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Conserved domains on  [gi|2415034201|ref|WP_268989223|]
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3-hydroxybutyryl-CoA dehydrogenase [Cupriavidus necator]

Protein Classification

3-hydroxybutyryl-CoA dehydrogenase( domain architecture ID 11481671)

3-hydroxybutyryl-CoA dehydrogenase (BHBD) catalyzes the NAD-dependent oxidation of beta-hydroxybutyryl-CoA to acetoacetyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-287 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


:

Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 547.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDM 85
Cdd:PRK05808    1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTS 165
Cdd:PRK05808   81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 166 DATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTM 245
Cdd:PRK05808  161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 246 LAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK05808  241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
 
Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-287 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 547.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDM 85
Cdd:PRK05808    1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTS 165
Cdd:PRK05808   81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 166 DATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTM 245
Cdd:PRK05808  161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 246 LAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK05808  241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 7-287 1.39e-152

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: 427.60  E-value: 1.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   7 AIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMK 86
Cdd:COG1250     1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:COG1250    81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 167 ATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTML 246
Cdd:COG1250   161 ETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2415034201 247 AVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:COG1250   241 AVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 10-187 7.24e-81

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 242.06  E-value: 7.24e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  10 TVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMKAAD 89
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  90 IVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDATH 169
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*...
gi 2415034201 170 AAVEALSKQLGKCPITVK 187
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVK 178
PaaC-3OHAcCoADH TIGR02279
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the ...
 10-287 1.27e-72

3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families.


Pssm-ID: 188207 [Multi-domain]  Cd Length: 503  Bit Score: 231.37  E-value: 1.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  10 TVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMKAAD 89
Cdd:TIGR02279   7 TVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLHALADAG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  90 IVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDATH 169
Cdd:TIGR02279  87 LVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLATAAEVA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 170 AAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTMLAVM 249
Cdd:TIGR02279 167 EQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHDVNFAVT 246

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2415034201 250 -EVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:TIGR02279 247 cSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDY 285
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 9-159 1.22e-03

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: 39.61  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   9 KTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAgslDRLIkkekltEAQKADALARIQGSTTyhdmKAA 88
Cdd:cd05188   136 DTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGA---DHVI------DYKEEDLEEELRLTGG----GGA 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2415034201  89 DIVIEAA--TENYDLKVKILKQIdgivGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELI 159
Cdd:cd05188   203 DVVIDAVggPETLAQALRLLRPG----GRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
 
Name Accession Description Interval E-value
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-287 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 547.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDM 85
Cdd:PRK05808    1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTDLDDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTS 165
Cdd:PRK05808   81 KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 166 DATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTM 245
Cdd:PRK05808  161 DATHEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGCNHPIGPLALADLIGLDTC 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 246 LAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK05808  241 LAIMEVLYEGFGDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 7-287 1.39e-152

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: 427.60  E-value: 1.39e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   7 AIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMK 86
Cdd:COG1250     1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:COG1250    81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 167 ATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTML 246
Cdd:COG1250   161 ETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPMGPFELADLVGLDTAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2415034201 247 AVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:COG1250   241 AVLEVLYEALGDPRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-287 3.06e-136

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 386.67  E-value: 3.06e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDM 85
Cdd:PRK07530    2 MAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAKGKISEEARAAALARISTATDLEDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTS 165
Cdd:PRK07530   82 ADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIATD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 166 DATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTM 245
Cdd:PRK07530  162 EATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGANHPMGPLELADFIGLDTC 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 246 LAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK07530  242 LSIMQVLHDGLADSKYRPCPLLVKYVEAGWLGRKTGRGFYDY 283
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 8-289 3.34e-128

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 366.36  E-value: 3.34e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   8 IKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMKA 87
Cdd:PLN02545    4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATLGRIRCTTNLEELRD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  88 ADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDA 167
Cdd:PLN02545   84 ADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 168 THAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTMLA 247
Cdd:PLN02545  164 VFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTNHPMGPLHLADFIGLDTCLS 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 248 VMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGYNQ 289
Cdd:PLN02545  244 IMKVLHEGLGDSKYRPCPLLVQYVDAGRLGRKSGRGVYHYDG 285
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-287 2.99e-109

