd:PRK08268 81 LADLADCDLVV-EAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129993 158 APWTSPSAVERTRDLMLSLGQRPVtLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRyalLGSLE 236
Cdd:PRK08268 160 GLATDPAVADALYALARAWGKTPV-RAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFR---MGPFE 234
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
1-227 |
6.84e-27 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 106.88 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKD---LHRLEEQSALRGNiRASEQFALIGVTTR 77
Cdd:PRK06035 1 MDIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSED-EAKAIMARIRTSTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 78 LEELTrEAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVP 157
Cdd:PRK06035 80 YESLS-DADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 158 APWTSPSAVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGL 227
Cdd:PRK06035 159 AALTSEETFNTTVELSKKIGKIPIEVA-DVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGF 227
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-237 |
4.34e-18 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 82.73 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEqsalRGNIRASEQFALIG---VTTR 77
Cdd:PRK07819 3 DAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVS----RGKLTERERDAALArlrFTTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 78 LEELT-REAVhiQECVPEVLHLKKSLYSQLDELLEE-QTVVASSTSTfMPSLYSEGLQKR-QQMLVAHPLNPPYFIPLVE 154
Cdd:PRK07819 79 LGDFAdRQLV--IEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSS-IPIMKLAAATKRpGRVLGLHFFNPVPVLPLVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 155 IVPAPWTSPSAVERTRDLMLS-LGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLG-----LR 228
Cdd:PRK07819 156 LVPTLVTSEATVARAEEFASDvLGKQVVRAQ-DRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAhpmgpLR 234
|
....*....
gi 20129993 229 YALLGSLET 237
Cdd:PRK07819 235 LSDLVGLDT 243
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-218 |
1.22e-17 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 81.21 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRleeQSAlRGNIRASEQ---FALIGVTTR 77
Cdd:PRK07530 2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLAR---QVA-KGKISEEARaaaLARISTATD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 78 LEELTREAVHIqECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVP 157
Cdd:PRK07530 78 LEDLADCDLVI-EAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129993 158 APWTSPSAVERTRDLMLSLGqRPVTLKREIQGFATNRIQYAILNEVWRLVGSGILSVADVD 218
Cdd:PRK07530 157 GIATDEATFEAAKEFVTKLG-KTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAID 216
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
189-256 |
2.52e-16 |
|
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.
Pssm-ID: 395588 [Multi-domain] Cd Length: 97 Bit Score: 73.02 E-value: 2.52e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129993 189 GFATNRIQYAILNEVWRLVGSGILSVADVDRVLSQGLGLRYALLGSLETAHLNAPGGVADYFQRFGGE 256
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGD 68
|
|
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
5-221 |
6.09e-10 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 59.91 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 5 KIGIVGSGLIGRAWAMLFAA-AGYRVQLYDILESQLATALQELDKdlhRLEEQSALRgNIRASE---QFALIGVTTRLEE 80
Cdd:PRK11154 311 KVGVLGGGLMGGGIAYVTATkAGLPVRIKDINPQGINHALKYSWD---LLDKKVKRR-HLKPSErdkQMALISGTTDYRG 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 81 LTREAVHIqECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPW 160
Cdd:PRK11154 387 FKHADVVI-EAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAK 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129993 161 TSPSAVERTRDLMLSLGQRPVTLKREiQGFATNRIQYAILNEVWRLVGSGIlSVADVDRVL 221
Cdd:PRK11154 466 TSAETIATTVALAKKQGKTPIVVRDG-AGFYVNRILAPYINEAARLLLEGE-PIEHIDAAL 524
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
6-220 |
6.07e-09 |
|
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).
