|
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: 827.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 1 MNNFNLHTPTRILFGKDAIADLRAQIPADARVLITYGGGSVKKTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKI 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 81 AREENITFLLAVGGGSVLDGTKFIAAAAHYADGIDPWHILETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDK 160
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
Cdd:PRK15138 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778416 321 ARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLEEHGMTHLGEHGDITLDVSRRIYEAAR 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: 694.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 1 MNNFNLHTPTRILFGKDAIADLRAQIPAD-ARVLITYGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNA 77
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYgKKVLLVYGGGSIKKNGLYDQVKAALKeaGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 78 VKIAREENITFLLAVGGGSVLDGTKFIAAAAHYaDGiDPWHILeTRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTT 157
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKY-DG-DPWDIL-TGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 158 GDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGILLTLIEEGPKALKEPEN 237
Cdd:COG1979 158 KEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 238 YDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWNITEG 317
Cdd:COG1979 238 YDARANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 318 SDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLEEHGMTHLGEHGDITLDVSRRIYEAAR 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: 552.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 3 NFNLHTPTRILFGKDAIADLRAQIPA-DARVLITYGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVK 79
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKKyGKKVLLVYGGGSIKKNGLYDRVVASLKeaGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 80 IAREENITFLLAVGGGSVLDGTKFIAAAAHYaDGiDPWHILeTRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGD 159
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKY-DG-DVWDFF-TGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 160 KQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGILLTLIEEGPKALKEPENYD 239
Cdd:cd08187 158 KLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 240 VRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWNIT-EGS 318
Cdd:cd08187 238 ARANLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDpGGD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495778416 319 DDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLEEHGMTHLGeHGDITLDVSRRIYE 384
Cdd:cd08187 318 DEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGG-FKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-356 |
7.54e-99 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 297.98 E-value: 7.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPA-DARVLITYGGGSVKkTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAREEN 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSLK-SGLLDKVLASLEeaGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 86 ITFLLAVGGGSVLDGTKFIAAAAHYadGIDPWHILETRgSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFMN 165
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTN--PGDVWDYLGGK-PLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 166 EHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTyPVNAKIQDRFAEGILLTLIEEGPKALKEPENYDVRANVM 245
Cdd:pfam00465 157 PKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-KGANPLTDALALEAIRLIAENLPRAVADGEDLEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 246 WAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWnitEGSDDARIDA 325
Cdd:pfam00465 236 LASTLAGLAFSNAGLG---AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG---EDSDEEAAEE 309
|
330 340 350
....*....|....*....|....*....|.
gi 495778416 326 AIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:pfam00465 310 AIEALRELLRELGLPTTLSELGVTEEDLDAL 340
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-361 |
1.88e-70 |
|
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: 222.24 E-value: 1.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRA-QIPADARVLITYGGGSVKktGVLDQVYSALD-GLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEiKRRGFDRALVVSDEGVVK--GVGEKVADSLKkGLAVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTKFIAAAAhyadgidpwhiletrgsdiKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFMne 166
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAALL-------------------NRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 167 HVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEqyvtypvnakiqdrfaegilltlieegpkalkepenydvRANVMW 246
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 247 AATQALNGLIgaGVPQDWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAkllqyaervwnitegsddarIDAA 326
Cdd:cd07766 179 AATLAGMGLF--ESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE--------------------PEAA 236
|
330 340 350
....*....|....*....|....*....|....*
gi 495778416 327 IEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLE 361
Cdd:cd07766 237 IEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-356 |
1.88e-69 |
|
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: 222.71 E-value: 1.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQI--PADARVLITYGGGsVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAREE 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELkaLGGKKVLLVTDPG-LVKAGLLDKVLESLKaaGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 85 NITFLLAVGGGSVLDGTKFIAAAAHYADGIDPWhilETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFM 164
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDY---EGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 165 NEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAkIQDRFA-EGIllTLIEEG-PKALKEPENYDVRA 242
Cdd:cd08551 157 SPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANP-ISDALAlEAI--RLIGKNlRRAVADGSDLEARE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 243 NVMWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWNITEG-SDDA 321
Cdd:cd08551 234 AMLLASLLAGIAFGNAGL---GAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGlSDEE 310
|
330 340 350
....*....|....*....|....*....|....*
gi 495778416 322 RIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:cd08551 311 AAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPEL 345
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
2-356 |
4.63e-64 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 209.21 E-value: 4.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 2 NNFNLHTPTRILFGKDAIADLRAQIPA--DARVLITyGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNA 77
