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Conserved domains on  [gi|1478748801|gb|RIQ41261|]
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3-hydroxyacyl-CoA dehydrogenase family protein [Bordetella avium]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase family protein( domain architecture ID 11482062)

3-hydroxyacyl-CoA dehydrogenase family protein similar to Mesorhizobium japonicum 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid (FHMPC) 5-dehydrogenase, which is an NAD(+)-dependent dismutase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 2-310 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


:

Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 517.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   2 GFPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPNDVA-ACLARIRMEPGLQAAA-DC 79
Cdd:PRK06130    1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIAsAGMGRIRMEAGLAAAVsGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  80 DLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDAT 159
Cdd:PRK06130   81 DLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 160 ADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 239
Cdd:PRK06130  161 VATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 240 HLAIVDYLYADLENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERRERVLREKSAALAALVQWLNTQKLD 310
Cdd:PRK06130  241 HLAVASYLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPERREEVLADKSAALVEVRAWLESREPV 311
 
Name Accession Description Interval E-value
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 2-310 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 517.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   2 GFPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPNDVA-ACLARIRMEPGLQAAA-DC 79
Cdd:PRK06130    1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIAsAGMGRIRMEAGLAAAVsGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  80 DLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDAT 159
Cdd:PRK06130   81 DLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 160 ADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 239
Cdd:PRK06130  161 VATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 240 HLAIVDYLYADLENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERRERVLREKSAALAALVQWLNTQKLD 310
Cdd:PRK06130  241 HLAVASYLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPERREEVLADKSAALVEVRAWLESREPV 311
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 4-281 4.46e-127

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: 363.66  E-value: 4.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAA 77
Cdd:COG1250     1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLdklvkkGKLTEEEADAALARITPTTDLAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  78 DCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:COG1250    81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVRVNrDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMNGL 237
Cdd:COG1250   161 ETVATAVAFARRLGKTPVVVK-DTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPM---GPFELADLVGL 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1478748801 238 DVHLAIVDYLYADLEN-RVTPSDLLKRKVEAGELGAKTGQGFYDW 281
Cdd:COG1250   237 DTALAVLEVLYEALGDpRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 7-178 1.39e-76

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 231.66  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAADCD 80
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLerlvekGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  81 LVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDATA 160
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*...
gi 1478748801 161 DLAMAVLRAGGKRPVRVN 178
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVK 178
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-279 5.34e-41

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: 151.53  E-value: 5.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPNDVAACLARIRMEPGLQAAAD----- 78
Cdd:TIGR02441 334 PVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDysgfk 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  79 -CDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:TIGR02441 414 nADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSK 493

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVRVnRDIPGFIANRIQHALAREAMSLLEKGVASAeDIDEVVKwSLGIRLaltGPLEQRDMNGL 237
Cdd:TIGR02441 494 DTLASAVAVGLKQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLLQEGVDPK-KLDKLTT-KFGFPV---GAATLADEVGV 567

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1478748801 238 DVHLAIVDYLYADLENRVT--PSDLLKRKVEAGELGAKTGQGFY 279
Cdd:TIGR02441 568 DVAEHVAEDLGKAFGERFGggSAELLSELVKAGFLGRKSGKGIF 611
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 4-148 9.63e-05

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: 43.08  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAaaiieRQLGVYAPNDVAACLARIRMepGLQAAADCDLVI 83
Cdd:cd05188   134 PGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELA-----KELGADHVIDYKEEDLEEEL--RLTGGGGADVVI 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478748801  84 EAVPEKLDLkRQLFAQLDALCKPATVFATnTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVE 148
Cdd:cd05188   207 DAVGGPETL-AQALRLLRPGGRIVVVGGT-SGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALD 269
 
Name Accession Description Interval E-value
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 2-310 0e+00

