|
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: 837.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 1 MNNFNLHTPTRILFGKGAIAGLREQIPHDARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKL 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 81 VREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDK 160
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLTLIEDGPKALKEPENYDV 240
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
Cdd:PRK15138 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446981546 321 ERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTQLGENHDITLDVSRRIYEAAR 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 446981546 1 MNNFNLHTPTRILFGKGAIAGLREQIPHD-ARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNA 77
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYgKKVLLVYGGGSIKKNGLYDQVKAALKeaGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 78 VKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILqTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTT 157
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDG--DPWDIL-TGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 158 GDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLTLIEDGPKALKEPEN 237
Cdd:COG1979 158 KEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 238 YDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEG 317
Cdd:COG1979 238 YDARANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 318 SDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTQLGENHDITLDVSRRIYEAAR 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: 568.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 3 NFNLHTPTRILFGKGAIAGLREQIP-HDARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVK 79
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKkYGKKVLLVYGGGSIKKNGLYDRVVASLKeaGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 80 LVREQKVTFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILqTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGD 159
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKYDG--DVWDFF-TGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 160 KQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLTLIEDGPKALKEPENYD 239
Cdd:cd08187 158 KLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 240 VRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNIT-EGS 318
Cdd:cd08187 238 ARANLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDpGGD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446981546 319 DDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTqLGENHDITLDVSRRIYE 384
Cdd:cd08187 318 DEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGL-GGGFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-356 |
3.60e-103 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 309.15 E-value: 3.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIP-HDARVLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQK 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKrLGARALIVTDPGSLK-SGLLDKVLASLEeaGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 86 VTFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILqTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHS 165
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPG--DVWDYL-GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 166 AHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkIQDRFAEGILLTLIEDGPKALKEPENYDVRANVM 245
Cdd:pfam00465 157 PKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANP-LTDALALEAIRLIAENLPRAVADGEDLEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 246 WAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWnitEGSDDERIDA 325
Cdd:pfam00465 236 LASTLAGLAFSNAGLG---AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG---EDSDEEAAEE 309
|
330 340 350
....*....|....*....|....*....|.
gi 446981546 326 AIAATRNFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:pfam00465 310 AIEALRELLRELGLPTTLSELGVTEEDLDAL 340
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-361 |
3.74e-83 |
|
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: 254.60 E-value: 3.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLRE-QIPHDARVLITYGGGSVKktGVLDQVLDALK-GMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEiKRRGFDRALVVSDEGVVK--GVGEKVADSLKkGLAVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTKFIAAAANypenidpwhilqtggkeikSAIPMGCVLTLPATGSESNAGAVISRKTTGDKqaFHSA 166
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAALLN-------------------RGIPFIIVPTTASTDSEVSPKSVITDKGGKNK--QVGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 167 HVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEqyvtkpvdakiqdrfaegilltliedgpkalkepenydvRANVMW 246
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 247 AATQALNGLIgaGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAkllqyaervwnitegsdderIDAA 326
Cdd:cd07766 179 AATLAGMGLF--ESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE--------------------PEAA 236
|
330 340 350
....*....|....*....|....*....|....*
gi 446981546 327 IAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLE 361
Cdd:cd07766 237 IEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-383 |
4.14e-81 |
|
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: 252.75 E-value: 4.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQI--PHDARVLITYGGGsVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQ 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELkaLGGKKVLLVTDPG-LVKAGLLDKVLESLKaaGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 85 KVTFLLAVGGGSVLDGTKFIAAAANYPENIDPWhilQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFH 164
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDY---EGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 165 SAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkIQDRFA-EGILLtLIEDGPKALKEPENYDVRAN 243
Cdd:cd08551 157 SPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANP-ISDALAlEAIRL-IGKNLRRAVADGSDLEAREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 244 VMWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEG-SDDER 322
Cdd:cd08551 235 MLLASLLAGIAFGNAGL---GAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGlSDEEA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446981546 323 IDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTQLGENHDITLDVSRRIY 383
Cdd:cd08551 312 AEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
2-356 |
1.05e-67 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 218.45 E-value: 1.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 2 NNFNLHTPTRILFGKGAIAGLREQIPH--DARVLITyGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNA 77
