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Conserved domains on  [gi|268576991|ref|XP_002643477|]
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Protein CBG16139 [Caenorhabditis briggsae]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase family protein( domain architecture ID 11441205)

3-hydroxyacyl-CoA dehydrogenase (HCDH) family protein such as mitochondrial HCDH, which plays an essential role in the beta-oxidation of short chain fatty acids

CATH:  3.40.50.720|1.10.1040.10
EC:  1.1.1.-
Gene Ontology:  GO:0003857|GO:0006635|GO:0070403
PubMed:  3479790
SCOP:  4000107

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 21-308 1.41e-140

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: 397.94  E-value: 1.41e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  21 KINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMSTN 100
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250   76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 181 HNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 268576991 261 GLDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:COG1250  235 GLDTALAVLEVLYEALGDP-RYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 21-308 1.41e-140

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: 397.94  E-value: 1.41e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  21 KINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMSTN 100
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250   76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 181 HNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 268576991 261 GLDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:COG1250  235 GLDTALAVLEVLYEALGDP-RYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 19-308 1.21e-115

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 335.16  E-value: 1.21e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  19 LSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMS 98
Cdd:PLN02545   1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATL-----GRIRCT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  99 TNVsDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEV 178
Cdd:PLN02545  76 TNL-EELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 179 VRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSD 258
Cdd:PLN02545 155 IRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLAD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 268576991 259 YVGLDTCKFIMDGWHKQYpDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PLN02545 235 FIGLDTCLSIMKVLHEGL-GDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 24-209 2.28e-80

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 241.29  E-value: 2.28e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   24 NVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQtalvsSVLDRIKMSTNVSD 103
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-----AALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  104 SVkDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRHND 183
Cdd:pfam02737  76 AV-DADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 268576991  184 TSDDTFQKLMEYGKAVGKTTVACKDT 209
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 22-308 3.60e-52

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: 182.34  E-value: 3.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKhaddakAQTAL-VSSVLDRIKMSTN 100
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRK------KITSLeRDSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVR 180
Cdd:TIGR02441 409 YSG-FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  181 HNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMPDIDvAMKLGAGYPMGPFELSDYV 260
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEG-VDPKKLD-KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 268576991  261 GLDTCKFIMDGWHKQYPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-115 1.83e-06

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 48.47  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   7 TAAVRGLSTTAQLSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKaqkgiesslqrvAKKKHADDakaqta 86
Cdd:cd05188  120 ATAYHALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLEL------------AKELGADH------ 181

                         90       100
                 ....*....|....*....|....*....
gi 268576991  87 lVSSVLDRIKMSTNVSDSVKDADLVIEAI 115
Cdd:cd05188  182 -VIDYKEEDLEEELRLTGGGGADVVIDAV 209
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 21-308 1.41e-140

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: 397.94  E-value: 1.41e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  21 KINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMSTN 100
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250   76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 181 HNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250  155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 268576991 261 GLDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:COG1250  235 GLDTALAVLEVLYEALGDP-RYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 19-308 1.21e-115

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 335.16  E-value: 1.21e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  19 LSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMS 98
Cdd:PLN02545   1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATL-----GRIRCT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  99 TNVsDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEV 178
Cdd:PLN02545  76 TNL-EELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 179 VRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSD 258
Cdd:PLN02545 155 IRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLAD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 268576991 259 YVGLDTCKFIMDGWHKQYpDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PLN02545 235 FIGLDTCLSIMKVLHEGL-GDSKYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 22-308 2.15e-103

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 303.81  E-value: 2.15e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMSTNV 101
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAAL-----ARITGTTDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 102 SDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK05808  78 DD-LKDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 182 NDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYVG 261
Cdd:PRK05808 157 LATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 268576991 262 LDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK05808 237 LDTCLAIMEVLYEGFGDS-KYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 16-308 7.05e-103

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 310.24  E-value: 7.05e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  16 TAQLSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRI 95
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAAL-----ARL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  96 KMSTNVSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKL 175
Cdd:PRK08268  76 RPVEALAD-LADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 176 LEVVRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFE 255
Cdd:PRK08268 155 VEVVSGLATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFE 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 268576991 256 LSDYVGLDTCKFIMDGWHKQYPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK08268 235 LMDLIGLDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 20-309 1.01e-97