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 517.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   2 GFPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPNDVA-ACLARIRMEPGLQAAA-DC 79
Cdd:PRK06130    1 MNPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIAsAGMGRIRMEAGLAAAVsGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  80 DLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDAT 159
Cdd:PRK06130   81 DLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 160 ADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 239
Cdd:PRK06130  161 VATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 240 HLAIVDYLYADLENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERRERVLREKSAALAALVQWLNTQKLD 310
Cdd:PRK06130  241 HLAVASYLYQDLENRTTPSPLLEEKVEAGELGAKSGQGFYAWPPERREEVLADKSAALVEVRAWLESREPV 311
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 4-281 4.46e-127

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: 363.66  E-value: 4.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAA 77
Cdd:COG1250     1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLdklvkkGKLTEEEADAALARITPTTDLAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  78 DCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:COG1250    81 DADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVRVNrDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMNGL 237
Cdd:COG1250   161 ETVATAVAFARRLGKTPVVVK-DTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFPM---GPFELADLVGL 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1478748801 238 DVHLAIVDYLYADLEN-RVTPSDLLKRKVEAGELGAKTGQGFYDW 281
Cdd:COG1250   237 DTALAVLEVLYEALGDpRYRPPPLLKKLVEAGRLGRKTGRGFYDY 281
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 5-281 6.57e-90

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 269.53  E-value: 6.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAAD 78
Cdd:PRK05808    3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLdrlvkkGKMTEADKEAALARITGTTDLDDLKD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  79 CDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDA 158
Cdd:PRK05808   83 ADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATSDA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 159 TADLAMAVLRAGGKRPVRVNrDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKwsLGIRLALtGPLEQRDMNGLD 238
Cdd:PRK05808  163 THEAVEALAKKIGKTPVEVK-NAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMK--LGCNHPI-GPLALADLIGLD 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1478748801 239 VHLAIVDYLYADL-ENRVTPSDLLKRKVEAGELGAKTGQGFYDW 281
Cdd:PRK05808  239 TCLAIMEVLYEGFgDSKYRPCPLLRKMVAAGWLGRKTGRGFYDY 282
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 1-287 1.36e-86

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 268.25  E-value: 1.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   1 MGFPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQ 74
Cdd:PRK08268    3 ALPSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLaklvekGKLTAEQADAALARLRPVEALA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  75 AAADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDE 154
Cdd:PRK08268   83 DLADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 155 TSDATADLAMAVLRAGGKRPVRVnRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDM 234
Cdd:PRK08268  163 TDPAVADALYALARAWGKTPVRA-KDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFRM---GPFELMDL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1478748801 235 NGLDVHLAIVDYLYADL--ENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERRE 287
Cdd:PRK08268  239 IGLDVNHAVMESVYRQFyqEPRFRPSLIQQELVAAGRLGRKSGQGFYRYADGAKQ 293
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 5-286 2.17e-86

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 260.82  E-value: 2.17e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAAD 78
Cdd:PLN02545    4 IKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLarlvkkGKMSQEEADATLGRIRCTTNLEELRD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  79 CDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDA 158
Cdd:PLN02545   84 ADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADTSDE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 159 TADLAMAVLRAGGKRPVrVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKwsLGIRLALtGPLEQRDMNGLD 238
Cdd:PLN02545  164 VFDATKALAERFGKTVV-CSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMK--LGTNHPM-GPLHLADFIGLD 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1478748801 239 VHLAIVDYLYADL-ENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERR 286
Cdd:PLN02545  240 TCLSIMKVLHEGLgDSKYRPCPLLVQYVDAGRLGRKSGRGVYHYDGKKR 288
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 7-178 1.39e-76

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 231.66  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAADCD 80
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLerlvekGRITEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  81 LVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDATA 160
Cdd:pfam02737  81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160

                         170
                  ....*....|....*...
gi 1478748801 161 DLAMAVLRAGGKRPVRVN 178
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVK 178
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
5-286 1.19e-75