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRlgAKRALIV-TDPGLAKLGLLDRVLDALEaaGIEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 78 VKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILqtGGKEI-KSAIPMGCVLTLPATGSESNAGAVISRKT 156
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDL--EDYL--GIKKVpGPPLPLIAIPTTAGTGSEVTPFAVITDPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 157 TGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PV-DAkiqdrFA-EGIllTLIEDG-PK 230
Cdd:COG1454 156 TGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKganPLtDA-----LAlEAI--RLIARNlPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 231 ALKEPENYDVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRakl 304
Cdd:COG1454 229 AVADGDDLEAREKMALASLLAgmafANAGLG-------AVHALAHPLGGLFHVPHGLANAILLPHVlrFNAPAAPER--- 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446981546 305 lqYAE--RVWNITEG-SDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:COG1454 299 --YAEiaRALGLDVGlSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPEL 351
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-358 |
2.10e-62 |
|
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: 204.65 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 7 HTPTRILFGKGAIAGLREQI-PHDARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVRE 83
Cdd:cd08185 2 YQPTRILFGAGKLNELGEEAlRPGKKALIVTGKGSSKKTGLLDRVKKLLEkaGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILQ--TGGKEI-KSAIPMGCVLTLPATGSESNAGAVISRKTTGDK 160
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMATNPGDI--WDYIFggTGKGPPpEKALPIIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PvdakIQDRFA-EGILLtLIEDGPKALKEPE 236
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKnanP----FSDMLAlEAIRL-VAKYLPRAVKDGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 237 NYDVRANVMWAATQA--LNGLIGAGVPqdwatHMLGHELTAMHG-LDHAQTLAIVLPALWNEKRDTKRAKLLQYAERvwN 313
Cdd:cd08185 235 DLEAREKMAWASTLAgiVIANSGTTLP-----HGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA--E 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446981546 314 ITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLK 358
Cdd:cd08185 308 ASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAE 352
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-359 |
3.96e-54 |
|
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: 182.78 E-value: 3.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 4 FNLHTPTRILFGKGAIAGLRE---QIPHDARVLITygGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKL 80
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDiikELGGKRGLLVT--DPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 81 VREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDpwHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDK 160
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIE--DYLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PvdakIQDRFAEG----ILLTLiedgPKALK 233
Cdd:cd08196 157 APLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSInhqP----ISDALALEaaklVLENL----EKAYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 234 EPENYDVRANVMWAATQAlnGLigA-GVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVw 312
Cdd:cd08196 229 NPNDKEAREKMALASLLA--GL--AfSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446981546 313 niteGSDDerIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKK 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 |
7.99e-54 |
|
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: 182.35 E-value: 7.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGkgaiAGLREQIP------HDARVLITYGGGsVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKL 80
Cdd:cd14863 5 LTPVIFG----AGAVEQIGellkelGCKKVLLVTDKG-LKKAGIVDKIIDLLEeaGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 81 VREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDK 160
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPI--IDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PVDakiqDRFAEGILLTLIEDGPKALKEPEN 237
Cdd:cd14863 158 KSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKlanPMT----DALALQAIRLIVKNLPRAVKDGDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 238 YDVRANVMWAATQALNGLIGAGVpqdWATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYAERVwNIT 315
Cdd:cd14863 234 LEARENMLLASNLAGIAFNNAGT---HIGHAIAHALGALYHIPHGLACALALPVVleFNAEAYPEKVKKIAKALGV-SFP 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446981546 316 EGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLK 358
Cdd:cd14863 310 GESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAE 352
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-349 |
7.93e-50 |
|
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: 171.99 E-value: 7.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLReQIPHdARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd08179 5 PRDIYFGEGALEYLK-TLKG-KRAFIVTGGGSMKRNGFLDKVEDYLKeaGMEVKVFEGVEPDPSVETVEKGAEAMREFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTKFIAAAANYPE-----NIDPWHILQTGGKEIKSAIPmgcvlTLPATGSESNAGAVISRKTTGDKQ 161
Cdd:cd08179 83 DWIIAIGGGSVIDAAKAMWVFYEYPEltfedALVPFPLPELRKKARFIAIP-----STSGTGSEVTRASVITDTEKGIKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 162 AFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkIQDRFAEGILLTLIEDGPKALKEPENYDVR 241
Cdd:cd08179 158 PLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLAND-FTDALALGAILDIFENLPKSYNGGKDLEAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 242 ANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQyaervwNIT 315
Cdd:cd08179 237 EKMHNASCLAgmafSNSGLG-------IVHSMAHKGGAFFGIPHGLANAILLPYVieFNSKDPEARARYAA------LLI 303
|
330 340 350
....*....|....*....|....*....|....
gi 446981546 316 EGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLD 349
Cdd:cd08179 304 GLTDEELVEDLIEAIEELNKKLGIPLSFKEAGID 337
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-304 |
8.23e-48 |
|
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: 166.22 E-value: 8.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 6 LHTPTRILFGKGAIAGLREQIPHDA-RVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVR 82
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGkKALIVTGKHSAKKNGSLDDVTEALEenGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPwhiLQTGGKEiKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQA 162
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKDGDED---LFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 163 FHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDaKIQDRFAEGILLTLIEDGPKALKEPENYDVRA 242
Cdd:cd08181 157 FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKAT-PLSDALALEALRLIGECLPNLLGDELDEEDRE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446981546 243 NVMWAATqaLNGLI----GAGVPqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKL 304
