|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-387 |
0e+00 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 823.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 1 MNNFNLHTPTRILFGKGAIAELRDQIPQDARVLVTYGGGSVKKTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKI 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 81 VRDEKVTFLLAVGGGSVLDGTKFIAAAAQYADGIDPWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDK 160
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGKIQDRFAEGILLTLVEEGPKALQEPENYNV 240
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWNITEGSDD 320
Cdd:PRK15138 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489934859 321 QRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTKLGEHQDITLEVSRRIYEAAR 387
Cdd:PRK15138 321 ERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHGMTQLGEHHDITLDVSRRIYEAAR 387
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-387 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 696.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 1 MNNFNLHTPTRILFGKGAIAELRDQIPQD-ARVLVTYGGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNA 77
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYgKKVLLVYGGGSIKKNGLYDQVKAALKeaGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 78 VKIVRDEKVTFLLAVGGGSVLDGTKFIAAAAQYaDGiDPWRILeTHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTT 157
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKY-DG-DPWDIL-TGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 158 GDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGKIQDRFAEGILLTLVEEGPKALQEPEN 237
Cdd:COG1979 158 KEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 238 YNVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWNITEG 317
Cdd:COG1979 238 YDARANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 318 SDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTKLGEHQDITLEVSRRIYEAAR 387
Cdd:COG1979 318 DDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-384 |
0e+00 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 558.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 3 NFNLHTPTRILFGKGAIAELRDQIPQ-DARVLVTYGGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVK 79
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKKyGKKVLLVYGGGSIKKNGLYDRVVASLKeaGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 80 IVRDEKVTFLLAVGGGSVLDGTKFIAAAAqYADGiDPWRILeTHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGD 159
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGA-KYDG-DVWDFF-TGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 160 KLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGKIQDRFAEGILLTLVEEGPKALQEPENYN 239
Cdd:cd08187 158 KLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 240 VRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWNIT-EGS 318
Cdd:cd08187 238 ARANLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDpGGD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489934859 319 DDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTkLGEHQDITLEVSRRIYE 384
Cdd:cd08187 318 DEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGL-GGGFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-359 |
1.37e-103 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 310.30 E-value: 1.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQ-DARVLVTYGGGSVKkTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDEK 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSLK-SGLLDKVLASLEeaGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 86 VTFLLAVGGGSVLDGTKfiAAAAQYADGIDPWRILEThGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFMT 165
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAK--AIALLLTNPGDVWDYLGG-KPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 166 PFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFAEGILLTLVEEGPKALQEPENYNVRANVM 245
Cdd:pfam00465 157 PKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-KGANPLTDALALEAIRLIAENLPRAVADGEDLEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 246 WAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWnitEGSDDQRIDA 325
Cdd:pfam00465 236 LASTLAGLAFSNAGLG---AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG---EDSDEEAAEE 309
|
330 340 350
....*....|....*....|....*....|....
gi 489934859 326 AIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:pfam00465 310 AIEALRELLRELGLPTTLSELGVTEEDLDALAEA 343
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-360 |
2.91e-76 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 236.88 E-value: 2.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRD-QIPQDARVLVTYGGGSVKktGVLAQVQDALK-GLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEiKRRGFDRALVVSDEGVVK--GVGEKVADSLKkGLAVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKFIAAAAQyadgidpwrilethgndvtSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFmtP 166
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAALLN-------------------RGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVG--P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 167 FVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEqyvtypvdgkiqdrfaegilltlveegpkalqepenynvRANVMW 246
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 247 AATQALNGLIgaGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAkllqyaeriwnitegsddqrIDAA 326
Cdd:cd07766 179 AATLAGMGLF--ESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE--------------------PEAA 236
|
330 340 350
....*....|....*....|....*....|....
gi 489934859 327 IAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKL 360
Cdd:cd07766 237 IEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-383 |
1.89e-72 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 230.41 E-value: 1.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQI--PQDARVLVTYGGGsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDE 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELkaLGGKKVLLVTDPG-LVKAGLLDKVLESLKaaGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 85 KVTFLLAVGGGSVLDGTKFIAAAAQYadgidPWRILETHGND--VTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLA 162
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATN-----GGSIRDYEGIGkvPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 163 FMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVT---YPvdgkIQDRFA-EGILLtLVEEGPKALQEPENY 238
Cdd:cd08551 155 IVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSkkaNP----ISDALAlEAIRL-IGKNLRRAVADGSDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 239 NVRANVMWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWNITEG- 317
Cdd:cd08551 230 EAREAMLLASLLAGIAFGNAGL---GAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGl 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489934859 318 SDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTKLGEHQDITLEVSRRIY 383
Cdd:cd08551 307 SDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
2-359 |