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 233.53  E-value: 1.19e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIER------QLGVYAPNDVAACLARIRMEPGL-QAAA 77
Cdd:PRK09260    1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASifeqgvARGKLTEAARQAALARLSYSLDLkAAVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  78 DCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:PRK09260   81 DADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVRVNrDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKwsLGIRLALtGPLEQRDMNGL 237
Cdd:PRK09260  161 ETVQVAKEVAEQMGKETVVVN-EFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIR--LGLNFPM-GPLELGDLVGL 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1478748801 238 DVHLAIVDYLYADLENRVTPSDLLKRKVEAGELGAKTGQGFYDWPAERR 286
Cdd:PRK09260  237 DTRLNNLKYLHETLGEKYRPAPLLEKYVKAGRLGRKTGRGVYDYTNREN 285
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 4-284 4.34e-73

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 226.81  E-value: 4.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQAAA 77
Cdd:PRK07530    3 AIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLarqvakGKISEEARAAALARISTATDLEDLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  78 DCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:PRK07530   83 DCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIATDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVrVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKwsLGIRLALtGPLEQRDMNGL 237
Cdd:PRK07530  163 ATFEAAKEFVTKLGKTIT-VAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMK--LGANHPM-GPLELADFIGL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1478748801 238 DVHLAIVDYLY---ADLENRvtPSDLLKRKVEAGELGAKTGQGFYDWPAE 284
Cdd:PRK07530  239 DTCLSIMQVLHdglADSKYR--PCPLLVKYVEAGWLGRKTGRGFYDYRGE 286
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 5-280 2.43e-69

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 217.44  E-value: 2.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIE------RQL---GVYAPNDVAACLARIRMEPGLQA 75
Cdd:PRK06035    3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIEsgpyglRNLvekGKMSEDEAKAIMARIRTSTSYES 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  76 AADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDET 155
Cdd:PRK06035   83 LSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAALT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 156 SDATADLAMAVLRAGGKRPVRVNrDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMN 235
Cdd:PRK06035  163 SEETFNTTVELSKKIGKIPIEVA-DVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFPM---GPFELMDII 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 236 GLDVHLAIVDYLYADL-ENRVTPSDLLKRKVEAGELGAKTGQ-----GFYD 280
Cdd:PRK06035  239 GIDTVYHIAEYLYEETgDPQFIPPNSLKQMVLNGYVGDKKVKygskgGWFD 289
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 4-297 1.34e-62

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 200.65  E-value: 1.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPND------VAACLARIRMEPGL-QAA 76
Cdd:PRK06129    1 PMGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDlldgeaPDAVLARIRVTDSLaDAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  77 ADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETS 156
Cdd:PRK06129   81 ADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 157 DATADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMN- 235
Cdd:PRK06129  161 PATLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDLNa 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478748801 236 --GLDVHLAIVDYLYADlenrvtpsdllkrkveageLGAKTGQGFyDWPAERRERVLREKSAAL 297
Cdd:PRK06129  241 pgGVADYAQRYGPMYRR-------------------MAAERGQPV-PWDGELVARVEAERRAAL 284
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-281 2.36e-62

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 199.06  E-value: 2.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   1 MGFPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQL------GVYAPNDVAACLARIRMEPGLQ 74
Cdd:PRK07819    1 MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLeravsrGKLTERERDAALARLRFTTDLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  75 AAADCDLVIEAVPEKLDLKRQLFAQLDALC-KPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVR-- 151
Cdd:PRK07819   81 DFADRQLVIEAVVEDEAVKTEIFAELDKVVtDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPtl 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 152 --GDETSDATADLAMAVLragGKRPVRVnRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPL 229
Cdd:PRK07819  161 vtSEATVARAEEFASDVL---GKQVVRA-QDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCAHPM---GPL 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1478748801 230 EQRDMNGLDVHLAIVDYLYADL-ENRVTPSDLLKRKVEAGELGAKTGQGFYDW 281
Cdd:PRK07819  234 RLSDLVGLDTVKAIADSMYEEFkEPLYAPPPLLLRMVEAGLLGKKSGRGFYTY 286
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
5-282 9.96e-60

