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Conserved domains on  [gi|489187308|ref|WP_003096713|]
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MULTISPECIES: L-carnitine dehydrogenase [Pseudomonas]

Protein Classification

carnitine 3-dehydrogenase( domain architecture ID 11482549)

carnitine 3-dehydrogenase catalyzes the NAD(+)-dependent oxidation of carnitine to 3-dehydrocarnitine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07066 PRK07066
L-carnitine dehydrogenase;
1-321 0e+00

L-carnitine dehydrogenase;


:

Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 663.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   1 MSFVTEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEEC 80
Cdd:PRK07066   1 MAVITDIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPARLRFVATIEAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  81 VGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERT 160
Cdd:PRK07066  81 VADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 161 AAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLA 240
Cdd:PRK07066 161 APEAVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 241 GGNAGMRHFMAQFGPALQLPWTYLPAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIRETKARHGFAFA 320
Cdd:PRK07066 241 GGDAGMRHFMQQFGPALELPWTKLVAPELTDALIDRVVEGTAEQQGPRSIKALERYRDECITEVLEAIAAVKARHGMRFE 320


                 .
gi 489187308 321 E 321
Cdd:PRK07066 321 D 321
 
Name Accession Description Interval E-value
PRK07066 PRK07066
L-carnitine dehydrogenase;
1-321 0e+00

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 663.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   1 MSFVTEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEEC 80
Cdd:PRK07066   1 MAVITDIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPARLRFVATIEAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  81 VGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERT 160
Cdd:PRK07066  81 VADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 161 AAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLA 240
Cdd:PRK07066 161 APEAVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 241 GGNAGMRHFMAQFGPALQLPWTYLPAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIRETKARHGFAFA 320
Cdd:PRK07066 241 GGDAGMRHFMQQFGPALELPWTKLVAPELTDALIDRVVEGTAEQQGPRSIKALERYRDECITEVLEAIAAVKARHGMRFE 320


                 .
gi 489187308 321 E 321
Cdd:PRK07066 321 D 321
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 6-286 1.50e-82

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: 251.18  E-value: 1.50e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   6 EIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGL----APGAAQERLRFVASIEEcV 81
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKlteeEADAALARITPTTDLAA-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  82 GDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTA 161
Cdd:COG1250   80 ADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 162 AEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRwsfMGTFLTYTLAG 241
Cdd:COG1250  160 DETVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFP---MGPFELADLVG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489187308 242 GNAgMRHFMAQFGPALQLPWtyLPAPELTEALIDRVVEGTAEQQG 286
Cdd:COG1250  236 LDT-ALAVLEVLYEALGDPR--YRPPPLLKKLVEAGRLGRKTGRG 277
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 11-183 7.27e-50

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 163.86  E-value: 7.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   11 AALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLA----PGAAQERLRFVASIEECVgDADF 86
Cdd:pfam02737   3 AVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRIteeeVDAALARISFTTDLAAAV-DADL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   87 IQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVR 166
Cdd:pfam02737  82 VIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETVA 161

                         170
                  ....*....|....*..
gi 489187308  167 AAMRVYESLGMRPLHVR 183
Cdd:pfam02737 162 TTVELAKKIGKTPVVVK 178
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 6-210 6.66e-13

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: 69.10  E-value: 6.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308    6 EIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAW-PALRKQGLApgaAQERLRFVASIEECVG-- 82
Cdd:TIGR02441 334 PVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKIT---SLERDSILSNLTPTLDys 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   83 ---DADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGER 159
Cdd:TIGR02441 411 gfkNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDG 490

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489187308  160 TAAEAVRAAMRVYESLGmRPLHVRKEVPGFIADRLLEALWREALHLVNDGV 210
Cdd:TIGR02441 491 TSKDTLASAVAVGLKQG-KVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGV 540
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 16-87 5.76e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 37.93  E-value: 5.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187308  16 GVIGSGWIAR-----ALAHGLDVVAWDPAPGAEAALRARVanawpalrkqglapgaaqeRLRFVASIEECVGDADFI 87
Cdd:cd12174  139 GVIGLGNIGRlvanaALALGMKVIGYDPYLSVEAAWKLSV-------------------EVQRVTSLEELLATADYI 196
 
Name Accession Description Interval E-value
PRK07066 PRK07066
L-carnitine dehydrogenase;
1-321 0e+00

L-carnitine dehydrogenase;