3.86e-66 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 214.60 E-value: 3.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 2 NNFNLHTPTRILFGKGAIAELRDQIPQ--DARVL-VTygGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMN 76
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRlgAKRALiVT--DPGLAKLGLLDRVLDALEaaGIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 77 AVKIVRDEKVTFLLAVGGGSVLDGTKfiAAAAQYADGIDPWRILETHGNDVTS----AIPmgsvlTLPATGSESNSGAVI 152
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAK--AIALLATNPGDLEDYLGIKKVPGPPlpliAIP-----TTAGTGSEVTPFAVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 153 SRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV----TYPVDGkiqdrFA-EGIllTLVEE 227
Cdd:COG1454 152 TDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVskgaNPLTDA-----LAlEAI--RLIAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 228 G-PKALQEPENYNVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTK 300
Cdd:COG1454 225 NlPRAVADGDDLEAREKMALASLLAgmafANAGLG-------AVHALAHPLGGLFHVPHGLANAILLPHVlrFNAPAAPE 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489934859 301 RakllqYAE--RIWNITEG-SDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:COG1454 298 R-----YAEiaRALGLDVGlSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAEL 354
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-358 |
3.01e-57 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 191.56 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 7 HTPTRILFGKGAIAELRDQIPQDA-RVLVTYGGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRD 83
Cdd:cd08185 2 YQPTRILFGAGKLNELGEEALRPGkKALIVTGKGSSKKTGLLDRVKKLLEkaGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAAqyADGIDPWRIL---ETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDK 160
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMA--TNPGDIWDYIfggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFA-EGILLtLVEEGPKALQEPENYN 239
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYIS-KNANPFSDMLAlEAIRL-VAKYLPRAVKDGSDLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 240 VRANVMWAATQA--LNGLIGAGVPqdwatHMLGHELTAMHG-LDHAQTLAIVLPALWNEKRDTKRAKLLQYAERiwNITE 316
Cdd:cd08185 238 AREKMAWASTLAgiVIANSGTTLP-----HGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA--EASG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489934859 317 GSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLE 358
Cdd:cd08185 311 LSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAE 352
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-359 |
6.34e-53 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 179.70 E-value: 6.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 4 FNLHTPTRILFGKGAIAELRDQIPQDAR---VLVTygGGSVKKTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKI 80
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGGkrgLLVT--DPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 81 VRDEKVTFLLAVGGGSVLDGTKFIAAAAQYADGIDpwRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDK 160
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIE--DYLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYvtYPVDG-KIQDRFAEG----ILLTLveegPKALQEP 235
Cdd:cd08196 157 APLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAY--WSINHqPISDALALEaaklVLENL----EKAYNNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 236 ENYNVRANVMWAATQAlnGLigA-GVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIwni 314
Cdd:cd08196 231 NDKEAREKMALASLLA--GL--AfSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL--- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489934859 315 teGSDDqrIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:cd08196 304 --GFKD--AEELADKIEELKKRIGLRTRLSELGITEEDLEEIVEE 344
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-358 |
5.71e-52 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 177.73 E-value: 5.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDA--RVLVTYGGGsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDE 84
Cdd:cd14863 5 LTPVIFGAGAVEQIGELLKELGckKVLLVTDKG-LKKAGIVDKIIDLLEeaGIEVVVFDDVEPDPPDEIVDEAAEIAREE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 85 KVTFLLAVGGGSVLDGTKFIAAAAqyADGIDPWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFM 164
Cdd:cd14863 84 GADGVIGIGGGSVLDTAKAIAVLL--TNPGPIIDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 165 TPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFAEGILLTLVEEGPKALQEPENYNVRANV 244
Cdd:cd14863 162 GPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-KLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 245 MWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEkrDTKRAKLLQYAErIWNI--TEGSDD 320
Cdd:cd14863 241 LLASNLAGIAFNNAGT---HIGHAIAHALGALYHIPHGLACALALPVVleFNA--EAYPEKVKKIAK-ALGVsfPGESDE 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 489934859 321 QRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLE 358
Cdd:cd14863 315 ELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAE 352
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-359 |
4.02e-47 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 165.02 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 4 FNLHTPTRILFGKGAIAELRDQIPQDAR---VLVTYGGgsVKKTGVLAQVQDALKGL--DVLEFGGIEPNPSYETLMNAV 78
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGArrpLIVTDKG--LAAAGLLKKVEDALGDAieIVGVFDDVPPDSSVAVVNEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 79 KIVRDEKVTFLLAVGGGSVLDGTKfiAAAAQYADGIDpwRILETHGNDVTSA--IPMGSVLTLPATGSESNSGAVISRKT 156
Cdd:cd14865 79 ARAREAGADGIIAVGGGSVIDTAK--GVNILLSEGGD--DLDDYGGANRLTRplKPLIAIPTTAGTGSEVTLVAVIKDEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 157 TGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV---TYPvdgkIQDRFAEGILLTLVEEGPKALQ 233
Cdd:cd14865 155 KKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTslqKNP----ISDALALQAIRLISENLPKAVK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 234 EPENYNVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKR-AKLLQ 306
Cdd:cd14865 231 NGKDLEARLALAIAATMAgiafSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVmrYNLDAAAERyAELAL 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489934859 307 YAERIWNITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:cd14865 304 ALAYGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAEL 356
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-304 |
4.77e-47 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 163.91 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 6 LHTPTRILFGKGAIAELRDQIPQDA-RVLVTYGGGSVKKTGVLAQVQDALKGLDV--LEFGGIEPNPSYETLMNAVKIVR 82
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGkKALIVTGKHSAKKNGSLDDVTEALEENGIeyFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 83 DEKVTFLLAVGGGSVLDGTKFIAAAAqyADGIDPWRILEthGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLA 162
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLA--ANKDGDEDLFQ--NGKYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 163 FMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDgKIQDRFAEGILLTLVEEGPKALQEPENYNVRA 242