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 192.46  E-value: 9.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARA-------AAIIERQLGVYAPNDVAACLARIRMEPGL-QAA 76
Cdd:PRK08293    3 IKNVTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAkeriaklADRYVRDLEATKEAPAEAALNRITLTTDLaEAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  77 ADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFftpADVI---PLVEVVRGD 153
Cdd:PRK08293   83 KDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHF---ANEIwknNTAEIMGHP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 154 ETSDATADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVvkWSLGIRlALTGPLEQRD 233
Cdd:PRK08293  160 GTDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKT--WMIATG-APMGPFGILD 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 234 MNGLDVHLAIVDYLYADL--ENRVTPSDLLKRKVEAGELGAKTGQGFYDWP 282
Cdd:PRK08293  237 IVGLDTAYNITSNWAEATddENAKKAAALLKEYIDKGKLGVATGEGFYNYP 287
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 16-303 3.93e-58

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 189.11  E-value: 3.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  16 MGSGIAALFASRGLPVVLID--PVDGA-----LARAAAIIER------QLGVYAPNDVAACLARIRMEPGLQAA---ADC 79
Cdd:PRK08269    1 MGQGIALAFAFAGHDVTLIDfkPRDAAgwralDAEARAEIERtlaalvALGRIDAAQADAVLARIAVVARDGAAdalADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  80 DLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSDAT 159
Cdd:PRK08269   81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 160 ADLAMAVLRAGGKRPVrVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNGLDV 239
Cdd:PRK08269  161 VDRLAALLERIGKVPV-VCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLGLLEFIDWGGCDI 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 240 HLAIVDYLYADL-ENRVTPSDLLKRKVEAGELGAKTGQGFYDW-----PAERRERvLREKSAALAALVQW 303
Cdd:PRK08269  240 LYYASRYLAGEIgPDRFAPPAIVVRNMEEGRDGLRTGAGFYDYagvdvPAYRRQR-LGEFARLLDHLGLA 308
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
4-302 4.51e-44

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 159.64  E-value: 4.51e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGAL----ARAAAIIERQL--GVYAPNDVAACLARIRmePGLQAA- 76
Cdd:PRK11730  312 PVKQAAVLGAGIMGGGIAYQSASKGVPVIMKDINQKALdlgmTEAAKLLNKQVerGKIDGAKMAGVLSSIR--PTLDYAg 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  77 -ADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDET 155
Cdd:PRK11730  390 fERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKT 469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 156 SDATADLAMAVLRAGGKRPVRVNrDIPGFIANRIQ----HALAReamsLLEKGvASAEDIDEVVKWSLGIRLaltGPLEQ 231
Cdd:PRK11730  470 SDETIATVVAYASKMGKTPIVVN-DCPGFFVNRVLfpyfAGFSQ----LLRDG-ADFRQIDKVMEKQFGWPM---GPAYL 540

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 232 RDMNGLD--VHLAIV------DYLYADLENrvtPSDLLkrkVEAGELGAKTGQGFYDWPAERR---ERVLREKSAALAAL 300
Cdd:PRK11730  541 LDVVGIDtaHHAQAVmaegfpDRMKKDYRD---AIDVL---FEAKRFGQKNGKGFYRYEEDKKgkpKKEVDPAVYELLAP 614


                  ..
gi 1478748801 301 VQ 302
Cdd:PRK11730  615 VV 616
PRK07066 PRK07066
L-carnitine dehydrogenase;
5-227 2.22e-42

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 148.45  E-value: 2.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGA-------LARAAAIIERQlGVyAPndvAACLARIRMEPGLQA-A 76
Cdd:PRK07066    7 IKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAeaalranVANAWPALERQ-GL-AP---GASPARLRFVATIEAcV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  77 ADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETS 156
Cdd:PRK07066   82 ADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERTA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478748801 157 DATADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTG 227
Cdd:PRK07066  162 PEAVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMG 232
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 4-279 5.34e-41