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRlgAKRALIV-TDPGLAKLGLLDRVLDALEaaGIEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 78 VKIAREENITFLLAVGGGSVLDGTKfiAAAAHYADGIDPWHILETRGSDIKS----AIPmgsvlTLPATGSESNKGAVIS 153
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAK--AIALLATNPGDLEDYLGIKKVPGPPlpliAIP-----TTAGTGSEVTPFAVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 154 RKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNA-KIQDRFA-EGIllTLIEEG-PK 230
Cdd:COG1454 153 DPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVS--KGAnPLTDALAlEAI--RLIARNlPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 231 ALKEPENYDVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRakl 304
Cdd:COG1454 229 AVADGDDLEAREKMALASLLAgmafANAGLG-------AVHALAHPLGGLFHVPHGLANAILLPHVlrFNAPAAPER--- 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 495778416 305 lqYAE--RVWNITEG-SDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:COG1454 299 --YAEiaRALGLDVGlSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPEL 351
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-356 |
1.89e-55 |
|
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: 186.55 E-value: 1.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 7 HTPTRILFGKDAIADLRAQIPADA-RVLITYGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIARE 83
Cdd:cd08185 2 YQPTRILFGAGKLNELGEEALRPGkKALIVTGKGSSKKTGLLDRVKKLLEkaGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 84 ENITFLLAVGGGSVLDGTKFIAAAAhYADGIDPWHILETRGSDI--KSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQ 161
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMA-TNPGDIWDYIFGGTGKGPppEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 162 AFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNAK-IQDRFA-EGILLtLIEEGPKALKEPENYD 239
Cdd:cd08185 161 GIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYIS--KNANpFSDMLAlEAIRL-VAKYLPRAVKDGSDLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 240 VRANVMWAATQA--LNGLIGAGVPqdwatHMLGHELTAMHG-LDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVWNITE 316
Cdd:cd08185 238 AREKMAWASTLAgiVIANSGTTLP-----HGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAEASGLS 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 495778416 317 GSDDARidAAIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:cd08185 313 DAKAAE--DFIEALRKLLKDIGLDDLLSDLGVTEEDIPWL 350
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-358 |
2.40e-51 |
|
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: 175.80 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGkdaiADLRAQIPADA------RVLITYGGGsVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKI 80
Cdd:cd14863 5 LTPVIFG----AGAVEQIGELLkelgckKVLLVTDKG-LKKAGIVDKIIDLLEeaGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 81 AREENITFLLAVGGGSVLDGTKFIAAAAHYadGIDPWHILETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDK 160
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTN--PGPIIDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTyPVNAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
Cdd:cd14863 158 KSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-KLANPMTDALALQAIRLIVKNLPRAVKDGDNLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 241 RANVMWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQYAERVwNITEGS 318
Cdd:cd14863 237 RENMLLASNLAGIAFNNAGT---HIGHAIAHALGALYHIPHGLACALALPVVleFNAEAYPEKVKKIAKALGV-SFPGES 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 495778416 319 DDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLA 358
Cdd:cd14863 313 DEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAE 352
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-360 |
2.59e-51 |
|
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: 175.46 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 4 FNLHTPTRILFGKDAIADLR---AQIPADARVLITygGGSVKKTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKI 80
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPdiiKELGGKRGLLVT--DPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 81 AREENITFLLAVGGGSVLDGTKFIAAAAHYADGIDpwHILETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDK 160
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIE--DYLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYvtYPVNA-KIQDRFAEG----ILLTLieegPKALKEP 235
Cdd:cd08196 157 APLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAY--WSINHqPISDALALEaaklVLENL----EKAYNNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 236 ENYDVRANVMWAATQAlnGLigA-GVPQDWATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVwni 314
Cdd:cd08196 231 NDKEAREKMALASLLA--GL--AfSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL--- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 495778416 315 teGSDDarIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPaLLAKL 360
Cdd:cd08196 304 --GFKD--AEELADKIEELKKRIGLRTRLSELGITEEDLE-EIVEE 344
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-304 |
7.46e-49 |
|
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: 168.92 E-value: 7.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 6 LHTPTRILFGKDAIADLRAQIPADA-RVLITYGGGSVKKTGVLDQVYSALDGLDVRE--FGGIEPNPSYETLMNAVKIAR 82
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGkKALIVTGKHSAKKNGSLDDVTEALEENGIEYfiFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIAAAAHYADGIDPwhiLETRGSDiKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQA 162
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKDGDED---LFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 163 FMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNA-KIQDRFAEGILLTLIEEGPKALKEPENYDVR 241
Cdd:cd08181 157 FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLS--VKAtPLSDALALEALRLIGECLPNLLGDELDEEDR 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778416 242 ANVMWAATqaLNGLI----GAGVPqdwatHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKL 304
Cdd:cd08181 235 EKLMYAST--LAGMViaqtGTTLP-----HGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKV 294
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-349 |
3.55e-43 |
|
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: 154.27 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLrAQIPaDARVLITYGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd08179 5 PRDIYFGEGALEYL-KTLK-GKRAFIVTGGGSMKRNGFLDKVEDYLKeaGMEVKVFEGVEPDPSVETVEKGAEAMREFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTKfiAAAAHY-------ADGIDPWHILETRGSDIKSAIPMGSvltlpATGSESNKGAVISRKTTGD 159
Cdd:cd08179 83 DWIIAIGGGSVIDAAK--AMWVFYeypeltfEDALVPFPLPELRKKARFIAIPSTS-----GTGSEVTRASVITDTEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 160 KQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTyPVNAKIQDRFAEGILLTLIEEGPKALKEPENYD 239
