|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 732.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 1 MQNFTYWNPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKG 80
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGGSIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 81 VALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEK 160
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 161 YGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNTPYQDRMCESLLRTVIETAPKLINDLENYEL 240
Cdd:COG1979 161 LGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 241 RETILYTGTIALNGMLSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVRVFDIDEtgKS 320
Cdd:COG1979 241 RANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITE--GD 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 321 DEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANG--AFGQFKSLQKEDVLAILKASL 387
Cdd:COG1979 319 DEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGmtALGEFKDLTPEDVREILELAL 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: 660.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 3 NFTYWNPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVA 82
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 83 LCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYG 162
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 163 WGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELRE 242
Cdd:cd08187 161 FGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 243 TILYTGTIALNGMLSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVRVFDIDEtGKSDE 322
Cdd:cd08187 241 NLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDP-GGDDE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494650708 323 EIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGA-FGQFKSLQKEDVLAILK 384
Cdd:cd08187 320 ETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGlGGGFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-369 |
8.43e-128 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 371.94 E-value: 8.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLK-SGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPLV 168
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 169 YPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRETILYTG 248
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGAN-PLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 249 TIALNGMLSMGaRGdwATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVRVFdidetGKSDEEIALEG 328
Cdd:pfam00465 239 TLAGLAFSNAG-LG--AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG-----EDSDEEAAEEA 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 494650708 329 ISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFG 369
Cdd:pfam00465 311 IEALRELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLA 351
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-386 |
1.61e-110 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 328.68 E-value: 1.61e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 1 MQNFTYWNPTKLIFGKGEVEKLPEEIkPYGKNVLLVYGGGSIKRSGLYDQVTELLKkaGVTVHELAGVEPNPRVSTVNKG 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQI-PADARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 81 VALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDG--DAWDIV-TKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWET 157
Cdd:PRK15138 78 VKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILeTGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 158 QEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNTPYQDRMCESLLRTVIETAPKLINDLEN 237
Cdd:PRK15138 158 GDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 238 YELRETILYTGTIALNGMLSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVRVFDIDEt 317
Cdd:PRK15138 238 YDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITE- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494650708 318 GKSDEEIAlEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANG--AFGQFKSLQKEDVLAILKAS 386
Cdd:PRK15138 317 GSDDERID-AAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHGmtQLGEHHDITLDVSRRIYEAA 386
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-384 |
3.81e-109 |
|
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: 324.84 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 6 YWNPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCK 85
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIV----TKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKY 161
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIfggtGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 162 GWGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYEL 240
Cdd:cd08185 161 GIGHPALFPKVSIVDPELMLTVPPRVTAYtGF-DALFHAFESYI-SKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 241 RETILYTGTIAlnGMlSMGARGDWATHNIEHAVSAVY-DIPHAGGLAILFPNWMRHVLKENPARFKQLAvrvfDIDETGK 319
Cdd:cd08185 239 REKMAWASTLA--GI-VIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVA----RAEASGL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 320 SDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAfGQF----KSLQKEDVLAILK 384
Cdd:cd08185 312 SDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETMG-GLFannpVELTEEDIVEIYE 379
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
2-387 |
1.29e-98 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 298.19 E-value: 1.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 2 QNFTYWNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVyGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKG 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGaKRALIV-TDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 81 VALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEK 160
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 161 YGWGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYfhhTSN--TPYQDRMCESLLRTVIETAPKLINDLEN 237
Cdd:COG1454 160 KGIADPELLPDVAILDPELTLTLPPSLTAAtGM-DALTHAIEAY---VSKgaNPLTDALALEAIRLIARNLPRAVADGDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 238 YELRETILYTGTIAlnGM----LSMGargdwATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFD 313
Cdd:COG1454 236 LEAREKMALASLLA--GMafanAGLG-----AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIA-RALG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494650708 314 IDeTGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFGQF-KSLQKEDVLAILKASL 387
Cdd:COG1454 308 LD-VGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNpRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-383 |
1.75e-93 |
|
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: 284.73 E-value: 1.75e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGgKKVLLVTDPG-LVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPL 167
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 168 VYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYfhhTSN--TPYQDRMCESLLRTVIETAPKLINDLENYELRETI 244
Cdd:cd08551 160 LLPDVAILDPELTLSLPPSVTAAtGM-DALTHAIEAY---TSKkaNPISDALALEAIRLIGKNLRRAVADGSDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 245 LYTGTIAlnGMlSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFDIDETGKSDEEI 324
Cdd:cd08551 236 LLASLLA--GI-AFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIA-EALGEDVEGLSDEEA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494650708 325 ALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANG--AFGQFKSLQKEDVLAIL 383
