|
Name |
Accession |
Description |
Interval |
E-value |
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-383 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 696.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 1 MQNFTFHNPTRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALT--DFTLLEFGGIEPNPTYETLMQA 77
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKyGKKVLLVYGGGSIKKNGLYDQVKAALKeaGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 78 VALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDK 157
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDAKVQDRFAEGLLLTLIEDGPKALAEADNYAV 237
Cdd:COG1979 161 LGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 238 RANLMWTATLALNGLIGAGVPQDWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIWDLHDGDED 317
Cdd:COG1979 241 RANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEGDDE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521995257 318 ARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQNVDLEQSRQVLALA 383
Cdd:COG1979 321 ERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELA 386
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-379 |
0e+00 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 624.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 1 MQNFTFHNPTRILFGSGQIAAIHQEIPSGARVLMTYGGGSVVKTGTLAEVKAALTDFTLLEFGGIEPNPTYETLMQAVAL 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 81 ARREQVDFLLAVGGGSVIDGTKFIAAAI--PFAGEPWDIL-AKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDK 157
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAAnyPENIDPWHILeTGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDAKVQDRFAEGLLLTLIEDGPKALAEADNYAV 237
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEPENYDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 238 RANLMWTATLALNGLIGAGVPQDWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIWDLHDGDED 317
Cdd:PRK15138 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEGSDD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521995257 318 ARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQNVDLEQSRQV 379
Cdd:PRK15138 321 ERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHGMTQLGEHHDITLDVSRRI 382
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-380 |
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: 559.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 3 NFTFHNPTRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVA 79
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKKyGKKVLLVYGGGSIKKNGLYDRVVASLKEagIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 80 LARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLG 159
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 160 FGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDAKVQDRFAEGLLLTLIEDGPKALAEADNYAVRA 239
Cdd:cd08187 161 FGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 240 NLMWTATLALNGLIGAGVPQDWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIWDLH-DGDEDA 318
Cdd:cd08187 241 NLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDpGGDDEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521995257 319 RIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQnVDLEQSRQVL 380
Cdd:cd08187 321 TALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKP-LTREDIEEIL 381
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-356 |
1.31e-100 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 302.60 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVvKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALARREQ 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSL-KSGLLDKVLASLEEagIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 86 VDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNPLV 165
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 166 FPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTyPDDAKVQDRFAEGLLLTLIEDGPKALAEADNYAVRANLMWTA 245
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-KGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 246 TLALNGLIGAGVPqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIWdlhDGDEDARIDTAIR 325
Cdd:pfam00465 239 TLAGLAFSNAGLG---AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG---EDSDEEAAEEAIE 312
|
330 340 350
....*....|....*....|....*....|.
gi 521995257 326 RTRDFFESLQVPTRLSSYGIGPEAITPLVRA 356
Cdd:pfam00465 313 ALRELLRELGLPTTLSELGVTEEDLDALAEA 343
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-354 |
3.14e-65 |
|
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: 211.97 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQAVAL 80
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRpGKKALIVTGKGSSKKTGLLDRVKKLLEkagvEVVV--FDKVEPNPLTTTVMEGAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 81 ARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDIL----AKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQD 156
Cdd:cd08185 79 AKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIfggtGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 157 KLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLtypddAKVQDRFAEGLLLT---LIEDG-PKALAEA 232
Cdd:cd08185 159 KKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYI-----SKNANPFSDMLALEairLVAKYlPRAVKDG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 233 DNYAVRANLMWTATLA--LNGLIGAGVPqdwatHMLGHEITALHG-LDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIW 309
Cdd:cd08185 234 SDLEAREKMAWASTLAgiVIANSGTTLP-----HGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAEA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 521995257 310 DLHDGDEDARidTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLV 354
Cdd:cd08185 309 SGLSDAKAAE--DFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA 351
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-380 |
7.51e-65 |
|
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: 210.77 E-value: 7.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI--PSGARVLMTYGGGsVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALARRE 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELkaLGGKKVLLVTDPG-LVKAGLLDKVLESLKAagIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 85 QVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNPL 164
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 165 VFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLtypddAKVQDRFAEGLLL---TLI-EDGPKALAEADNYAVRAN 240
Cdd:cd08551 160 LLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYT-----SKKANPISDALALeaiRLIgKNLRRAVADGSDLEAREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 241 LMWTATLALNGLIGAGVpqdWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIW-DLHDGDEDAR 319
Cdd:cd08551 235 MLLASLLAGIAFGNAGL---GAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGeDVEGLSDEEA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521995257 320 IDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQNVDLEQSRQVL 380
Cdd:cd08551 312 AEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
2-364 |
9.71e-65 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 210.75 E-value: 9.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 2 QNFTFHNPTRILFGSGQIAAIHQEIPS-GAR--VLMTygGGSVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQ 76
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRlGAKraLIVT--DPGLAKLGLLDRVLDALEAagIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 77 AVALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQD 156
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 157 KLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLtypddAKVQDRFAEGLLL---TLIEDG-PKALAEA 232
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYV-----SKGANPLTDALALeaiRLIARNlPRAVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 233 DNYAVRANLMWTATLA----LNGLIGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQyAARI 308
Cdd:COG1454 234 DDLEAREKMALASLLAgmafANAGLG-------AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAE-IARA 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 521995257 309 WDLHDG-DEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVR-ALERHGMTA 364
Cdd:COG1454 306 LGLDVGlSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAElALADRCLAN 363
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-301 |
1.29e-53 |
|
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: 181.24 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQAVAL 80
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAAlGKKALIVTGKHSAKKNGSLDDVTEALEengiEYFI--FDEVEENPSIETVEKGAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 81 ARREQVDFLLAVGGGSVIDGTKFIAAaipFAGEPWDI--LAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKL 158
Cdd:cd08181 79 ARKEGADFVIGIGGGSPLDAAKAIAL---LAANKDGDedLFQNGKYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 159 GFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDaKVQDRFAEGLLLTLIEDGPKALAEADNYAVR 238
Cdd:cd08181 156 SFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKAT-PLSDALALEALRLIGECLPNLLGDELDEEDR 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521995257 239 ANLMWTATLAlnGLI----GAGVPqdwatHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKL 301
Cdd:cd08181 235 EKLMYASTLA--GMViaqtGTTLP-----HGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKV 294
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-358 |
1.07e-52 |
|
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: 176.02 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI-PSGARVLMTYGGGsvVKTGTLAEVKAALTDF-TLLEFGGIEPNPTYETLMQAVALARREQV 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKrRGFDRALVVSDEG--VVKGVGEKVADSLKKGlAVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 87 DFLLAVGGGSVIDGTKFIAAAipfagepwdilakqapITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFgnPLVF 166
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAAL----------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVG--PHYN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 167 PRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEqyltypddakvqdrfaegllltliedgpkalaeadnyavRANLMWTAT 246
Cdd:cd07766 141 PDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 247 LALNGLIgaGVPQDWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREkllqyaariwdlhdgdedarIDTAIRR 326
Cdd:cd07766 182 LAGMGLF--ESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE--------------------PEAAIEA 239
|
330 340 350
....*....|....*....|....*....|..