Cdd:cd08179 156 KYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVS-TLANDFTDALALGAILDIFENLPKSYNGGKDLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 240 VRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQyaervwN 313
Cdd:cd08179 235 AREKMHNASCLAgmafSNSGLG-------IVHSMAHKGGAFFGIPHGLANAILLPYVieFNSKDPEARARYAA------L 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 495778416 314 ITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLD 349
Cdd:cd08179 302 LIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGID 337
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-356 |
5.02e-43 |
|
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: 153.85 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 4 FNLHTPTRILFGKDAIADLRAQI---PADARVLITYGGgsVKKTGVLDQVYSALDGL--DVREFGGIEPNPSYETLMNAV 78
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELarlGARRPLIVTDKG--LAAAGLLKKVEDALGDAieIVGVFDDVPPDSSVAVVNEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 79 KIAREENITFLLAVGGGSVLDGTKfiAAAAHYADGIDpwHILETRGSDIKSA--IPMGSVLTLPATGSESNKGAVISRKT 156
Cdd:cd14865 79 ARAREAGADGIIAVGGGSVIDTAK--GVNILLSEGGD--DLDDYGGANRLTRplKPLIAIPTTAGTGSEVTLVAVIKDEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 157 TGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAkIQDRFAEGILLTLIEEGPKALKEPE 236
Cdd:cd14865 155 KKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNP-ISDALALQAIRLISENLPKAVKNGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 237 NYDVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKR-AKLLQYAE 309
Cdd:cd14865 234 DLEARLALAIAATMAgiafSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVmrYNLDAAAERyAELALALA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495778416 310 RVWNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:cd14865 307 YGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAI 353
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-359 |
2.11e-41 |
|
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: 149.58 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPAD--ARVLI-TYGGgsVKKTGVLDQVYSAL--DGLDVREFGGIEPNPSYETLMNAVKIARE 83
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALgiRRPLLvTDPG--LAALGIVDRVLEALgaAGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 84 ENITFLLAVGGGSVLDGTKFIAAAAHYadGIDPWHILETRGSDIKSAIPMGSVLTLP---ATGSESNKGAVISRKTTGDK 160
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATH--PGPLWDYEDGEGGPAAITPAVPPLIAIPttaGTGSEVGRAAVITDDDTGRK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVtypvnAKIQDRFAEGILL---TLIEEG-PKALKEPE 236
Cdd:cd14861 159 KIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYL-----SPGFHPMADGIALeglRLISEWlPRAVADGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 237 NYDVRANVMWAATQA----LNGLiGagvpqdwATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERVw 312
Cdd:cd14861 234 DLEARGEMMMAALMGavafQKGL-G-------AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARAL- 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495778416 313 niteGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAK 359
Cdd:cd14861 305 ----GLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAEL 347
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
4-356 |
8.21e-41 |
|
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: 148.08 E-value: 8.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 4 FNLHTPTRILFGKDAIAdlraQIPADAR------VLITYGGGSVKkTGVLDQVYSALD--GLDVREFGGIEPNPSYETLM 75
Cdd:cd08176 1 NRFVLNPTSYFGWGAIE----EIGEEAKkrgfkkALIVTDKGLVK-FGIVDKVTDVLKeaGIAYTVFDEVKPNPTIENVM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 76 NAVKIAREENITFLLAVGGGSVLDGTKFIA-AAAHyaDGIDpwhILETRG-SDIKS-AIPMGSVLTLPATGSESNKGAVI 152
Cdd:cd08176 76 AGVAAYKESGADGIIAVGGGSSIDTAKAIGiIVAN--PGAD---VRSLEGvAPTKNpAVPIIAVPTTAGTGSEVTINYVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 153 SRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypvnaKIQDRFAEGILL---TLIEEG- 228
Cdd:cd08176 151 TDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-----KGAWELSDMLALkaiELIAKNl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 229 PKALKEPENYDVRANVMWAAT---QALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAVVLPALWnekRDTKRAKLL 305
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYiagMAFSN-VGLGI-----VHSMAHPLSAFYDTPHGVANAILLPYVM---EFNAPATGE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 495778416 306 QYAE--RVWNI--TEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:cd08176 297 KYRDiaRAMGVdtTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEAL 351
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-382 |
9.37e-39 |
|
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: 142.36 E-value: 9.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 1 MNNFNlhtPTRILFGKDAIADLrAQIPaDARVLITYGGGsVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAV 78
Cdd:cd14862 1 MWYFS---SPKIVFGEDALSHL-EQLS-GKRALIVTDKV-LVKLGLLKKVLKRLLqaGFEVEVFDEVEPEPPLETVLKGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 79 KIAREENITFLLAVGGGSVLDGTKfiAAAAHY-ADGIDPWHI--LETRGSDIKS---AIPmgsvlTLPATGSESNKGAVI 152
Cdd:cd14862 75 EAMREFEPDLIIALGGGSVMDAAK--AAWVLYeRPDLDPEDIspLDLLGLRKKAkliAIP-----TTSGTGSEATWAIVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 153 SRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNaKIQDRFAEGILLTLIEEGPKAL 232
Cdd:cd14862 148 TDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSN-DFSDALALKAIELIFKYLPRAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 233 KEPENYDVRANVMWAATQAlnGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQ 306
Cdd:cd14862 227 KDGDDLEAREKMHNAATIA--GLafgnSQAGL-----AHALGHSLGAVFHVPHGIAVGLFLPYVieFYAKVTDERYDLLK 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778416 307 YAERvwnitEGSDDA-RIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLEEHGMthlgehGDITLDVSRRI 382
Cdd:cd14862 300 LLGI-----EARDEEeALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAM------EDSCTITSPRP 365
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-358 |
1.36e-38 |
|
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: 141.98 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQI--PADARVLITYGGGSVKKTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd08182 1 PVKIIFGPGALAELKDLLggLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTKFIaAAAHYADGIDPWHILETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFMNE 166
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAI-AALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 167 HVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYvtYPVNA-KIQDRFA----EGILLTLieegPKALKEPENYDVR 241