Cdd:cd08551 312 AEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGrlLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-385 |
9.08e-84 |
|
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: 260.16 E-value: 9.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 5 TYWNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVAL 83
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGcKKVLLVTDKG-LKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 84 CKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWD-IVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYG 162
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 163 WGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELR 241
Cdd:cd14863 160 LLGPFLVPDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKLAN-PMTDALALQAIRLIVKNLPRAVKDGDNLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 242 ETILYTGTIAlnGMlSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFDIDETGKSD 321
Cdd:cd14863 238 ENMLLASNLA--GI-AFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIA-KALGVSFPGESD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494650708 322 EEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFG-QFKSLQKEDVLAILKA 385
Cdd:cd14863 314 EELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMfNPRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-383 |
7.59e-72 |
|
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: 229.00 E-value: 7.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 4 FTYWNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVyGGGSIKRSGLYDQVTELLKKAGVTVHElaGVEPNPRVSTVNKGVA 82
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGgKRGLLV-TDPSFIKSGLAKRIVESLKGRIVAVFS--DVEPNPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 83 LCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDI-VTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKY 161
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 162 GWGSPLVYPKFSILDPVNTFTVPKDHT-IYGMvDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYEL 240
Cdd:cd08196 158 PLVSPGFYPDIAIVDPELTYSMPPKVTaSTGI-DALCHAIEAYWSINHQ-PISDALALEAAKLVLENLEKAYNNPNDKEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 241 RETILYTGTIAlnGMlsmgARGDWAThNIEHAVS----AVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvrvfdiDE 316
Cdd:cd08196 236 REKMALASLLA--GL----AFSQTRT-TASHACSypltSHFGIPHGEACALTLPSFIRLNAEALPGRLDELA------KQ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494650708 317 TGKSDEEIALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIADKAMA-NGAFGQFKSLQKEDVLAIL 383
Cdd:cd08196 303 LGFKDAEELADKIEELKK---RIGLRTRLSELGITEEDLEEIVEESFHpNRANNNPVEVTKEDLEKLL 367
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-384 |
5.51e-64 |
|
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: 208.91 E-value: 5.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 4 FTYWNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVA 82
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKGLVK-LGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 83 LCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYG 162
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 163 WGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELR 241
Cdd:cd08188 160 IVDWNVTPTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEAYV-STGATPLTDALALEAIRLIAENLPKAVANGKDLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 242 ETILYTGTIAlnGM------LSMgargdwaTHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAvRVFD 313
Cdd:cd08188 238 ENMAYAQFLA--GMafnnagLGY-------VHAMAHQLGGFYNLPH--GVcnAILLPHVMEFNLPACPERFADIA-RALG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494650708 314 IDETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANG-AFGQFKSLQKEDVLAILK 384
Cdd:cd08188 306 ENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDAcGPTNPRQATKEDVIAIYR 377
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-384 |
7.62e-64 |
|
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: 208.55 E-value: 7.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 3 NFTYWNPTkLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGV 81
Cdd:cd08176 1 NRFVLNPT-SYFGWGAIEEIGEEAKKRGfKKALIVTDKGLVK-FGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 82 ALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDG------DAWDIVTKKHQPKEALPfgtvlTLAATGSEMNSGSVITNW 155
Cdd:cd08176 79 AAYKESGADGIIAVGGGSSIDTAKAIGIIVANPGadvrslEGVAPTKNPAVPIIAVP-----TTAGTGSEVTINYVITDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 156 ETQEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYfhhTS--NTPYQDRMCESLLRTVIETAPKLI 232
Cdd:cd08176 154 EKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGY---ITkgAWELSDMLALKAIELIAKNLRKAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 233 NDLENYELRETILYTGTIAlnGM-LSMGARGdwATHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAv 309
Cdd:cd08176 230 ANPNNVEARENMALAQYIA--GMaFSNVGLG--IVHSMAHPLSAFYDTPH--GVanAILLPYVMEFNAPATGEKYRDIA- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 310 RVFDIDETGKSDEEI---ALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIADKAMANGAF-GQFKSLQKEDVLAILK 384
Cdd:cd08176 303 RAMGVDTTGMSDEEAaeaAVDAVKKLSK---DVGIPQKLSELGVKEEDIEALAEDALNDVCTpGNPREATKEDIIALYK 378
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
9-384 |
6.47e-62 |
|
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: 202.82 E-value: 6.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGV--TVHElaGVEPNPRVSTVNKGVALCKE 86
Cdd:cd08181 4 PTKVYFGKNCVEKHADELAALGKKALIVTGKHSAKKNGSLDDVTEALEENGIeyFIFD--EVEENPSIETVEKGAELARK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 87 NSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKhQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSP 166
Cdd:cd08181 82 EGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNG-KYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 167 LVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELRETILY 246
Cdd:cd08181 161 LIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYL-SVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 247 TGTIAlnGMLSMGArGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENParfkqlavrvfdidetGKSDEEIAL 326
Cdd:cd08181 240 ASTLA--GMVIAQT-GTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEP----------------EKVDKILKL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494650708 327 EGISRLSDFWTSLgapNRLADYD--ISDEKLDTIADKAMANGAFGQF-KSLQKEDVLAILK 384
Cdd:cd08181 301 LGFGSIEEFQKFL---NRLLGKKeeLSEEELEKYADEAMKAKNKKNTpGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-387 |
1.41e-58 |
|
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: 194.79 E-value: 1.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 10 TKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGiDKVIIVTGRSSYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKY-DGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPL 167
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYgGKTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 168 VYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRETILYT 247
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSS-PYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 248 GTIA----LNGMLSMgargdwaTHNIEHAVSAVY-DIPHAGGLAILFPNWMRHVlkeNPARFKQLAVRVFDIDETGKSDE 322