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: 151.53  E-value: 5.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAAAIIERQLGVYAPNDVAACLARIRMEPGLQAAAD----- 78
Cdd:TIGR02441 334 PVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLDysgfk 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  79 -CDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDETSD 157
Cdd:TIGR02441 414 nADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSK 493

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 158 ATADLAMAVLRAGGKRPVRVnRDIPGFIANRIQHALAREAMSLLEKGVASAeDIDEVVKwSLGIRLaltGPLEQRDMNGL 237
Cdd:TIGR02441 494 DTLASAVAVGLKQGKVVIVV-KDGPGFYTTRCLGPMLAEVIRLLQEGVDPK-KLDKLTT-KFGFPV---GAATLADEVGV 567

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1478748801 238 DVHLAIVDYLYADLENRVT--PSDLLKRKVEAGELGAKTGQGFY 279
Cdd:TIGR02441 568 DVAEHVAEDLGKAFGERFGggSAELLSELVKAGFLGRKSGKGIF 611
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
4-279 6.11e-41

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 150.82  E-value: 6.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASR-GLPVVLIDPVDGALARAAAiierqlgvYAPNDVAACLARIRMEPGLQAA------ 76
Cdd:PRK11154  308 PVNKVGVLGGGLMGGGIAYVTATKaGLPVRIKDINPQGINHALK--------YSWDLLDKKVKRRHLKPSERDKqmalis 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  77 --------ADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVE 148
Cdd:PRK11154  380 gttdyrgfKHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVE 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 149 VVRGDETSDATADLAMAVLRAGGKRPVRVnRDIPGFIANRIQHALAREAMSLLEKGVaSAEDIDE-VVKWSLGIrlaltG 227
Cdd:PRK11154  460 VIPHAKTSAETIATTVALAKKQGKTPIVV-RDGAGFYVNRILAPYINEAARLLLEGE-PIEHIDAaLVKFGFPV-----G 532

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1478748801 228 PLEQRDMNGLDVHLAIVDYLYADLENRVTPSDLLKRKVEAGELGAKTGQGFY 279
Cdd:PRK11154  533 PITLLDEVGIDVGTKIIPILEAALGERFSAPAAFDKLLNDDRKGRKNGRGFY 584
PRK07531 PRK07531
carnitine 3-dehydrogenase;
4-230 1.57e-38

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 142.18  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDP-------VDGALARAAAIIERQLGVYAPNDvaaclARIRMEPGLQ-A 75
Cdd:PRK07531    3 MIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPhpeaeriIGEVLANAERAYAMLTDAPLPPE-----GRLTFCASLAeA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  76 AADCDLVIEAVPEKLDLKRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVEVVRGDET 155
Cdd:PRK07531   78 VAGADWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKT 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478748801 156 SDATADLAMAVLRAGGKRPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLALTGPLE 230
Cdd:PRK07531  158 SPETIRRAKEILREIGMKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLRWAQMGLFE 232
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 183-281 6.03e-27

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: 101.14  E-value: 6.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 183 GFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLaltGPLEQRDMNGLDVHLAIVDYLYADLENR-VTPSDLL 261
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPM---GPFELSDLVGLDVGYHILEVLAEEFGDRaYRPPPLL 77

                          90       100
                  ....*....|....*....|
gi 1478748801 262 KRKVEAGELGAKTGQGFYDW 281
Cdd:pfam00725  78 EKLVEAGRLGRKTGKGFYKY 97
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 145-268 1.31e-10

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 61.79  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 145 PLVEVVRGDETSDATADLAMAVLRAGGKrPVRVNRDIPGFIANRIQHALAREAMSLLEKGVASAEDIDEVVKWSLGIRLa 224
Cdd:PRK08268  379 KRRTLMAAPATSPAARDAAHALFQQDGK-AVSVIRDSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLNYPL- 456

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1478748801 225 ltGPLEQRDMNGLDVHLAIVDYLYADL-ENRVTPSDLLKRKVEAG 268
Cdd:PRK08268  457 --GPLAWGDRLGAARILRVLENLQALYgDPRYRPSPWLRRRAALG 499
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
9-87 4.61e-06

