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Conserved domains on  [gi|17549919|ref|NP_509584|]
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putative 3-hydroxyacyl-CoA dehydrogenase B0272.3 [Caenorhabditis elegans]

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 3.57e-137

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: 389.47  E-value: 3.57e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  21 KINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMSTN 100
Cdd:COG1250   1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250  76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 181 HTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17549919 261 GLDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 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 3.57e-137

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: 389.47  E-value: 3.57e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  21 KINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMSTN 100
Cdd:COG1250   1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250  76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 181 HTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17549919 261 GLDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:COG1250 235 GLDTALAVLEVLYEALGDP-RYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 19-308 2.72e-112

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 326.69  E-value: 2.72e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   19 LSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMS 98
Cdd:PLN02545   1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATL-----GRIRCT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   99 TNVsDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEV 178
Cdd:PLN02545  76 TNL-EELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  179 VRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSD 258
Cdd:PLN02545 155 IRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLAD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 17549919  259 YVGLDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PLN02545 235 FIGLDTCLSIMKVLHEGLGDS-KYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 24-209 1.50e-79

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 239.36  E-value: 1.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919    24 NVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQtalvsSVLDRIKMSTNVSD 103
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-----AALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   104 SVkDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRHTE 183
Cdd:pfam02737  76 AV-DADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 17549919   184 TSDATFNQLVDYGKTVGKTTVACKDT 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 3.08e-51

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: 180.03  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919    22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKhaddaaAQTALV-SSVLDRIKMSTN 100
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRK------KITSLErDSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVR 180
Cdd:TIGR02441 409 YSG-FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   181 HTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMEDIDvAMKLGAGYPMGPFELSDYV 260
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEG-VDPKKLD-KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 17549919   261 GLDTCKFIMDGWHAQYPEEVAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-115 2.95e-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: 47.70  E-value: 2.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   7 TAAVRGLSTTAQLSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKaqqgianslkrvAKKKHADDAAaqTA 86
Cdd:cd05188 120 ATAYHALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLEL------------AKELGADHVI--DY 185

                        90       100
                ....*....|....*....|....*....
gi 17549919  87 LVSSVLDRIKMSTnvsdsVKDADLVIEAI 115
Cdd:cd05188 186 KEEDLEEELRLTG-----GGGADVVIDAV 209
 
Name Accession Description Interval E-value
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 21-308 3.57e-137

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: 389.47  E-value: 3.57e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  21 KINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMSTN 100
Cdd:COG1250   1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAAL-----ARITPTTD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVR 180
Cdd:COG1250  76 LAA-LADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919 181 HTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:COG1250 155 GPATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLV 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17549919 261 GLDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:COG1250 235 GLDTALAVLEVLYEALGDP-RYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 19-308 2.72e-112

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 326.69  E-value: 2.72e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   19 LSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMS 98
Cdd:PLN02545   1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATL-----GRIRCT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   99 TNVsDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEV 178
Cdd:PLN02545  76 TNL-EELRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  179 VRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSD 258
Cdd:PLN02545 155 IRGADTSDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLAD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 17549919  259 YVGLDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PLN02545 235 FIGLDTCLSIMKVLHEGLGDS-KYRPCPLLVQYVDAGRLGRKSGRGVYHY 283
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 16-308 8.56e-103

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 309.85  E-value: 8.56e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   16 TAQLSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRI 95
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAAL-----ARL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   96 KMSTNVSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKL 175
Cdd:PRK08268  76 RPVEALAD-LADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  176 LEVVRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFE 255
Cdd:PRK08268 155 VEVVSGLATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFE 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17549919  256 LSDYVGLDTCKFIMDGWHAQYPEEVAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK08268 235 LMDLIGLDVNHAVMESVYRQFYQEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 22-308 9.54e-100

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 294.56  E-value: 9.54e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMSTNV 101
Cdd:PRK05808   3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAAL-----ARITGTTDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  102 SDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK05808  78 DD-LKDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  182 TETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYVG 261
Cdd:PRK05808 157 LATSDATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17549919  262 LDTCKFIMDGWHAQYPEEvAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK05808 237 LDTCLAIMEVLYEGFGDS-KYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 20-308 6.75e-95