Cdd:cd08186 241 SMIAgiaiDNGLLHL-------THALEHPLSGLKpELPHGLGLALLGPAVVKYI---YKAVPETLADILRPIVPGLKGTP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 323 EIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFGQFKSL-----QKEDVLAILKASL 387
Cdd:cd08186 311 DEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLLLSLapvevTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-366 |
2.96e-58 |
|
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: 193.84 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 7 WNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKRsGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCK 85
Cdd:cd08189 3 WPEPELFEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAkydgdawdivTKKHQP-----------KEALPFGTVLTLAATGSEMNSGSVITN 154
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAARA----------ANPKKSvrklkgllkvrKKLPPLIAVPTTAGTGSEATIAAVITD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 155 WETQEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLIN 233
Cdd:cd08189 152 PETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYI-SRSATKETDEYALEAVKLIFENLPKAYE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 234 DLENYELRETIL----YTG---TIALNGMlsmgargdwaTHNIEHAVSAVYDIPHAGGLAILFPnwmrHVLKEN----PA 302
Cdd:cd08189 230 DGSDLEARENMLlasyYAGlafTRAYVGY----------VHAIAHQLGGLYGVPHGLANAVVLP----HVLEFYgpaaEK 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494650708 303 RFKQLAVRVfDIDETGKSDEEIALEGISRLSDFWTSLGAPNRLAdyDISDEKLDTIADKAMANG 366
Cdd:cd08189 296 RLAELADAA-GLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPEIAKRALKEA 356
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-367 |
5.65e-58 |
|
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: 193.13 E-value: 5.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKP-YGKNVLLVyGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASlGGKRALIV-TDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPL 167
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 168 VYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYfhhTSN--TPYQDRMCESLLRTVIETAPKLINDLENYELRETIL 245
Cdd:cd08194 160 LLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAY---VSRkaQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 246 YTGT---IALN--------GMlsmgARgdwathniehAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAvRVF 312
Cdd:cd08194 237 LAALeagIAFSnssvalvhGM----SR----------PIGALFHVPH--GLsnAMLLPAVTEFSLPGAPERYAEIA-RAM 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 313 DIDETGKSDEEIALEGISRLSDFWTSLGAPnRLADYDISDEK----LDTIADKAMANGA 367
Cdd:cd08194 300 GIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEfeaaLDKMAEDALASGS 357
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-387 |
9.85e-58 |
|
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: 192.76 E-value: 9.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 4 FTYWNPTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVA 82
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGaRRPLIVTDKG-LAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 83 LCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEAL-PFGTVLTLAATGSEMNSGSVITNWETQEKY 161
Cdd:cd14865 80 RAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLkPLIAIPTTAGTGSEVTLVAVIKDEEKKVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 162 GWGSPLVYPKFSILDPVNTFTVPKDHT-IYGMvDMMSHVFEQYfHHTSNTPYQDRMCESLLRTVIETAPKLINDLENYEL 240
Cdd:cd14865 160 LFVSPFLLPDVAILDPRLTLSLPPKLTaATGM-DALTHAIEAY-TSLQKNPISDALALQAIRLISENLPKAVKNGKDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 241 RETILYTGTIA----LNGMLSMgargdwaTHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVR-VFDID 315
Cdd:cd14865 238 RLALAIAATMAgiafSNSMVGL-------VHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALAlAYGVT 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494650708 316 ETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGA-FGQFKSLQKEDVLAILKASL 387
Cdd:cd14865 311 PAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAiLFNPREVDPEDILAILEAAY 383
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-367 |
2.86e-57 |
|
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: 191.63 E-value: 2.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 6 YWNPTKLIFGKGEVEKLpEEIKpyGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCK 85
Cdd:cd08179 2 FFVPRDIYFGEGALEYL-KTLK--GKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKkhqPKEALPFGT------VLTLAATGSEMNSGSVITNWETQE 159
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALV---PFPLPELRKkarfiaIPSTSGTGSEVTRASVITDTEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 160 KYGWGSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENY 238
Cdd:cd08179 156 KYPLASFEITPDVAILDPELTMTMPPHVTANtGM-DALTHAIEAYVSTLAN-DFTDALALGAILDIFENLPKSYNGGKDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 239 ELRETILYTGTIA----LNGMLSMgargdwaTHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAvrvf 312
Cdd:cd08179 234 EAREKMHNASCLAgmafSNSGLGI-------VHSMAHKGGAFFGIPH--GLanAILLPYVIEFNSKDPEARARYAA---- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 313 diDETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDE----KLDTIADKAMANGA 367
Cdd:cd08179 301 --LLIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDeffaKLDEMAENAMNDAC 357
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-384 |
6.18e-55 |
|
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: 185.40 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIkRSGLYDQVTELLKKAGVTVHELAGVEpNPRVSTVNKGVALCKENS 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSL-RSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDG---DAWDIV-TKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWG 164
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGsvlDYLEVVgKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 165 SPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRET 243
Cdd:cd08183 159 SPSMLPDVALVDPELTLSLPPEVTAAsGL-DALTQLIEPYVSRKAN-PLTDALAREGLRLAARSLRRAYEDGEDLEARED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 244 ILYT---GTIAL-NGMLsmGargdwATHNIEHAVSAVYDIPHagGL--AILFPNWMR---HVLKENPARFKQLAVRVFDI 314
Cdd:cd08183 237 MALAsllGGLALaNAGL--G-----AVHGLAGPLGGMFGAPH--GAicAALLPPVLEanlRALREREPDSPALARYRELA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494650708 315 DETGKSDEEIALEGISRLSDFWTSLGAPnRLADYDISDEKLDTIADKAMANGafgqfkSLQ-------KEDVLAILK 384
Cdd:cd08183 308 GILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSS------SMKgnpielsDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-383 |
2.64e-52 |
|
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: 178.19 E-value: 2.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHElaGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGaRRVLLVTGPSAVRESGAADILDALGGRIPVVVFS--DFSPNPDLEDLERGIELFRES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKE--ALPFGTVLTLAATGSEMNSGSVItnW--ETQEKYGW 163
Cdd:cd08182 79 GPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEenALPLIAIPTTAGTGSEVTPFATI--WdeAEGKKYSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 164 GSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRET 243
Cdd:cd08182 157 AHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNAN-PESRAYALRAIRLILENLPLLLENLPNLEAREA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 244 ILY-----------TGTIALngmlsmgargdwatHNIEHAVSAVYDIPHagGLAILFpnWMRHVLKENparfkqlaVRVF 312
Cdd:cd08182 236 MAEasllaglaisiTKTTAA--------------HAISYPLTSRYGVPH--GHACAL--TLPAVLRYN--------AGAD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 313 DIDETGKSDEEIAL--------EGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFGQF-KSLQKEDVLAIL 383