Cdd:cd08182 160 SLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESI--WSVNAnPESRAYAlraiRLILENL----PLLLENLPNLEAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 242 ANVMWAATQAlnGLigagvpqdwA-----T---HMLGHELTAMHGLDHAQTLAVVLPALW--NEKRDTKRAKLLQYAErv 311
Cdd:cd08182 234 EAMAEASLLA--GL---------AisitkTtaaHAISYPLTSRYGVPHGHACALTLPAVLryNAGADDECDDDPRGRE-- 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495778416 312 wnITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLA 358
Cdd:cd08182 301 --ILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-386 |
3.40e-37 |
|
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: 138.17 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 10 TRILFGKDAIADLRAqIPADA---RVLITYGGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAREE 84
Cdd:cd08186 2 TTLYFGVGAIAKIKD-ILKDLgidKVIIVTGRSSYKKSGAWDDVEKALEenGIEYVVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 85 NITFLLAVGGGSVLDGTKFIAAAAHYADGIdPWHILETRGSDIKsAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFM 164
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLLAYGGKT-ARDLYGFRFAPER-ALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 165 NEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGIllTLIEEG-PKALKEPENYDVRAN 243
Cdd:cd08186 159 YDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAI--RLIAEYlPRALANPKDLEARYW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 244 VMWAAtqalngLIgAGVPQDWA----THMLGHELTAM-HGLDHAQTLAVVLPAL--WNEKRdtkRAKLLQYAER--VWNI 314
Cdd:cd08186 237 LLYAS------MI-AGIAIDNGllhlTHALEHPLSGLkPELPHGLGLALLGPAVvkYIYKA---VPETLADILRpiVPGL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495778416 315 TEGSDDAriDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPallaKLEEHGMTHLGEHG-------DITLDVSRRIYEAA 386
Cdd:cd08186 307 KGTPDEA--EKAARGVEEFLFSVGFTEKLSDYGFTEDDVD----RLVELAFTTPSLDLllslapvEVTEEVVREIYEES 379
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-359 |
2.36e-36 |
|
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: 136.09 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPADAR--VLITygGGSVKKTGVLDQVYSAL--DGLDVREFGGI-EPNPsyETLMNAVKIARE 83
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKraLLVT--GRSSLRSGRLARLLEALeaAGIEVALFSVSgEPTV--ETVDAAVALARE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 84 ENITFLLAVGGGSVLDGTKfiAAAAHYADGIDPWHILETRGSDIK---SAIPMGSVLTLPATGSESNKGAVISRKTTGDK 160
Cdd:cd08183 77 AGCDVVIAIGGGSVIDAAK--AIAALLTNEGSVLDYLEVVGKGRPltePPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAkIQDRFA-EGIllTLIEEG-PKALKEPENY 238
Cdd:cd08183 155 VSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANP-LTDALArEGL--RLAARSlRRAYEDGEDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 239 DVRANVMWAAtqALNGLI----GAGvpqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WN----EKRDTKRAKLLQYA 308
Cdd:cd08183 232 EAREDMALAS--LLGGLAlanaGLG-----AVHGLAGPLGGMFGAPHGAICAALLPPVleANlralREREPDSPALARYR 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 495778416 309 ErVWNITEGSDDARIDAAIEATRSFFEGLGVPtRLSGYGLDGSSIPALLAK 359
Cdd:cd08183 305 E-LAGILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEK 353
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-359 |
5.26e-35 |
|
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: 132.25 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 4 FNLHTPTRILFGKDAIADLRAQIPADA--RVLITYGGGSVKkTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVK 79
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgkKALIVTDKGLVK-LGLVKKVTDVLEeaGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 80 IAREENITFLLAVGGGSVLDGTKFIAaaahyadgidpwhILETRGSDI----------KSAIPMGSVLTLPATGSESNKG 149
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIG-------------ILATNGGEIedyegvdkskKPGLPLIAINTTAGTASEVTRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 150 AVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNA-KIQDRFA-EGIllTLIEE 227
Cdd:cd08188 147 AVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVS--TGAtPLTDALAlEAI--RLIAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 228 G-PKALKEPENYDVRANVMWA---ATQALNgliGAGVPqdwATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAK 303
Cdd:cd08188 223 NlPKAVANGKDLEARENMAYAqflAGMAFN---NAGLG---YVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPER 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 495778416 304 LLQYAERVW-NITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAK 359
Cdd:cd08188 297 FADIARALGeNTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAEN 353
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-359 |
1.61e-32 |
|
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: 125.80 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 6 LHTPTRILFGKDAIADL---------RAQIPADARVLitygggsvkKTGVLDQVYSALD--GLDVREFGGIEPNPSYETL 74
Cdd:cd08191 1 LRSPSRLLFGPGARRALgrvaarlgsRVLIVTDPRLA---------STPLVAELLAALTaaGVAVEVFDGGQPELPVSTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 75 MNAVKIAREENITFLLAVGGGSVLDGTKFIAAA-AHyadGIDPWHILetrgSDIKSAIPMGSVLTLP---ATGSESNKGA 150
Cdd:cd08191 72 ADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLlAH---GGDPRDYY----GEDRVPGPVLPLIAVPttaGTGSEVTPVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 151 VISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNA--------------KIQDRF 216
Cdd:cd08191 145 VLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPfprldpdpvyvgknPLTDLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 217 A-EGIllTLIEEG-PKALKEPENYDVRANVMWAATQAlnGL-IG-AGVPqdwATHMLGHELTAMHGLDHAQTLAVVLPAL 292
Cdd:cd08191 225 AlEAI--RLIGRHlPRAVRDGDDLEARSGMALAALLA--GLaFGtAGTA---AAHALQYPIGALTHTSHGVGNGLLLPYV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495778416 293 WNEKRDTKRAKLLQYAERVWNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAK 359
Cdd:cd08191 298 MRFNRPARAAELAEIARALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEK 364
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-356 |
3.69e-32 |
|
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: 124.50 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 8 TPTrILFGKDAIADLRAQIPAD--ARVLITYGGGSVKkTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIARE 83
Cdd:cd08189 5 EPE-LFEGAGSLLQLPEALKKLgiKRVLIVTDKGLVK-LGLLDPLLDALKkaGIEYVVFDGVVPDPTIDNVEEGLALYKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 84 ENITFLLAVGGGSVLDGTKFIAAAAHyadgiDPWHILET-RGSD--IKSAIPMGSVLTLPATGSESNKGAVISRKTTGDK 160
Cdd:cd08189 83 NGCDAIIAIGGGSVIDCAKVIAARAA-----NPKKSVRKlKGLLkvRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYV-TYpvNAKIQDRFAEgILLTLIEEG-PKALKEPENY 238
Cdd:cd08189 158 YAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYIsRS--ATKETDEYAL-EAVKLIFENlPKAYEDGSDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 239 DVRANVMWAA-------TQALNGLIgagvpqdwatHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERV 311