Cdd:cd08181 236 KLMYAST--LAGMViaqtGTTLP-----HGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKV 294
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-359 |
6.72e-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: 164.25 E-value: 6.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 4 FNLHTPTRILFGKGAIaglrEQIPHD------ARVLITYGGGsVKKTGVLDQVLDALKG--MDVLEFGGIEPNPAYETLM 75
Cdd:cd14865 1 FEFFNPTKIVSGAGAL----ENLPAElarlgaRRPLIVTDKG-LAAAGLLKKVEDALGDaiEIVGVFDDVPPDSSVAVVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 76 NAVKLVREQKVTFLLAVGGGSVLDGTKfiAAAANYPENIDpwHILQTGGKEIKSA--IPMGCVLTLPATGSESNAGAVIS 153
Cdd:cd14865 76 EAAARAREAGADGIIAVGGGSVIDTAK--GVNILLSEGGD--DLDDYGGANRLTRplKPLIAIPTTAGTGSEVTLVAVIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 154 RKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV---TKPvdakIQDRFAEGILLTLIEDGPK 230
Cdd:cd14865 152 DEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTslqKNP----ISDALALQAIRLISENLPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 231 ALKEPENYDVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKR-AK 303
Cdd:cd14865 228 AVKNGKDLEARLALAIAATMAgiafSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVmrYNLDAAAERyAE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446981546 304 LLQYAERVWNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKK 359
Cdd:cd14865 301 LALALAYGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAEL 356
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-359 |
1.60e-45 |
|
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: 160.37 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIPHD--ARVLI-TYGGgsVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVRE 83
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALgiRRPLLvTDPG--LAALGIVDRVLEALGaaGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILQTGGKEIKSAI-PMGCVLTLPATGSESNAGAVISRKTTGDKQA 162
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEDGEGGPAAITPAVpPLIAIPTTAGTGSEVGRAAVITDDDTGRKKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 163 FHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkiqdrFAEGILLtlieDG--------PKALKE 234
Cdd:cd14861 161 IFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHP-----MADGIAL----EGlrlisewlPRAVAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 235 PENYDVRANVMWAATQA----LNGLiGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAER 310
Cdd:cd14861 232 GSDLEARGEMMMAALMGavafQKGL-G-------AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARA 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446981546 311 VwniteGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKK 359
Cdd:cd14861 304 L-----GLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAEL 347
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
4-356 |
1.62e-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: 157.71 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 4 FNLHTPTRILFGKGAIaglrEQIPHDAR------VLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLM 75
Cdd:cd08176 1 NRFVLNPTSYFGWGAI----EEIGEEAKkrgfkkALIVTDKGLVK-FGIVDKVTDVLKeaGIAYTVFDEVKPNPTIENVM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 76 NAVKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYP-ENIDPWhilqTGGKEIKS-AIPMGCVLTLPATGSESNAGAVIS 153
Cdd:cd08176 76 AGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVANPgADVRSL----EGVAPTKNpAVPIIAVPTTAGTGSEVTINYVIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 154 RKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTkpvdaKIQDRFAEGILL---TLI-EDGP 229
Cdd:cd08176 152 DTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-----KGAWELSDMLALkaiELIaKNLR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 230 KALKEPENYDVRANVMWAAT---QALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALWnekRDTKRAKLLQ 306
Cdd:cd08176 227 KAVANPNNVEARENMALAQYiagMAFSN-VGLGI-----VHSMAHPLSAFYDTPHGVANAILLPYVM---EFNAPATGEK 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446981546 307 YAE--RVWNI--TEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:cd08176 298 YRDiaRAMGVdtTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEAL 351
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-382 |
1.56e-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: 341484 [Multi-domain] Cd Length: 375 Bit Score: 155.08 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 1 MNNFNlhtPTRILFGKGAIAGLrEQIPhDARVLITYGGGsVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAV 78
Cdd:cd14862 1 MWYFS---SPKIVFGEDALSHL-EQLS-GKRALIVTDKV-LVKLGLLKKVLKRLLqaGFEVEVFDEVEPEPPLETVLKGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 79 KLVREQKVTFLLAVGGGSVLDGTKfiAAAANY------PENIDPwhiLQTGGKEIKS---AIPmgcvlTLPATGSESNAG 149
Cdd:cd14862 75 EAMREFEPDLIIALGGGSVMDAAK--AAWVLYerpdldPEDISP---LDLLGLRKKAkliAIP-----TTSGTGSEATWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 150 AVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTkPVDAKIQDRFAEGILLTLIEDGP 229
Cdd:cd14862 145 IVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLS-TWSNDFSDALALKAIELIFKYLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 230 KALKEPENYDVRANVMWAATQAlnGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAK 303
Cdd:cd14862 224 RAYKDGDDLEAREKMHNAATIA--GLafgnSQAGL-----AHALGHSLGAVFHVPHGIAVGLFLPYVieFYAKVTDERYD 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446981546 304 LLQYAErvwnITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEEHGMTqlgenhDITLDVSRRI 382
Cdd:cd14862 297 LLKLLG----IEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAME------DSCTITSPRP 365
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-358 |
1.76e-41 |
|
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: 149.68 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQI--PHDARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd08182 1 PVKIIFGPGALAELKDLLggLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTKFIAAAANYPENiDPWHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHSA 166
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGE-NLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 167 HVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PVDAKIQDRFAEGILLTLiedgPKALKEPENYDVRAN 243
Cdd:cd08182 160 SLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVnanPESRAYALRAIRLILENL----PLLLENLPNLEAREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 244 VMWAATQAlnGLigagvpqdwA-----T---HMLGHELTAMHGLDHAQTLAIVLPALW--NEKRDTKRAKLLQYAERVWN 313
Cdd:cd08182 236 MAEASLLA--GL---------AisitkTtaaHAISYPLTSRYGVPHGHACALTLPAVLryNAGADDECDDDPRGREILLA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446981546 314 ITEGSDDEridaAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLK 358