Cdd:cd08182 290 DECDDDPRGREILLalgasdpaEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNpVRLSEEDLLRLL 369
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-387 |
1.06e-51 |
|
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: 176.55 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALGiRRPLLVTDPG-LAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKK----HQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGW 163
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEDGEggpaAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 164 GSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFhhtsnTPYQDRMCESL----LRTVIETAPKLINDLENY 238
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPRLTAAtGM-DALTHCIEAYL-----SPGFHPMADGIalegLRLISEWLPRAVADGSDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 239 ELREtilytgtialnGML---SMGA----RGDWATHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAV 309
Cdd:cd14861 236 EARG-----------EMMmaaLMGAvafqKGLGAVHALAHALGALYGLHH--GLlnAILLPYVLRFNRPAVEDKLARLAR 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 310 RVFDIDETGKSdeeiALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIADKAMANGAFGQF-KSLQKEDVLAILKASL 387
Cdd:cd14861 303 ALGLGLGGFDD----FIAWVEDLNE---RLGLPATLSELGVTEDDLDELAELALADPCHATNpRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
1.24e-46 |
|
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: 163.94 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVyGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVLIV-TDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPLV 168
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 169 YPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSN--------------TPYQDRMCESLLRTVIETAPKLIND 234
Cdd:cd08191 163 RPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPpfprldpdpvyvgkNPLTDLLALEAIRLIGRHLPRAVRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 235 LENYELRETILYTGTIAlnGMlSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFDI 314
Cdd:cd08191 243 GDDLEARSGMALAALLA--GL-AFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIA-RALGV 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 315 DETGKSdEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMA------NGAfgqfKSLQKEDVLAILKASL 387
Cdd:cd08191 319 TTAGTS-EEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSvtrliaNNP----RPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-363 |
1.31e-45 |
|
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: 160.85 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 5 TYWNPTKLIFGKGEVEKLPEEIkpyGKNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALC 84
Cdd:cd14862 2 WYFSSPKIVFGEDALSHLEQLS---GKRALIVTDKV-LVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 85 KENSIDFLLAVGGGSVIDCTKaiAAGAKYDGDawDIVTKKHQPKEALPFGTVLTLAA------TGSEMNSGSVITNWETQ 158
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAK--AAWVLYERP--DLDPEDISPLDLLGLRKKAKLIAipttsgTGSEATWAIVLTDTEEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 159 EKYGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENY 238
Cdd:cd14862 154 RKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSN-DFSDALALKAIELIFKYLPRAYKDGDDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 239 ELRETILYTGTIA----LNGMLSMgargdwaTHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAVrvfdI 314
Cdd:cd14862 233 EAREKMHNAATIAglafGNSQAGL-------AHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL----L 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 494650708 315 DETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDIS----DEKLDTIADKAM 363
Cdd:cd14862 302 GIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISeeefEEKLDELVEYAM 354
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-364 |
3.85e-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: 341489 [Multi-domain] Cd Length: 374 Bit Score: 154.24 E-value: 3.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 13 IFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENSIDF 91
Cdd:cd17814 8 IFGVGARKLAGRYAKNLGaRKVLVVTDPGVIK-AGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 92 LLAVGGGSVIDCTKAIAAGAKYDGDAWDI--VTKKHQPkeALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPLVY 169
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNGGHILDYegVDKVRRP--LPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 170 PKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELRETILYTGT 249
Cdd:cd17814 165 PDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-SNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 250 IAlnGM----LSMGargdwATHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAvRVFDIDETGKSDEE 323
Cdd:cd17814 244 QA--GLafsnASLG-----AVHAMAHSLGGLLDLPH--GEcnALLLPHVIRFNFPAAPERYRKIA-EAMGLDVDGLDDEE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 494650708 324 IALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMA 364
Cdd:cd17814 314 VAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAMK 354
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-362 |
4.26e-42 |
|
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: 148.67 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKrsGLYDQVTELLKKaGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVK--GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDgdawdivtkkhqpkeaLPFGTVLTLAATGSEMNSGSVITnwETQEKYGWGSPLV 168
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLNRG----------------IPFIIVPTTASTDSEVSPKSVIT--DKGGKNKQVGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 169 YPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEqyfhhtsntpyqdrmcesllrtvietapklindlenyelRETILYTG 248
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVEAA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 249 TIALNGMLSMGarGDWATHNIEHAVSAVYDIPHAGGLAILFPnwmrHVLKENParfkqlavrvfdiDETGKSDEEialeg 328
Cdd:cd07766 181 TLAGMGLFESP--GLGLAHAIGHALTAFEGIPHGEAVAVGLP----YVLKVAN-------------DMNPEPEAA----- 236
|
330 340 350
....*....|....*....|....*....|....
gi 494650708 329 ISRLSDFWTSLGAPNRLADYDISDEKLDTIADKA 362
Cdd:cd07766 237 IEAVFKFLEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-385 |
5.15e-42 |
|
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: 151.25 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHElaGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGaSRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFS--GVRQHTPREDVLEAARAVREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIA------------AGAKYDGDAWD-IVTKKHQPKEALPfgTvlTLAatGSEMNSGSVITN 154
Cdd:cd08192 79 GADLLVSLGGGSPIDAAKAVAlalaedvtdvdqLDALEDGKRIDpNVTGPTLPHIAIP--T--TLS--GAEFTAGAGATD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 155 WETQEKYGWGSPLVYPKFSILDPVNTFTVPKD---HTiyGM--VDmmsHVFEQYFHHTSNtPYQDRMCESLLRTVIETAP 229
Cdd:cd08192 153 DDTGHKQGFAHPELGPDAVILDPELTLHTPERlwlST--GIraVD---HAVETLCSPQAT-PFVDALALKALRLLFEGLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 230 KLINDLENYELReTILYTGTI-ALNGMLSMGARGdwATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLA 308
Cdd:cd08192 227 RSKADPEDLEAR-LKCQLAAWlSLFGLGSGVPMG--ASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 309 VRVFDIDETGKSDEEIALEgisRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMA--NGAFGQFKSLQKEDVLAILKA 385