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 46.70  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   9 AIIGAGAMGSGIAALFASRGLPVVLI--DPvdgalARAAAIIERqlgvYAPNDVAACLArirmepglQAAADCDLVIEAV 86
Cdd:COG2085     2 GIIGTGNIGSALARRLAAAGHEVVIGsrDP-----EKAAALAAE----LGPGARAGTNA--------EAAAAADVVVLAV 64


                  .
gi 1478748801  87 P 87
Cdd:COG2085    65 P 65
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 7-251 6.56e-06

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 46.73  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVlidpvdGALARAAAIIERqlgvyapndVAACLARIRMEPGLQAAADCDLVIEAV 86
Cdd:COG5495     5 KIGIIGAGRVGTALAAALRAAGHEVV------GVYSRSPASAER---------AAALLGAVPALDLEELAAEADLVLLAV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  87 PEK--LDLKRQLfAQLDALCKPATVFatNTSG-LSINAIAQAVSRRDRFVGMHfftPA--------DVIPLVEVVRGDET 155
Cdd:COG5495    70 PDDaiAEVAAGL-AAAGALRPGQLVV--HTSGaLGSDVLAPAARAGALTGSFH---PLqtfsgpreDLERLAGIPFAIEG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801 156 SDATADLAMAVLRAGGKRPVRVNRdipgfiANRIQ-HA-----------LAREAMSLLEK-GVASAED-----IDEVVK- 216
Cdd:COG5495   144 DEEALPVLEALAEALGGEPFVIDS------EQRPLyHAaavfasnflvtLVALAAELLEAaGLEDAFDallplIRETLDn 217

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1478748801 217 -WSLGIRLALTGPLEQRDMNGLDVHLAIVDYLYADL 251
Cdd:COG5495   218 iLELGPAAALTGPAARGDAGTVAKHLAALAELDPEL 253
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 5-136 7.27e-05

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: 43.58  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   5 IQNLAIIGAGAMGSGIAALFASRGLP--VVLIDPVDGALARAaaiieRQLGVyaPNDVAACLARirmepglqAAADCDLV 82
Cdd:COG0287     1 FMRIAIIGLGLIGGSLALALKRAGLAheVVGVDRSPETLERA-----LELGV--IDRAATDLEE--------AVADADLV 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1478748801  83 IEAVPekLDLKRQLFAQLDALCKPATVFaTNTS---GLSINAIAQAVSRRDRFVGMH 136
Cdd:COG0287    66 VLAVP--VGATIEVLAELAPHLKPGAIV-TDVGsvkGAVVEAAEALLPDGVRFVGGH 119
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 4-148 9.63e-05

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: 43.08  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   4 PIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARAaaiieRQLGVYAPNDVAACLARIRMepGLQAAADCDLVI 83
Cdd:cd05188   134 PGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELA-----KELGADHVIDYKEEDLEEEL--RLTGGGGADVVI 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478748801  84 EAVPEKLDLkRQLFAQLDALCKPATVFATnTSGLSINAIAQAVSRRDRFVGMHFFTPADVIPLVE 148
Cdd:cd05188   207 DAVGGPETL-AQALRLLRPGGRIVVVGGT-SGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALD 269
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 7-83 9.82e-05

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 43.31  E-value: 9.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVLIDPVdgalARAAAIIERQLGVYAPnDVAACLARIRMEPGLQAAADCDLVI 83
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARG----AHAEALRENGLRLESP-DGDRTTVPVPAVTDPEELGPADLVL 73
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 6-172 1.63e-04

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 42.36  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   6 QNLAIIGAGAMGSGIAALFASRGLP---VVLIDPVDGALARaaaiIERQLGVYAPNDVAAclarirmepglqAAADCDLV 82
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEA----LAERYGVRVTTDNAE------------AAAQADVV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801  83 IEAV-PEKLdlkRQLFAQLDALCKPATVFATNTSGLSINAIAQAVSRRDRFVgmhffTPADV----IPLvevVRGDETSD 157
Cdd:COG0345    67 VLAVkPQDL---AEVLEELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVrampnTPALVgegvTAL---AAGEAVSE 140