Cdd:cd08182 305 LGASDPAE----AAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-358 |
7.19e-41 |
|
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: 148.00 E-value: 7.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 8 TPTrILFGKGAIAGLREQIPHD--ARVLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVRE 83
Cdd:cd08189 5 EPE-LFEGAGSLLQLPEALKKLgiKRVLIVTDKGLVK-LGLLDPLLDALKkaGIEYVVFDGVVPDPTIDNVEEGLALYKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANYPENidpwHILQTGG--KEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQ 161
Cdd:cd08189 83 NGCDAIIAIGGGSVIDCAKVIAARAANPKK----SVRKLKGllKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 162 AFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV----TKPVDAK----IQdrfaegilltLI-EDGPKAL 232
Cdd:cd08189 159 AINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYIsrsaTKETDEYaleaVK----------LIfENLPKAY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 233 KEPENYDVRANVMWAA-------TQALNGLIgagvpqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLL 305
Cdd:cd08189 229 EDGSDLEARENMLLASyyaglafTRAYVGYV----------HAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446981546 306 QYAERVWNITEG-SDDERIDAAIAATRNFFEQLGVPTHLSdyGLDGSSIPALLK 358
Cdd:cd08189 299 ELADAAGLGDSGeSDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPEIAK 350
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-359 |
1.65e-40 |
|
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: 147.28 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 4 FNLHTPTRILFGKGAIAGLREQI-PHDA-RVLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVK 79
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELkKLGGkKALIVTDKGLVK-LGLVKKVTDVLEeaGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 80 LVREQKVTFLLAVGGGSVLDGTKFIAaaanypenidpwhILQTGGKEI----------KSAIPMGCVLTLPATGSESNAG 149
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIG-------------ILATNGGEIedyegvdkskKPGLPLIAINTTAGTASEVTRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 150 AVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTkpVDA-KIQDRFA-EGIllTLI-E 226
Cdd:cd08188 147 AVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVS--TGAtPLTDALAlEAI--RLIaE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 227 DGPKALKEPENYDVRANVMWA---ATQALNgliGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAK 303
Cdd:cd08188 223 NLPKAVANGKDLEARENMAYAqflAGMAFN---NAGLG---YVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPER 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446981546 304 LLQYAERVW-NITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKK 359
Cdd:cd08188 297 FADIARALGeNTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAEN 353
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-359 |
2.65e-40 |
|
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: 146.49 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIPHDAR--VLITygGGSVKKTGVLDQVLDALK--GMDVLEFGGI-EPNPayETLMNAVKLVRE 83
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKraLLVT--GRSSLRSGRLARLLEALEaaGIEVALFSVSgEPTV--ETVDAAVALARE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPWHILQTGGKEIKS------AIPmgcvlTLPATGSESNAGAVISRKTT 157
Cdd:cd08183 77 AGCDVVIAIGGGSVIDAAKAIAALLTNEGSVLDYLEVVGKGRPLTEpplpfiAIP-----TTAGTGSEVTKNAVLSSPEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 158 GDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTK---PV-DAkiqdrFA-EGIllTLIEDG-PKA 231
Cdd:cd08183 152 GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRkanPLtDA-----LArEGL--RLAARSlRRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 232 LKEPENYDVRANVMWAAtqALNGLI----GAGvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WN----EKRDTKR 301
Cdd:cd08183 225 YEDGEDLEAREDMALAS--LLGGLAlanaGLG-----AVHGLAGPLGGMFGAPHGAICAALLPPVleANlralREREPDS 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446981546 302 AKLLQYAErVWNITEGSDDERIDAAIAATRNFFEQLGVPtHLSDYGLDGSSIPALLKK 359
Cdd:cd08183 298 PALARYRE-LAGILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEK 353
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-386 |
2.76e-38 |
|
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: 141.25 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 10 TRILFGKGAIAGLREQIPHDA--RVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQK 85
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGidKVIIVTGRSSYKKSGAWDDVEKALEenGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 86 VTFLLAVGGGSVLDGTKFIAAAANYPENIDPWhiLQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHS 165
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYGGKTARD--LYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 166 AHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLtLIEDGPKALKEPENYDVRANVM 245
Cdd:cd08186 160 DCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRL-IAEYLPRALANPKDLEARYWLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 246 WAAtqalngLIgAGVPQDWA----THMLGHELTAM-HGLDHAQTLAIVLPAL----WNEKRDTKrAKLLQYAERVWNITE 316
Cdd:cd08186 239 YAS------MI-AGIAIDNGllhlTHALEHPLSGLkPELPHGLGLALLGPAVvkyiYKAVPETL-ADILRPIVPGLKGTP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446981546 317 GsDDERIDAAIaatRNFFEQLGVPTHLSDYGLDGSSIPallkKLEEHGMTQLGENH-------DITLDVSRRIYEAA 386
Cdd:cd08186 311 D-EAEKAARGV---EEFLFSVGFTEKLSDYGFTEDDVD----RLVELAFTTPSLDLllslapvEVTEEVVREIYEES 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-386 |
2.93e-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: 138.90 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 6 LHTPTRILFGKGAiaglREQIPHDA-----RVLItygggsVK-----KTGVLDQVLDALK--GMDVLEFGGIEPNPAYET 73
Cdd:cd08191 1 LRSPSRLLFGPGA----RRALGRVAarlgsRVLI------VTdprlaSTPLVAELLAALTaaGVAVEVFDGGQPELPVST 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 74 LMNAVKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENI-DPWHILQTGGKeiksAIPMGCVLTLPATGSESNAGAVI 152
Cdd:cd08191 71 VADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPrDYYGEDRVPGP----VLPLIAVPTTAGTGSEVTPVAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 153 SRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDA--------------KIQDRFA- 217
Cdd:cd08191 147 TDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPfprldpdpvyvgknPLTDLLAl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 218 EGIllTLIEDG-PKALKEPENYDVRANVMWAATQAlnGL-IG-AGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWN 294
Cdd:cd08191 227 EAI--RLIGRHlPRAVRDGDDLEARSGMALAALLA--GLaFGtAGTA---AAHALQYPIGALTHTSHGVGNGLLLPYVMR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 295 EKRDTKRAKLLQYAERVWNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKleEHGMTQLGENHDI 374
Cdd:cd08191 300 FNRPARAAELAEIARALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEK--ALSVTRLIANNPR 377
|
410
....*....|....