Cdd:cd08192 304 RALGLVTGGLGREAADAAD---AIDALIRELGLPRTLRDVGVGRDQLEKIAENALTdvWCRTNPRPITDKDDVLEILES 379
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-364 |
4.92e-38 |
|
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: 141.14 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 10 TKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRLGaKKVLVVTDPG-LAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTK-----KHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGW 163
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHPGDFLDYVNApigkgKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 164 GSPLVYPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFHHTSNT-----------PYQ------DRMCESLLRTVI 225
Cdd:cd08190 161 SSRYLRPTLAIVDPLLTLTLPPRVTASsGF-DVLCHALESYTARPYNArprpanpderpAYQgsnpisDVWAEKAIELIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 226 ETAPKLINDLENYELRETILYTGTIAlnGMlSMGARGDWATHNIEHAVSAV-------------YDIPHAGGLAILFPNW 292
Cdd:cd08190 240 KYLRRAVNDGDDLEARSNMLLASTLA--GI-GFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALTAPAV 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494650708 293 MRHVLKENPARFKQLAvRVFDIDETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMA 364
Cdd:cd08190 317 FRFTAPACPERHLEAA-ELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLP 387
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-384 |
4.20e-37 |
|
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: 136.85 E-value: 4.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLpEEIKpyGKNVLLVyGGGSIKRSGLYDQVTELLKKAgVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd08180 4 KTKIYSGEDSLERL-KELK--GKRVFIV-TDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAgakydgDAWDIVTKKHQPKealpFGTVLTLAATGSEMNSGSVITNWETQEKYgwgsPLV 168
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIY------FALKQKGNIKKPL----FIAIPTTSGTGSEVTSFAVITDPEKGIKY----PLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 169 ----YPKFSILDPVNTFTVPKDHTIY-GMvDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELRET 243
Cdd:cd08180 145 ddsmLPDIAILDPELVKSVPPKVTADtGM-DVLTHALEAYV-STNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 244 ILYTGTIAlnGM----LSMGargdwATHNIEHAVSAVYDIPHagGL--AILFPnwmrHVLKenparfkqlavrvFDIdet 317
Cdd:cd08180 223 MHNASCMA--GIafnnAGLG-----INHSLAHALGGRFHIPH--GRanAILLP----YVIE-------------FLI--- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494650708 318 gksdeeialEGISRLSDfwtSLGAPNRLADYDISDE----KLDTIADKAMANGAF-GQFKSLQKEDVLAILK 384
Cdd:cd08180 274 ---------AAIRRLNK---KLGIPSTLKELGIDEEefekAIDEMAEAALADRCTaTNPRKPTAEDLIELLR 333
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-365 |
5.32e-37 |
|
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: 137.64 E-value: 5.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYG-KNVLLVYGGGsIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGaRRVLLVTDPG-LVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDI--VTKKHQPKeaLPFGTVLTLAATGSEMNSGSVITNwETQEKYGWGS 165
Cdd:cd08193 83 GADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIygVGKATGPR--LPLILVPTTAGTGSEVTPISIVTT-GETEKKGVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 166 PLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNTPYQDRM-CE--SLLRTVIETApklINDLENYELRE 242
Cdd:cd08193 160 PQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALaREalRLLGANLRRA---VEDGSDLEARE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 243 TILYTGTIAlnGML----SMGargdwATHNIEHAVSAVYDIPHagGL--AILFPNWMRHVLKENPARFKQLAvRVFDIDE 316
Cdd:cd08193 237 AMLLGSMLA--GQAfanaPVA-----AVHALAYPLGGHFHVPH--GLsnALVLPHVLRFNLPAAEALYAELA-RALLPGL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 494650708 317 TGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMAN 365
Cdd:cd08193 307 AFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQ 355
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-385 |
4.36e-35 |
|
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: 132.42 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 8 NPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSiKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKEN 87
Cdd:cd14864 3 IPPNIVFGADSLERIGEEVKEYGSRFLLITDPVL-KESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPL 167
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 168 VYPKFSILDP-VNTFTVPKDHTIYGMvDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRETILY 246
Cdd:cd14864 162 GLPKAVIVDPnLMASLTGNQTAAMAL-AALALAVEAYLSKKSN-FFSDALALKAIELVSENLDGALADPKNTPAEELLAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 247 TGtiALNGML-SMGARGdwATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFDIDETGKSDEEIA 325
Cdd:cd14864 240 AG--CLAGLAaSSSSPG--LATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIA-RALGEDVEGASPEEAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494650708 326 LEGISRLSDFWTSLGAPNRLADYDISDeKLDTIADKAMANGAFGQF-KSLQKEDVLAILKA 385
Cdd:cd14864 315 IAAVEGVRRLIAQLNLPTRLKDLDLAS-SLEQLAAIAEDAPKLNGLpRSMSSDDIFDILKA 374
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-387 |
7.25e-34 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 129.30 E-value: 7.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 1 MQNFTYWNPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKG 80
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 81 VALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEK 160
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 161 YGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFhHTSNTPYQDRMCESLLRTVIETAPKLINDLENYEL 240
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYV-SIAATPITDACALKAVTMIAENLPLAVEDGSNAKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 241 RETILYTGTIAlnGMLSMGARGDWaTHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLAvRVFDIDETGKS 320
Cdd:PRK09860 240 REAMAYAQFLA--GMAFNNASLGY-VHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCA-AAMGVNVTGKN 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 321 DEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANgAFGQFKSLQ--KEDVLAILKASL 387
Cdd:PRK09860 316 DAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKD-ACGFTNPIQatHEEIVAIYRAAM 383
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-362 |
1.36e-33 |
|
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: 128.84 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPyGKNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENS 88
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPG-VKRAFIVTDRVLYK-LGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQ---------PKE-------ALPfgtvlTLAATGSEMNSGSVI 152
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMdirkrvykfPKLgkkaklvAIP-----TTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 153 TNWETQEKYgwgsPLV-Y---PKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYfhhTSN--TPYQDRMCESLLRTVIE 226
Cdd:cd08178 156 TDDKTGKKY----PLAdYaltPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAY---VSVmaSDYTDGLALQAIKLIFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 227 TAPKLINDLENYELRETILYTGTIAlnGM------LSMgargdwaTHNIEHAVSAVYDIPHagGL--AILFPnwmrHVLK 298
Cdd:cd08178 229 YLPRSYNNGNDIEAREKMHNAATIA--GMafanafLGI-------CHSLAHKLGAAFHIPH--GRanAILLP----HVIR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 299 EN--PARFKQLA-------------VRVFD-IDETGKSDEEIALEGISRLSDFWTSLGAPNRLADYDISDE----KLDTI 358
Cdd:cd08178 294 YNatDPPTKQAAfpqykyyvakeryAEIADlLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEAdflaAVDKL 373
|
....