Cdd:cd08181 157 FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKAT-PLSDALALEALRLIGECLPNLLGDELDEEDRE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489934859 243 NVMWAATqaLNGLI----GAGVPqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKL 304
Cdd:cd08181 236 KLMYAST--LAGMViaqtGTTLP-----HGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKV 294
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-386 |
1.71e-46 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 163.13 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRdQIPqDARVLVTYGGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd08179 5 PRDIYFGEGALEYLK-TLK-GKRAFIVTGGGSMKRNGFLDKVEDYLKeaGMEVKVFEGVEPDPSVETVEKGAEAMREFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKFIAAAAQY-----ADGIDPWRILETHGNDVTSAIPMGSvltlpATGSESNSGAVISRKTTGDKL 161
Cdd:cd08179 83 DWIIAIGGGSVIDAAKAMWVFYEYpeltfEDALVPFPLPELRKKARFIAIPSTS-----GTGSEVTRASVITDTEKGIKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 162 AFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGkIQDRFAEGILLTLVEEGPKALQEPENYNVR 241
Cdd:cd08179 158 PLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLAND-FTDALALGAILDIFENLPKSYNGGKDLEAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 242 ANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQyaeriwNIT 315
Cdd:cd08179 237 EKMHNASCLAgmafSNSGLG-------IVHSMAHKGGAFFGIPHGLANAILLPYVieFNSKDPEARARYAA------LLI 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489934859 316 EGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDG----SSIPALLEKLQAHGGTKLGEHQdITLEVSRRIYEAA 386
Cdd:cd08179 304 GLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEdeffAKLDEMAENAMNDACTGTNPRK-PTVEEMKELLKAA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-359 |
2.72e-44 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 157.29 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQD--ARVL-VTYGGgsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRD 83
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALgiRRPLlVTDPG--LAALGIVDRVLEALGaaGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAA-------QYADGIDPWRilethgnDVTSAI-PMGSVLTLPATGSESNSGAVISRK 155
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMAthpgplwDYEDGEGGPA-------AITPAVpPLIAIPTTAGTGSEVGRAAVITDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 156 TTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTypvdgkiqDRF---AEGILL---TLVEEG- 228
Cdd:cd14861 154 DTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLS--------PGFhpmADGIALeglRLISEWl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 229 PKALQEPENYNVRANVMWAATQA----LNGLiGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKL 304
Cdd:cd14861 226 PRAVADGSDLEARGEMMMAALMGavafQKGL-G-------AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489934859 305 LQYAERIwniteGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:cd14861 298 ARLARAL-----GLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAEL 347
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
4-358 |
5.25e-44 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 156.55 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 4 FNLHTPTRILFGKGAIAElrdqIPQDAR-------VLVTYGGgsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETL 74
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEE----IGEEAKkrgfkkaLIVTDKG--LVKFGIVDKVTDVLKeaGIAYTVFDEVKPNPTIENV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 75 MNAVKIVRDEKVTFLLAVGGGSVLDGTKFIaaaaqyadgidpwRILETH-GNDVTS----------AIPMGSVLTLPATG 143
Cdd:cd08176 75 MAGVAAYKESGADGIIAVGGGSSIDTAKAI-------------GIIVANpGADVRSlegvaptknpAVPIIAVPTTAGTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 144 SESNSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTypvdgKIQDRFAEGILL- 222
Cdd:cd08176 142 SEVTINYVITDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-----KGAWELSDMLALk 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 223 --TLVEEG-PKALQEPENYNVRANVMWAAT---QALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALWnek 296
Cdd:cd08176 217 aiELIAKNlRKAVANPNNVEARENMALAQYiagMAFSN-VGLGI-----VHSMAHPLSAFYDTPHGVANAILLPYVM--- 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489934859 297 RDTKRAKLLQYAE--RIWNI--TEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLE 358
Cdd:cd08176 288 EFNAPATGEKYRDiaRAMGVdtTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-360 |
1.25e-40 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 147.37 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 1 MNNFNlhtPTRILFGKGAIAELrDQIPQDARVLVTygGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAV 78
Cdd:cd14862 1 MWYFS---SPKIVFGEDALSHL-EQLSGKRALIVT--DKVLVKLGLLKKVLKRLLqaGFEVEVFDEVEPEPPLETVLKGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 79 KIVRDEKVTFLLAVGGGSVLDGTKfiAAAAQY-ADGIDPWRI--LETHGNDVTS---AIPmgsvlTLPATGSESNSGAVI 152
Cdd:cd14862 75 EAMREFEPDLIIALGGGSVMDAAK--AAWVLYeRPDLDPEDIspLDLLGLRKKAkliAIP-----TTSGTGSEATWAIVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 153 SRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFAEGILLTLVEEGPKAL 232
Cdd:cd14862 148 TDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLS-TWSNDFSDALALKAIELIFKYLPRAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 233 QEPENYNVRANVMWAATQAlnGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQ 306
Cdd:cd14862 227 KDGDDLEAREKMHNAATIA--GLafgnSQAGL-----AHALGHSLGAVFHVPHGIAVGLFLPYVieFYAKVTDERYDLLK 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489934859 307 YAEriwnITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKL 360
Cdd:cd14862 300 LLG----IEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDEL 349
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-386 |
1.55e-39 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 144.72 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 10 TRILFGKGAIAELRDqIPQDA---RVLVTYGGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDE 84
Cdd:cd08186 2 TTLYFGVGAIAKIKD-ILKDLgidKVIIVTGRSSYKKSGAWDDVEKALEenGIEYVVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 85 KVTFLLAVGGGSVLDGTKFIAAAAQYADGIDpwRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFM 164
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLLAYGGKTA--RDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 165 TPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTypvdgkiqdRFAEGILLTLVEEG--------PKALQEPE 236
Cdd:cd08186 159 YDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATT---------KVSSPYVITLAKEAirliaeylPRALANPK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 237 NYNVRANVMWAAtqalngLIgAGVPQDWA----THMLGHELTAM-HGLDHAQTLAIVLPALWNEkrdTKRAKlLQYAERI 311
Cdd:cd08186 230 DLEARYWLLYAS------MI-AGIAIDNGllhlTHALEHPLSGLkPELPHGLGLALLGPAVVKY---IYKAV-PETLADI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 312 WNITEGSDDQRIDAAIAATRA---FFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTKLGEHQ---DITLEVSRRIYEA 385
Cdd:cd08186 299 LRPIVPGLKGTPDEAEKAARGveeFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLLLSLapvEVTEEVVREIYEE 378
|
.