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 289.60  E-value: 1.01e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  20 SKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQR-VAKKKHADDAKAQTalvssvLDRIKMS 98
Cdd:PRK07530   2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARqVAKGKISEEARAAA------LARISTA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  99 TNVSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEV 178
Cdd:PRK07530  76 TDLED-LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 179 VRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEAL-RLYErGDASMPDIDVAMKLGAGYPMGPFELS 257
Cdd:PRK07530 155 IRGIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELA 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268576991 258 DYVGLDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRKSGEGFYKYK 309
Cdd:PRK07530 234 DFIGLDTCLSIMQVLHDGLADS-KYRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 20-308 1.56e-94

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 281.49  E-value: 1.56e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  20 SKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQR-VAKKKHADDAKAQTalvssvLDRIKMS 98
Cdd:PRK07819   3 DAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERaVSRGKLTERERDAA------LARLRFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  99 TNVSDsVKDADLVIEAIVENIDIKRKLFAEVEAA-AKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLE 177
Cdd:PRK07819  77 TDLGD-FADRQLVIEAVVEDEAVKTEIFAELDKVvTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 178 VVRHNDTSDDTFQKLMEYGKAV-GKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFEL 256
Cdd:PRK07819 156 LVPTLVTSEATVARAEEFASDVlGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268576991 257 SDYVGLDTCKFIMDGWHKQYpDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK07819 236 SDLVGLDTVKAIADSMYEEF-KEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
22-308 4.21e-83

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 252.40  E-value: 4.21e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQTALvssvlDRIKMSTNV 101
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAAL-----ARLSYSLDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 102 SDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK09260  76 KAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 182 NDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYVG 261
Cdd:PRK09260 156 LETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 268576991 262 LDTCKFIMDGWHKQYPDEvaFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK09260 236 LDTRLNNLKYLHETLGEK--YRPAPLLEKYVKAGRLGRKTGRGVYDY 280
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 24-209 2.28e-80

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 241.29  E-value: 2.28e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   24 NVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQtalvsSVLDRIKMSTNVSD 103
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-----AALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  104 SVkDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRHND 183
Cdd:pfam02737  76 AV-DADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 268576991  184 TSDDTFQKLMEYGKAVGKTTVACKDT 209
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
22-309 2.29e-73

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 227.52  E-value: 2.29e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIEsslqRVAKKKHADDAKAQTALVSSVLDRIKMSTNV 101
Cdd:PRK08293   3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 102 SDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLrladIGLNLKDKT----RFGGLHFFNPVPMMKLLE 177
Cdd:PRK08293  79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTL----LPSQFAEATgrpeKFLALHFANEIWKNNTAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 178 VVRHNDTSDDTFQKLMEYGKAVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFEL 256
Cdd:PRK08293 155 IMGHPGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGI 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 268576991 257 SDYVGLDTCKFIMDGWHKQYPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKYK 309
Cdd:PRK08293 235 LDIVGLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 22-300 2.78e-73

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 227.45  E-value: 2.78e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESS---LQRVAKKKHADDAKAQtalvsSVLDRIKMS 98
Cdd:PRK06035   3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAK-----AIMARIRTS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  99 TNVSdSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEV 178
Cdd:PRK06035  78 TSYE-SLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 179 VRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSD 258
Cdd:PRK06035 157 VRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMD 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 268576991 259 YVGLDTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKTGRK 300
Cdd:PRK06035 237 IIGIDTVYHIAEYLYEETGDP-QFIPPNSLKQMVLNGYVGDK 277
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 22-308 1.33e-66

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 210.78  E-value: 1.33e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAqtalvssvldRIKMSTNV 101
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGMG----------RIRMEAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 102 SDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK06130  74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 182 NDTSDDTFQKLMEYGKAVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPM---GPFELS 257
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268576991 258 DYVGLDTCKFIMDgwhKQYPD-EVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK06130 234 DMNGLDVHLAVAS---YLYQDlENRTTPSPLLEEKVEAGELGAKSGQGFYAW 282
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
9-309 1.35e-65

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 218.58  E-value: 1.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   9 AVRGLS--TTAQLSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKHADDAKAQta 86
Cdd:PRK11730 298 YVKGKAkkLAKDAKPVKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGAKMA-- 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  87 lvsSVLDRIKMSTNVSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHF 166
Cdd:PRK11730 376 ---GVLSSIRPTLDYAG-FERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHF 451