gi 494650708 359 ADKA 362
Cdd:cd08178 374 AEDA 377
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-387 |
1.91e-30 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 120.10 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 1 MQNFTYWNPTKLiFGKGEVEKLPEEIKPYG-KNVLLVYGGGSIKrSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNK 79
Cdd:PRK10624 1 MANRMILNETAY-FGRGAIGALTDEVKRRGfKKALIVTDKTLVK-CGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 80 GVALCKENSIDFLLAVGGGSVIDCTKAIAAgAKYDGDAWDIV-------TKKHqpkeALPFGTVLTLAATGSEMNSGSVI 152
Cdd:PRK10624 79 GVEVFKASGADYLIAIGGGSPQDTCKAIGI-ISNNPEFADVRslegvapTKKP----SVPIIAIPTTAGTAAEVTINYVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 153 TNWETQEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFhhtsnTPYQDRMCESLLRTVIETAPKLI 232
Cdd:PRK10624 154 TDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYI-----TRGAWALTDMLHLKAIEIIAGAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 233 NDL--ENYELRETILYTGTIAlnGM----LSMGargdwATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQ 306
Cdd:PRK10624 229 RGAvaGDKEAGEGMALGQYIA--GMgfsnVGLG-----LVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 307 LAvRVFDIDETGKSDEEI---ALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIADKAMANGAF-GQFKSLQKEDVLAI 382
Cdd:PRK10624 302 IA-RAMGVKVEGMSLEEArnaAVEAVKALNR---DVGIPPHLRDVGVKEEDIPALAQAAFDDVCTgGNPREATLEDIVEL 377
|
....*
gi 494650708 383 LKASL 387
Cdd:PRK10624 378 YKKAW 382
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-385 |
4.65e-28 |
|
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: 113.48 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 4 FTYWnPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSI-KRSGLYDQVTELL--KKAGVtvheLAGVEPNPRVSTVNKG 80
Cdd:cd14866 1 HDYP-PLRLFSGRGALARLGRELDRLGARRALVVCGSSVgANPDLMDPVRAALgdRLAGV----FDGVRPHSPLETVEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 81 VALCKENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVT------KKHQPKEA---LPFGTVLTlAATGSEMNSGSV 151
Cdd:cd14866 76 AEALREADADAVVAVGGGSAIVTARAASILLAEDRDVRELCTrraedgLMVSPRLDapkLPIFVVPT-TPTTADVKAGSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 152 ITNWETQEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKL 231
Cdd:cd14866 155 VTDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHAD-PLADATLMHALRLLADGLPRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 232 INDLENYELRETILYT---GTIALNGMLSMgargdwaTHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENPARFKQLA 308
Cdd:cd14866 234 ADDDDPAARADLVLAAvlaGYGTDHTGGGV-------IHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 309 vRVFDIDETGksDEEIALEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMANGAFGQ--FKSLQKEDVLAILKA 385
Cdd:cd14866 307 -EALGVADAG--DEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNnpRPVPTAEELEALLEA 382
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-362 |
2.25e-25 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 108.35 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPyGKNVLLVYGGGSIKRsGLYDQVTELLKK--AGVTVHELAGVEPNPRVSTVNKGVALCKE 86
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDG-KKRAFIVTDRFMVEL-GYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 87 NSIDFLLAVGGGSVIDCTKAIaagakydgdaW------------------DI---VTK--KHQPKE---ALPfgtvlTLA 140
Cdd:PRK13805 538 FKPDTIIALGGGSPMDAAKIM----------WlfyehpetdfedlaqkfmDIrkrIYKfpKLGKKAklvAIP-----TTS 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 141 ATGSEMNSGSVITNWETQEKYgwgsPLV-Y---PKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYfhhTSN--TPYQD 214
Cdd:PRK13805 603 GTGSEVTPFAVITDDKTGVKY----PLAdYeltPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAY---VSVmaSDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 215 RMCESLLRTVIETAPKLI-NDLENYELRETILYTGTIAlnGM------LSMGargdwatHNIEHAVSAVYDIPHagGL-- 285
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYkNGAKDPEAREKMHNASTIA--GMafanafLGIC-------HSMAHKLGAEFHIPH--GRan 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 286 AILFPNWMRHVLKENParfKQLA---VRVFDIDE-----------TGKSDEEIA---LEGISRLSDfwtSLGAPNRLADY 348
Cdd:PRK13805 745 AILLPHVIRYNATDPP---KQAAfpqYEYPRADEryaeiarhlglPGSTTEEKVeslIKAIEELKA---ELGIPMSIKEA 818
|
410
....*....|....*...
gi 494650708 349 DIS----DEKLDTIADKA 362
Cdd:PRK13805 819 GVDeadfLAKLDELAELA 836
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-366 |
6.13e-25 |
|
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: 104.09 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVHeLAGVEPNPRVSTVNKGVALCKENS 88
Cdd:COG0371 6 PRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAG--DRLEESLEDAGIEVE-VEVFGGECSEEEIERLAEEAKEQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAGAKydgdawdivtkkhqpkeaLPFGTVLTLAAT---GSemnSGSVI-TNWETQEKYgwg 164
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAVAYRLG------------------LPVVSVPTIASTdapAS---PLSVIyTEDGAFDGY--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 165 spLVYPK---FSILDPvntfTV----PKDHTIYGMVDMMSHVFEQYFHHTSNTPYQD-----------RMCeslLRTVIE 226
Cdd:COG0371 139 --SFLAKnpdLVLVDT----DIiakaPVRLLAAGIGDALAKWYEARDWSLAHRDLAGeyyteaavalaRLC---AETLLE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 227 TAPKLINDLENYELRE--------TILYTGTialnGMLSMGARGdwAT---HNIEHAVSAVYDIPHAG-----GLAILFp 290
Cdd:COG0371 210 YGEAAIKAVEAGVVTPalervveaNLLLSGL----AMGIGSSRP--GSgaaHAIHNGLTALPETHHALhgekvAFGTLV- 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494650708 291 nwmrhvlkenparfkQLAVRvfdidetGKSDEeialegISRLSDFWTSLGAPNRLADYDISD---EKLDTIADKAMANG 366
Cdd:COG0371 283 ---------------QLVLE-------GRPEE------IEELLDFLRSVGLPTTLADLGLDDeteEELLTVAEAARPER 333
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-363 |
8.38e-23 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 98.95 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 5 TYWNPTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGLYDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALC 84
Cdd:PRK15454 23 TFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 85 KENSIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWG 164
Cdd:PRK15454 103 RESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 165 SPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYfHHTSNTPYQDRMCESLLRTVIETAPKLINDLENYELRETI 244