Cdd:cd08189 235 EARENMLLASyyaglafTRAYVGYV----------HAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495778416 312 WnITEGSDDARIDAA--IEATRSFFEGLGVPTRLSgyGLDGSSIPAL 356
Cdd:cd08189 305 G-LGDSGESDSEKAEafIAAIRELNRRMGIPTTLE--ELKEEDIPEI 348
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-360 |
3.65e-31 |
|
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: 121.87 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIpADA---RVLITYGGGSVKkTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIARE 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEA-ASLggkRALIVTDKVMVK-LGLVDKVTQLLAeaGIAYAVFDDVVSEPTDEMVEEGLALYKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 84 ENITFLLAVGGGSVLDGTKFIAAAA----HYADgidpwhiLETRGSDIKSAIPMGSVLTLPATGSESNKGAVISRKTTGD 159
Cdd:cd08194 79 GGCDFIVALGGGSPIDTAKAIAVLAtnggPIRD-------YMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 160 KQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNA-KIQDRFA----EGILLTLieegPKALKE 234
Cdd:cd08194 152 KMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVS--RKAqPLTDTLAlsaiKLIGRNL----RRAYAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 235 PENYDVRANVMWAATQAlnGL----------------IGA--GVPqdwathmlgheltamHGLDHAQTLAVVLpalwnek 296
Cdd:cd08194 226 GDDLEAREAMMLAALEA--GIafsnssvalvhgmsrpIGAlfHVP---------------HGLSNAMLLPAVT------- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495778416 297 RDTKRAKLLQYAE--RVWNI--TEGSDDARIDAAIEATRSFFEGLGVPTrLSGYGLDGSSIPALLAKL 360
Cdd:cd08194 282 EFSLPGAPERYAEiaRAMGIatEGDSDEEAAEKLVEALERLCADLEIPT-LREYGIDEEEFEAALDKM 348
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-359 |
2.81e-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: 116.49 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 12 ILFGKDAI-------ADLRAQipadaRVLITYGGGsVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAR 82
Cdd:cd17814 7 FIFGVGARklagryaKNLGAR-----KVLVVTDPG-VIKAGWVDEVLDSLEaeGLEYVVFSDVTPNPRDFEVMEGAELYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIAAAAHyadgiDPWHILETRGSDiKSAIPMGSVLTLPAT-GSESN--KGAVISRKTTGD 159
Cdd:cd17814 81 EEGCDGIVAVGGGSPIDCAKGIGIVVS-----NGGHILDYEGVD-KVRRPLPPLICIPTTaGSSADvsQFAIITDTERRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 160 KQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypvNAK--IQDRFA-EGILLtLIEEGPKALKEPE 236
Cdd:cd17814 155 KMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVS---NASspLTDLHAlEAIRL-ISENLPKAVADPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 237 NYDVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLLQYAERV- 311
Cdd:cd17814 231 DLEAREKMMLASLQAglafSNASLG-------AVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMg 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 495778416 312 WNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPaLLAK 359
Cdd:cd17814 304 LDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIP-ELAK 350
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-356 |
9.91e-29 |
|
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: 115.04 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPAD--ARVLITYGGGSVKKTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLgaSRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTK----FIAAAAHYADGIDPWHILETRGSDIKSaiPMGSVLTLPAT--GSESNKGAVISRKTTGDK 160
Cdd:cd08192 81 DLLVSLGGGSPIDAAKavalALAEDVTDVDQLDALEDGKRIDPNVTG--PTLPHIAIPTTlsGAEFTAGAGATDDDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPAR-QVANGV--VDafvHTVEQYvtYPVNAK-IQDRFAEGILLTLIEEGPKALKEPE 236
Cdd:cd08192 159 QGFAHPELGPDAVILDPELTLHTPERlWLSTGIraVD---HAVETL--CSPQATpFVDALALKALRLLFEGLPRSKADPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 237 NYDVRANVM---WAATQALNGLIGAGvpqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQYAERV 311
Cdd:cd08192 234 DLEARLKCQlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPHGITSCIMLPAVlrFNAPVNAERQRLIARALGL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 495778416 312 WNITEGSDDARIDAAIEAtrsFFEGLGVPTRLSGYGLDGSSIPAL 356
Cdd:cd08192 309 VTGGLGREAADAADAIDA---LIRELGLPRTLRDVGVGRDQLEKI 350
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-386 |
2.02e-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: 111.55 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQI--PADARVLITYGGGSVKKTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd14866 5 PLRLFSGRGALARLGRELdrLGARRALVVCGSSVGANPDLMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTKfiAAAAHYADGIDPWHILETRGSDIKS--------AIPMGSVLTLPATGSESNKGAVISRKtTG 158
Cdd:cd14866 85 DAVVAVGGGSAIVTAR--AASILLAEDRDVRELCTRRAEDGLMvsprldapKLPIFVVPTTPTTADVKAGSAVTDPP-AG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 159 DKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAkiqdrFAEGIL---LTLIEEGPKALKEP 235
Cdd:cd14866 162 QRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADP-----LADATLmhaLRLLADGLPRLADD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 236 ENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQYAERVWn 313
Cdd:cd14866 237 DDPAARADLVLAAVLAGYGTDHTGGG---VIHALGHAIGARYGVQNGVVHAILLPHVlrFNAPATDGRLDRLAEALGVA- 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495778416 314 itEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPALLAKLEEHGMTHLGEHGDITLDVSRRIYEAA 386
Cdd:cd14866 313 --DAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVPTAEELEALLEAA 383
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-356 |
9.20e-27 |
|
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: 110.33 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 10 TRILFGKDAIADLraqipadARVLITYGGGSV--------KKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVK 79
Cdd:cd08190 2 SNIRFGPGATREL-------GMDLKRLGAKKVlvvtdpglAKLGLVERVLESLEkaGIEVVVYDGVRVEPTDESFEEAIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 80 IAREENITFLLAVGGGSVLDGTKfiaAAAHYAdgidpwhileTRGSDI---------KSAIPMGSVLTLPA------TGS 144
Cdd:cd08190 75 FAKEGDFDAFVAVGGGSVIDTAK---AANLYA----------THPGDFldyvnapigKGKPVPGPLKPLIAipttagTGS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 145 ESNKGAVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAK------------- 211
Cdd:cd08190 142 ETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARprpanpderpayq 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 212 ----IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM--------HGL 279
Cdd:cd08190 222 gsnpISDVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVH---LPHAMAYPIAGLvkdyrppgYPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 280 DHAQT---LAVVLPA----LWNEKRDTKR----AKLLQYaervwNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGL 348
Cdd:cd08190 299 DHPHVphgLSVALTApavfRFTAPACPERhleaAELLGA-----DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGY 373
|
....*...