gi 489934859 386 A 386
Cdd:cd08186 379 S 379
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-359 |
1.74e-39 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 144.58 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 4 FNLHTPTRILFGKGAIAELRDQIPQDA--RVLVTYGGGSVKkTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVK 79
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgkKALIVTDKGLVK-LGLVKKVTDVLEeaGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 80 IVRDEKVTFLLAVGGGSVLDGTKFIAaaaqyadgidpwrILETHGNDVT----------SAIPMGSVLTLPATGSESNSG 149
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIG-------------ILATNGGEIEdyegvdkskkPGLPLIAINTTAGTASEVTRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 150 AVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVT---YPvdgkIQDRFAEGILLTLVE 226
Cdd:cd08188 147 AVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVStgaTP----LTDALALEAIRLIAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 227 EGPKALQEPENYNVRANVMWA---ATQALNgliGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAK 303
Cdd:cd08188 223 NLPKAVANGKDLEARENMAYAqflAGMAFN---NAGLG---YVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPER 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489934859 304 LLQYAERIW-NITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:cd08188 297 FADIARALGeNTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAEN 353
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-364 |
2.92e-39 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 143.52 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQI--PQDARVLVTYGGGSVKKTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd08182 1 PVKIIFGPGALAELKDLLggLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKFIAAAAqYADGIDPWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFMTP 166
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALL-GSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 167 FVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQY--V-TYPVDGKIQDRFAEGILLTLveegPKALQEPENYNVRAN 243
Cdd:cd08182 160 SLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIwsVnANPESRAYALRAIRLILENL----PLLLENLPNLEAREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 244 VMWAATQAlnGLigagvpqdwA-----T---HMLGHELTAMHGLDHAQTLAIVLPALW--NEKRDTKRAKLLQYAEriwn 313
Cdd:cd08182 236 MAEASLLA--GL---------AisitkTtaaHAISYPLTSRYGVPHGHACALTLPAVLryNAGADDECDDDPRGRE---- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489934859 314 ITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHG 364
Cdd:cd08182 301 ILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPE 351
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-359 |
4.51e-39 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 143.41 E-value: 4.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDAR--VLVTygGGSVKKTGVLAQVQDALK--GLDVLEFGGI-EPNPsyETLMNAVKIVRD 83
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKraLLVT--GRSSLRSGRLARLLEALEaaGIEVALFSVSgEPTV--ETVDAAVALARE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAAQ-------YADGIDPWRILETHGndvtsaIPMGSVLTLPATGSESNSGAVISRKT 156
Cdd:cd08183 77 AGCDVVIAIGGGSVIDAAKAIAALLTnegsvldYLEVVGKGRPLTEPP------LPFIAIPTTAGTGSEVTKNAVLSSPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 157 TGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTypvdgkiqdRFAEgiLLT--LVEEG------ 228
Cdd:cd08183 151 HGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVS---------RKAN--PLTdaLAREGlrlaar 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 229 --PKALQEPENYNVRANVMWAAtqALNGLI----GAGvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WN----EK 296
Cdd:cd08183 220 slRRAYEDGEDLEAREDMALAS--LLGGLAlanaGLG-----AVHGLAGPLGGMFGAPHGAICAALLPPVleANlralRE 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489934859 297 RDTKRAKLLQYAErIWNITEGSDDQRIDAAIAATRAFFEQMGVPtRLSDYGLDGSSIPALLEK 359
Cdd:cd08183 293 REPDSPALARYRE-LAGILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEK 353
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-356 |
6.41e-37 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 137.60 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 8 TPTrILFGKGAIAELRDQIPQD--ARVL-VTygGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVR 82
Cdd:cd08189 5 EPE-LFEGAGSLLQLPEALKKLgiKRVLiVT--DKGLVKLGLLDPLLDALKkaGIEYVVFDGVVPDPTIDNVEEGLALYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 83 DEKVTFLLAVGGGSVLDGTKFIAAAAqyadgidpwrilethGNDVTSAIPMGSVL-----TLP--------ATGSESNSG 149
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAARA---------------ANPKKSVRKLKGLLkvrkkLPPliavpttaGTGSEATIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 150 AVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV-TYpvDGKIQDRFAE----GILLTL 224
Cdd:cd08189 147 AVITDPETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYIsRS--ATKETDEYALeavkLIFENL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 225 veegPKALQEPENYNVRANVMWAA-------TQALNGLIgagvpqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKR 297
Cdd:cd08189 225 ----PKAYEDGSDLEARENMLLASyyaglafTRAYVGYV----------HAIAHQLGGLYGVPHGLANAVVLPHVLEFYG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 298 DTKRAKLLQYAERIWNITEG-SDDQRIDAAIAATRAFFEQMGVPTRLSdyGLDGSSIPAL 356
Cdd:cd08189 291 PAAEKRLAELADAAGLGDSGeSDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPEI 348
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-386 |
7.53e-37 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 137.75 E-value: 7.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 6 LHTPTRILFGKGAiaelRDQIPQDARVLvtygGGSV--------KKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLM 75
Cdd:cd08191 1 LRSPSRLLFGPGA----RRALGRVAARL----GSRVlivtdprlASTPLVAELLAALTaaGVAVEVFDGGQPELPVSTVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 76 NAVKIVRDEKVTFLLAVGGGSVLDGTKFIAaaaqyadgidpwrILETHGNDVTS-----AIPmGSVLTLPA------TGS 144
Cdd:cd08191 73 DAAAAARAFDPDVVIGLGGGSNMDLAKVVA-------------LLLAHGGDPRDyygedRVP-GPVLPLIAvpttagTGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 145 ESNSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVD------------GK- 211
Cdd:cd08191 139 EVTPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPpfprldpdpvyvGKn 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 212 -IQDRFA-EGILLtLVEEGPKALQEPENYNVRANVMWAATQAlnGL-IG-AGVPqdwATHMLGHELTAMHGLDHAQTLAI 287
Cdd:cd08191 219 pLTDLLAlEAIRL-IGRHLPRAVRDGDDLEARSGMALAALLA--GLaFGtAGTA---AAHALQYPIGALTHTSHGVGNGL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 288 VLPALWNEKRDTKRAKLLQYAERIWNITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEklQAHGGTK 367
Cdd:cd08191 293 LLPYVMRFNRPARAAELAEIARALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAE--KALSVTR 370
|
410 420
....*....|....*....|.