gi 446981546 375 TLDVS--RRIYEAA 386
Cdd:cd08191 378 PPTEEdlLRILRAA 391
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
8-349 |
3.95e-35 |
|
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: 133.08 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 8 TPTRILFGKGAIAGLREQIPHDARVLITYGGGSVKKtGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQK 85
Cdd:cd08178 2 VPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKL-GYVDKVLDVLEarGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 86 VTFLLAVGGGSVLDGTKFIAAAANYPEN---------IDP----WHILQTGGKEIKSAIPmgcvlTLPATGSESNAGAVI 152
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETkfedlaqrfMDIrkrvYKFPKLGKKAKLVAIP-----TTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 153 SRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVtkpvdAKIQDRFAEGI----LLTLIEDG 228
Cdd:cd08178 156 TDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYV-----SVMASDYTDGLalqaIKLIFEYL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 229 PKALKEPENYDVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRD-TKR 301
Cdd:cd08178 231 PRSYNNGNDIEAREKMHNAATIA--GMAFAnaflGI-----CHSLAHKLGAAFHIPHGRANAILLPHVirYNATDPpTKQ 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446981546 302 AKLLQYAERV-----------WNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLD 349
Cdd:cd08178 304 AAFPQYKYYVakeryaeiadlLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGID 362
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-349 |
1.16e-34 |
|
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: 131.50 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIP--HDARVLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQ 84
Cdd:cd08194 1 PRTIIIGGGALEELGEEAAslGGKRALIVTDKVMVK-LGLVDKVTQLLAeaGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 85 KVTFLLAVGGGSVLDGTKFIAAAANYPENI-DpwhiLQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAF 163
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGGPIrD----YMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 164 HSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKpvdaKIQ---DRFAEGILLTLIEDGPKALKEPENYDV 240
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSR----KAQpltDTLALSAIKLIGRNLRRAYADGDDLEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 241 RANVMWAATQAlnGL----------------IGA--GVPqdwathmlgheltamHGLDHAQTLAIVLpalwnekRDTKRA 302
Cdd:cd08194 232 REAMMLAALEA--GIafsnssvalvhgmsrpIGAlfHVP---------------HGLSNAMLLPAVT-------EFSLPG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446981546 303 KLLQYAE--RVWNI--TEGSDDERIDAAIAATRNFFEQLGVPThLSDYGLD 349
Cdd:cd08194 288 APERYAEiaRAMGIatEGDSDEEAAEKLVEALERLCADLEIPT-LREYGID 337
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-386 |
8.77e-32 |
|
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: 124.19 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 10 TRILFGKGAiagLREqIPHDARvliTYGGGSV--------KKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVK 79
Cdd:cd08190 2 SNIRFGPGA---TRE-LGMDLK---RLGAKKVlvvtdpglAKLGLVERVLESLEkaGIEVVVYDGVRVEPTDESFEEAIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 80 LVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENI-----DPwhilqTG-GKEIKSAI-PMGCVLTLPATGSESNAGAVI 152
Cdd:cd08190 75 FAKEGDFDAFVAVGGGSVIDTAKAANLYATHPGDFldyvnAP-----IGkGKPVPGPLkPLIAIPTTAGTGSETTGVAIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 153 SRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAK-----------------IQDR 215
Cdd:cd08190 150 DLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARprpanpderpayqgsnpISDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 216 FAEGILLTLIEDGPKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM-----------------HG 278
Cdd:cd08190 230 WAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVH---LPHAMAYPIAGLvkdyrppgypvdhphvpHG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 279 LdhaqTLAIVLPA--LWNEKRDTKR----AKLLQYaervwNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSS 352
Cdd:cd08190 307 L----SVALTAPAvfRFTAPACPERhleaAELLGA-----DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDD 377
|
410 420 430
....*....|....*....|....*....|....*
gi 446981546 353 IPALLKK-LEEHGMTQLGeNHDITLDVSRRIYEAA 386
Cdd:cd08190 378 IPALVEGtLPQQRLLKLN-PRPVTEEDLEEIFEDA 411
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
7-386 |
4.16e-31 |
|
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: 121.85 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 7 HTPTRILFGKGAIAGLREQI-PHDA-RVLITYGGGsVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVR 82
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLrELGArRVLLVTDPG-LVKAGLADPALAALEaaGIAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAAAANYPENI-DPWHILQTGGKEIksaiPMGCVLTLPATGSESNAGAVIsrkTTGD-- 159
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVALLAGSDQPLdDIYGVGKATGPRL----PLILVPTTAGTGSEVTPISIV---TTGEte 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 160 KQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILLTLIEDGPKALKEPENYD 239
Cdd:cd08193 154 KKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALAREALRLLGANLRRAVEDGSDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 240 VRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM----HGLDHAQTLAIVLpalwneKRDTKRAKLLqYAERVWNI- 314
Cdd:cd08193 234 AREAMLLGSMLAGQAFANAPVA---AVHALAYPLGGHfhvpHGLSNALVLPHVL------RFNLPAAEAL-YAELARALl 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446981546 315 ---TEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPallkKLEEHGMTQ--LGENH--DITLDVSRRIYEAA 386
Cdd:cd08193 304 pglAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLP----MLAEDAMKQtrLLVNNprEVTEEDALAIYQAA 378
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-359 |
5.87e-30 |
|
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: 118.41 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 12 ILFGKGAiaglREQIPHDA------RVLITYGGGsVKKTGVLDQVLDALK--GMDVLEFGGIEPNP-AYEtLMNAVKLVR 82
Cdd:cd17814 7 FIFGVGA----RKLAGRYAknlgarKVLVVTDPG-VIKAGWVDEVLDSLEaeGLEYVVFSDVTPNPrDFE-VMEGAELYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAA-AANypenidPWHILQ-TGGKEIKSAI-PMGCVLTLPATGSESNAGAVISRKTTGD 159
Cdd:cd17814 81 EEGCDGIVAVGGGSPIDCAKGIGIvVSN------GGHILDyEGVDKVRRPLpPLICIPTTAGSSADVSQFAIITDTERRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 160 KQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkIQDRFA-EGILLtLIEDGPKALKEPENY 238
Cdd:cd17814 155 KMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSP-LTDLHAlEAIRL-ISENLPKAVADPDDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 239 DVRANVMWAATQA----LNGLIGagvpqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERV-WN 313
Cdd:cd17814 233 EAREKMMLASLQAglafSNASLG-------AVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMgLD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446981546 314 ITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKK 359
Cdd:cd17814 306 VDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKR 351
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-356 |
2.00e-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: 116.96 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIP--HDARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELAtlGASRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTK----FIAAAANYPENIDPWHILQTGGKEIKSA-IPMGCVltlPAT--GSESNAGAVISRKTTGD 159
Cdd:cd08192 81 DLLVSLGGGSPIDAAKavalALAEDVTDVDQLDALEDGKRIDPNVTGPtLPHIAI---PTTlsGAEFTAGAGATDDDTGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 160 KQAFHSAHVQPVFAVLDPVYTYTLPPR-QVANGV--VDafvHTVE-QYVTKPVDAkiQDRFAEGILLTLIEDGPKALKEP 235
Cdd:cd08192 158 KQGFAHPELGPDAVILDPELTLHTPERlWLSTGIraVD---HAVEtLCSPQATPF--VDALALKALRLLFEGLPRSKADP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 236 ENYDVRANVM---WAATQALNGLIGAGvpqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYAER 310
Cdd:cd08192 233 EDLEARLKCQlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPHGITSCIMLPAVlrFNAPVNAERQRLIARALG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446981546 311 VWNITEGSDDERIDAAIAAtrnFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:cd08192 308 LVTGGLGREAADAADAIDA---LIRELGLPRTLRDVGVGRDQLEKI 350
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-351 |
1.48e-25 |
|
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: 106.23 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 7 HTPTRILFGKGAIAGLREQIPHDAR--VLITygGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVR 82
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYGSrfLLIT--DPVLKESGLADKIVSSLEkaGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDPwhiLQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQA 162
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYD---FLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 163 FHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKpvDAK-IQDRFAEGILLTLIEDGPKALKEPENYDVR 241
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSK--KSNfFSDALALKAIELVSENLDGALADPKNTPAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 242 ANVMWAAtqALNGLIGAGVPQDWAThMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKL--LQYAERVwNITEGSD 319
Cdd:cd14864 235 ELLAQAG--CLAGLAASSSSPGLAT-ALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYakIARALGE-DVEGASP 310
|
330 340 350
....*....|....*....|....*....|..