gi 495778416 349 DGSSIPAL 356
Cdd:cd08190 374 SEDDIPAL 381
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
8-362 |
2.75e-26 |
|
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: 108.81 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 8 TPTRILFGKDAIADLRAQIPADARVLITYGGGSVKKtGVLDQVYSAL--DGLDVREFGGIEPNPSYETLMNAVKIAREEN 85
Cdd:cd08178 2 VPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKL-GYVDKVLDVLeaRGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 86 ITFLLAVGGGSVLD------------GTKFIAAAAHYADGIDPWHILETRGSDIK-SAIPmgsvlTLPATGSESNKGAVI 152
Cdd:cd08178 81 PDVIIALGGGSAMDaakimwlfyehpETKFEDLAQRFMDIRKRVYKFPKLGKKAKlVAIP-----TTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 153 SRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGILLtLIEEGPKAL 232
Cdd:cd08178 156 TDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKL-IFEYLPRSY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 233 KEPENYDVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRD-TKRAKLL 305
Cdd:cd08178 235 NNGNDIEAREKMHNAATIA--GMAFAnaflGI-----CHSLAHKLGAAFHIPHGRANAILLPHVirYNATDPpTKQAAFP 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495778416 306 QYAERV-----------WNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSsipALLAKLEE 362
Cdd:cd08178 308 QYKYYVakeryaeiadlLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEA---DFLAAVDK 372
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
7-386 |
7.36e-24 |
|
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: 101.43 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 7 HTPTRILFGKDAIADLRAQIPAD--ARVLITYGGGsVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAR 82
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgaRRVLLVTDPG-LVKAGLADPALAALEaaGIAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIAAAAHYADGIDpwhilETRGSDIKSA--IPMGSVLTLPATGSESNKGAVIsrkTTGD- 159
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVALLAGSDQPLD-----DIYGVGKATGprLPLILVPTTAGTGSEVTPISIV---TTGEt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 160 -KQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTYPVNAKIQDRFAEGILLTLIEEGPKALKEPENY 238
Cdd:cd08193 153 eKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALAREALRLLGANLRRAVEDGSDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 239 DVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM----HGLDHAQTLAVVLpalwneKRDTKRAKLLqYAERVWNI 314
Cdd:cd08193 233 EAREAMLLGSMLAGQAFANAPVA---AVHALAYPLGGHfhvpHGLSNALVLPHVL------RFNLPAAEAL-YAELARAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 315 ----TEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSSIPallaKLEEHGM--THLGEH--GDITLDVSRRIYEAA 386
Cdd:cd08193 303 lpglAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLP----MLAEDAMkqTRLLVNnpREVTEEDALAIYQAA 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-290 |
1.11e-22 |
|
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: 97.56 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQipADARVLItygggsV-----KKTGVLDQVYSALDGL-DVREFGGIEPNPSYETLMNAVKIAR 82
Cdd:cd08180 4 KTKIYSGEDSLERLKEL--KGKRVFI------VtdpfmVKSGMVDKVTDELDKSnEVEIFSDVVPDPSIEVVAKGLAKIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIAAAAHYADGI--DPWHIletrgsdiksAIPMGSvltlpATGSESNKGAVISRKTTGDK 160
Cdd:cd08180 76 EFKPDTIIALGGGSAIDAAKAIIYFALKQKGNikKPLFI----------AIPTTS-----GTGSEVTSFAVITDPEKGIK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 161 QAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNAK-IQDRFAEGILLTLIEEGPKALKEPENYD 239
Cdd:cd08180 141 YPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVS--TNANdFTDALAEKAIKLVFENLPRAYRDGDDLE 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495778416 240 VRANVMWAATQA-----LNGLigaGVpqdwaTHMLGHELTAMHGLDHAQTLAVVLP 290
Cdd:cd08180 219 AREKMHNASCMAgiafnNAGL---GI-----NHSLAHALGGRFHIPHGRANAILLP 266
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
39-356 |
3.69e-22 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 96.95 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 39 GSVKKTGVLDQVYSALDGLDVRE--FGGIEPNPSYETLMNAVKIAREENITFLLAVGGGSVLDGTKFIAAAAhyADGIDp 116
Cdd:PRK09860 40 NMLTKLGMAGDVQKALEERNIFSviYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVA--ANGGD- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 117 whILETRGSD--IKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVD 194
Cdd:PRK09860 117 --IRDYEGVDrsAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 195 AFVHTVEQYVTYPVNAkIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAatQALNGLIGAGVPQDWaTHMLGHELT 274
Cdd:PRK09860 195 ALTHAIEAYVSIAATP-ITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYA--QFLAGMAFNNASLGY-VHAMAHQLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 275 AMHGLDHAQTLAVVLPAL--WNEKRDTKRAKLLQYAERVwNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSS 352
Cdd:PRK09860 271 GFYNLPHGVCNAVLLPHVqvFNSKVAAARLRDCAAAMGV-NVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEED 349
|
....