gi 489934859 368 LGEHQDITLEVS--RRIYEAA 386
Cdd:cd08191 371 LIANNPRPPTEEdlLRILRAA 391
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-360 |
8.87e-32 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 123.41 E-value: 8.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIpqdAR------VLVTygGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKI 80
Cdd:cd08194 1 PRTIIIGGGALEELGEEA---ASlggkraLIVT--DKVMVKLGLVDKVTQLLAeaGIAYAVFDDVVSEPTDEMVEEGLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 81 VRDEKVTFLLAVGGGSVLDGTKfiAAAAQYADGiDPWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDK 160
Cdd:cd08194 76 YKEGGCDFIVALGGGSPIDTAK--AIAVLATNG-GPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVT---YPvdgkIQDRFAEGILLTLVEEGPKALQEPEN 237
Cdd:cd08194 153 MLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSrkaQP----LTDTLALSAIKLIGRNLRRAYADGDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 238 YNVRANVMWAATQAlnGL----------------IGA--GVPqdwathmlgheltamHGLDHAQTLAIVLpalwnekRDT 299
Cdd:cd08194 229 LEAREAMMLAALEA--GIafsnssvalvhgmsrpIGAlfHVP---------------HGLSNAMLLPAVT-------EFS 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489934859 300 KRAKLLQYAE--RIWNI--TEGSDDQRIDAAIAATRAFFEQMGVPTrLSDYGLDGSSIPALLEKL 360
Cdd:cd08194 285 LPGAPERYAEiaRAMGIatEGDSDEEAAEKLVEALERLCADLEIPT-LREYGIDEEEFEAALDKM 348
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
8-360 |
5.02e-30 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 119.21 E-value: 5.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 8 TPTRILFGKGAIAELRDQIPQDARVLVTYGGGSVKKtGVLAQVQDALKGLDVL--EFGGIEPNPSYETLMNAVKIVRDEK 85
Cdd:cd08178 2 VPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKL-GYVDKVLDVLEARGVEteVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 86 VTFLLAVGGGSVLD------------GTKFIAAAAQYADgI--DPWRILETHGNDVTSAIPmgsvlTLPATGSESNSGAV 151
Cdd:cd08178 81 PDVIIALGGGSAMDaakimwlfyehpETKFEDLAQRFMD-IrkRVYKFPKLGKKAKLVAIP-----TTSGTGSEVTPFAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 152 ISRKTTGDK--LA--FMTPFVqpvfAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV-TYPVDgkiqdrFAEGI----LL 222
Cdd:cd08178 155 ITDDKTGKKypLAdyALTPDM----AIVDPELVMTMPKRLTADTGIDALTHAIEAYVsVMASD------YTDGLalqaIK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 223 TLVEEGPKALQEPENYNVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEK 296
Cdd:cd08178 225 LIFEYLPRSYNNGNDIEAREKMHNAATIA--GMAFAnaflGI-----CHSLAHKLGAAFHIPHGRANAILLPHVirYNAT 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489934859 297 RD-TKRAKLLQ---------YAE--RIWNITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKL 360
Cdd:cd08178 298 DPpTKQAAFPQykyyvakerYAEiaDLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKL 373
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-358 |
7.87e-30 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 118.12 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQD--ARVLVTYGGGSVKKTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLgaSRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTK----FIAAAAQYADGIDPWRILETHGNDVTSaiPMGSVLTLPAT--GSESNSGAVISRKTTGDK 160
Cdd:cd08192 81 DLLVSLGGGSPIDAAKavalALAEDVTDVDQLDALEDGKRIDPNVTG--PTLPHIAIPTTlsGAEFTAGAGATDDDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPR-QVANGV--VDafvHTVEQY----VTYPVdgkiqDRFAEGILLTLVEEGPKALQ 233
Cdd:cd08192 159 QGFAHPELGPDAVILDPELTLHTPERlWLSTGIraVD---HAVETLcspqATPFV-----DALALKALRLLFEGLPRSKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 234 EPENYNVRANVM---WAATQALNGLIGAGvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYA 308
Cdd:cd08192 231 DPEDLEARLKCQlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPHGITSCIMLPAVlrFNAPVNAERQRLIARA 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489934859 309 ERIWNITEGSDDQRIDAAIAatrAFFEQMGVPTRLSDYGLDGSSIPALLE 358
Cdd:cd08192 306 LGLVTGGLGREAADAADAID---ALIRELGLPRTLRDVGVGRDQLEKIAE 352
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-386 |
3.67e-29 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 116.88 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 10 TRILFGKGAIAELrdqipqdARVLVTYGGGSV--------KKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVK 79
Cdd:cd08190 2 SNIRFGPGATREL-------GMDLKRLGAKKVlvvtdpglAKLGLVERVLESLEkaGIEVVVYDGVRVEPTDESFEEAIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 80 IVRDEKVTFLLAVGGGSVLDGTKfiaAAAQYAdgidpwrileTHGNDVTSAI---------PMGSVLTLPA------TGS 144
Cdd:cd08190 75 FAKEGDFDAFVAVGGGSVIDTAK---AANLYA----------THPGDFLDYVnapigkgkpVPGPLKPLIAipttagTGS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 145 ESNSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGK------------- 211
Cdd:cd08190 142 ETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARprpanpderpayq 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 212 ----IQDRFAEGILLTLVEEGPKALQEPENYNVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM----------- 276
Cdd:cd08190 222 gsnpISDVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVH---LPHAMAYPIAGLvkdyrppgypv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 277 ------HGLdhaqTLAIVLPA--LWNEKRDTKR----AKLLQYaeriwNITEGSDDQRIDAAIAATRAFFEQMGVPTRLS 344
Cdd:cd08190 299 dhphvpHGL----SVALTAPAvfRFTAPACPERhleaAELLGA-----DTSGASDRDAGEVLADALIKLMRDIGIPNGLS 369
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489934859 345 DYGLDGSSIPALLEK-LQAHGGTKLGeHQDITLEVSRRIYEAA 386
Cdd:cd08190 370 ALGYSEDDIPALVEGtLPQQRLLKLN-PRPVTEEDLEEIFEDA 411
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-359 |
8.99e-29 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 115.33 E-value: 8.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 12 ILFGKGAiaelRDQIPQDA------RVLVTYGGGsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRD 83
Cdd:cd17814 7 FIFGVGA----RKLAGRYAknlgarKVLVVTDPG-VIKAGWVDEVLDSLEaeGLEYVVFSDVTPNPRDFEVMEGAELYRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAAqyADGIDpwrILETHGNDVTSaIPMGSVLTLPAT-GSESNSG--AVISRKTTGDK 160
Cdd:cd17814 82 EGCDGIVAVGGGSPIDCAKGIGIVV--SNGGH---ILDYEGVDKVR-RPLPPLICIPTTaGSSADVSqfAIITDTERRVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 161 LAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFA-EGILLtLVEEGPKALQEPENYN 239
Cdd:cd17814 156 MAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVS-NASSPLTDLHAlEAIRL-ISENLPKAVADPDDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 240 VRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERI-WNI 314