Pssm-ID: 168796 [Multi-domain]  Cd Length: 321  Bit Score: 663.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   1 MSFVTEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEEC 80
Cdd:PRK07066   1 MAVITDIKTFAAIGSGVIGSGWVARALAHGLDVVAWDPAPGAEAALRANVANAWPALERQGLAPGASPARLRFVATIEAC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  81 VGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERT 160
Cdd:PRK07066  81 VADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGERT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 161 AAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLA 240
Cdd:PRK07066 161 APEAVDAAMGIYRALGMRPLHVRKEVPGFIADRLLEALWREALHLVNEGVATTGEIDDAIRFGAGIRWSFMGTFLTYTLA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 241 GGNAGMRHFMAQFGPALQLPWTYLPAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIRETKARHGFAFA 320
Cdd:PRK07066 241 GGDAGMRHFMQQFGPALELPWTKLVAPELTDALIDRVVEGTAEQQGPRSIKALERYRDECITEVLEAIAAVKARHGMRFE 320


                 .
gi 489187308 321 E 321
Cdd:PRK07066 321 D 321
PRK07531 PRK07531
carnitine 3-dehydrogenase;
5-316 2.63e-137

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 398.34  E-value: 2.63e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   5 TEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQERLRFVASIEECVGDA 84
Cdd:PRK07531   2 TMIMKAACIGGGVIGGGWAARFLLAGIDVAVFDPHPEAERIIGEVLANAERAYAMLTDAPLPPEGRLTFCASLAEAVAGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  85 DFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEA 164
Cdd:PRK07531  82 DWIQESVPERLDLKRRVLAEIDAAARPDALIGSSTSGFLPSDLQEGMTHPERLFVAHPYNPVYLLPLVELVGGGKTSPET 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 165 VRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGNA 244
Cdd:PRK07531 162 IRRAKEILREIGMKPVHIAKEIDAFVGDRLLEALWREALWLVKDGIATTEEIDDVIRYSFGLRWAQMGLFETYRIAGGEA 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187308 245 GMRHFMAQFGPALQLPWTYL-PAPELTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIretKARHG 316
Cdd:PRK07531 242 GMRHFLAQFGPCLKWPWTKLmDVPDLDDALVDKIAGQSDAQSGGLSIRELERIRDENLVGIMQAL---KAGDG 311
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 6-286 1.50e-82

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: 251.18  E-value: 1.50e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   6 EIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGL----APGAAQERLRFVASIEEcV 81
Cdd:COG1250    1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKlteeEADAALARITPTTDLAA-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  82 GDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTA 161
Cdd:COG1250   80 ADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRGPATS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 162 AEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRwsfMGTFLTYTLAG 241
Cdd:COG1250  160 DETVATAVAFARRLGKTPVVV-KDTPGFIVNRILVPYLNEAIRLLEEGVASPEDIDAAMRLGFGFP---MGPFELADLVG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489187308 242 GNAgMRHFMAQFGPALQLPWtyLPAPELTEALIDRVVEGTAEQQG 286
Cdd:COG1250  236 LDT-ALAVLEVLYEALGDPR--YRPPPLLKKLVEAGRLGRKTGRG 277
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 11-309 2.94e-75

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 233.40  E-value: 2.94e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  11 AALGSGVIGSGW---IARAlahGLDVVAWDPAPGAEAALRARVANAWPALRKQGL----APGAAQERLRFVASIEECVGD 83
Cdd:PRK06129   6 AIIGAGLIGRAWaivFARA---GHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLldgeAPDAVLARIRVTDSLADAVAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  84 ADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAE 163
Cdd:PRK06129  83 ADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTAPA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 164 AVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLaggN 243
Cdd:PRK06129 163 TLARAEALYRAAGQSPVRLRREIDGFVLNRLQGALLREAFRLVADGVASVDDIDAVIRDGLGLRWSFMGPFETIDL---N 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187308 244 A--GMRHFMAQFGPA---------LQLPWtylpapelTEALIDRVVEGTAEQQGARSIAELERYRDDCLLAVLGAIR 309
Cdd:PRK06129 240 ApgGVADYAQRYGPMyrrmaaergQPVPW--------DGELVARVEAERRAALPLDQLAARQAWRDRRLMALAAHRR 308
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 5-241 6.17e-57