Cdd:PRK15454 183 HASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAY-SALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 245 LYTGTIAlnGMlSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWM---RHVLKEnpaRFKQLAVRVfdidETGKSD 321
Cdd:PRK15454 262 LLASCMA--GM-AFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMefnRMVCRE---RFSQIGRAL----RTKKSD 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 494650708 322 EeiaLEGISRLSDFWTSLGAPNRLADYDISDEKLDTIADKAM 363
Cdd:PRK15454 332 D---RDAINAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL 370
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-385 |
2.58e-19 |
|
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: 87.95 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSikRSGLYDQVTELLKKAGVTVHELAgVEPNPrVSTVNKGVALCKENS 88
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAGVFDGA-VMHVP-VEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 89 IDFLLAVGGGSVIDCTKAIAAgakydgdawdivtKKHQPKEALPfgTvlTLAatGSEMNSgsvitNW-ETQE--KYGWGS 165
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKAIAL-------------RTGLPIVAVP--T--TYA--GSEMTP-----IWgETEDgvKTTGRD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 166 PLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNtPYQDRMCESLLRTVIETAPKLINDLENYELRETIL 245
Cdd:cd08177 133 PRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDAN-PITSLLAEEGIRALARALPRLVADPSDLEARSDAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 246 YtGT----IALnGMLSMGARgdwatHNIEHAVSAVYDIPHAGGLAILFPnwmrHVLKENPARFKQLAVRVFDIDETGKsd 321
Cdd:cd08177 212 Y-GAwlagVVL-GSVGMGLH-----HKLCHVLGGTFDLPHAETHAVVLP----HVLAYNAPAAPDAMARLARALGGGD-- 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494650708 322 eeiALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIADKAMANgAFGQFKSLQKEDVLAILKA 385
Cdd:cd08177 279 ---AAGGLYDLAR---RLGAPTSLRDLGMPEDDIDRAADLALAN-PYPNPRPVERDALRALLER 335
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-366 |
8.08e-18 |
|
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: 83.74 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVH-ELAGVEPNPRvsTVNKGVALCKEN 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVG--EKLEKSLEEAGIDYEvEVFGGECTEE--NIERLAEKAKEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKydgdawdivtkkhqpkeaLPFGTVLTLAATGSEMNSGSVITNWETQEKYGWG--- 164
Cdd:cd08550 77 GADVIIGIGGGKVLDTAKAVADRLG------------------LPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLlkr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 165 SP-LVypkfsILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNTP-------YQdrMCESLLRTVIETAPKLINDLE 236
Cdd:cd08550 139 SPdLV-----LVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPDdlalqaaVQ--LAKLAYDLLLEYGVQAVEDVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 237 N----YELRET----ILYTGTIalNGMLSMGARGDWAtHNIEHAVSAVYDIPHAG-----GLAILFpnwmrhvlkenpar 303
Cdd:cd08550 212 QgkvtPALEDVvdaiILLAGLV--GSLGGGGCRTAAA-HAIHNGLTKLPETHGTLhgekvAFGLLV-------------- 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494650708 304 fkQLAVrvfdideTGKSDEEIAlegisRLSDFWTSLGAPNRLAD--YDISDEKLDTIADKAMANG 366
Cdd:cd08550 275 --QLAL-------EGRSEEEIE-----ELIEFLRRLGLPVTLEDlgLELTEEELRKIAEYACDPP 325
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
13-272 |
5.07e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 71.18 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 13 IFGKGEVEKLPEEI-KPYGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVHELAGVEPNPRVSTVNKGVALCKENSIDF 91
Cdd:pfam13685 1 VIGPGALGRLGEYLaELGFRRVALVADANTYAAAG--RKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 92 LLAVGGGSVIDCTKAIAAgakydgdawdivtkkhqpKEALPFGTVLTLAATGSEMNSGSVITnwETQEKYGWgsPLVYPK 171
Cdd:pfam13685 79 VVGVGGGTVIDLAKYAAF------------------KLGKPFISVPTAASNDGFASPGASLT--VDGKKRSI--PAAAPF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 172 FSILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSNT-PYQDRMCESLLRTVIETAPKLINDLENYELRETILYTGTI 250
Cdd:pfam13685 137 GVIADTDVIAAAPRRLLASGVGDLLAKITAVADWELAHAeEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAM 216
|
250 260
....*....|....*....|..
gi 494650708 251 alnGMLSMGARGDWATHNIEHA 272
Cdd:pfam13685 217 ---GGAGSSRPASGSEHLISHA 235
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
9-142 |
1.35e-13 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; 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.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVHELA-GVEpnprVS--TVNKGVALCK 85
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVG--ERLEESLEKAGLEVVFEVfGGE----CSreEIERLAAIAR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAKydgdawdivtkkhqpkeaLPFGTVLTLAAT 142
Cdd:cd08170 75 ANGADVVIGIGGGKTIDTAKAVADYLG------------------LPVVIVPTIAST 113
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
9-112 |
9.06e-11 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 62.91 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPYGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVHElagvEPNPRVST---VNKGVALCK 85
Cdd:PRK09423 8 PSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVG--DRVEASLKEAGLTVVF----EVFNGECSdneIDRLVAIAE 81
|
90 100
....*....|....*....|....*..
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAK 112
Cdd:PRK09423 82 ENGCDVVIGIGGGKTLDTAKAVADYLG 108
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-108 |
4.93e-10 |
|
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: 60.26 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKP--YGKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVH--ELAGVEpnpRVSTVNKGVALC 84
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKllLGKRALIITGPNTYKIAG--KRVEDLLESSGVEVVivDIATIE---EAAEVEKVKKLI 76
|
90 100
....*....|....*....|....
gi 494650708 85 KENSIDFLLAVGGGSVIDCTKAIA 108
Cdd:cd08173 77 KESKADFIIGVGGGKVIDVAKYAA 100
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-108 |
4.22e-09 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 57.60 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPY--GKNVLLVYGGGSIKRSGlyDQVTELLKKAG-VTVHELagvePNPRVSTVNKGVALCK 85
Cdd:PRK00843 11 PRDVVVGHGVLDDIGDVCSDLklTGRALIVTGPTTKKIAG--DRVEENLEDAGdVEVVIV----DEATMEEVEKVEEKAK 84
|
90 100
....*....|....*....|...