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 282.26  E-value: 6.75e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   20 SKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKR-VAKKKHADDAAAQTalvssvLDRIKMS 98
Cdd:PRK07819   3 DAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERaVSRGKLTERERDAA------LARLRFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   99 TNVSDsVKDADLVIEAIVENIDIKRKLFAEV-EVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLE 177
Cdd:PRK07819  77 TDLGD-FADRQLVIEAVVEDEAVKTEIFAELdKVVTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  178 VVRHTETSDATFNQLVDYGKTV-GKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFEL 256
Cdd:PRK07819 156 LVPTLVTSEATVARAEEFASDVlGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17549919  257 SDYVGLDTCKFIMDGWHAQYPEEVaFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK07819 236 SDLVGLDTVKAIADSMYEEFKEPL-YAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 20-309 4.20e-94

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 280.36  E-value: 4.20e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   20 SKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKR-VAKKKHADDAAAQTalvssvLDRIKMS 98
Cdd:PRK07530   2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARqVAKGKISEEARAAA------LARISTA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   99 TNVSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEV 178
Cdd:PRK07530  76 TDLED-LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  179 VRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEAL-RLYErGDASMEDIDVAMKLGAGYPMGPFELS 257
Cdd:PRK07530 155 IRGIATDEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIyTLYE-GVGSVEAIDTAMKLGANHPMGPLELA 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17549919  258 DYVGLDTCKFIMDGWHaqypEEVA---FTPSPLLNSLVDSGKNGRKSGEGFYKYK 309
Cdd:PRK07530 234 DFIGLDTCLSIMQVLH----DGLAdskYRPCPLLVKYVEAGWLGRKTGRGFYDYR 284
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
22-308 6.73e-81

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 246.63  E-value: 6.73e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTALvssvlDRIKMSTNV 101
Cdd:PRK09260   1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAAL-----ARLSYSLDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  102 SDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK09260  76 KAAVADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  182 TETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYVG 261
Cdd:PRK09260 156 LETSDETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 17549919  262 LDTCKFIMDGWHAQYPEEvaFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK09260 236 LDTRLNNLKYLHETLGEK--YRPAPLLEKYVKAGRLGRKTGRGVYDY 280
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 24-209 1.50e-79

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 239.36  E-value: 1.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919    24 NVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQtalvsSVLDRIKMSTNVSD 103
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVD-----AALARISFTTDLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   104 SVkDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRHTE 183
Cdd:pfam02737  76 AV-DADLVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEK 154

                         170       180
                  ....*....|....*....|....*.
gi 17549919   184 TSDATFNQLVDYGKTVGKTTVACKDT 209
Cdd:pfam02737 155 TSPETVATTVELAKKIGKTPVVVKDT 180
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 22-300 1.70e-72

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 225.52  E-value: 1.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANS---LKRVAKKKHADDAAAQtalvsSVLDRIKMS 98
Cdd:PRK06035   3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAK-----AIMARIRTS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   99 TNVSdSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEV 178
Cdd:PRK06035  78 TSYE-SLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  179 VRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSD 258
Cdd:PRK06035 157 VRAALTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMD 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 17549919  259 YVGLDTCKFImdgwhAQY----PEEVAFTPSPLLNSLVDSGKNGRK 300
Cdd:PRK06035 237 IIGIDTVYHI-----AEYlyeeTGDPQFIPPNSLKQMVLNGYVGDK 277
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
22-309 1.79e-72

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 225.20  E-value: 1.79e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIAnslkRVAKKKHADDAAAQTALVSSVLDRIKMSTNV 101
Cdd:PRK08293   3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIA----KLADRYVRDLEATKEAPAEAALNRITLTTDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  102 SDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK08293  79 AEAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  182 TETSDATFNQLVDYGKTVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYV 260
Cdd:PRK08293 159 PGTDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 17549919  261 GLDTCKFIMDGWHAQYPEEVAFTPSPLLNSLVDSGKNGRKSGEGFYKYK 309
Cdd:PRK08293 239 GLDTAYNITSNWAEATDDENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 22-308 6.97e-67

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 211.55  E-value: 6.97e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAqtalvssvldRIKMSTNV 101
Cdd:PRK06130   4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGMG----------RIRMEAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  102 SDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK06130  74 AAAVSGADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  182 TETSDATFNQLVDYGKTVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPM---GPFELS 257
Cdd:PRK06130 154 DKTSPQTVATTMALLRSIGKRPVLVkKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQR 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17549919  258 DYVGLDTCKFIMDGWHAQYPEEVafTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK06130 234 DMNGLDVHLAVASYLYQDLENRT--TPSPLLEEKVEAGELGAKSGQGFYAW 282
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
9-309 1.32e-66