gi 446981546 320 DERIDAAIAATRNFFEQLGVPTHLSDYGLDGS 351
Cdd:cd14864 311 EEAAIAAVEGVRRLIAQLNLPTRLKDLDLASS 342
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-356 |
1.81e-25 |
|
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: 106.16 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIP-HDA-RVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd14866 5 PLRLFSGRGALARLGRELDrLGArRALVVCGSSVGANPDLMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTKFIAAAANYPENIDPW--HILQTGGKEI----KSAIPMGCVLTLPATGSESnAGAVISRKTTGDK 160
Cdd:cd14866 85 DAVVAVGGGSAIVTARAASILLAEDRDVRELctRRAEDGLMVSprldAPKLPIFVVPTTPTTADVK-AGSAVTDPPAGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkiqdrFAEGIL---LTLIEDGPKALKEPEN 237
Cdd:cd14866 164 LALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADP-----LADATLmhaLRLLADGLPRLADDDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 238 YDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYAERVWnit 315
Cdd:cd14866 239 PAARADLVLAAVLAGYGTDHTGGG---VIHALGHAIGARYGVQNGVVHAILLPHVlrFNAPATDGRLDRLAEALGVA--- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446981546 316 EGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:cd14866 313 DAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAI 353
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-362 |
8.82e-25 |
|
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: 103.34 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQipHDARVLItygggsV-----KKTGVLDQVLDALKGM-DVLEFGGIEPNPAYETLMNAVKLVR 82
Cdd:cd08180 4 KTKIYSGEDSLERLKEL--KGKRVFI------VtdpfmVKSGMVDKVTDELDKSnEVEIFSDVVPDPSIEVVAKGLAKIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAAAANYpenidpwhilQTGGKEIKS--AIPmgcvlTLPATGSESNAGAVISRKTTGDK 160
Cdd:cd08180 76 EFKPDTIIALGGGSAIDAAKAIIYFALK----------QKGNIKKPLfiAIP-----TTSGTGSEVTSFAVITDPEKGIK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 161 QAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV-TKPVDakIQDRFAEGILLTLIEDGPKALKEPENYD 239
Cdd:cd08180 141 YPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVsTNAND--FTDALAEKAIKLVFENLPRAYRDGDDLE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 240 VRANVMWAATQA-----LNGLigaGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALwnekrdtkrakllqyaervwni 314
Cdd:cd08180 219 AREKMHNASCMAgiafnNAGL---GI-----NHSLAHALGGRFHIPHGRANAILLPYV---------------------- 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446981546 315 tegsdderIDAAIAATRNFFEQLGVPTHLSDYGLDgssIPALLKKLEE 362
Cdd:cd08180 269 --------IEFLIAAIRRLNKKLGIPSTLKELGID---EEEFEKAIDE 305
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-362 |
2.56e-23 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 102.19 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIPHDARVLITYGGGSVKKtGVLDQVLDALK----GMDVLEFGGIEPNPAYETLMNAVKLVREQ 84
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDGKKRAFIVTDRFMVEL-GYVDKVTDVLKkrenGVEYEVFSEVEPDPTLSTVRKGAELMRSF 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 85 KVTFLLAVGGGSVLDGTKFIAAAANYPEN---------IDPwhilqtgGKEIKSAIPMG------CVLTLPATGSESNAG 149
Cdd:PRK13805 539 KPDTIIALGGGSPMDAAKIMWLFYEHPETdfedlaqkfMDI-------RKRIYKFPKLGkkaklvAIPTTSGTGSEVTPF 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 150 AVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTkpVDAkiqDRFAEGILL----TLI 225
Cdd:PRK13805 612 AVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVS--VMA---SDYTDGLALqaikLVF 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 226 EDGPKALKE-PENYDVRANVMWAATQAlnGLIGA----GVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WNEKRD 298
Cdd:PRK13805 687 EYLPRSYKNgAKDPEAREKMHNASTIA--GMAFAnaflGI-----CHSMAHKLGAEFHIPHGRANAILLPHVirYNATDP 759
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446981546 299 TKRAKLLQY---------AE--RVWNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSsipALLKKLEE 362
Cdd:PRK13805 760 PKQAAFPQYeypraderyAEiaRHLGLPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEA---DFLAKLDE 831
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
39-356 |
3.41e-23 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 99.64 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 39 GSVKKTGVLDQVLDAL--KGMDVLEFGGIEPNPAYETLMNAVKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIDP 116
Cdd:PRK09860 40 NMLTKLGMAGDVQKALeeRNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 117 WHILQtggKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAF 196
Cdd:PRK09860 120 YEGVD---RSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 197 VHTVEQYVTKPVdAKIQDRFAEGILLTLIEDGPKALKEPENYDVRANVMWAatQALNGLIGAGVPQDWaTHMLGHELTAM 276
Cdd:PRK09860 197 THAIEAYVSIAA-TPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYA--QFLAGMAFNNASLGY-VHAMAHQLGGF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 277 HGLDHAQTLAIVLPAL--WNEKRDTKRAKLLQYAERVwNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIP 354
Cdd:PRK09860 273 YNLPHGVCNAVLLPHVqvFNSKVAAARLRDCAAAMGV-NVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFA 351
|
..