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIA 108
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAA 107
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-201 |
4.87e-09 |
|
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: 57.28 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKPY-----GKNVLLVygGGSIKRSGLYDQvteLLKKAGVTVHELAgVEPNPRVSTVNKGVAL 83
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERrksnnDYVVFFI--DDVFKGKPLLDR---LPLQNGDLLIFVD-TTDEPKTDQIDALRAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 84 CKENSIDFLLAV---GGGSVIDCTKAIA-------AGAKYDGdaWDIVTKKHQPKEALPfgtvlTLAATGSEMNSGSVIT 153
Cdd:cd08184 75 IRAENDKLPAAVvgiGGGSTMDIAKAVSnmltnpgSAADYQG--WDLVKNPGIYKIGVP-----TLSGTGAEASRTAVLT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494650708 154 NWEtqEKYGWGSPLVYPKFSILDPVNTFTVPKDHTIYGMVDMMSHVFE 201
Cdd:cd08184 148 GPE--KKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE 193
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-365 |
7.30e-09 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 56.76 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 15 GKGEVEKLPEEIKPYGKNVLLVygGGSIKRSGLYDQVTELLKKAGVTV--HELAGVEpnprvST---VNKGVALCKENSI 89
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVI--GGKKALAAAKPKLRAALEGSGLEItdFIWYGGE-----ATyenVEKLKANPEVQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 90 DFLLAVGGGSVIDCTKAIAagakydgdawdIVTKKhqpkealPFGTVLTLAATGSEMNSGSVITNwetqEKYGWGSPlVY 169
Cdd:cd08171 80 DMIFAVGGGKAIDTVKVLA-----------DRLNK-------PVFTFPTIASNCAAVTAVSVMYN----PDGSFKEY-YF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 170 PKFSildPVNTF-------TVPKDHTIYGMVDMMSHVFEQYF-------HHTSNTPYQ-DRMC-ESLLR---TVIETApk 230
Cdd:cd08171 137 LKRP---PVHTFidteiiaEAPEKYLWAGIGDTLAKYYEVEFsargdelDHTNALGVAiSKMCsEPLLKygvQALEDC-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 231 lINDLENYELRETILytgTIALN-GMLSMGARGDWATHnIEHAV-SAVYDIPHAGGlailfpnwmRH---------VLke 299
Cdd:cd08171 212 -RANKVSDALEQVVL---DIIVTtGLVSNLVEPDYNSS-LAHALyYGLTTLPQIEE---------EHlhgevvsygVL-- 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494650708 300 nparfKQLAVrvfdideTGKSDEeiaLEgisRLSDFWTSLGAPNRLADYDISDEKLDTIADKAMAN 365
Cdd:cd08171 276 -----VLLTV-------DGQFEE---LE---KVYAFNKSIGLPTCLADLGLTVEDLEKVLDKALKT 323
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-385 |
2.38e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 49.05 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 15 GKGEVEKLPEEIKPYG-KNVLLVYGGGSIK------RSGLYDQVTELLKKAGVTVHElagvepnprvstVNKGVALCKEN 87
Cdd:cd08172 7 EEGALKELPELLSEFGiKRPLIIHGEKSWQaakpylPKLFEIEYPVLRYDGECSYEE------------IDRLAEEAKEH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIAAGAKydgdawdivtkkhqpkeaLPFGTVLTLAATGSEMNSGSVITNWETQ-EKYGwgsp 166
Cdd:cd08172 75 QADVIIGIGGGKVLDTAKAVADKLN------------------IPLILIPTLASNCAAWTPLSVIYDEDGEfIGYD---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 167 lVYPK---FSILDP---VNTftvPKDHTIYGMVD----------MMSH-----VFEQYFHHTSntpyqdRMCESLLRTVI 225
Cdd:cd08172 133 -YFPRsayLVLVDPrllLDS---PKDYFVAGIGDtlakwyeadaILRQleelpAFLQLARQAA------KLCRDILLKDS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 226 ETApklINDLENYELR-------ETIlytgtIALNGML-SMGAR-----GDWATHNiehAVSAVYDIPHA--G---GLAI 287
Cdd:cd08172 203 EQA---LADLEAGKLTpafikvvETI-----IALAGMVgGFGDEygrsaGAHAIHN---GLTKLPETHHFlhGekvAYGI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 288 LFpnwmrhvlkenparfkQLAVrvfdideTGKSDEeialegISRLSDFWTSLGAPNRLAD---YDISDEKLDTIADKAMA 364
Cdd:cd08172 272 LV----------------QLAL-------EGKWDE------IKKLLPFYRRLGLPTSLADlglTDDTEEALQKIAAFAAS 322
|
410 420
....*....|....*....|...
gi 494650708 365 -NGAFGQ-FKSLQKEDVLAILKA 385
Cdd:cd08172 323 pEESIHLlPPDVTAEEVLQAIEK 345
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
94-385 |
2.47e-06 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 49.14 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 94 AVGGGSVIDCTKAIAagAKYDGDAWDIVTKKHQPKEALPFGTVLTLAATGSEMNSGSVITNWETQEKYGWGSPLVYPKFS 173
Cdd:cd14860 84 AIGGGTVIDIAKLLA--LKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 174 ILDPVNTFTVPKDHTIYGMVDMMSHVFEQYFHHTSnTPYQD----RMCESLLRTVIETAPK----LINDLENYELRETil 245
Cdd:cd14860 162 VLIPELLKGLPYKVFATSSIDALIHAIESYLSPKA-TPYTEmfsyKAIEMILEGYQEIAEKgeeaRFPLLGDFLIASN-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 246 YTGtialngmLSMGARGDWATHNIEHAVSAVYDIPHAGGLAILFPNWMRHVLKENP-ARFKQLAVRVFDIDETgksDEEI 324
Cdd:cd14860 239 YAG-------IAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPdGEIKKLNEFLAKILGC---DEED 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494650708 325 ALEGISRLSDfwtSLGAPNRLADYDISDEKLDTIAD-------KAMANGafgqFKSLQKEDVLAILKA 385
Cdd:cd14860 309 VYDELEELLN---KILPKKPLHEYGMKEEEIDEFADsvmenqqRLLANN----YVPLDREDVAEIYKE 369
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
9-112 |
1.37e-05 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 46.74 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIKP---YGKNVLLVYGGGSIKRsgLYDQVTELLKKAGVTVHelagVEPNPRVSTVNKGVALCK 85
Cdd:cd08174 1 PLILKIEEGALEHLGKYLADrnqGFGKVAIVTGEGIDEL--LGEDILESLEEAGEIVT----VEENTDNSAEELAEKAFS 74
|
90 100
....*....|....*....|....*..
gi 494650708 86 ENSIDFLLAVGGGSVIDCTKAIAAGAK 112
Cdd:cd08174 75 LPKVDAIVGIGGGKVLDVAKYAAFLSK 101
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
9-108 |
9.78e-04 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 40.63 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 9 PTKLIFGKGEVEKLPEEIK-PYGKNVLLVYGGGSikrsglYDQVTELLKKAGVTVHELAGVEpnprvSTVNKGVALCKEN 87
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKkLNLKRVLIITGKNT------KAKYCRFFYDQLKTVCDIVYYD-----NIDNLEDELKKYT 69
|
90 100
....*....|....*....|.
gi 494650708 88 SIDFLLAVGGGSVIDCTKAIA 108
Cdd:cd08549 70 FYDCVIGIGGGRSIDTGKYLA 90
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
11-108 |
1.76e-03 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 40.19 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494650708 11 KLIFGKGEVEKLPEEIKPY--GKNVLLVYGGGSIKRSGlyDQVTELLKKAGVTVHEL-AGVEPNPRVSTVNKG-VALCKE 86
Cdd:cd08175 3 EIVIGEGALKKLPEYLKELfgGKKVLVVADENTYAAAG--EEVEAALEEAGVTVCLLiFPGEGDLIADEAAVGkVLLELE 80
|
90 100
....*....|....*....|..
gi 494650708 87 NSIDFLLAVGGGSVIDCTKAIA 108
Cdd:cd08175 81 KDTDLIIAVGSGTINDLTKYAA 102
|
|
| |