Cdd:cd17814 234 AREKMMLASLQAglafSNASLG-------AVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMgLDV 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489934859 315 TEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEK 359
Cdd:cd17814 307 DGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKR 351
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-358 |
3.46e-27 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 111.17 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDA--RVLVTYGGGSVKKTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd14866 5 PLRLFSGRGALARLGRELDRLGarRALVVCGSSVGANPDLMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKfiAAAAQYADGIDPwRILETH---GNDVTSAIPMG------SVLTLPATGSESNSGAVISRKTt 157
Cdd:cd14866 85 DAVVAVGGGSAIVTAR--AASILLAEDRDV-RELCTRraeDGLMVSPRLDApklpifVVPTTPTTADVKAGSAVTDPPA- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 158 GDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEqyVTYPVDGkiqDRFAEGIL---LTLVEEGPKALQE 234
Cdd:cd14866 161 GQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVE--GLYSRHA---DPLADATLmhaLRLLADGLPRLAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 235 PENYNVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIWNI 314
Cdd:cd14866 236 DDDPAARADLVLAAVLAGYGTDHTGGG---VIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489934859 315 TEGSDDQrIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLE 358
Cdd:cd14866 313 DAGDEAS-AAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAE 355
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
7-386 |
2.11e-26 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 108.75 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 7 HTPTRILFGKGAIAELRDQIPQD--ARVL-VTYGGgsVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIV 81
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgaRRVLlVTDPG--LVKAGLADPALAALEaaGIAVTVFDDVVADPPEAVVEAAVEQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 82 RDEKVTFLLAVGGGSVLDGTKFIAAaaqYADGIDPWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVIsrkTTGD-- 159
Cdd:cd08193 80 REAGADGVIGFGGGSSMDVAKLVAL---LAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIV---TTGEte 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 160 KLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDGKIQDRFAEGILLTLVEEGPKALQEPENYN 239
Cdd:cd08193 154 KKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALAREALRLLGANLRRAVEDGSDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 240 VRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM----HGLDHAQTLAIVLpalwneKRDTKRAKLLqYAE--RIWN 313
Cdd:cd08193 234 AREAMLLGSMLAGQAFANAPVA---AVHALAYPLGGHfhvpHGLSNALVLPHVL------RFNLPAAEAL-YAElaRALL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489934859 314 ITEGSDDQRIDAA--IAATRAFFEQMGVPTRLSDYGLDGSSIPALLEklQAHGGTKLGEH--QDITLEVSRRIYEAA 386
Cdd:cd08193 304 PGLAFGSDAAAAEafIDALEELVEASGLPTRLRDVGVTEEDLPMLAE--DAMKQTRLLVNnpREVTEEDALAIYQAA 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-349 |
8.61e-26 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 106.04 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQipQDARVL-VTygGGSVKKTGVLAQVQDALKGL-DVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd08180 4 KTKIYSGEDSLERLKEL--KGKRVFiVT--DPFMVKSGMVDKVTDELDKSnEVEIFSDVVPDPSIEVVAKGLAKILEFKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKFIAA-AAQYADGIDPWRILethgndvtsAIPMGSvltlpATGSESNSGAVISRKTTGDKLAFMT 165
Cdd:cd08180 80 DTIIALGGGSAIDAAKAIIYfALKQKGNIKKPLFI---------AIPTTS-----GTGSEVTSFAVITDPEKGIKYPLVD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 166 PFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV-----TYpvdgkiQDRFAEGILLTLVEEGPKALQEPENYNV 240
Cdd:cd08180 146 DSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVstnanDF------TDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 241 RANVMWAATQA-----LNGLigaGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALwnekrdtkrakllqyaeriwnit 315
Cdd:cd08180 220 REKMHNASCMAgiafnNAGL---GI-----NHSLAHALGGRFHIPHGRANAILLPYV----------------------- 268
|
330 340 350
....*....|....*....|....*....|....
gi 489934859 316 egsddqrIDAAIAATRAFFEQMGVPTRLSDYGLD 349
Cdd:cd08180 269 -------IEFLIAAIRRLNKKLGIPSTLKELGID 295
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
39-356 |
7.21e-24 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 101.57 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 39 GSVKKTGVLAQVQDALKGLDVLE--FGGIEPNPSYETLMNAVKIVRDEKVTFLLAVGGGSVLDGTKFIAAAAqyADGIDp 116
Cdd:PRK09860 40 NMLTKLGMAGDVQKALEERNIFSviYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVA--ANGGD- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 117 wrILETHGNDVTSA--IPMGSVLTLPATGSESNSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVD 194
Cdd:PRK09860 117 --IRDYEGVDRSAKpqLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 195 AFVHTVEQYVTYPVDgKIQDRFAEGILLTLVEEGPKALQEPENYNVRANVMWAatQALNGLIGAGVPQDWaTHMLGHELT 274
Cdd:PRK09860 195 ALTHAIEAYVSIAAT-PITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYA--QFLAGMAFNNASLGY-VHAMAHQLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 275 AMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERIW-NITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSI 353
Cdd:PRK09860 271 GFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGvNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDF 350
|
...
gi 489934859 354 PAL 356
Cdd:PRK09860 351 AVL 353
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-351 |
1.88e-22 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 97.37 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 7 HTPTRILFGKGAIAELRDQIPQDAR--VLVTygGGSVKKTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVR 82
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYGSrfLLIT--DPVLKESGLADKIVSSLEkaGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 83 DEKVTFLLAVGGGSVLDGTKFIAAAAQYADGIDPWRILETHGNDvtsAIPMGSVLTLPATGSESNSGAVISRKTTGDKLA 162
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKK---PLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 163 FMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFAEGILLTLVEEGPKALQEPENYNVRA 242
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-KKSNFFSDALALKAIELVSENLDGALADPKNTPAEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 243 NVMWAAtqALNGLIGAGVPQDWAThMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAeRIWN--ITEGSDD 320
Cdd:cd14864 236 LLAQAG--CLAGLAASSSSPGLAT-ALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIA-RALGedVEGASPE 311
|
330 340 350
....*....|....*....|....*....|.