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 221.27  E-value: 1.32e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919    9 AVRGLS--TTAQLSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEkaqQGI--ANSL--KRVAKKKHADDAA 82
Cdd:PRK11730 298 YVKGKAkkLAKDAKPVKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALD---LGMteAAKLlnKQVERGKIDGAKM 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   83 AQtalvssVLDRIKMSTNVSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFG 162
Cdd:PRK11730 375 AG------VLSSIRPTLDYAG-FERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFC 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  163 GLHFFNPVPMMKLLEVVRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMEDIDVA 242
Cdd:PRK11730 448 GMHFFNPVHRMPLVEVIRGEKTSDETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDG-ADFRQIDKV 526

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17549919  243 MKLGAGYPMGPFELSDYVGLDTckfimdGWHAQ------YPEEVAFTPSPLLNSLVDSGKNGRKSGEGFYKYK 309
Cdd:PRK11730 527 MEKQFGWPMGPAYLLDVVGIDT------AHHAQavmaegFPDRMKKDYRDAIDVLFEAKRFGQKNGKGFYRYE 593
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
15-309 6.32e-63

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 211.29  E-value: 6.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   15 TTAQLSKINNVTIIGAGLMGSGIAQVSA-NAKLNVTVVDSNQsalekaqQGIANSL--------KRVaKKKH--ADDAAA 83
Cdd:PRK11154 302 SDAKPRPVNKVGVLGGGLMGGGIAYVTAtKAGLPVRIKDINP-------QGINHALkyswdlldKKV-KRRHlkPSERDK 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   84 QTALVSSVLDrikmstnvSDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGG 163
Cdd:PRK11154 374 QMALISGTTD--------YRGFKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIG 445

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  164 LHFFNPVPMMKLLEVVRHTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMEDIDVAM 243
Cdd:PRK11154 446 LHYFSPVEKMPLVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAAL 524

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17549919  244 kLGAGYPMGPFELSDYVGLDTCKFIMDGWHAQYPEEvaFTPSPLLNSLVDSGKNGRKSGEGFYKYK 309
Cdd:PRK11154 525 -VKFGFPVGPITLLDEVGIDVGTKIIPILEAALGER--FSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 22-308 3.08e-51

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: 180.03  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919    22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKhaddaaAQTALV-SSVLDRIKMSTN 100
Cdd:TIGR02441 335 VKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRK------KITSLErDSILSNLTPTLD 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   101 VSDsVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVR 180
Cdd:TIGR02441 409 YSG-FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   181 HTETSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGdASMEDIDvAMKLGAGYPMGPFELSDYV 260
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEG-VDPKKLD-KLTTKFGFPVGAATLADEV 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 17549919   261 GLDTCKFIMDGWHAQYPEEVAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:TIGR02441 566 GVDVAEHVAEDLGKAFGERFGGGSAELLSELVKAGFLGRKSGKGIFIY 613
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 211-308 9.75e-50

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: 160.46  E-value: 9.75e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   211 GFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYVGLDTCKFIMDGWHAQYPEEvAFTPSPLLNS 290
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDR-AYRPPPLLEK 79

                          90
                  ....*....|....*...
gi 17549919   291 LVDSGKNGRKSGEGFYKY 308
Cdd:pfam00725  80 LVEAGRLGRKTGKGFYKY 97
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 33-308 3.53e-39

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 139.81  E-value: 3.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   33 MGSGIAQVSANAKLNVTVVDSNQSALEKAQQgiansLKRVAKKKHADDAAAQTAL-------VSSVLDRIKMST--NVSD 103
Cdd:PRK08269   1 MGQGIALAFAFAGHDVTLIDFKPRDAAGWRA-----LDAEARAEIERTLAALVALgridaaqADAVLARIAVVArdGAAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  104 SVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRHTE 183
Cdd:PRK08269  76 ALADADLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  184 TSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYP---MGPFELSDYV 260
Cdd:PRK08269 156 TDPAVVDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRfavLGLLEFIDWG 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17549919  261 GLDTCkfimdgWHA-QYPE----EVAFTPSPLLNSLVDSGKNGRKSGEGFYKY 308
Cdd:PRK08269 236 GCDIL------YYAsRYLAgeigPDRFAPPAIVVRNMEEGRDGLRTGAGFYDY 282
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 22-258 3.40e-38

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 137.10  E-value: 3.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   22 INNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAAQTalvssVLDRIKMSTNV 101
Cdd:PRK06129   2 MGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDA-----VLARIRVTDSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  102 SDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLEVVRH 181
Cdd:PRK06129  77 ADAVADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  182 TETSDATFNQLVDYGKTVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYP---MGPFELS 257
Cdd:PRK06129 157 PWTAPATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRwsfMGPFETI 236