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 186.52  E-value: 6.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   5 TEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPGAAQeRLRFVASIEECVGDA 84
Cdd:PRK06130   2 NPIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPLGIASAGMG-RIRMEAGLAAAVSGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  85 DFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEA 164
Cdd:PRK06130  81 DLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187308 165 VRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAG 241
Cdd:PRK06130 161 VATTMALLRSIGKRPVLVKKDIPGFIANRIQHALAREAISLLEKGVASAEDIDEVVKWSLGIRLALTGPLEQRDMNG 237
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 11-183 7.27e-50

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 163.86  E-value: 7.27e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   11 AALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLA----PGAAQERLRFVASIEECVgDADF 86
Cdd:pfam02737   3 AVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRIteeeVDAALARISFTTDLAAAV-DADL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   87 IQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVR 166
Cdd:pfam02737  82 VIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETVA 161

                         170
                  ....*....|....*..
gi 489187308  167 AAMRVYESLGMRPLHVR 183
Cdd:pfam02737 162 TTVELAKKIGKTPVVVK 178
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
5-234 6.79e-36

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 130.83  E-value: 6.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   5 TEIKTFAALGSGVIGSGwIA-RALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQGLAPG-----AAQERLRFVASIE 78
Cdd:PRK08293   1 MDIKNVTVAGAGVLGSQ-IAfQTAFHGFDVTIYDISDEALEKAKERIAKLADRYVRDLEATKeapaeAALNRITLTTDLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  79 ECVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGE 158
Cdd:PRK08293  80 EAVKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187308 159 RTAAEAVRAAMRVYESLGMRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGlrwSFMGTF 234
Cdd:PRK08293 160 GTDPEVFDTVVAFAKAIGMVPIVLKKEQPGYILNSLLVPFLSAALALWAKGVADPETIDKTWMIATG---APMGPF 232
PLN02545 PLN02545
3-hydroxybutyryl-CoA dehydrogenase
 5-225 4.25e-35

3-hydroxybutyryl-CoA dehydrogenase


Pssm-ID: 215300 [Multi-domain]  Cd Length: 295  Bit Score: 129.08  E-value: 4.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   5 TEIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQG-LAPGAAQE---RLRFVASIEEc 80
Cdd:PLN02545   2 AEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGkMSQEEADAtlgRIRCTTNLEE- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  81 VGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERT 160
Cdd:PLN02545  81 LRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187308 161 AAEAVRAAMRVYESLGMRPLhVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAG 225
Cdd:PLN02545 161 SDEVFDATKALAERFGKTVV-CSQDYPGFIVNRILMPMINEAFYALYTGVASKEDIDTGMKLGTN 224
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
7-223 3.70e-33

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 123.75  E-value: 3.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   7 IKTFAALGSGVIGSGwIARALA-HGLDVVAWDPAPGAEAALRARVANAWPALRKQG----LAPGAAQERLRFVASIEECV 81
Cdd:PRK09260   1 IEKLVVVGAGVMGRG-IAYVFAvSGFQTTLVDIKQEQLESAQQEIASIFEQGVARGklteAARQAALARLSYSLDLKAAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  82 GDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTA 161
Cdd:PRK09260  80 ADADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187308 162 AEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFG 223
Cdd:PRK09260 160 DETVQVAKEVAEQMGKETVVV-NEFPGFVTSRISALVGNEAFYMLQEGVATAEDIDKAIRLG 220
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 1-234 9.80e-33

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 126.50  E-value: 9.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   1 MSFVTEIKTFAALGSGVIGSGwIAR-ALAHGLDVVAWDPAPGAEAALRARVANAWPALRKQG-LAPGAAQ---ERLRFVA 75
Cdd:PRK08268   1 MMALPSIATVAVIGAGAMGAG-IAQvAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGkLTAEQADaalARLRPVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  76 SIEEcVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERcLVG-HPFNPVYLLPLVEV 154
Cdd:PRK08268  80 ALAD-LADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPER-VAGlHFFNPVPLMKLVEV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308 155 VGGERTAAEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRwsfMGTF 234
Cdd:PRK08268 158 VSGLATDPAVADALYALARAWGKTPVRA-KDTPGFIVNRAARPYYTEALRVLEEGVADPATIDAILREAAGFR---MGPF 233
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 7-224 1.92e-28