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 318.08  E-value: 2.99e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDM 85
Cdd:PRK07819    3 DAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRFTTDLGDF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGE-NVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQT 164
Cdd:PRK07819   83 ADRQLVIEAVVEDEAVKTEIFAELDKVVTDpDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTLVT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 165 SDATHAAVEAL-SKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLD 243
Cdd:PRK07819  163 SEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPMGPLRLSDLVGLD 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2415034201 244 TMLAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK07819  243 TVKAIADSMYEEFKEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 3-287 7.86e-108

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 322.18  E-value: 7.86e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   3 SREMAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTY 82
Cdd:PRK08268    2 MALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRPVEAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  83 HDMKAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGL 162
Cdd:PRK08268   82 ADLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 163 QTSDATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGL 242
Cdd:PRK08268  162 ATDPAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRMGPFELMDLIGL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2415034201 243 DTMLAVMEVLYSEF-ADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK08268  242 DVNHAVMESVYRQFyQEPRFRPSLIQQELVAAGRLGRKSGQGFYRY 287
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
8-287 1.09e-97

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 288.61  E-value: 1.09e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   8 IKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHD-MK 86
Cdd:PRK09260    1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGKLTEAARQAALARLSYSLDLKAaVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:PRK09260   81 DADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 167 ATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTML 246
Cdd:PRK09260  161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLGLNFPMGPLELGDLVGLDTRL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2415034201 247 AVMEVLYSEFADpKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK09260  241 NNLKYLHETLGE-KYRPAPLLEKYVKAGRLGRKTGRGVYDY 280
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 10-187 7.24e-81

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 242.06  E-value: 7.24e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  10 TVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMKAAD 89
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  90 IVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDATH 169
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*...
gi 2415034201 170 AAVEALSKQLGKCPITVK 187
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVK 178
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 6-279 8.24e-80

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 243.24  E-value: 8.24e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGS---LDRLIKKEKLTEAQKADALARIQGSTTY 82
Cdd:PRK06035    1 MDIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESGpygLRNLVEKGKMSEDEAKAIMARIRTSTSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  83 HDMKAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGL 162
Cdd:PRK06035   81 ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 163 QTSDATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGL 242
Cdd:PRK06035  161 LTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPMGPFELMDIIGI 240

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2415034201 243 DTMLAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRK 279
Cdd:PRK06035  241 DTVYHIAEYLYEETGDPQFIPPNSLKQMVLNGYVGDK 277
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
7-287 2.60e-74

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 240.92  E-value: 2.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   7 AIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMK 86
Cdd:PRK11730  312 PVKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALDLGMTEAAKLLNKQVERGKIDGAKMAGVLSSIRPTLDYAGFE 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:PRK11730  392 RVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSD 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 167 ATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINeAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTML 246
Cdd:PRK11730  472 ETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFA-GFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAH 550

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2415034201 247 AVMEVLYSEFAD---PKYRPAMLLreMVAAGYLGRKTGRGVYGY 287
Cdd:PRK11730  551 HAQAVMAEGFPDrmkKDYRDAIDV--LFEAKRFGQKNGKGFYRY 592
PaaC-3OHAcCoADH TIGR02279
3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the ...
 10-287 1.27e-72

3-hydroxyacyl-CoA dehydrogenase PaaC; This 3-hydroxyacyl-CoA dehydrogenase is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring. The sequences included in this model are all found in aparrent operons with other related genes such as paaA, paaB, paaD, paaE, paaF and paaN. Some genomes contain these other genes without an apparent paaC in the same operon - possibly in these cases a different dehydrogenase involved in fatty acid degradation may fill in the needed activity. This enzyme has domains which are members of the pfam02737 and pfam00725 families.