gi 521995257 327 TRDFFESLQVPTRLSSYGIGPEAITPLVRALE 358
Cdd:cd07766 240 VFKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-356 |
9.10e-48 |
|
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: 166.22 E-value: 9.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 4 FTFHNPTRILFGSGQIAAIHQEIP--SGARVLMTyGGGSVVKTGTLAEVKAALTDFTLLEFGGIEPNPTYETLMQAVALA 81
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKelGGKRGLLV-TDPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 82 RREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILA-KQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGF 160
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEgKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 161 GNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQY---LTYPddakVQDRFAEG---LLLTLIEdgpKALAEADN 234
Cdd:cd08196 160 VSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYwsiNHQP----ISDALALEaakLVLENLE---KAYNNPND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 235 YAVRANLMWTATLAlnGLigA-GVPQDWATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIwdlhd 313
Cdd:cd08196 233 KEAREKMALASLLA--GL--AfSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL----- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 521995257 314 GDEDarIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRA 356
Cdd:cd08196 304 GFKD--AEELADKIEELKKRIGLRTRLSELGITEEDLEEIVEE 344
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-384 |
1.49e-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: 341485 [Multi-domain] Cd Length: 380 Bit Score: 155.39 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 5 TFHNPTRILFGSG---QIAAIHQEIPsGARVLMTYGGGsVVKTGTLAEVKAALTDFTLL--EFGGIEPNPTYETLMQAVA 79
Cdd:cd14863 1 TYSQLTPVIFGAGaveQIGELLKELG-CKKVLLVTDKG-LKKAGIVDKIIDLLEEAGIEvvVFDDVEPDPPDEIVDEAAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 80 LARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWD-ILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKL 158
Cdd:cd14863 79 IAREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 159 GFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQY---LTYPddakVQDRFAEGLLLTLIEDGPKALAEADNY 235
Cdd:cd14863 159 SLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYtskLANP----MTDALALQAIRLIVKNLPRAVKDGDNL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 236 AVRANLMWTATLALNGLIGAGVpqdWATHMLGHEITALHGLDHAQTLAIVLPAMLQIR---RRDKREKLlqyaARIWDLH 312
Cdd:cd14863 235 EARENMLLASNLAGIAFNNAGT---HIGHAIAHALGALYHIPHGLACALALPVVLEFNaeaYPEKVKKI----AKALGVS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521995257 313 DGDEDAR--IDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHgMTALGERQNVDLEQSRQVLALAC 384
Cdd:cd14863 308 FPGESDEelGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKD-PFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-357 |
1.67e-41 |
|
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: 149.72 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 10 TRILFGSGQIAAIhQEIPSGA---RVLMTYGGGSVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALARRE 84
Cdd:cd08186 2 TTLYFGVGAIAKI-KDILKDLgidKVIIVTGRSSYKKSGAWDDVEKALEEngIEYVVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 85 QVDFLLAVGGGSVIDGTKFIAAAIPFAGE-PWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNP 163
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLLAYGGKtARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 164 LVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTypddaKVQDRFAEGLLLTLI----EDGPKALAEADNYAVRA 239
Cdd:cd08186 161 CIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATT-----KVSSPYVITLAKEAIrliaEYLPRALANPKDLEARY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 240 NLMWTATLalngligAGVPQDWA----THMLGHEITAL-HGLDHAQTLAIVLPAMLQIRRRDKREKLlqyaARIWDLHDG 314
Cdd:cd08186 236 WLLYASMI-------AGIAIDNGllhlTHALEHPLSGLkPELPHGLGLALLGPAVVKYIYKAVPETL----ADILRPIVP 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 521995257 315 D-----EDAriDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRAL 357
Cdd:cd08186 305 GlkgtpDEA--EKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELA 350
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-349 |
1.65e-40 |
|
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: 146.95 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIhQEIPsGARVLMTYGGGSVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALARR 83
Cdd:cd08179 2 FFVPRDIYFGEGALEYL-KTLK-GKRAFIVTGGGSMKRNGFLDKVEDYLKEagMEVKVFEGVEPDPSVETVEKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 84 EQVDFLLAVGGGSVIDGTK------------FIAAAIPFAGEPwdiLAKQApITAAVPfgsvlTLPATGSEMNSFSVITR 151
Cdd:cd08179 80 FEPDWIIAIGGGSVIDAAKamwvfyeypeltFEDALVPFPLPE---LRKKA-RFIAIP-----STSGTGSEVTRASVITD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 152 AATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQY-LTYPDDakVQDRFAEGLLLTLIEDGPKALA 230
Cdd:cd08179 151 TEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYvSTLAND--FTDALALGAILDIFENLPKSYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 231 EADNYAVRANLMWTATLA----LNGLIGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKllqyAA 306
Cdd:cd08179 229 GGKDLEAREKMHNASCLAgmafSNSGLG-------IVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEAR----AR 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 521995257 307 RIWDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEA 349
Cdd:cd08179 298 YAALLIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDE 340
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-353 |
5.01e-40 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 145.76 E-value: 5.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 4 FTFHNPTRILFGSGQIAAIHQEIPS-GAR--VLMTYGGgsVVKTGTLAEVKAALTDFTLLE--FGGIEPNPTYETLMQAV 78