Pssm-ID: 131494 [Multi-domain] Cd Length: 737 Bit Score: 57.15 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 6 IGIVGSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRGNIRASeqfALIGVTTRLE-ELTRE 84
Cdd:TIGR02441 338 LAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDS---ILSNLTPTLDySGFKN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 85 AVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPAPWTSPS 164
Cdd:TIGR02441 415 ADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 20129993 165 AVERTRDLMLSLGQRPVTLKrEIQGFATNRIQYAILNEVWRLVGSGIlSVADVDRV 220
Cdd:TIGR02441 495 TLASAVAVGLKQGKVVIVVK-DGPGFYTTRCLGPMLAEVIRLLQEGV-DPKKLDKL 548
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
7-226 |
1.13e-08 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 56.02 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 7 GIVGSGLigrawAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLEEQSALRG--------NIRASEQFALIGvttrl 78
Cdd:PRK11730 322 GIMGGGI-----AYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGakmagvlsSIRPTLDYAGFE----- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129993 79 eeltrEAVHIQECVPEVLHLKKSLYSQLDELLEEQTVVASSTSTFMPSLYSEGLQKRQQMLVAHPLNPPYFIPLVEIVPA 158
Cdd:PRK11730 392 -----RVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRG 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129993 159 PWTSPSAVERTRDLMLSLGQRPVTLkREIQGFATNRIQYAILNEVWRLVGSGilsvAD---VDRVLSQGLG 226
Cdd:PRK11730 467 EKTSDETIATVVAYASKMGKTPIVV-NDCPGFFVNRVLFPYFAGFSQLLRDG----ADfrqIDKVMEKQFG 532
|
|
| PRK08267 |
PRK08267 |
SDR family oxidoreductase; |
10-47 |
1.04e-05 |
|
SDR family oxidoreductase;
Pssm-ID: 236210 [Multi-domain] Cd Length: 260 Bit Score: 46.08 E-value: 1.04e-05
10 20 30
....*....|....*....|....*....|....*...
gi 20129993 10 GSGlIGRAWAMLFAAAGYRVQLYDILESQLATALQELD 47
Cdd:PRK08267 10 ASG-IGRATALLFAAEGWRVGAYDINEAGLAALAAELG 46
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
6-31 |
1.28e-04 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 42.46 E-value: 1.28e-04
10 20
....*....|....*....|....*.
gi 20129993 6 IGIVGSGLIGRAWAMLFAAAGYRVQL 31
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVI 26
|
|
| SDR_c9 |
cd08931 |
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ... |
10-47 |
5.11e-04 |
|
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and 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: 187636 [Multi-domain] Cd Length: 227 Bit Score: 40.90 E-value: 5.11e-04
10 20 30
....*....|....*....|....*....|....*...
gi 20129993 10 GSGlIGRAWAMLFAAAGYRVQLYDILESQLATALQELD 47
Cdd:cd08931 9 ASG-IGRETALLFARNGWFVGLYDIDEDGLAALAAELG 45
|
|
| fabG |
PRK05653 |
3-oxoacyl-ACP reductase FabG; |
10-70 |
1.70e-03 |
|
3-oxoacyl-ACP reductase FabG;
Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 39.37 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129993 10 GSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQELDKDLHRLeeqSALRGNIRASEQFA 70
Cdd:PRK05653 13 ASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEA---RVLVFDVSDEAAVR 70
|
|
| LDH |
cd12186 |
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ... |
1-34 |
3.56e-03 |
|
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.
Pssm-ID: 240662 Cd Length: 329 Bit Score: 38.67 E-value: 3.56e-03
10 20 30
....*....|....*....|....*....|....
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYDI 34
Cdd:cd12186 143 IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDP 176
|
|
| CtBP_dh |
cd05299 |
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ... |
1-33 |
4.29e-03 |
|
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.
Pssm-ID: 240624 [Multi-domain] Cd Length: 312 Bit Score: 38.26 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|...
gi 20129993 1 MSSQKIGIVGSGLIGRAWAMLFAAAGYRVQLYD 33
Cdd:cd05299 140 LRGLTLGLVGFGRIGRAVAKRAKAFGFRVIAYD 172
|
|
| adh_short |
pfam00106 |
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
5-46 |
6.53e-03 |
|
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 37.21 E-value: 6.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 20129993 5 KIGIV--GSGLIGRAWAMLFAAAGYRVQLYDILESQLATALQEL 46
Cdd:pfam00106 1 KVALVtgASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL 44
|
|
| |