Pssm-ID: 188207 [Multi-domain]  Cd Length: 503  Bit Score: 231.37  E-value: 1.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  10 TVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMKAAD 89
Cdd:TIGR02279   7 TVAVIGAGAMGAGIAQVAASAGHQVLLYDIRAEALARAIAGIEARLNSLVTKGKLTAEECERTLKRLIPVTDLHALADAG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  90 IVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDATH 169
Cdd:TIGR02279  87 LVIEAIVENLEVKKALFAQLEELCPADTIIASNTSSLSITAIAAGLARPERVAGLHFFNPAPVMALVEVVSGLATAAEVA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 170 AAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTMLAVM 249
Cdd:TIGR02279 167 EQLYETALAWGKQPVHCHSTPGFIVNRVARPYYAEALRALEEQVAAPAVLDAALRDGAGFPMGPFELTDLIGHDVNFAVT 246

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2415034201 250 -EVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:TIGR02279 247 cSVFNAFWQDRRFLPSLVQQELVIAGRLGRKSGLGVYDY 285
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 8-287 1.22e-68

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 215.41  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   8 IKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAvqkgLATVAGSLDRLIKKEklteAQKADALARIQGSTTYHDMKA 87
Cdd:PRK06130    4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGA----LERARGVIERALGVY----APLGIASAGMGRIRMEAGLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  88 A----DIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQ 163
Cdd:PRK06130   76 AvsgaDLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 164 TSDATHAAVEALSKQLGKCPITVKSS-PGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPI---GPLALADM 239
Cdd:PRK06130  156 TSPQTVATTMALLRSIGKRPVLVKKDiPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDM 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2415034201 240 IGLDTMLAVMEVLYSEFADpKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK06130  236 NGLDVHLAVASYLYQDLEN-RTTPSPLLEEKVEAGELGAKSGQGFYAW 282
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 5-289 4.42e-68

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: 224.72  E-value: 4.42e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   5 EMAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHD 84
Cdd:TIGR02441 332 QRPVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDYSG 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  85 MKAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQT 164
Cdd:TIGR02441 412 FKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGT 491

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 165 SDATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLaSPEEIDE-GMKLGcnHPIGPLALADMIGLD 243
Cdd:TIGR02441 492 SKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGV-DPKKLDKlTTKFG--FPVGAATLADEVGVD 568

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2415034201 244 TMLAVMEVLYSEFAdPKYR--PAMLLREMVAAGYLGRKTGRGVYGYNQ 289
Cdd:TIGR02441 569 VAEHVAEDLGKAFG-ERFGggSAELLSELVKAGFLGRKSGKGIFIYQE 615
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
7-288 1.98e-65

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 217.07  E-value: 1.98e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   7 AIKTVGIVGAGTMGNGI--VQACAVvGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHD 84
Cdd:PRK11154  308 PVNKVGVLGGGLMGGGIayVTATKA-GLPVRIKDINPQGINHALKYSWDLLDKKVKRRHLKPSERDKQMALISGTTDYRG 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  85 MKAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQT 164
Cdd:PRK11154  387 FKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKT 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 165 SDATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGlASPEEIDEGM-KLGcnHPIGPLALADMIGLD 243
Cdd:PRK11154  467 SAETIATTVALAKKQGKTPIVVRDGAGFYVNRILAPYINEAARLLLEG-EPIEHIDAALvKFG--FPVGPITLLDEVGID 543

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2415034201 244 TMLAVMEVLYSEFADpKYRPAMLLREMVAAGYLGRKTGRGVYGYN 288
Cdd:PRK11154  544 VGTKIIPILEAALGE-RFSAPAAFDKLLNDDRKGRKNGRGFYLYG 587
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
6-287 1.15e-58

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 189.00  E-value: 1.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   6 MAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKAD-ALARIQGSTTYHD 84
Cdd:PRK08293    1 MDIKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKEAPAEaALNRITLTTDLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  85 -MKAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQ 163
Cdd:PRK08293   81 aVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 164 TSDATHAAVEALSKQLGKCPITV-KSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGL 242
Cdd:PRK08293  161 TDPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATGAPMGPFGILDIVGL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2415034201 243 DTMLAVMEVlYSEFADPKYRP--AMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK08293  241 DTAYNITSN-WAEATDDENAKkaAALLKEYIDKGKLGVATGEGFYNY 286
FadB TIGR02437
fatty oxidation complex, alpha subunit FadB; Members represent alpha subunit of ...
 7-287 3.44e-58