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARlGARrpLIVTDKG--LAAAGLLKKVEDALGDAIEIVgvFDDVPPDSSVAVVNEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 79 ALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGE-PWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDK 157
Cdd:cd14865 79 ARAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDdLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYL---TYPddakVQDRFAEGLLLTLIEDGPKALAEADN 234
Cdd:cd14865 159 LLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTslqKNP----ISDALALQAIRLISENLPKAVKNGKD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 235 YAVRANLMWTATLA----LNGLIGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQ---IRRRDKREKLLQYAAR 307
Cdd:cd14865 235 LEARLALAIAATMAgiafSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVMRynlDAAAERYAELALALAY 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 521995257 308 IWDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPL 353
Cdd:cd14865 308 GVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAI 353
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-356 |
4.35e-39 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 143.13 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI--PSGARVLMTYGGGSVVKTGTLAEVKAALTDFTLLEFGGIEPNPTYETLMQAVALARREQV 86
Cdd:cd08182 1 PVKIIFGPGALAELKDLLggLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 87 DFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILA--KQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNPL 164
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRtgEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 165 VFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQY---------LTYPDDAkvqdrfAEGLLLTLiedgPKALAEADNY 235
Cdd:cd08182 161 LYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIwsvnanpesRAYALRA------IRLILENL----PLLLENLPNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 236 AVRANLMWTATLAlnGL--------IGagvpqdwatHMLGHEITALHGLDH----AQTLAIVLPAMLQIRRRDKREKLLQ 303
Cdd:cd08182 231 EAREAMAEASLLA--GLaisitkttAA---------HAISYPLTSRYGVPHghacALTLPAVLRYNAGADDECDDDPRGR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 521995257 304 YAARIWDLHDGDEdaridtAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRA 356
Cdd:cd08182 300 EILLALGASDPAE------AAERLRALLESLGLPTRLSEYGVTAEDLEALAAS 346
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-356 |
1.43e-38 |
|
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: 141.87 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIPS-GARVLMTyGGGSVVKTGTLAEVKAALT--DFTLLEFGGIEpNPTYETLMQAVALARREQ 85
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAElGKRALLV-TGRSSLRSGRLARLLEALEaaGIEVALFSVSG-EPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 86 VDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDIL----AKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFG 161
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGSVLDYLevvgKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 162 NPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLT---YPddakVQDRFA-EGL------LLTLIEDGpkalae 231
Cdd:cd08183 159 SPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSrkaNP----LTDALArEGLrlaarsLRRAYEDG------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 232 aDNYAVRANLMWTA-----TLALNGLiGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQ-----IRRRDKREKL 301
Cdd:cd08183 229 -EDLEAREDMALASllgglALANAGL-G-------AVHGLAGPLGGMFGAPHGAICAALLPPVLEanlraLREREPDSPA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 521995257 302 LQYAARIWDLHDGDEDARIDTAIRRTRDFFESLQVPtRLSSYGIGPEAITPLVRA 356
Cdd:cd08183 300 LARYRELAGILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEK 353
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-356 |
2.37e-37 |
|
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: 138.41 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 7 HNPTRILFGSGQIAAIHQEIPS-GAR--VLMTYGGgsVVKTGTLAEVKAALTD----FTLleFGGIEPNPTYETLMQAVA 79
Cdd:cd14861 1 NYPTRIRFGAGAIAELPEELKAlGIRrpLLVTDPG--LAALGIVDRVLEALGAaglsPAV--FSDVPPNPTEADVEAGVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 80 LARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAK---QAPITAAVPFgsVLTLP---ATGSEMNSFSVITRAA 153
Cdd:cd14861 77 AYREGGCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEDGeggPAAITPAVPP--LIAIPttaGTGSEVGRAAVITDDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 154 TQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLtypddAKVQDRFAEGLLL---TLIEDG-PKAL 229
Cdd:cd14861 155 TGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYL-----SPGFHPMADGIALeglRLISEWlPRAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 230 AEADNYAVRANLMWTATLA----LNGLiGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYA 305
Cdd:cd14861 230 ADGSDLEARGEMMMAALMGavafQKGL-G-------AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLA 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 521995257 306 ARIwdlhdGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRA 356
Cdd:cd14861 302 RAL-----GLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAEL 347
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
4-355 |
1.76e-36 |
|
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: 136.14 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 4 FTFHNPTRILFGSGQIAAIHQEIPS-GAR--VLMTYGGgsVVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQ 76
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKrGFKkaLIVTDKG--LVKFGIVDKVTDVLKeagiAYTV--FDEVKPNPTIENVMA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 77 AVALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITA-AVPFGSVLTLPATGSEMNSFSVITRAATQ 155