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 110.82  E-value: 1.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   7 IKTFAALGSGVIGSGwIARALA-HGLDVVAWDPApgaEAALR---ARVANAWPALRKQGLAPGAAQERL--RFVASIE-E 79
Cdd:PRK05808   3 IQKIGVIGAGTMGNG-IAQVCAvAGYDVVMVDIS---DAAVDrglATITKSLDRLVKKGKMTEADKEAAlaRITGTTDlD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  80 CVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGER 159
Cdd:PRK05808  79 DLKDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187308 160 TAAEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGA 224
Cdd:PRK05808 159 TSDATHEAVEALAKKIGKTPVEV-KNAPGFVVNRILIPMINEAIFVLAEGVATAEDIDEGMKLGC 222
PRK08269 PRK08269
3-hydroxybutyryl-CoA dehydrogenase; Validated
 23-232 3.97e-26

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181340 [Multi-domain]  Cd Length: 314  Bit Score: 105.52  E-value: 3.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  23 IARALAH-GLDVVAWDPAPGAEAALRARVANAWPALRKQ--------GLAPGAAQE---RLRFVA--SIEECVGDADFIQ 88
Cdd:PRK08269   5 IALAFAFaGHDVTLIDFKPRDAAGWRALDAEARAEIERTlaalvalgRIDAAQADAvlaRIAVVArdGAADALADADLVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  89 ESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVRAA 168
Cdd:PRK08269  85 EAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAVVDRL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187308 169 MRVYESLGMRPLhVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMG 232
Cdd:PRK08269 165 AALLERIGKVPV-VCGPSPGYIVPRIQALAMNEAARMVEEGVASAEDIDKAIRTGFGLRFAVLG 227
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 6-234 1.02e-24

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 101.10  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   6 EIKTFAALGSGVIGSGwIARALAH-GLDVVAWDPAPGA-EAALRArVANAWPALR---KQGLAP----GAAQERLRFVAS 76
Cdd:PRK06035   2 DIKVIGVVGSGVMGQG-IAQVFARtGYDVTIVDVSEEIlKNAMEL-IESGPYGLRnlvEKGKMSedeaKAIMARIRTSTS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  77 IEEcVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVG 156
Cdd:PRK06035  80 YES-LSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187308 157 GERTAAEAVRAAMRVYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRwsfMGTF 234
Cdd:PRK06035 159 AALTSEETFNTTVELSKKIGKIPIEV-ADVPGFFTTRFIEGWLLEAIRSFEIGIATIKDIDEMCKLAFGFP---MGPF 232
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 14-225 2.53e-22

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 94.28  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  14 GSGVIGSGwIARALA-HGLDVVAWDPAPGAEAALRARVANAWP-ALRKQGLAPG---AAQERLRFVASIEEcVGDADFIQ 88
Cdd:PRK07819  12 GAGQMGAG-IAEVCArAGVDVLVFETTEELATAGRNRIEKSLErAVSRGKLTERerdAALARLRFTTDLGD-FADRQLVI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  89 ESAPERLDLKLDLHARISAA-ARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGERTAAEAVRA 167
Cdd:PRK07819  90 EAVVEDEAVKTEIFAELDKVvTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTLVTSEATVAR 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489187308 168 AMR-VYESLGMRPLHVrKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAG 225
Cdd:PRK07819 170 AEEfASDVLGKQVVRA-QDRSGFVVNALLVPYLLSAIRMVESGFATAEDIDKAMVLGCA 227
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 5-224 1.95e-20

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 89.30  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   5 TEIKTFAALGSGVIGSGwIAR--ALAhGLDVVAWDPAPGA-EAALRARVANAWPALRKQGLAPGAAQERLRFVASIE--E 79
Cdd:PRK07530   2 MAIKKVGVIGAGQMGNG-IAHvcALA-GYDVLLNDVSADRlEAGLATINGNLARQVAKGKISEEARAAALARISTATdlE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  80 CVGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGER 159
Cdd:PRK07530  80 DLADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187308 160 TAAEAVRAAMRVYESLGmRPLHVRKEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGA 224
Cdd:PRK07530 160 TDEATFEAAKEFVTKLG-KTITVAEDFPAFIVNRILLPMINEAIYTLYEGVGSVEAIDTAMKLGA 223
3HCDH pfam00725
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ...
 188-275 5.34e-17