                         170
                  ....*....|....*
gi 1478748801 158 ATADLAMAVLRAGGK 172
Cdd:COG0345   141 EDRELVEALFSAVGK 155
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 9-109 3.34e-04

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 40.29  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   9 AIIGAGAMGSGIAALFASRGLPVVLIDPvdgaLARAAAIIERQLGVYAPNDVAACLARIRMEPGlQAAADCDLVIEAVpe 88
Cdd:pfam02558   2 AILGAGAIGSLLGARLAKAGHDVTLILR----GAELAAIKKNGLRLTSPGGERIVPPPAVTSAS-ESLGPIDLVIVTV-- 74

                          90       100
                  ....*....|....*....|..
gi 1478748801  89 K-LDLKRQLfAQLDALCKPATV 109
Cdd:pfam02558  75 KaYQTEEAL-EDIAPLLGPNTV 95
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
6-117 4.10e-04

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 41.59  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   6 QNLAIIGAGAMGSGIAALFASRGLPVVL--IDPvdgalARAAAI-IERQLGVYAPNdvAACLARIRMEPGLQAA-ADCDL 81
Cdd:PRK00094    2 MKIAVLGAGSWGTALAIVLARNGHDVTLwaRDP-----EQAAEInADRENPRYLPG--IKLPDNLRATTDLAEAlADADL 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1478748801  82 VIEAVPEK-LdlkRQLFAQLDALCKPATVFATNTSGL 117
Cdd:PRK00094   75 ILVAVPSQaL---REVLKQLKPLLPPDAPIVWATKGI 108
PRK12921 PRK12921
oxidoreductase;
9-110 8.57e-04

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 40.23  E-value: 8.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   9 AIIGAGAMGSGIAALFASRGLPVVLIdpvdGALARAAAIIERQLGVYAPNDVAACLARIRMEPGlQAAADCDLVIEAVpe 88
Cdd:PRK12921    4 AVVGAGAVGGTFGGRLLEAGRDVTFL----VRPKRAKALRERGLVIRSDHGDAVVPGPVITDPE-ELTGPFDLVILAV-- 76

                          90       100
                  ....*....|....*....|....*
gi 1478748801  89 K---LDlkrQLFAQLDALCKPATVF 110
Cdd:PRK12921   77 KayqLD---AAIPDLKPLVGEDTVI 98
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 9-117 1.25e-03

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 38.71  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   9 AIIGAGAMGSGIAALFASRGLPVVLIdpvdgalARAAAIIE-----RQLGVYAPNdvAACLARIRMEPGL-QAAADCDLV 82
Cdd:pfam01210   3 AVLGAGSWGTALAKVLADNGHEVRLW-------GRDEELIEeinttHENVRYLPG--IKLPENLKATTDLaEALKGADII 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1478748801  83 IEAVPEKldLKRQLFAQLDALCKPATVFATNTSGL 117
Cdd:pfam01210  74 VIVVPSQ--ALREVLKQLKGLLKPDAILVSLSKGI 106
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 6-87 1.64e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 39.63  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   6 QNLAIIGAGAMGSGIAALFASRGLPVVL--IDPvdgalARAAAI-IERQLGVYAPNdvaaclarIRMEPGLQ-------A 75
Cdd:COG0240     1 MKIAVLGAGSWGTALAKVLARNGHEVTLwgRDP-----EVAEEInETRENPRYLPG--------VKLPENLRatsdleeA 67

                          90
                  ....*....|..
gi 1478748801  76 AADCDLVIEAVP 87
Cdd:COG0240    68 LAGADLVLLAVP 79
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 9-86 2.11e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 39.35  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   9 AIIGAGAMGSGIAALFASRGL-PVVLIDPVDGALARAaaiieRQLGV-----YAPNDVAACLARIRMEPGlqaaadCDLV 82
Cdd:COG1063   166 LVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLELA-----RELGAdavvnPREEDLVEAVRELTGGRG------ADVV 234