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 167 FNPVPMMKLLEVVRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMPDIDVAMKLG 246
Cdd:PRK11730 452 FNPVHRMPLVEVIRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKVMEKQ 530

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268576991 247 AGYPMGPFELSDYVGLDTckfimdGWHKQ------YPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKYK 309
Cdd:PRK11730 531 FGWPMGPAYLLDVVGIDT------AHHAQavmaegFPDRMKKDYRDAIDVLFEAKRFGQKNGKGFYRYE 593
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
15-309 1.60e-61

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 207.44  E-value: 1.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  15 TTAQLSKINNVTVIGAGLMGSGIAQVSA-NAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKH--ADDAKAQTALVSSV 91
Cdd:PRK11154 302 SDAKPRPVNKVGVLGGGLMGGGIAYVTAtKAGLPVRIKDINPQGINHALKYSWDLLDKKVKRRHlkPSERDKQMALISGT 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  92 LDrikmstnvSDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVP 171
Cdd:PRK11154 382 TD--------YRGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVE 453

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 172 MMKLLEVVRHNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMPDIDVAMkLGAGYPM 251
Cdd:PRK11154 454 KMPLVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL-VKFGFPV 531

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 268576991 252 GPFELSDYVGLDTCKFIMDGWHKQYPDEvaFKPSPLLDSLVDAGKTGRKSGEGFYKYK 309
Cdd:PRK11154 532 GPITLLDEVGIDVGTKIIPILEAALGER--FSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 22-308 3.60e-52

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: 182.34  E-value: 3.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAKKKhaddakAQTAL-VSSVLDRIKMSTN 100
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRK------KITSLeRDSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVR 180
Cdd:TIGR02441 409 YSG-FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  181 HNDTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMPDIDvAMKLGAGYPMGPFELSDYV 260
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEG-VDPKKLD-KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 268576991  261 GLDTCKFIMDGWHKQYPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 211-308 2.78e-48

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: 156.61  E-value: 2.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  211 GFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYVGLDTCKFIMDGWHKQYPDEvAFKPSPLLDS 290
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDR-AYRPPPLLEK 79

                          90
                  ....*....|....*...
gi 268576991  291 LVDAGKTGRKSGEGFYKY 308
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 33-308 8.86e-40

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 141.35  E-value: 8.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  33 MGSGIAQVSANAKLNVVVVDSNQ------SALDKAQKG-IESSLQRVAKKKHADDAKAQtalvsSVLDRIKMST--NVSD 103
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPrdaagwRALDAEARAeIERTLAALVALGRIDAAQAD-----AVLARIAVVArdGAAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 104 SVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRHND 183
Cdd:PRK08269  76 ALADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 184 TSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYP---MGPFELSDYV 260
Cdd:PRK08269 156 TDPAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 268576991 261 GLDTCkFIMDGWHKQYPDEVAFKPSPLLDSLVDAGKTGRKSGEGFYKY 308
Cdd:PRK08269 236 GCDIL-YYASRYLAGEIGPDRFAPPAIVVRNMEEGRDGLRTGAGFYDY 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 22-258 8.59e-37

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 133.63  E-value: 8.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVAkkkHADDAKAQTALvsSVLDRIKMSTNV 101
Cdd:PRK06129   2 MGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLA---AFDLLDGEAPD--AVLARIRVTDSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 102 SDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK06129  77 ADAVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 182 NDTSDDTFQKLMEYGKAVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYP---MGPFELS 257
Cdd:PRK06129 157 PWTAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETI 236


                 .
gi 268576991 258 D 258
Cdd:PRK06129 237 D 237
PRK07066 PRK07066
L-carnitine dehydrogenase;
19-254 1.73e-26

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 106.07  E-value: 1.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  19 LSKINNVTVIGAGLMGSG-IAQVSANAkLNVVVVDSNQSALDKAQKGIES---SLQRVAKKKHADdakaqtalvssvLDR 94
Cdd:PRK07066   4 ITDIKTFAAIGSGVIGSGwVARALAHG-LDVVAWDPAPGAEAALRANVANawpALERQGLAPGAS------------PAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  95 IKMSTNVSDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMK 174
Cdd:PRK07066  71 LRFVATIEACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 175 LLEVVRHNDTSDDTFQKLMEYGKAVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYP--- 250
Cdd:PRK07066 151 LVEVLGGERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsf 230