Cdd:cd08176 77 GVAAYKESGADGIIAVGGGSSIDTAKAIGIIVANPGADVRSLEGVAPTKNpAVPIIAVPTTAGTGSEVTINYVITDTEKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 156 DKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTypddaKVQDRFAEGLLL---TLI-EDGPKALAE 231
Cdd:cd08176 157 RKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-----KGAWELSDMLALkaiELIaKNLRKAVAN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 232 ADNYAVRANLMWTATLALNGL--IGAGVpqdwaTHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKllqYA--AR 307
Cdd:cd08176 232 PNNVEARENMALAQYIAGMAFsnVGLGI-----VHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEK---YRdiAR 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521995257 308 IWDLhDG----DEDARiDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVR 355
Cdd:cd08176 304 AMGV-DTtgmsDEEAA-EAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-380 |
3.68e-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: 341484 [Multi-domain] Cd Length: 375 Bit Score: 132.73 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 11 RILFGSGQIAAIHQEIpsGARVLMTYGGGsVVKTGTLAEVKAAL--TDFTLLEFGGIEPNPTYETLMQAVALARREQVDF 88
Cdd:cd14862 8 KIVFGEDALSHLEQLS--GKRALIVTDKV-LVKLGLLKKVLKRLlqAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 89 LLAVGGGSVIDGTKfiaAA--------IPFAGEP--WDILAKQAPITAAVPfgsvlTLPATGSEMNSFSVITRAATQDKL 158
Cdd:cd14862 85 IIALGGGSVMDAAK---AAwvlyerpdLDPEDISplDLLGLRKKAKLIAIP-----TTSGTGSEATWAIVLTDTEEPRKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 159 GFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYL-TYPDDakvqdrFAEGLLLTLIEDG----PKALAEAD 233
Cdd:cd14862 157 AVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLsTWSND------FSDALALKAIELIfkylPRAYKDGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 234 NYAVRANLMWTATLAlnGL----IGAGVpqdwaTHMLGHEITALHGLDHAQTLAIVLPAMLQ--IRRRDKREKLLQYAar 307
Cdd:cd14862 231 DLEAREKMHNAATIA--GLafgnSQAGL-----AHALGHSLGAVFHVPHGIAVGLFLPYVIEfyAKVTDERYDLLKLL-- 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521995257 308 iwDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPE----AITPLVRALERHGMTALGERQnVDLEQSRQVL 380
Cdd:cd14862 302 --GIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEefeeKLDELVEYAMEDSCTITSPRP-PSEEDLKKLF 375
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-356 |
4.49e-34 |
|
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: 130.04 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIHQEI-PSGARVLMtygggsV-----VKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQA 77
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAaRLGSRVLI------VtdprlASTPLVAELLAALTAagVAVEVFDGGQPELPVSTVADA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 78 VALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDK 157
Cdd:cd08191 75 AAAARAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLT---YPDDAKVQDRFAEGL-LLT---------LIED 224
Cdd:cd08191 155 VGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTArdfPPFPRLDPDPVYVGKnPLTdllaleairLIGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 225 G-PKALAEADNYAVRANLMWTATLALNGLIGAGVPqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQ 303
Cdd:cd08191 235 HlPRAVRDGDDLEARSGMALAALLAGLAFGTAGTA---AAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 521995257 304 YAARIWDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRA 356
Cdd:cd08191 312 IARALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEK 364
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-350 |
1.66e-33 |
|
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: 128.02 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 4 FTFHNPTRILFGSGQIAAIHQEIPS--GARVLMTYGGGsVVKTGTLAEVKAAL----TDFTLleFGGIEPNPTYETLMQA 77
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKlgGKKALIVTDKG-LVKLGLVKKVTDVLeeagIEYVI--FDGVQPNPTVTNVNEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 78 VALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWD-----ILAKQAPitaavPFGSVLTLPATGSEMNSFSVITRA 152
Cdd:cd08188 78 LELFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDyegvdKSKKPGL-----PLIAINTTAGTASEVTRFAVITDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 153 ATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTyPDDAKVQDRFAEGLLLTLIEDGPKALAEA 232
Cdd:cd08188 153 ERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVS-TGATPLTDALALEAIRLIAENLPKAVANG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 233 DNYAVRANLMWTATLA----LNGLIGagvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARI 308
Cdd:cd08188 232 KDLEARENMAYAQFLAgmafNNAGLG-------YVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARAL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 521995257 309 W-DLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAI 350
Cdd:cd08188 305 GeNTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDF 347
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-383 |
3.32e-31 |
|
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: 121.97 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI-PSGA-RVLMTYGGGSVVKTGTLAEVKAALTDFTLLEFGGIEPNPTYETLMQAVALARREQV 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELaTLGAsRVFIVTSKSLATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 87 DFLLAVGGGSVIDGTKFIAAAI---PFAGEPWDILAKQAPITAAV--PFGSVLTLPAT--GSEMNSFSVITRAATQDKLG 159
Cdd:cd08192 81 DLLVSLGGGSPIDAAKAVALALaedVTDVDQLDALEDGKRIDPNVtgPTLPHIAIPTTlsGAEFTAGAGATDDDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 160 FGNPLVFPRFSVLDPTKTYTLPPR-QVANGV--IDAFV----HIAEQYLTypddakvqDRFAEGLLLTLIEDGPKALAEA 232
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERlWLSTGIraVDHAVetlcSPQATPFV--------DALALKALRLLFEGLPRSKADP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 233 DNYAVRANLM---WTATLALNGLIGAGvpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARIW 309