gi 489934859 321 QRIDAAIAATRAFFEQMGVPTRLSDYGLDGS 351
Cdd:cd14864 312 EAAIAAVEGVRRLIAQLNLPTRLKDLDLASS 342
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-349 |
2.33e-20 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 92.94 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDARVLVTYGGGSVKKtGVLAQVQDALK----GLDVLEFGGIEPNPSYETLMNAVKIVRDE 84
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDGKKRAFIVTDRFMVEL-GYVDKVTDVLKkrenGVEYEVFSEVEPDPTLSTVRKGAELMRSF 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 85 KVTFLLAVGGGSVLDGTK------------FIAAAAQYADgIDPwRI--LETHGNDVTS-AIPmgsvlTLPATGSESNSG 149
Cdd:PRK13805 539 KPDTIIALGGGSPMDAAKimwlfyehpetdFEDLAQKFMD-IRK-RIykFPKLGKKAKLvAIP-----TTSGTGSEVTPF 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 150 AVISRKTTGDK--LA--FMTPFVqpvfAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV-TYPVDgkiqdrFAEGILL-- 222
Cdd:PRK13805 612 AVITDDKTGVKypLAdyELTPDV----AIVDPNLVMTMPKSLTADTGIDALTHALEAYVsVMASD------YTDGLALqa 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 223 --TLVEEGPKALQE-PENYNVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--W 293
Cdd:PRK13805 682 ikLVFEYLPRSYKNgAKDPEAREKMHNASTIA--GMAFAnaflGI-----CHSMAHKLGAEFHIPHGRANAILLPHVirY 754
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489934859 294 NEKRDTKRAKLLQY---------AE--RIWNITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLD 349
Cdd:PRK13805 755 NATDPPKQAAFPQYeypraderyAEiaRHLGLPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVD 821
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
69-347 |
2.62e-19 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 88.55 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 69 PSYETLMNAVKIVRDEKVTFLLAVGGGSVLDGTKFIAAAAQyadgiDPWRILE--THGNDVTSAIPMGSVLTLPATGSES 146
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVT-----NPDSTLAemSETSVLQPRLPLIAIPTTAGTGSET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 147 NSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDgKIQDRFAEGILLTLVE 226
Cdd:PRK15454 165 TNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNAT-PFTDSLAIGAIAMIGK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 227 EGPKALQEPENYNVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQ 306
Cdd:PRK15454 244 SLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLG---LCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQ 320
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489934859 307 YAERIWNitEGSDDQRidaAIAATRAFFEQMGVPTRLSDYG 347
Cdd:PRK15454 321 IGRALRT--KKSDDRD---AINAVSELIAEVGIGKRLGDVG 356
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-386 |
3.95e-19 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 88.13 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 14 FGKGAIAELRDQIPQDA--RVLVTYGGGSVKkTGVLAQVQDALK--GLDVLEFGGIEPNPSYETLMNAVKIVRDEKVTFL 89
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGfkKALIVTDKTLVK-CGVVAKVTDVLDaaGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 90 LAVGGGSVLDGTKFIA---AAAQYADgidpWRILETHGNDVTSAIPMGSVLTLPATGSESNSGAVISRKTTGDKLAFMTP 166
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGiisNNPEFAD----VRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 167 FVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFA----EGI---LLTLVEEGPKALQEpenyn 239
Cdd:PRK10624 168 HDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-RGAWALTDMLHlkaiEIIagaLRGAVAGDKEAGEG----- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 240 vranvMwAATQALNGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WN-----EK-RDTKRAKLLqy 307
Cdd:PRK10624 242 -----M-ALGQYIAGMgfsnVGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHVmeYNadftgEKyRDIARAMGV-- 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489934859 308 aeriwNITEGSDDQRIDAAIAATRAFFEQMGVPTRLSDYGLDGSSIPALLEKLQAHGGTKlGEHQDITLEVSRRIYEAA 386
Cdd:PRK10624 309 -----KVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTG-GNPREATLEDIVELYKKA 381
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-355 |
2.54e-12 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 67.14 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQD--ARVLVTYGGGSvkkTGVLAQVQDALKGLDVLEFGGIEPNPSYETLMNAVKIVRDEKV 86
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLgaRRALVLSTPRQ---RALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 87 TFLLAVGGGSVLDGTKFIAaaaqyadgidpwrilethgndVTSAIPmgsVLTLPAT--GSE-------SNSGavisRKTT 157
Cdd:cd08177 78 DGLVAIGGGSAIGLAKAIA---------------------LRTGLP---IVAVPTTyaGSEmtpiwgeTEDG----VKTT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 158 GDklafmTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYvtYPVDgkiqdrfAEGILLTLVEEG--------P 229
Cdd:cd08177 130 GR-----DPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEAL--YAPD-------ANPITSLLAEEGiralaralP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 230 KALQEPENynvranvMWAATQALNGLIGAGVPQDWAT----HMLGHELTAMHGLDHAQTLAIVLP-ALWNEKRDTKRAkl 304
Cdd:cd08177 196 RLVADPSD-------LEARSDALYGAWLAGVVLGSVGmglhHKLCHVLGGTFDLPHAETHAVVLPhVLAYNAPAAPDA-- 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489934859 305 lqyAERIWNITEGSDdqridaAIAATRAFFEQMGVPTRLSDYGLDGSSIPA 355
Cdd:cd08177 267 ---MARLARALGGGD------AAGGLYDLARRLGAPTSLRDLGMPEDDIDR 308
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-387 |
1.71e-11 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 64.80 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQI-PQDARVLVTYGGGSVKKTGvlAQVQDALKG----LDVLEFGGiepNPSYETLMNAVKIVRD 83
Cdd:COG0371 6 PRRYVQGEGALDELGEYLaDLGKRALIITGPTALKAAG--DRLEESLEDagieVEVEVFGG---ECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAAQyadgidpwrilethgndvtsaIPMGSVLTLPATGSESNSGAVIsrKTTGDKLAF 163
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLG---------------------LPVVSVPTIASTDAPASPLSVI--YTEDGAFDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 164 MTPFVQPVFAVL-DpvytYTL----PPRQVANGVVDAFVHTVEQYVTYPVDGKIQDR--------FAEGILLTLVEEGPK 230
Cdd:COG0371 138 YSFLAKNPDLVLvD----TDIiakaPVRLLAAGIGDALAKWYEARDWSLAHRDLAGEyyteaavaLARLCAETLLEYGEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 231 ALQEPENYNVR---ANVMWAATqALNGLIGAGVPQDWAT---HMLGHELTAMHGLDHAQ--------TLAIvlpaLWNEK 296
Cdd:COG0371 214 AIKAVEAGVVTpalERVVEANL-LLSGLAMGIGSSRPGSgaaHAIHNGLTALPETHHALhgekvafgTLVQ----LVLEG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 297 RDTKRAKLlqyaeriwnitegsddqridaaiaatRAFFEQMGVPTRLSDYGLDGSSIPALL---EKLQAHGGTKLGEHQD 373
Cdd:COG0371 289 RPEEIEEL--------------------------LDFLRSVGLPTTLADLGLDDETEEELLtvaEAARPERYTILNLPFE 342
|
410
....*....|....