                 .
gi 17549919  258 D 258
Cdd:PRK06129 237 D 237
PRK07066 PRK07066
L-carnitine dehydrogenase;
19-254 1.98e-24

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 100.68  E-value: 1.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   19 LSKINNVTIIGAGLMGSG-IAQVSANAkLNVTVVDSNQSALEKAQQGIANSLKRVAKKKHADDAAaqtalvssvLDRIKM 97
Cdd:PRK07066   4 ITDIKTFAAIGSGVIGSGwVARALAHG-LDVVAWDPAPGAEAALRANVANAWPALERQGLAPGAS---------PARLRF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   98 STNVSDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKLLE 177
Cdd:PRK07066  74 VATIEACVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  178 VVRHTETSDATFNQLVDYGKTVGKTTVAC-KDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYP---MGP 253
Cdd:PRK07066 154 VLGGERTAPEAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRwsfMGT 233


                 .
gi 17549919  254 F 254
Cdd:PRK07066 234 F 234
PRK07531 PRK07531
carnitine 3-dehydrogenase;
19-255 4.59e-24

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 101.74  E-value: 4.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   19 LSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLKrvakkkhaddaaAQTALVSSVL---DRI 95
Cdd:PRK07531   1 MTMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAER------------AYAMLTDAPLppeGRL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   96 KMSTNVSDSVKDADLVIEAIVENIDIKRKLFAEVEVAAKPTTLITTNTSSLRLADIGLNLKDKSRFGGLHFFNPVPMMKL 175
Cdd:PRK07531  69 TFCASLAEAVAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  176 LEVVRHTETSDATFNQLVDYGKTVG-KTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGY---PM 251
Cdd:PRK07531 149 VELVGGGKTSPETIRRAKEILREIGmKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLrwaQM 228


                 ....
gi 17549919  252 GPFE 255
Cdd:PRK07531 229 GLFE 232
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 184-288 3.56e-12

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 66.41  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  184 TSDATFNQLVDYGKTVGKTTVACKDTPGFIVNRLLVPYMFEALRLYERGDASMEDIDVAMKLGAGYPMGPFELSDYVGLD 263
Cdd:PRK08268 389 TSPAARDAAHALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLAWGDRLGAA 468

                         90       100
                 ....*....|....*....|....*
gi 17549919  264 TCKFIMDGWHAQYPEEvAFTPSPLL 288
Cdd:PRK08268 469 RILRVLENLQALYGDP-RYRPSPWL 492
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 22-140 1.89e-06

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: 48.20  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  22 INNVTIIGAGLMGSGIAQV--SANAKLNVTVVDSNQSALEKAQQ-GIAnslkrvakkkhaddaaaqtalvssvlDRIkmS 98
Cdd:COG0287   1 FMRIAIIGLGLIGGSLALAlkRAGLAHEVVGVDRSPETLERALElGVI--------------------------DRA--A 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17549919  99 TNVSDSVKDADLVI-----EAIVEnidikrkLFAEVEVAAKPTTLIT 140
Cdd:COG0287  53 TDLEEAVADADLVVlavpvGATIE-------VLAELAPHLKPGAIVT 92
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-115 2.95e-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: 47.70  E-value: 2.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919   7 TAAVRGLSTTAQLSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKaqqgianslkrvAKKKHADDAAaqTA 86
Cdd:cd05188 120 ATAYHALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLEL------------AKELGADHVI--DY 185

                        90       100
                ....*....|....*....|....*....
gi 17549919  87 LVSSVLDRIKMSTnvsdsVKDADLVIEAI 115
Cdd:cd05188 186 KEEDLEEELRLTG-----GGGADVVIDAV 209
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 24-115 2.71e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 38.93  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17549919  24 NVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQGIANSLkrvakkkhaddaaaqTALVSSvldrikmSTNVSD 103
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRV---------------TTLYSN-------PANLEE 227

                        90
                ....*....|..
gi 17549919 104 SVKDADLVIEAI 115
Cdd:cd05305 228 ALKEADLVIGAV 239
trkA PRK09496
Trk system potassium transporter TrkA;
24-62 3.00e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 38.95  E-value: 3.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 17549919   24 NVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQ 62
Cdd:PRK09496   2 KIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQ 40
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
17-58 4.26e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 38.36  E-value: 4.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 17549919   17 AQLSKINNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSAL 58
Cdd:PRK04965 136 TQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLL 177
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 23-63 4.96e-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: 38.12  E-value: 4.96e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17549919  23 NNVTIIGAGLMGSGIAQVSANAKLNVTVVDSNQSALEKAQQ 63
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAE 136
 
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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