Cdd:cd08192 233 EDLEARLKCQlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521995257 310 DLHDGDEDARIDTAiRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQNVDLEQSRQVLALA 383
Cdd:cd08192 308 LVTGGLGREAADAA-DAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKDDVLEILESA 380
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-349 |
1.34e-29 |
|
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: 117.63 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIPS--GARVLMTyGGGSVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALARRE 84
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASlgGKRALIV-TDKVMVKLGLVDKVTQLLAEagIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 85 QVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNPL 164
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 165 VFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLT---YPddakVQDRFAEGLLLTLIEDGPKALAEADNYAVRANL 241
Cdd:cd08194 160 LLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSrkaQP----LTDTLALSAIKLIGRNLRRAYADGDDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 242 MWTATLAlnGL----------------IGA--GVPqdwathmlgheitalHGLDHaqtlAIVLPAMLQIRRRDKREKllq 303
Cdd:cd08194 236 MLAALEA--GIafsnssvalvhgmsrpIGAlfHVP---------------HGLSN----AMLLPAVTEFSLPGAPER--- 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 521995257 304 YA--ARIWDL---HDGDEDArIDTAIRRTRDFFESLQVPTrLSSYGIGPEA 349
Cdd:cd08194 292 YAeiARAMGIateGDSDEEA-AEKLVEALERLCADLEIPT-LREYGIDEEE 340
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
38-342 |
5.83e-28 |
|
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: 112.95 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 38 GGSVVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQAVALARREQVDFLLAVGGGSVIDGTKFIAAAipfAGE 113
Cdd:cd08189 35 DKGLVKLGLLDPLLDALKkagiEYVV--FDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIAAR---AAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 114 PWDILA---------KQAPITAAVPfgsvlTLPATGSEMNSFSVITRAATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQ 184
Cdd:cd08189 110 PKKSVRklkgllkvrKKLPPLIAVP-----TTAGTGSEATIAAVITDPETHEKYAINDPKLIPDAAVLDPELTLGLPPAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 185 VANGVIDAFVHIAEQYL--TYPDDAKVQDRFAEGLLLtliEDGPKALAEADNYAVRANLMWT---ATLALN-GLIGagvp 258
Cdd:cd08189 185 TAATGMDALTHAVEAYIsrSATKETDEYALEAVKLIF---ENLPKAYEDGSDLEARENMLLAsyyAGLAFTrAYVG---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 259 qdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIrRRDKREKLLQYAARIWDLHDGDEDARI--DTAIRRTRDFFESLQV 336
Cdd:cd08189 258 ---YVHAIAHQLGGLYGVPHGLANAVVLPHVLEF-YGPAAEKRLAELADAAGLGDSGESDSEkaEAFIAAIRELNRRMGI 333
|
....*.
gi 521995257 337 PTRLSS 342
Cdd:cd08189 334 PTTLEE 339
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-380 |
5.60e-26 |
|
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: 108.02 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 10 TRILFGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQAVALARRE 84
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRlGAKKVLVVTDPGLAKLGLVERVLESLEkagiEVVV--YDGVRVEPTDESFEEAIEFAKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 85 QVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAkqAPITAAVPF-GSVLTLPA------TGSEMNSFSVITRAATQDK 157
Cdd:cd08190 80 DFDAFVAVGGGSVIDTAKAANLYATHPGDFLDYVN--APIGKGKPVpGPLKPLIAipttagTGSETTGVAIFDLEELKVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDAK-----------------VQDRFAEGLLLT 220
Cdd:cd08190 158 TGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARprpanpderpayqgsnpISDVWAEKAIEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 221 LIEDGPKALAEADNYAVRANLMWTATLALNGLIGAGVPqdwATHMLGHEITAL-----------------HGLdhaqTLA 283
Cdd:cd08190 238 IGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVH---LPHAMAYPIAGLvkdyrppgypvdhphvpHGL----SVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 284 IVLPAMLQIRRRDKREKLLQyAARIWDLHD---GDEDARiDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVR-ALER 359
Cdd:cd08190 311 LTAPAVFRFTAPACPERHLE-AAELLGADTsgaSDRDAG-EVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEgTLPQ 388
|
410 420
....*....|....*....|.
gi 521995257 360 HGMTALGERQnVDLEQSRQVL 380
Cdd:cd08190 389 QRLLKLNPRP-VTEEDLEEIF 408
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
6-200 |
2.12e-22 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 96.79 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIhQEIPsGARVLMtygggsV-----VKTGTLAEVKAALTDFTLLE-FGGIEPNPTYETLMQAVA 79
Cdd:cd08180 1 FSLKTKIYSGEDSLERL-KELK-GKRVFI------VtdpfmVKSGMVDKVTDELDKSNEVEiFSDVVPDPSIEVVAKGLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 80 LARREQVDFLLAVGGGSVIDGTKfiaAAIPFAGEPWDILAKQAPItaAVPFGSvltlpATGSEMNSFSVITRAATQDKLG 159
Cdd:cd08180 73 KILEFKPDTIIALGGGSAIDAAK---AIIYFALKQKGNIKKPLFI--AIPTTS-----GTGSEVTSFAVITDPEKGIKYP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521995257 160 FGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQY 200
Cdd:cd08180 143 LVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAY 183
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-345 |
2.27e-22 |
|
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: 97.64 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIPSGARVL-MTygGGSVVKTGTLAEVKAAL--TDFTLLEFGGIEPNPTYETLMQAVALARREQ 85
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPGVKRAFiVT--DRVLYKLGYVDKVLDVLeaRGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 86 VDFLLAVGGGSVID------------GTKFIAAAIPFAgepwDI---------LAKQApITAAVPfgsvlTLPATGSEMN 144
Cdd:cd08178 81 PDVIIALGGGSAMDaakimwlfyehpETKFEDLAQRFM----DIrkrvykfpkLGKKA-KLVAIP-----TTSGTGSEVT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 145 SFSVITRAATQDKLgfgnPL----VFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYL-TYPDDakvqdrFAEGL-- 217