gi 446981546 355 AL 356
Cdd:PRK09860 352 VL 353
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
69-347 |
1.70e-21 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 95.09 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 69 PAYETLMNAVKLVREQKVTFLLAVGGGSVLDGTKFIAAAANYPENIdpwHILQTGGKEIKSAIPMGCVLTLPATGSESNA 148
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDST---LAEMSETSVLQPRLPLIAIPTTAGTGSETTN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 149 GAVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVdAKIQDRFAEGILLTLIEDG 228
Cdd:PRK15454 167 VTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNA-TPFTDSLAIGAIAMIGKSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 229 PKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYA 308
Cdd:PRK15454 246 PKAVGYGHDLAARESMLLASCMAGMAFSSAGLG---LCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIG 322
|
250 260 270
....*....|....*....|....*....|....*....
gi 446981546 309 ERVWNitEGSDDERidaAIAATRNFFEQLGVPTHLSDYG 347
Cdd:PRK15454 323 RALRT--KKSDDRD---AINAVSELIAEVGIGKRLGDVG 356
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-356 |
2.19e-20 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 91.60 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 14 FGKGAIaglrEQIPHDA------RVLITYGGGSVKkTGVLDQVLDALK--GMDVLEFGGIEPNPAYETLMNAVKLVREQK 85
Cdd:PRK10624 13 FGRGAI----GALTDEVkrrgfkKALIVTDKTLVK-CGVVAKVTDVLDaaGLAYEIYDGVKPNPTIEVVKEGVEVFKASG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 86 VTFLLAVGGGSVLDGTKFIAAAANYPENIDPwHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHS 165
Cdd:PRK10624 88 ADYLIAIGGGSPQDTCKAIGIISNNPEFADV-RSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 166 AHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAkIQDRFAegilLTLIEDGPKALKEPENYDVRANVM 245
Cdd:PRK10624 167 PHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWA-LTDMLH----LKAIEIIAGALRGAVAGDKEAGEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 246 WAATQALNGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPAL--WN-----EK-RDTKRAkllqYAERVwn 313
Cdd:PRK10624 242 MALGQYIAGMgfsnVGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHVmeYNadftgEKyRDIARA----MGVKV-- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446981546 314 iTEGSDDERIDAAIAATRNFFEQLGVPTHLSDYGLDGSSIPAL 356
Cdd:PRK10624 311 -EGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPAL 352
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-355 |
3.77e-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: 66.76 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIPHD--ARVLITYGGGSvkkTGVLDQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKV 86
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLgaRRALVLSTPRQ---RALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 87 TFLLAVGGGSVLDGTKFIAaaanypenidpwhiLQTGGKEIksAIPmgcvlTLPAtGSE-------SNAGavisRKTTGD 159
Cdd:cd08177 78 DGLVAIGGGSAIGLAKAIA--------------LRTGLPIV--AVP-----TTYA-GSEmtpiwgeTEDG----VKTTGR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 160 kqafhSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTKPVDAKIQDRFAEGILlTLIEDGPKALKEPENYD 239
Cdd:cd08177 132 -----DPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIR-ALARALPRLVADPSDLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 240 VRANVMWAATqalngLigAGVPQDWAT----HMLGHELTAMHGLDHAQTLAIVLP-ALWNEKRDTKRAkllqyAERVWNI 314
Cdd:cd08177 206 ARSDALYGAW-----L--AGVVLGSVGmglhHKLCHVLGGTFDLPHAETHAVVLPhVLAYNAPAAPDA-----MARLARA 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446981546 315 TEGSDderidaAIAATRNFFEQLGVPTHLSDYGLDGSSIPA 355
Cdd:cd08177 274 LGGGD------AAGGLYDLARRLGAPTSLRDLGMPEDDIDR 308
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-387 |
3.94e-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: 63.65 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQI-PHDARVLITYGGGSVKKTGvlDQVLDALKG----MDVLEFGGiepNPAYETLMNAVKLVRE 83
Cdd:COG0371 6 PRRYVQGEGALDELGEYLaDLGKRALIITGPTALKAAG--DRLEESLEDagieVEVEVFGG---ECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANypenidpwhilqtggkeiksaIPMGCVLTLPATGSESNAGAVIsrKTTGDKQAF 163
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLG---------------------LPVVSVPTIASTDAPASPLSVI--YTEDGAFDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 164 HSAHVQPVFAVL-DpvytYTL----PPRQVANGVVDAF-----VHTVEQ-----YVTKPVDAKIQdrFAEGILLTLIEDG 228
Cdd:COG0371 138 YSFLAKNPDLVLvD----TDIiakaPVRLLAAGIGDALakwyeARDWSLahrdlAGEYYTEAAVA--LARLCAETLLEYG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 229 PKALKEPENYDVR---ANVMWAATqALNGLIGAGVPQDWAT---HMLGHELTAMHGLDHAQ--------TLaiVLPALwn 294
Cdd:COG0371 212 EAAIKAVEAGVVTpalERVVEANL-LLSGLAMGIGSSRPGSgaaHAIHNGLTALPETHHALhgekvafgTL--VQLVL-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 295 ekrdtkrakllqyaervwnitEGSDDEridaaIAATRNFFEQLGVPTHLSDYGLDGSSIPALLKKLEE---HGMTQLGEN 371
Cdd:COG0371 287 ---------------------EGRPEE-----IEELLDFLRSVGLPTTLADLGLDDETEEELLTVAEAarpERYTILNLP 340
|
410
....*....|....*.