fatty oxidation complex, alpha subunit FadB; Members represent alpha subunit of multifunctional enzyme complex of the fatty acid degradation cycle. Activities include: enoyl-CoA hydratase (EC 4.2.1.17), dodecenoyl-CoA delta-isomerase activity (EC 5.3.3.8), 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3). A representative is E. coli FadB (SP:P21177). This model excludes the FadJ family represented by SP:P77399. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 131490 [Multi-domain]  Cd Length: 714  Bit Score: 197.74  E-value: 3.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   7 AIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHDMK 86
Cdd:TIGR02437 312 DVKQAAVLGAGIMGGGIAYQSASKGTPIVMKDINQHSLDLGLTEAAKLLNKQVERGRITPAKMAGVLNGITPTLSYAGFD 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:TIGR02437 392 NVDIVVEAVVENPKVKAAVLAEVEQHVREDAILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKSSD 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 167 ATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGlASPEEIDEGMKLGCNHPIGPLALADMIGLDT-- 244
Cdd:TIGR02437 472 ETIATVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFGGFSKLLRDG-ADFVRIDKVMEKQFGWPMGPAYLLDVVGIDTgh 550

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2415034201 245 -MLAVMEVLYSEFADPKYRPAmlLREMVAAGYLGRKTGRGVYGY 287
Cdd:TIGR02437 551 hAQAVMAEGFPDRMGKDGRDA--IDALFEAKRLGQKNGKGFYAY 592
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 19-287 2.59e-46

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 157.91  E-value: 2.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  19 MGNGIVQACAVVGLNVVMVDI---SDAAVQ----KGLATVAGSLDRLIKKEKLTEAQKADALARIQ---GSTTYHDMKAA 88
Cdd:PRK08269    1 MGQGIALAFAFAGHDVTLIDFkprDAAGWRaldaEARAEIERTLAALVALGRIDAAQADAVLARIAvvaRDGAADALADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  89 DIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSDAT 168
Cdd:PRK08269   81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 169 HAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMI---GLDTM 245
Cdd:PRK08269  161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLGLLEFIdwgGCDIL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2415034201 246 LAVMEVLYSEFADPKYRPAMLLREMVAAGYLGRKTGRGVYGY 287
Cdd:PRK08269  241 YYASRYLAGEIGPDRFAPPAIVVRNMEEGRDGLRTGAGFYDY 282
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 191-287 7.68e-43

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: 141.97  E-value: 7.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 191 GFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLALADMIGLDTMLAVMEVLYSEFADPKYRPAMLLREM 270
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFGDRAYRPPPLLEKL 80

                          90
                  ....*....|....*..
gi 2415034201 271 VAAGYLGRKTGRGVYGY 287
Cdd:pfam00725  81 VEAGRLGRKTGKGFYKY 97
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 11-226 1.02e-34

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 127.47  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  11 VGIVGAGTMGngivQACAVV----GLNVVMVDISDAAVQKGLATVAGSLDRLIKKEKLTEAQKADALARIQGSTTYHD-M 85
Cdd:PRK06129    5 VAIIGAGLIG----RAWAIVfaraGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEAPDAVLARIRVTDSLADaV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  86 KAADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTS 165
Cdd:PRK06129   81 ADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2415034201 166 DATHAAVEALSKQLGKCPITV-KSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLG 226
Cdd:PRK06129  161 PATLARAEALYRAAGQSPVRLrREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDG 222
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 156-274 1.48e-25

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 105.31  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 156 VELIRGLQTSDATHAAVEALSKQLGKCPITVKSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLGCNHPIGPLA 235
Cdd:PRK08268  381 RTLMAAPATSPAARDAAHALFQQDGKAVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPLGPLA 460

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2415034201 236 LADMIGLDTMLAVMEVLYSEFADPKYRPAMLLREMVAAG 274
Cdd:PRK08268  461 WGDRLGAARILRVLENLQALYGDPRYRPSPWLRRRAALG 499
PRK07066 PRK07066
L-carnitine dehydrogenase;
8-226 1.48e-24