Cdd:cd08178 151 PFAVITDDKTGKKY----PLadyaLTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVsVMASD------YTDGLal 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 218 --LLTLIEDGPKALAEADNYAVRANLMWTATLAlnGLIGA----GVpqdwaTHMLGHEITALHGLDHAQTLAIVLPAMLQ 291
Cdd:cd08178 221 qaIKLIFEYLPRSYNNGNDIEAREKMHNAATIA--GMAFAnaflGI-----CHSLAHKLGAAFHIPHGRANAILLPHVIR 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521995257 292 ---IRRRDKREKLLQYA-----------ARIWDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGI 345
Cdd:cd08178 294 ynaTDPPTKQAAFPQYKyyvakeryaeiADLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGI 361
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-380 |
1.41e-21 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 94.99 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIP-SGARVLMTYGGGSVVK-TGTLAEVKAALTDFTLLEFGGIEPNPTYETLMQAVALARREQV 86
Cdd:cd14866 5 PLRLFSGRGALARLGRELDrLGARRALVVCGSSVGAnPDLMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 87 DFLLAVGGGSVIDGTKfiAAAIPFA-GEPWDILAKQA--------PITAA--VPFGSVLTLPATGSEMNSFSViTRAATQ 155
Cdd:cd14866 85 DAVVAVGGGSAIVTAR--AASILLAeDRDVRELCTRRaedglmvsPRLDApkLPIFVVPTTPTTADVKAGSAV-TDPPAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 156 DKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEqyLTYPDDAkvqDRFAEGLL---LTLIEDGPKALAEA 232
Cdd:cd14866 162 QRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVE--GLYSRHA---DPLADATLmhaLRLLADGLPRLADD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 233 DNYAVRANLMWTATLALNGLIGAGVPqdwATHMLGHEITALHGLDHAQTLAIVLP---AMLQIRRRDKREKLlqyaARIW 309
Cdd:cd14866 237 DDPAARADLVLAAVLAGYGTDHTGGG---VIHALGHAIGARYGVQNGVVHAILLPhvlRFNAPATDGRLDRL----AEAL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521995257 310 DLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALERHGMTALGERQNVDLEQSRQVL 380
Cdd:cd14866 310 GVADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVPTAEELEALL 380
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-346 |
3.40e-21 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 93.90 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIHQEIPS-GARVL-----MTYGggsvvkTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQA 77
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEyGSRFLlitdpVLKE------SGLADKIVSSLEKagISVIVFDEIPASATSDTIDEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 78 VALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAAT-QD 156
Cdd:cd14864 75 AELARKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSrEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 157 KLgFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTyPDDAKVQDRFAEGLLLTLIEDGPKALAEADNYA 236
Cdd:cd14864 155 KL-LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-KKSNFFSDALALKAIELVSENLDGALADPKNTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 237 VRANLMWTAtlALNGLIGAGVPQDWAThMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQyAARIW--DLHDG 314
Cdd:cd14864 233 AEELLAQAG--CLAGLAASSSSPGLAT-ALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAK-IARALgeDVEGA 308
|
330 340 350
....*....|....*....|....*....|..
gi 521995257 315 DEDARIDTAIRRTRDFFESLQVPTRLSSYGIG 346
Cdd:cd14864 309 SPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLA 340
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-353 |
3.62e-21 |
|
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: 93.73 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 6 FHNPTRILFGSGQIAAIHQEI--PSGARVLMTYGGGsVVKTGTLAEVKAALTD--FTLLEFGGIEPNPTYETLMQAVALA 81
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLreLGARRVLLVTDPG-LVKAGLADPALAALEAagIAVTVFDDVVADPPEAVVEAAVEQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 82 RREQVDFLLAVGGGSVIDGTKFIAAaipFAGEPWDI-------LAK-------QAPITAAvpfgsvltlpaTGSEMNSFS 147
Cdd:cd08193 80 REAGADGVIGFGGGSSMDVAKLVAL---LAGSDQPLddiygvgKATgprlpliLVPTTAG-----------TGSEVTPIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 148 VITRAATQdKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPDDAKVQDRFA-EGLLLtLIEDGP 226
Cdd:cd08193 146 IVTTGETE-KKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALArEALRL-LGANLR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 227 KALAEADNYAVRANLMWTATLALNGLIGAGVPqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIrRRDKREKLlqYA- 305
Cdd:cd08193 224 RAVEDGSDLEAREAMLLGSMLAGQAFANAPVA---AVHALAYPLGGHFHVPHGLSNALVLPHVLRF-NLPAAEAL--YAe 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 521995257 306 -ARI--WDLHDGDEDARIDTAIRRTRDFFESLQVPTRLSSYGIGPEAITPL 353
Cdd:cd08193 298 lARAllPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPML 348
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
41-355 |
5.40e-19 |
|
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: 87.60 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 41 VVKTGTLAEVKAALT----DFTLleFGGIEPNPTYETLMQAVALARREQVDFLLAVGGGSVIDGTKFIAAAipfAGEPWD 116
Cdd:cd17814 37 VIKAGWVDEVLDSLEaeglEYVV--FSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIV---VSNGGH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 117 IL--------AKQAPITAAVPfgsvlTLPATGSEMNSFSVITRAATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANG 188
Cdd:cd17814 112 ILdyegvdkvRRPLPPLICIP-----TTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPETLTTMDPELTACT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 189 VIDAFVHIAEQY-------LTypddakvqDRFA-EGLLLtLIEDGPKALAEADNYAVRANLMW---TATLAL-NGLIGag 256
Cdd:cd17814 187 GMDALTHAIEAYvsnasspLT--------DLHAlEAIRL-ISENLPKAVADPDDLEAREKMMLaslQAGLAFsNASLG-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 257 vpqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARI-WDLHDGDEDARIDTAIRRTRDFFESLQ 335