                  ....
gi 1478748801  83 IEAV 86
Cdd:COG1063   235 IEAV 238
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
7-85 2.21e-03

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 39.02  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVlidpvdgalaraaAIIERQLGVyAPNDVAACLARIRMEPGLQAAADCDLVIEA 85
Cdd:COG1712     2 RIGLIGCGAIGSEVAEALADAGVELV-------------AVYDRDPER-AEALLASLGARVVSDVDELLAADPDLVVEA 66
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 7-86 2.26e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 39.06  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   7 NLAIIGAGAMGSGIAALFASRGLPVVLidpVDGALARAAAIieRQLGVYAPNDVAACLARIRMEPglQAAADCDLVIEAV 86
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQAGHDVTL---VARRGAHLDAL--NENGLRLEDGEITVPVLAADDP--AELGPQDLVILAV 74
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 6-92 4.22e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (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. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 38.11  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   6 QNLAIIGAGAMGSGIAALFASRGL-PVVLIDPVDGALARAaaiieRQLGVYA--PNDVAACLARIRmepGLQAAADCDLV 82
Cdd:cd08269   131 KTVAVIGAGFIGLLFLQLAAAAGArRVIAIDRRPARLALA-----RELGATEvvTDDSEAIVERVR---ELTGGAGADVV 202

                          90
                  ....*....|..
gi 1478748801  83 IEAV--PEKLDL 92
Cdd:cd08269   203 IEAVghQWPLDL 214
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 7-87 4.48e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 38.43  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   7 NLAIIGA-GAMGSGIAALFASRGLPVVLI--DPVDGALaraaaiIERQLGV-YAPNDVaaclarirmepglQAAADCDLV 82
Cdd:PRK08655    2 KISIIGGtGGLGKWFARFLKEKGFEVIVTgrDPKKGKE------VAKELGVeYANDNI-------------DAAKDADIV 62


                  ....*
gi 1478748801  83 IEAVP 87
Cdd:PRK08655   63 IISVP 67
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 8-83 4.69e-03

Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 38.08  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   8 LAIIGAGAMGSGIAALFASRGLP--VVLIDPVDGA-------LARAAAIIERQLGVYApNDVAAClarirmepglqaaAD 78
Cdd:COG0039     3 VAIIGAGNVGSTLAFRLASGGLAdeLVLIDINEGKaegealdLADAFPLLGFDVKITA-GDYEDL-------------AD 68


                  ....*
gi 1478748801  79 CDLVI 83
Cdd:COG0039    69 ADVVV 73
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 8-62 6.87e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 37.76  E-value: 6.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1478748801   8 LAIIGAGAMGSGIAALFASRGLPVVLID----PVDGALARAAAIIERQLGVYAPNDVAA 62
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLErgddPGSGASGRNAGLIHPGLRYLEPSELAR 60
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 3-87 7.33e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 37.48  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478748801   3 FPIQNLAIIGAGAMGSGIAALFASRGLPVVLIDPVDGALARA----AAIIERQL---GV-YAPNDVaacLARIRMEPGLQ 74
Cdd:COG0446   122 FKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLdpemAALLEEELrehGVeLRLGET---VVAIDGDDKVA 198

                          90
                  ....*....|....*....
gi 1478748801  75 AAA------DCDLVIEAVP 87
Cdd:COG0446   199 VTLtdgeeiPADLVVVAPG 217
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
9-62 8.42e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 37.58  E-value: 8.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1478748801   9 AIIGAGAMGSGIAALFASRGLPVVLID---PVDGALARAAAIIERQLGVYAPNDVAA 62
Cdd:COG0665     6 VVIGGGIAGLSTAYHLARRGLDVTVLErgrPGSGASGRNAGQLRPGLAALADRALVR 62
 
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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