gi 495778416 353 IPAL 356
Cdd:PRK09860 350 FAVL 353
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-362 |
5.48e-21 |
|
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: 93.13 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 7 HTPTRILFGKDAIADLRAQIPADAR--VLITygGGSVKKTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAR 82
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYGSrfLLIT--DPVLKESGLADKIVSSLEkaGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIAAAAHYADGIDPWHILETRGsdiKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQA 162
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPK---KKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 163 FMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTyPVNAKIQDRFAEGILLTLIEEGPKALKEPENYDVRA 242
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-KKSNFFSDALALKAIELVSENLDGALADPKNTPAEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 243 NVMWAAtqALNGLIGAGVPQDWAThMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKL--LQYAERVwNITEGSDD 320
Cdd:cd14864 236 LLAQAG--CLAGLAASSSSPGLAT-ALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYakIARALGE-DVEGASPE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 495778416 321 ARIDAAIEATRSFFEGLGVPTRLSGYGLDgSSIPALLAKLEE 362
Cdd:cd14864 312 EAAIAAVEGVRRLIAQLNLPTRLKDLDLA-SSLEQLAAIAED 352
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-362 |
2.03e-19 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 90.24 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPADARVLITYGGGSVKKtGVLDQVYSALD----GLDVREFGGIEPNPSYETLMNAVKIAREE 84
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDGKKRAFIVTDRFMVEL-GYVDKVTDVLKkrenGVEYEVFSEVEPDPTLSTVRKGAELMRSF 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 85 NITFLLAVGGGSVLDGTKFI-----AAAAHYADgidpwhiLETRGSDIKSAI----PMG------SVLTLPATGSESNKG 149
Cdd:PRK13805 539 KPDTIIALGGGSPMDAAKIMwlfyeHPETDFED-------LAQKFMDIRKRIykfpKLGkkaklvAIPTTSGTGSEVTPF 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 150 AVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNAkiqDRFAEGILL----TLI 225
Cdd:PRK13805 612 AVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVS--VMA---SDYTDGLALqaikLVF 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 226 EEGPKALKE-PENYDVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAVVLPAL--WNEKRD 298
Cdd:PRK13805 687 EYLPRSYKNgAKDPEAREKMHNASTIA--GMAFAnaflGI-----CHSMAHKLGAEFHIPHGRANAILLPHVirYNATDP 759
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495778416 299 TKRAKLLQY---------AE--RVWNITEGSDDARIDAAIEATRSFFEGLGVPTRLSGYGLDGSsipALLAKLEE 362
Cdd:PRK13805 760 PKQAAFPQYeypraderyAEiaRHLGLPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEA---DFLAKLDE 831
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
69-347 |
3.02e-18 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 85.46 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 69 PSYETLMNAVKIAREENITFLLAVGGGSVLDGTKFIAAAAhyadgIDPWHILE--TRGSDIKSAIPMGSVLTLPATGSES 146
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLV-----TNPDSTLAemSETSVLQPRLPLIAIPTTAGTGSET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 147 NKGAVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTypVNAK-IQDRFAEGILLTLI 225
Cdd:PRK15454 165 TNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSA--LNATpFTDSLAIGAIAMIG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 226 EEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAVVLPALWNEKRDTKRAKLL 305
Cdd:PRK15454 243 KSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLG---LCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFS 319
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 495778416 306 QYAERVWNitEGSDDARidaAIEATRSFFEGLGVPTRLSGYG 347
Cdd:PRK15454 320 QIGRALRT--KKSDDRD---AINAVSELIAEVGIGKRLGDVG 356
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
43-356 |
2.14e-17 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 82.74 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 43 KTGVLDQVYSALD--GLDVREFGGIEPNPSYETLMNAVKIAREENITFLLAVGGGSVLDGTKFIA---AAAHYAD----- 112
Cdd:PRK10624 43 KCGVVAKVTDVLDaaGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGiisNNPEFADvrsle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 113 GIDPwhileTRgsdiKSAIPMGSVLTLPATGSESNKGAVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGV 192
Cdd:PRK10624 123 GVAP-----TK----KPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 193 VDAFVHTVEQYVTyPVNAKIQDRFAegilLTLIEEGPKALKEPENYDVRANVMWAATQALNGL----IGAGVpqdwaTHM 268
Cdd:PRK10624 194 VDALTHAIEGYIT-RGAWALTDMLH----LKAIEIIAGALRGAVAGDKEAGEGMALGQYIAGMgfsnVGLGL-----VHG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 269 LGHELTAMHGLDHAQTLAVVLPAL--WN-----EK-RDTKRAkllqYAERVWNITEgsDDARiDAAIEATRSFFEGLGVP 340
Cdd:PRK10624 264 MAHPLGAFYNTPHGVANAILLPHVmeYNadftgEKyRDIARA----MGVKVEGMSL--EEAR-NAAVEAVKALNRDVGIP 336
|
330
....*....|....*.