Cdd:cd17814 256 -----AVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMgLDVDGLDDEEVAERLIEAIRDLREDLG 330
|
330 340
....*....|....*....|
gi 521995257 336 VPTRLSSYGIGPEAITPLVR 355
Cdd:cd17814 331 IPETLSELGVDEEDIPELAK 350
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
69-348 |
5.54e-19 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 87.78 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 69 PTYETLMQAVALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSV 148
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 149 ITRAATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYlTYPDDAKVQDRFAEGLLLTLIEDGPKA 228
Cdd:PRK15454 170 IIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAY-SALNATPFTDSLAIGAIAMIGKSLPKA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 229 LAEADNYAVRANLMWTATLALNGLIGAGVPqdwATHMLGHEITALHGLDHAQTLAIVLPAMLQIRRRDKREKLLQYAARI 308
Cdd:PRK15454 249 VGYGHDLAARESMLLASCMAGMAFSSAGLG---LCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL 325
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 521995257 309 WDLHDGDEDaridtAIRRTRDFFESLQVPTRLSSYGIGPE 348
Cdd:PRK15454 326 RTKKSDDRD-----AINAVSELIAEVGIGKRLGDVGATSA 360
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-287 |
1.90e-17 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 83.08 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 1 MQNFTFHNPTRILFGSGQI-AAIHQEIPSGARVLMTYGGGSVVKTGTLAEVKAALT--DFTLLEFGGIEPNPTYETLMQA 77
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLtDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEerNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 78 VALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEPWDILAKQAPITAAVPFGSVLTLPATGSEMNSFSVITRAATQDK 157
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 158 LGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLTYPdDAKVQDRFAEGLLLTLIEDGPKALAEADNYAV 237
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIA-ATPITDACALKAVTMIAENLPLAVEDGSNAKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 521995257 238 RANLMWTATLALNGLIGAGVPQdwaTHMLGHEITALHGLDHAQTLAIVLP 287
Cdd:PRK09860 240 REAMAYAQFLAGMAFNNASLGY---VHAMAHQLGGFYNLPHGVCNAVLLP 286
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-202 |
9.98e-14 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 71.95 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 14 FGSGQIAAIHQEIPS-GARVLMTYGGGSVVKTGTLAEVKAALTDFTLLE--FGGIEPNPTYETLMQAVALARREQVDFLL 90
Cdd:PRK10624 13 FGRGAIGALTDEVKRrGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYeiYDGVKPNPTIEVVKEGVEVFKASGADYLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 91 AVGGGSVIDGTKFIAAAI---PFAgepwDILAKQ--APIT-AAVPFGSVLTLPATGSEMNSFSVITRAATQDKLGFGNPL 164
Cdd:PRK10624 93 AIGGGSPQDTCKAIGIISnnpEFA----DVRSLEgvAPTKkPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPH 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 521995257 165 VFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYLT 202
Cdd:PRK10624 169 DIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT 206
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
62-345 |
3.78e-13 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 70.98 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 62 FGGIEPNPTYETLMQAVALARREQVDFLLAVGGGSVIDGTK------------FIAAAIPFAgepwDI---------LAK 120
Cdd:PRK13805 516 FSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKimwlfyehpetdFEDLAQKFM----DIrkriykfpkLGK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 121 QApITAAVPfgsvlTLPATGSEMNSFSVITRAATQDKLgfgnPLV----FPRFSVLDPTKTYTLPPRQVANGVIDAFVHI 196
Cdd:PRK13805 592 KA-KLVAIP-----TTSGTGSEVTPFAVITDDKTGVKY----PLAdyelTPDVAIVDPNLVMTMPKSLTADTGIDALTHA 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 197 AEQYL-TYPDDakvqdrFAEGLLL----TLIEDGPKALAE-ADNYAVRANLMWTATLAlnGLIGA----GVpqdwaTHML 266
Cdd:PRK13805 662 LEAYVsVMASD------YTDGLALqaikLVFEYLPRSYKNgAKDPEAREKMHNASTIA--GMAFAnaflGI-----CHSM 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 267 GHEITALHGLDHAQTLAIVLP--------------AMLQIRRRDKREKllqYA--ARIWDLHDGDEDARIDTAIRRTRDF 330
Cdd:PRK13805 729 AHKLGAEFHIPHGRANAILLPhvirynatdppkqaAFPQYEYPRADER---YAeiARHLGLPGSTTEEKVESLIKAIEEL 805
|
330
....*....|....*
gi 521995257 331 FESLQVPTRLSSYGI 345
Cdd:PRK13805 806 KAELGIPMSIKEAGV 820
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-368 |
5.26e-13 |
|
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: 69.46 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEIPS-GARVLMtygggsVVKTG---TLAE-VKAALTDFTLLEFGGIEPNPTYETLMQAVALARR 83
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERlGARRAL------VLSTPrqrALAErVAALLGDRVAGVFDGAVMHVPVEVAERALAAARE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 84 EQVDFLLAVGGGSVIdGtkfiaaaipfagepwdiLAKQAPITAAVPfgsVLTLPAT--GSEMNSFSVITRAATqdKLGFG 161
Cdd:cd08177 75 AGADGLVAIGGGSAI-G-----------------LAKAIALRTGLP---IVAVPTTyaGSEMTPIWGETEDGV--KTTGR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 162 NPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYltYPDDAK-VQDRFAEGLLLTLIEDGPKALAEADNYAVRAN 240
Cdd:cd08177 132 DPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEAL--YAPDANpITSLLAEEGIRALARALPRLVADPSDLEARSD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 241 LMWTATLalngligAGVpqdwathMLGHEITALH-----------GLDHAQTLAIVLP------------AMLQIRRRDK 297
Cdd:cd08177 210 ALYGAWL-------AGV-------VLGSVGMGLHhklchvlggtfDLPHAETHAVVLPhvlaynapaapdAMARLARALG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 298 REKLlqyAARIWDLHdgdedaridtairrtrdffESLQVPTRLSSYGIGPEAITPLV-----------RALERHGMTALG 366
Cdd:cd08177 276 GGDA---AGGLYDLA-------------------RRLGAPTSLRDLGMPEDDIDRAAdlalanpypnpRPVERDALRALL 333
|
..