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 100.68  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   8 IKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAGSLDRLikkEKLTEAQKADaLARIQGSTTYHD-MK 86
Cdd:PRK07066    7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPAL---ERQGLAPGAS-PARLRFVATIEAcVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  87 AADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELIRGLQTSD 166
Cdd:PRK07066   83 DADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERTAP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2415034201 167 ATHAAVEALSKQLGKCPITV-KSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLG 226
Cdd:PRK07066  163 EAVDAAMGIYRALGMRPLHVrKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFG 223
PRK07531 PRK07531
carnitine 3-dehydrogenase;
8-226 7.87e-18

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 83.25  E-value: 7.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   8 IKTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAvqkglatvagslDRLIKkEKLTEAQKA-----DALARIQGSTTY 82
Cdd:PRK07531    4 IMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEA------------ERIIG-EVLANAERAyamltDAPLPPEGRLTF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201  83 HDMKA-----ADIVIEAATENYDLKVKILKQIDGIVGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVE 157
Cdd:PRK07531   71 CASLAeavagADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201 158 LIRGLQTSDATHAAVEALSKQLGKCPITV-KSSPGFVVNRILCPMINEAFCVLGEGLASPEEIDEGMKLG 226
Cdd:PRK07531  151 LVGGGKTSPETIRRAKEILREIGMKPVHIaKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYS 220
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 9-92 2.71e-04

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 41.65  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   9 KTVGIVGAGTMGNGIVQACAVVGL-NVVMVDISDAAVQkGLAtvagsLDrlikkekLTEAQKADAL-ARIQGSTTYHDMK 86
Cdd:PRK06223    3 KKISIIGAGNVGATLAHLLALKELgDVVLFDIVEGVPQ-GKA-----LD-------IAEAAPVEGFdTKITGTNDYEDIA 69


                  ....*.
gi 2415034201  87 AADIVI 92
Cdd:PRK06223   70 GSDVVV 75
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 9-95 4.16e-04

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 41.25  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   9 KTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGL---ATVAGSldrlikkeklteAQKADALARIQGSTTyhdm 85
Cdd:COG1064   164 DRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARelgADHVVN------------SSDEDPVEAVRELTG---- 227

                          90
                  ....*....|
gi 2415034201  86 kaADIVIEAA 95
Cdd:COG1064   228 --ADVVIDTV 235
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 1-61 4.82e-04

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 40.95  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2415034201   1 MRSREMAIKTVGIVGAGTMGNGIVQACAVVGLNVVMVDIS--DAAVQKGLATVAGSLDRLIKK 61
Cdd:COG0111   133 FRGRELRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPSpkPEEAADLGVGLVDSLDELLAE 195
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 9-159 1.22e-03

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: 39.61  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   9 KTVGIVGAGTMGNGIVQACAVVGLNVVMVDISDAAVQKGLATVAgslDRLIkkekltEAQKADALARIQGSTTyhdmKAA 88
Cdd:cd05188   136 DTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGA---DHVI------DYKEEDLEEELRLTGG----GGA 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2415034201  89 DIVIEAA--TENYDLKVKILKQIdgivGENVIIASNTSSISITKLAAVTSRADRFIGMHFFNPVPVMALVELI 159
Cdd:cd05188   203 DVVIDAVggPETLAQALRLLRPG----GRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 9-105 3.03e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and 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. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 38.51  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2415034201   9 KTVGIVGAGTMGNGIVQACAVVGLN-VVMVDISDAAVQKglATVAGSLDrlikkekLTEAQKADALARIQGSTtyhDMKA 87
Cdd:cd08263   189 ETVAVIGVGGVGSSAIQLAKAFGASpIIAVDVRDEKLAK--AKELGATH-------TVNAAKEDAVAAIREIT---GGRG 256

                          90
                  ....*....|....*...
gi 2415034201  88 ADIVIEAATENYDLKVKI 105
Cdd:cd08263   257 VDVVVEALGKPETFKLAL 274
 
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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