gi 489934859 374 ITLEvsrRIYEAAR 387
Cdd:COG0371 343 VTPE---AVEAAIL 353
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-105 |
4.86e-07 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 51.01 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDA---RVLVTYGGGSVKKTGvlAQVQDALKGLDVLEFggIEPNPSYETLMN---AVKIVR 82
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLlgkRALIITGPNTYKIAG--KRVEDLLESSGVEVV--IVDIATIEEAAEvekVKKLIK 77
|
90 100
....*....|....*....|...
gi 489934859 83 DEKVTFLLAVGGGSVLDGTKFIA 105
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAKYAA 100
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
62-234 |
1.47e-06 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 49.91 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 62 FGGIEPNpsyETLMNAV-KIVRDEKVTFLLAVGGGSVLDGTKFIAAAaqyadGIDPWRILETHGNDVTSAIPMGSVLTLP 140
Cdd:cd14860 57 YGTGEPS---DEMVEAIyKDIKKYGYKRVIAIGGGTVIDIAKLLALK-----GISPVLDLFDGKIPLIKEKELIIVPTTC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 141 ATGSESNSGAVISRKTTGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDGKIQDRFA--- 217
Cdd:cd14860 129 GTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLS-PKATPYTEMFSyka 207
|
170 180
....*....|....*....|.
gi 489934859 218 -EGIL---LTLVEEGPKALQE 234
Cdd:cd14860 208 iEMILegyQEIAEKGEEARFP 228
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-105 |
2.14e-06 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 49.12 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 7 HTPTRILFGKGAIAELRDQIPQ---DARVLVTYGggsvKKTGVLA--QVQDALKgldvlEFGGIE----PNPSYETLMNA 77
Cdd:PRK00843 9 QLPRDVVVGHGVLDDIGDVCSDlklTGRALIVTG----PTTKKIAgdRVEENLE-----DAGDVEvvivDEATMEEVEKV 79
|
90 100
....*....|....*....|....*...
gi 489934859 78 VKIVRDEKVTFLLAVGGGSVLDGTKFIA 105
Cdd:PRK00843 80 EEKAKDVNAGFLIGVGGGKVIDVAKLAA 107
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-201 |
6.46e-06 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 47.65 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQdarvLVTYGGGSV--------KKTGVLAQV----QDALKGLDVLEfggiEPNPSY-ETLM 75
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAE----RRKSNNDYVvffiddvfKGKPLLDRLplqnGDLLIFVDTTD----EPKTDQiDALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 76 NAVKIVRDEKVTFLLAVGGGSVLDGTKFIA-------AAAQYADgidpWRILETHGNDvTSAIPmgsvlTLPATGSESNS 148
Cdd:cd08184 73 AQIRAENDKLPAAVVGIGGGSTMDIAKAVSnmltnpgSAADYQG----WDLVKNPGIY-KIGVP-----TLSGTGAEASR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489934859 149 GAVISRKttGDKLAFMTPFVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVE 201
Cdd:cd08184 143 TAVLTGP--EKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE 193
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-352 |
9.46e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 47.15 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 9 PTRILFGKGAIAELRDQIPQDA-RVLVTYGGGSVKKTGvlAQVQDALK--GLD--VLEFGGiepNPSYETLMNAVKIVRD 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGkKALIIGGKTALEAVG--EKLEKSLEeaGIDyeVEVFGG---ECTEENIERLAEKAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 84 EKVTFLLAVGGGSVLDGTKFIAAAAQyadgidpwrilethgndvtsaIPMGSVLTLPATGSESNSGAVIsRKTTGDKLAF 163
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAKAVADRLG---------------------LPVVTVPTIAATCAAWSALSVL-YDEEGEFLGY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 164 MtPFVQPVFAVL-DPVYTYTLPPRQVANGVVDAFVHTVEqyvTYPVDGKIQDRFAEGILL--------TLVEEGPKALQE 234
Cdd:cd08550 134 S-LLKRSPDLVLvDTDIIAAAPVRYLAAGIGDTLAKWYE---ARPSSRGGPDDLALQAAVqlaklaydLLLEYGVQAVED 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489934859 235 PENYNVR--------ANVMWAatqALNGLIGAGVPQDWATHMLGHELTAM---HGLDHAQTLAIVLPALWnekrdtkrak 303
Cdd:cd08550 210 VRQGKVTpaledvvdAIILLA---GLVGSLGGGGCRTAAAHAIHNGLTKLpetHGTLHGEKVAFGLLVQL---------- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489934859 304 llqyaeriwnITEGSDDQRIDAAIaatrAFFEQMGVPTRLSDYGLDGSS 352
Cdd:cd08550 277 ----------ALEGRSEEEIEELI----EFLRRLGLPVTLEDLGLELTE 311
|
|
| |