gi 521995257 367 ER 368
Cdd:cd08177 334 ER 335
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
62-201 |
4.69e-10 |
|
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: 60.69 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 62 FGGIEPNptyETLMQAV-ALARREQVDFLLAVGGGSVIDGTKFIAAAIPFAGEpwDILAKQAPITAAVPFGSVLTLPATG 140
Cdd:cd14860 57 YGTGEPS---DEMVEAIyKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVL--DLFDGKIPLIKEKELIIVPTTCGTG 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521995257 141 SEMNSFSVITRAATQDKLGFGNPLVFPRFSVLDPTKTYTLPPRQVANGVIDAFVHIAEQYL 201
Cdd:cd14860 132 SEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYL 192
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-380 |
7.31e-09 |
|
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: 56.71 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI-PSGARVLMTYGGGSVVKTGtlAEVKAALTD----FTLLEFGGiepNPTYETLMQAVALARR 83
Cdd:COG0371 6 PRRYVQGEGALDELGEYLaDLGKRALIITGPTALKAAG--DRLEESLEDagieVEVEVFGG---ECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 84 EQVDFLLAVGGGSVIDGTKFIAAAipfagepwdilakqapitAAVPFGSVLTLPAT---GSemnSFSVITraaTQDKlgf 160
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYR------------------LGLPVVSVPTIASTdapAS---PLSVIY---TEDG--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 161 gnplVFPRFSVLDPTKTYTL---------PPRQVANGVIDAfvhIAEQY-------------LTYPDDAKVQdrFAEGLL 218
Cdd:COG0371 134 ----AFDGYSFLAKNPDLVLvdtdiiakaPVRLLAAGIGDA---LAKWYeardwslahrdlaGEYYTEAAVA--LARLCA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 219 LTLIEDGPKALAEADNYAVRANLMWT--ATLALNGLIGAGVPQDWAT---HMLGHEITALHGLDHAQ--------TLaiv 285
Cdd:COG0371 205 ETLLEYGEAAIKAVEAGVVTPALERVveANLLLSGLAMGIGSSRPGSgaaHAIHNGLTALPETHHALhgekvafgTL--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 286 lpAMLQirrrdkrekllqyaariwdLHDGDEdaridtAIRRTRDFFESLQVPTRLSSYGIGPEAITPLVRALER---HGM 362
Cdd:COG0371 282 --VQLV-------------------LEGRPE------EIEELLDFLRSVGLPTTLADLGLDDETEEELLTVAEAarpERY 334
|
410
....*....|....*...
gi 521995257 363 TALGERQNVDLEQSRQVL 380
Cdd:COG0371 335 TILNLPFEVTPEAVEAAI 352
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-110 |
3.50e-06 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 48.35 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSG---QIAAIHQEIPSGARVLMTYGGgsvvKTGTLA--EVKAALTDFTLLEFGGIEpNPTYETLMQAVALARR 83
Cdd:PRK00843 11 PRDVVVGHGvldDIGDVCSDLKLTGRALIVTGP----TTKKIAgdRVEENLEDAGDVEVVIVD-EATMEEVEKVEEKAKD 85
|
90 100
....*....|....*....|....*....
gi 521995257 84 EQVDFLLAVGGGSVIDGTKFIA--AAIPF 110
Cdd:PRK00843 86 VNAGFLIGVGGGKVIDVAKLAAyrLGIPF 114
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
64-131 |
1.84e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 45.76 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 64 GIEPNPTYETLMQAVALARREQVDFLLAVGGGSVIDGTKFIAA-------AIPFA---------GEPWDILAKQAPITAA 127
Cdd:pfam13685 54 EVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAKYAAFklgkpfiSVPTAasndgfaspGASLTVDGKKRSIPAA 133
|
....
gi 521995257 128 VPFG 131
Cdd:pfam13685 134 APFG 137
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-348 |
9.68e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 40.98 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSGQIAAIHQEI-PSGARVLMTYGGGSvvktgtLAEVKAALT--------DFTLLEFGGiepNPTYETLMQAVA 79
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIaPLGKKALIIGGKTA------LEAVGEKLEksleeagiDYEVEVFGG---ECTEENIERLAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 80 LARREQVDFLLAVGGGSVIDGTKFIAaaipfagepwDILakQAPItAAVPfgsvlTLPATGSEMNSFSVI-TRAATQDKL 158
Cdd:cd08550 72 KAKEEGADVIIGIGGGKVLDTAKAVA----------DRL--GLPV-VTVP-----TIAATCAAWSALSVLyDEEGEFLGY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 159 GFgnPLVFPRFSVLDPTKTYTLPPRQVANGVIDAF-------VHIAEQYLTYPDDAKVQdrFAEGLLLTLIEDGPKALAE 231
Cdd:cd08550 134 SL--LKRSPDLVLVDTDIIAAAPVRYLAAGIGDTLakwyearPSSRGGPDDLALQAAVQ--LAKLAYDLLLEYGVQAVED 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 232 ADNYAVRANLMWT--ATLALNGLIGA---GVPQDWATHMLGHEITAL---HGLDHAQTLAIVLPAMLQIRRRDKREkllq 303
Cdd:cd08550 210 VRQGKVTPALEDVvdAIILLAGLVGSlggGGCRTAAAHAIHNGLTKLpetHGTLHGEKVAFGLLVQLALEGRSEEE---- 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 521995257 304 yaariwdlhdgdedaridtaIRRTRDFFESLQVPTRLSSYGIGPE 348
Cdd:cd08550 286 --------------------IEELIEFLRRLGLPVTLEDLGLELT 310
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-110 |
1.29e-03 |
|
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: 40.61 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521995257 9 PTRILFGSG---QIAAIHQEIPSGARVLMTYG-------GGSVVKtgtlaEVKAALTDFTLLEFGGIEpnpTYETLMQAV 78
Cdd:cd08173 2 PRNVVVGHGainKIGEVLKKLLLGKRALIITGpntykiaGKRVED-----LLESSGVEVVIVDIATIE---EAAEVEKVK 73
|
90 100 110
....*....|....*....|....*....|....
gi 521995257 79 ALARREQVDFLLAVGGGSVIDGTKFIA--AAIPF 110
Cdd:cd08173 74 KLIKESKADFIIGVGGGKVIDVAKYAAykLNLPF 107
|
|
| |