gi 495778416 341 TRLSGYGLDGSSIPAL 356
Cdd:PRK10624 337 PHLRDVGVKEEDIPAL 352
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-355 |
9.16e-10 |
|
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: 59.44 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPAD--ARVLITYGGGSvkkTGVLDQVYSALDGLDVREFGGIEPNPSYETLMNAVKIAREENI 86
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLgaRRALVLSTPRQ---RALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 87 TFLLAVGGGSVLDGTKFIAaaahyadgidpwhiLETRGSDIksAIPM---GSVLTlPATGsESNKGavisRKTTGDKQAf 163
Cdd:cd08177 78 DGLVAIGGGSAIGLAKAIA--------------LRTGLPIV--AVPTtyaGSEMT-PIWG-ETEDG----VKTTGRDPR- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 164 mnehVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYvtYPVNAK-IQDRFAEGILLTLIEEGPKALKEPENYDVRA 242
Cdd:cd08177 135 ----VLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEAL--YAPDANpITSLLAEEGIRALARALPRLVADPSDLEARS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 243 NVMWAATqalngLigAGVPQDWAT----HMLGHELTAMHGLDHAQTLAVVLP-ALWNEKRDTKRAkllqyAERVWNITEG 317
Cdd:cd08177 209 DALYGAW-----L--AGVVLGSVGmglhHKLCHVLGGTFDLPHAETHAVVLPhVLAYNAPAAPDA-----MARLARALGG 276
|
330 340 350
....*....|....*....|....*....|....*...
gi 495778416 318 SDdaridaAIEATRSFFEGLGVPTRLSGYGLDGSSIPA 355
Cdd:cd08177 277 GD------AAGGLYDLARRLGAPTSLRDLGMPEDDIDR 308
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
60-234 |
5.74e-08 |
|
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: 54.14 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 60 REFGGIEPNpsyETLMNAV-KIAREENITFLLAVGGGSVLDGTKFIAAAahyadGIDPWHILETRGSDIKSAIPMGSVLT 138
Cdd:cd14860 55 EKYGTGEPS---DEMVEAIyKDIKKYGYKRVIAIGGGTVIDIAKLLALK-----GISPVLDLFDGKIPLIKEKELIIVPT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 139 LPATGSESNKGAVISRKTTGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVEQYVTyPVNAKIQDRFA- 217
Cdd:cd14860 127 TCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLS-PKATPYTEMFSy 205
|
170 180
....*....|....*....|...
gi 495778416 218 ---EGIL---LTLIEEGPKALKE 234
Cdd:cd14860 206 kaiEMILegyQEIAEKGEEARFP 228
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-142 |
8.76e-08 |
|
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: 53.63 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQI-PADARVLITYGGGSVKKTGvlDQVYSALDG----LDVREFGGiepNPSYETLMNAVKIARE 83
Cdd:COG0371 6 PRRYVQGEGALDELGEYLaDLGKRALIITGPTALKAAG--DRLEESLEDagieVEVEVFGG---ECSEEEIERLAEEAKE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 495778416 84 ENITFLLAVGGGSVLDGTKfiaAAAHYADgidpwhiletrgsdiksaIPMGSVLTLPAT 142
Cdd:COG0371 81 QGADVIIGVGGGKALDTAK---AVAYRLG------------------LPVVSVPTIAST 118
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-114 |
5.46e-07 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 51.05 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 7 HTPTRILFGKDAIADLRA---QIPADARVLITYGGGSVKKTGvlDQVYSAL-DGLDVREFggIEPNPSYETLMNAVKIAR 82
Cdd:PRK00843 9 QLPRDVVVGHGVLDDIGDvcsDLKLTGRALIVTGPTTKKIAG--DRVEENLeDAGDVEVV--IVDEATMEEVEKVEEKAK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIA------------AAAHyaDGI 114
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAAyrlgipfisvptAASH--DGI 126
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-114 |
1.74e-06 |
|
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: 49.47 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQIPADA---RVLITYGGGSVKKTGvlDQVYSALDGLDVREFggIEPNPSYETLMN---AVKIAR 82
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLlgkRALIITGPNTYKIAG--KRVEDLLESSGVEVV--IVDIATIEEAAEvekVKKLIK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495778416 83 EENITFLLAVGGGSVLDGTKFIA------------AAAHyaDGI 114
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAKYAAyklnlpfisiptSASH--DGI 119
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-112 |
1.28e-04 |
|
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: 43.68 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 9 PTRILFGKDAIADLRAQI-PADARVLITYGGGSVKKTGvlDQVYSALD--GLDVR--EFGGiepNPSYETLMNAVKIARE 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIaPLGKKALIIGGKTALEAVG--EKLEKSLEeaGIDYEveVFGG---ECTEENIERLAEKAKE 75
|
90 100
....*....|....*....|....*....
gi 495778416 84 ENITFLLAVGGGSVLDGTKfiaAAAHYAD 112
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAK---AVADRLG 101
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
66-201 |
4.58e-04 |
|
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: 41.87 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495778416 66 EPNPSY-ETLMNAVKIAREENITFLLAVGGGSVLDGTKFIA-------AAAHYADgidpWHILETRGSDiKSAIPmgsvl 137
Cdd:cd08184 62 EPKTDQiDALRAQIRAENDKLPAAVVGIGGGSTMDIAKAVSnmltnpgSAADYQG----WDLVKNPGIY-KIGVP----- 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495778416 138 TLPATGSESNKGAVISRKttGDKQAFMNEHVQPVFAILDPVYTYTLPARQVANGVVDAFVHTVE 201
Cdd:cd08184 132 TLSGTGAEASRTAVLTGP--EKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE 193
|
|
| |