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: 74.95  E-value: 5.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  188 GFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAGLRWSFMGTFLTYTLAGGNAGMRHFMAQFGpalqlpWTYLPAP 267
Cdd:pfam00725   1 GFVVNRLLAPYLNEAIRLVEEGVATPEDIDAAMRLGLGLPMGPFELSDLVGLDVGYHILEVLAEEFG------DRAYRPP 74


                  ....*...
gi 489187308  268 ELTEALID 275
Cdd:pfam00725  75 PLLEKLVE 82
fa_ox_alpha_mit TIGR02441
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ...
 6-210 6.66e-13

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: 69.10  E-value: 6.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308    6 EIKTFAALGSGVIGSGWIARALAHGLDVVAWDPAPGAEAALRARVANAW-PALRKQGLApgaAQERLRFVASIEECVG-- 82
Cdd:TIGR02441 334 PVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLnKKVKRKKIT---SLERDSILSNLTPTLDys 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   83 ---DADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVGGER 159
Cdd:TIGR02441 411 gfkNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDG 490

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489187308  160 TAAEAVRAAMRVYESLGmRPLHVRKEVPGFIADRLLEALWREALHLVNDGV 210
Cdd:TIGR02441 491 TSKDTLASAVAVGLKQG-KVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGV 540
fadJ PRK11154
fatty acid oxidation complex subunit alpha FadJ;
6-223 8.05e-11

fatty acid oxidation complex subunit alpha FadJ;


Pssm-ID: 236864 [Multi-domain]  Cd Length: 708  Bit Score: 62.99  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308   6 EIKTFAALGSGVIGSGwIARALAH--GLDVVAWDPAP-GAEAALRArvanAWPALRKQ----GLAPGAAQERLRFVASIE 78
Cdd:PRK11154 308 PVNKVGVLGGGLMGGG-IAYVTATkaGLPVRIKDINPqGINHALKY----SWDLLDKKvkrrHLKPSERDKQMALISGTT 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  79 ECVG--DADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERCLVGHPFNPVYLLPLVEVVG 156
Cdd:PRK11154 383 DYRGfkHADVVIEAVFEDLALKQQMVAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIP 462

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187308 157 GERTAAEAVRAAMRVYESLGMRPLhVRKEVPGFIADRLLEALWREALHLVNDGVATTgEIDDA-IRFG 223
Cdd:PRK11154 463 HAKTSAETIATTVALAKKQGKTPI-VVRDGAGFYVNRILAPYINEAARLLLEGEPIE-HIDAAlVKFG 528
fadB PRK11730
fatty acid oxidation complex subunit alpha FadB;
81-210 3.98e-08

fatty acid oxidation complex subunit alpha FadB;


Pssm-ID: 183293 [Multi-domain]  Cd Length: 715  Bit Score: 54.48  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187308  81 VGDADFIQESAPERLDLKLDLHARISAAARPDVLIGSSTSGLLPSEFYAEASHPERcLVG-HPFNPVYLLPLVEVVGGER 159
Cdd:PRK11730 390 FERVDVVVEAVVENPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPEN-FCGmHFFNPVHRMPLVEVIRGEK 468

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489187308 160 TAAEAVrAAMRVYES-LGMRPLhVRKEVPGFIADRLLEALWREALHLVNDGV 210
Cdd:PRK11730 469 TSDETI-ATVVAYASkMGKTPI-VVNDCPGFFVNRVLFPYFAGFSQLLRDGA 518
PRK08268 PRK08268
3-hydroxy-acyl-CoA dehydrogenase; Validated
 160-225 9.04e-04

3-hydroxy-acyl-CoA dehydrogenase; Validated


Pssm-ID: 236211 [Multi-domain]  Cd Length: 507  Bit Score: 40.60  E-value: 9.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187308 160 TAAEAVRAAMRVYESLGMRPLHVRkEVPGFIADRLLEALWREALHLVNDGVATTGEIDDAIRFGAG 225
Cdd:PRK08268 389 TSPAARDAAHALFQQDGKAVSVIR-DSPGFVAQRTVAMIVNEAADIAQQGIASPADIDLAMRLGLN 453
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 16-87 5.76e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 37.93  E-value: 5.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187308  16 GVIGSGWIAR-----ALAHGLDVVAWDPAPGAEAALRARVanawpalrkqglapgaaqeRLRFVASIEECVGDADFI 87
Cdd:cd12174  139 GVIGLGNIGRlvanaALALGMKVIGYDPYLSVEAAWKLSV-------------------EVQRVTSLEELLATADYI 196
 
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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