gi 446981546 372 HDITLDvsrRIYEAAR 387
Cdd:COG0371 341 FEVTPE---AVEAAIL 353
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
91-204 |
5.34e-07 |
|
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: 51.06 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 91 AVGGGSVLDGTKFIAAAanypeNIDPWHILQTGGKEIKSAIPMGCVLTLPATGSESNAGAVISRKTTGDKQAFHSAHVQP 170
Cdd:cd14860 84 AIGGGTVIDIAKLLALK-----GISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYA 158
|
90 100 110
....*....|....*....|....*....|....
gi 446981546 171 VFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV 204
Cdd:cd14860 159 DKAVLIPELLKGLPYKVFATSSIDALIHAIESYL 192
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-352 |
1.28e-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: 49.84 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQI-PHDARVLITYGGGSVKKTGvlDQVLDALK--GMD--VLEFGGiepNPAYETLMNAVKLVRE 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIaPLGKKALIIGGKTALEAVG--EKLEKSLEeaGIDyeVEVFGG---ECTEENIERLAEKAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIAAAANypenidpwhilqtggkeiksaIPMGCVLTLPATGSESNAGAVIsRKTTGDKQAF 163
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAKAVADRLG---------------------LPVVTVPTIAATCAAWSALSVL-YDEEGEFLGY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 164 HsAHVQPVFAVL-DPVYTYTLPPRQVANGVVDAFVHTVEqyvTKPVDAKIQDRFAEGILL--------TLIEDGPKALKE 234
Cdd:cd08550 134 S-LLKRSPDLVLvDTDIIAAAPVRYLAAGIGDTLAKWYE---ARPSSRGGPDDLALQAAVqlaklaydLLLEYGVQAVED 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 235 PENYDVR--------ANVMWAatqALNGLIGAGVPQDWATHMLGHELTAM---HGLDHAQTLAIVLPALWnekrdtkrak 303
Cdd:cd08550 210 VRQGKVTpaledvvdAIILLA---GLVGSLGGGGCRTAAAHAIHNGLTKLpetHGTLHGEKVAFGLLVQL---------- 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446981546 304 llqyaervwnITEGSDDERIDAAIAatrnFFEQLGVPTHLSDYGLDGSS 352
Cdd:cd08550 277 ----------ALEGRSEEEIEELIE----FLRRLGLPVTLEDLGLELTE 311
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-111 |
1.58e-05 |
|
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: 46.39 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIPHDA---RVLITYGGGSVKKTGvlDQVLDALKGMDVLEFggIEPNPAYETLMN---AVKLVR 82
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLlgkRALIITGPNTYKIAG--KRVEDLLESSGVEVV--IVDIATIEEAAEvekVKKLIK 77
|
90 100
....*....|....*....|....*....
gi 446981546 83 EQKVTFLLAVGGGSVLDGTKFIAAAANYP 111
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAKYAAYKLNLP 106
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-105 |
3.27e-04 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 42.19 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 7 HTPTRILFGKGAIAGLREQIPH---DARVLITYGGGSVKKTGvlDQVLDALKGMDVLEFGGIEpNPAYETLMNAVKLVRE 83
Cdd:PRK00843 9 QLPRDVVVGHGVLDDIGDVCSDlklTGRALIVTGPTTKKIAG--DRVEENLEDAGDVEVVIVD-EATMEEVEKVEEKAKD 85
|
90 100
....*....|....*....|..
gi 446981546 84 QKVTFLLAVGGGSVLDGTKFIA 105
Cdd:PRK00843 86 VNAGFLIGVGGGKVIDVAKLAA 107
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-200 |
3.78e-03 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. 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. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 38.93 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 12 ILFGKGAIAGLREQIPHDARVLITYgggsVKKTGV-------LDQVLDALKGMDVLEFGGIEPNPAYETLMN------AV 78
Cdd:cd08169 4 VFFGEGVFESVNSYIPRDAFDQCLI----IVDSGVpdlivnyLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEeleraaAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 79 KLVREqkvTFLLAVGGGSVLDGTKFiaAAANYPENIDPWHILQTggkeiksaipmgcVLTLpatgSESNAGAVISRKTTG 158
Cdd:cd08169 80 HLNRH---SAVVAVGGGATGDVVGF--AAATYFRGIAFIRVPTT-------------LLAQ----SDSSVGIKVGINTRG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446981546 159 DKQAFHSAHvQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTV 200
Cdd:cd08169 138 GKNLLGAFY-PPRAVFADFSFLKTLPFRQVRAGMAELVKMAL 178
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-201 |
5.03e-03 |
|
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: 38.79 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 9 PTRILFGKGAIAGLREQIphdARVLITYGGGSV-------KKTGVLDQVldALKGMDVLEFGGIEPNPAYETLMNAVKLV 81
Cdd:cd08184 1 VPKYLFGRGSFDQLGELL---AERRKSNNDYVVffiddvfKGKPLLDRL--PLQNGDLLIFVDTTDEPKTDQIDALRAQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446981546 82 REQKVTFLLAV---GGGSVLDGTKFIA-------AAANYpeniDPWHILQTGGKEiKSAIPmgcvlTLPATGSESNAGAV 151
Cdd:cd08184 76 RAENDKLPAAVvgiGGGSTMDIAKAVSnmltnpgSAADY----QGWDLVKNPGIY-KIGVP-----TLSGTGAEASRTAV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446981546 152 ISRKttGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVE 201
Cdd:cd08184 146 LTGP--EKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE 193
|
|
| |