                 ....
gi 268576991 251 MGPF 254
Cdd:PRK07066 231 MGTF 234
PRK07531 PRK07531
carnitine 3-dehydrogenase;
19-255 1.24e-23

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 100.58  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  19 LSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSAldkaqkgiesslQRVAKKKHADDAKAQTALVSSVL---DRI 95
Cdd:PRK07531   1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA------------ERIIGEVLANAERAYAMLTDAPLppeGRL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  96 KMSTNVSDSVKDADLVIEAIVENIDIKRKLFAEVEAAAKPTTLITTNTSSLRLADIGLNLKDKTRFGGLHFFNPVPMMKL 175
Cdd:PRK07531  69 TFCASLAEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 176 LEVVRHNDTSDDTFQKLMEYGKAVG-KTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGY---PM 251
Cdd:PRK07531 149 VELVGGGKTSPETIRRAKEILREIGmKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQM 228


                 ....
gi 268576991 252 GPFE 255
Cdd:PRK07531 229 GLFE 232
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 183-297 6.22e-12

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 66.02  E-value: 6.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991 183 DTSDDTFQKLMEYGKAVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMPDIDVAMKLGAGYPMGPFELSDYVGL 262
Cdd:PRK08268 388 ATSPAARDAAHALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGA 467

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 268576991 263 DTCKFIMDGWHKQYPDEvAFKPSPLLDSLVDAGKT 297
Cdd:PRK08268 468 ARILRVLENLQALYGDP-RYRPSPWLRRRAALGLS 501
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 22-140 7.31e-07

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 49.74  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  22 INNVTVIGAGLMGSGIAQV--SANAKLNVVVVDSNQSALDKAQK-GiesslqrvakkkhaddakaqtalvssVLDRIkmS 98
Cdd:COG0287    1 FMRIAIIGLGLIGGSLALAlkRAGLAHEVVGVDRSPETLERALElG--------------------------VIDRA--A 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 268576991  99 TNVSDSVKDADLVI-----EAIVEnidikrkLFAEVEAAAKPTTLIT 140
Cdd:COG0287   53 TDLEEAVADADLVVlavpvGATIE-------VLAELAPHLKPGAIVT 92
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-115 1.83e-06

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 48.47  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991   7 TAAVRGLSTTAQLSKINNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKaqkgiesslqrvAKKKHADDakaqta 86
Cdd:cd05188  120 ATAYHALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLEL------------AKELGADH------ 181

                         90       100
                 ....*....|....*....|....*....
gi 268576991  87 lVSSVLDRIKMSTNVSDSVKDADLVIEAI 115
Cdd:cd05188  182 -VIDYKEEDLEEELRLTGGGGADVVIDAV 209
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 23-121 5.23e-03

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. 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: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 37.82  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  23 NNVTVI--GAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQKGIESSLQRVakkkhaddakaqTALVSSVLDRikmstn 100
Cdd:cd08935    5 NKVAVItgGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRA------------IALAADVLDR------ 66

                         90       100
                 ....*....|....*....|.
gi 268576991 101 vsDSVKDADLVIEAIVENIDI 121
Cdd:cd08935   67 --ASLERAREEIVAQFGTVDI 85
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 25-121 7.36e-03

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 37.82  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268576991  25 VTVIGAGLMGSGI-AQVSANAKLNVVVV-DSNqsaLDKAQKGIESSLQRVAKKKHADDAkaqtalvSSVLDRIKM-STNV 101
Cdd:COG4091   18 VGLIGAGQMGRGLlAQIRRMPGMEVVAIaDRN---PERARAALREAGIPEEDIRVVDTA-------AEADAAIAAgKTVV 87

                         90       100
                 ....*....|....*....|
gi 268576991 102 SDsvkDADLVIEAivENIDI 121
Cdd:COG4091   88 TD---DAELLIAA--DGIDV 102
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 23-62 9.80e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 36.97  E-value: 9.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 268576991  23 NNVTVIGAGLMGSGIAQVSANAKLNVVVVDSNQSALDKAQ 62
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLA 135
 
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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