|
Name |
Accession |
Description |
Interval |
E-value |
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
1-372 |
0e+00 |
|
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: 650.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 1 MEALRVVPKIFYFDTFKEFNEEFKIGKNDLVITNEFIYEPYMKPLGIDTNLIFQEKFGTGEPSDEMIDSMTKEMKKYNFD 80
Cdd:cd14860 1 MKEFRIKPEIYQFDTCKEFAEEFKLGKDDLVLTNEYIYEPYFEPLNLDCAVIFQEKYGTGEPSDEMVEAIYKDIKKYGYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 81 RIIAFGGGTIVDICKILALDVPEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLAVEETYADY 160
Cdd:cd14860 81 RVIAIGGGTVIDIAKLLALKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 161 AVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEEERFNHLRDFVLASNYA 240
Cdd:cd14860 161 AVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEIAEKGEEARFPLLGDFLIASNYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 241 GIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNGKIIKCTKILADALECDPnCDVYGELEKFLNK 320
Cdd:cd14860 241 GIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPDGEIKKLNEFLAKILGCDE-EDVYDELEELLNK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1527686801 321 LIAKKALREYGMVESQIDEFTDSTIANQQRLLANNYVELSREEIREIFANLY 372
Cdd:cd14860 320 ILPKKPLHEYGMKEEEIDEFADSVMENQQRLLANNYVPLDREDVAEIYKELY 371
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-372 |
2.02e-97 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 294.33 E-value: 2.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 1 MEALRVVPKIFY-FDTFKEFNEEFKI--GKNDLVITNEFIYE-PYMKPL-------GIDTnLIFQEkfGTGEPSDEMIDS 69
Cdd:COG1454 2 MFTFRLPTRIVFgAGALAELGEELKRlgAKRALIVTDPGLAKlGLLDRVldaleaaGIEV-VVFDD--VEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 70 MTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHT 147
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLAtnPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 148 KKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGE--EE 225
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDdlEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 226 RfnhlRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPnGKIIKctkiLADALECD 305
Cdd:COG1454 239 R----EKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAP-ERYAE----IARALGLD 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1527686801 306 PNC-------DVYGELEKFLNKLIAKKALREYGMVESQIDEFTDStiANQQRLLANNYVELSREEIREIFANLY 372
Cdd:COG1454 310 VGLsdeeaaeALIEAIRELLRDLGIPTRLSELGVTEEDLPELAEL--ALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-364 |
3.12e-89 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 272.94 E-value: 3.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 8 PKIFYF--DTFKEFNEEFK-IGKNDLVITNEF-----IYEPYMKPL---GIDTNlIFQEKfgTGEPSDEMIDSMTKEMKK 76
Cdd:pfam00465 1 PTRIVFgaGALAELGEELKrLGARALIVTDPGslksgLLDKVLASLeeaGIEVV-VFDGV--EPEPTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 77 YNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLAVE 154
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLtnPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 155 ETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEEErfNHLRDFV 234
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDL--EARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 235 LASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPnGKIIKCTKILADALECDPNCDVYGEL 314
Cdd:pfam00465 236 LASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAP-EKLAQLARALGEDSDEEAAEEAIEAL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1527686801 315 EKFLNKLIAKKALREYGMVESQIDEFTDSTIanQQRLLANNYVELSREEI 364
Cdd:pfam00465 315 RELLRELGLPTTLSELGVTEEDLDALAEAAL--RDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
26-368 |
4.84e-79 |
|
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: 246.98 E-value: 4.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 26 GKNDLVITNEFIY-----EPYMKPL---GIDTnLIFQEkfGTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKIL 97
Cdd:cd08551 23 GKKVLLVTDPGLVkagllDKVLESLkaaGIEV-EVFDD--VEPNPTVETVEAAAELAREEGADLVIAVGGGSVLDTAKAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 98 AL--DVPEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKF 175
Cdd:cd08551 100 AVlaTNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDVAILDPELTLSLPPSV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 176 FVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGE--EERfnhlRDFVLASNYAGIAFGNAGCAAVH 253
Cdd:cd08551 180 TAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSdlEAR----EAMLLASLLAGIAFGNAGLGAVH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 254 ALSYSIGGAFHVAHGEANYQFFTEVFK---MYSRKKpngkiikcTKILADALECDPN--------CDVYGELEKFLNKLI 322
Cdd:cd08551 256 ALAYPLGGRYHIPHGVANAILLPYVMEfnlPACPEK--------YAEIAEALGEDVEglsdeeaaEAAVEAVRELLRDLG 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1527686801 323 AKKALREYGMVESQIDEFTDSTIANqQRLLANNYVELSREEIREIF 368
Cdd:cd08551 328 IPTSLSELGVTEEDIPELAEDAMKS-GRLLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
59-372 |
4.04e-60 |
|
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: 198.53 E-value: 4.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 59 TGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSID-LFEGEVSPKKVKELVVVPTTCGTGSEVT 135
Cdd:cd14863 65 EPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAVLLtnPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 136 NVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGY 215
Cdd:cd14863 145 PIAVITDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 216 KKIVDKGE--EERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNgKIIK 293
Cdd:cd14863 225 PRAVKDGDnlEARENML----LASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPE-KVKK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 294 ctkiLADALECDPNCDVYGEL--------EKFLNKLIAKKALREYGMVESQIDEFTDSTIANQQRllANNYVELSREEIR 365
Cdd:cd14863 300 ----IAKALGVSFPGESDEELgeavadaiREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFA--MFNPRPITEEEVA 373
|
....*..
gi 1527686801 366 EIFANLY 372
Cdd:cd14863 374 EILEAIY 380
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
62-368 |
2.47e-54 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 182.78 E-value: 2.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVS-PKKVKELVVVPTTCGTGSEVTNVA 138
Cdd:cd08196 67 PTVENVDKCARLARENGADFVIAIGGGSVLDTAKAAACLAktDGSIEDYLEGKKKiPKKGLPLIAIPTTAGTGSEVTPVA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 139 IAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKI 218
Cdd:cd08196 147 VLTDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 219 VDKGE--EERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYqfFT-EVFKMYSRKKPNGKIikct 295
Cdd:cd08196 227 YNNPNdkEAREKMA----LASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACA--LTlPSFIRLNAEALPGRL---- 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1527686801 296 KILADALECDPNCDVYGELEKFLNKLIAKKALREYGMVESQIDEFT-DSTIANqqrLLANNYVELSREEIREIF 368
Cdd:cd08196 297 DELAKQLGFKDAEELADKIEELKKRIGLRTRLSELGITEEDLEEIVeESFHPN---RANNNPVEVTKEDLEKLL 367
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
61-368 |
3.12e-53 |
|
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: 181.20 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 61 EPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL------DVPEksiDLF----EGEVSPKKVKELVVVPTTCGT 130
Cdd:cd08190 63 EPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAANLyathpgDFLD---YVNapigKGKPVPGPLKPLIAIPTTAGT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 131 GSEVTNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKffVTSS--VDALIHAIESYLS--------PK----- 195
Cdd:cd08190 140 GSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPR--VTASsgFDVLCHALESYTArpynarprPAnpder 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 196 -----ASPFTEMYSLQAIKMIMDGYKKIVDKGE--EERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGG------- 261
Cdd:cd08190 218 payqgSNPISDVWAEKAIELIGKYLRRAVNDGDdlEARSNML----LASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 262 ------AFHVAHGE---------------ANYQFFTEVFKMYSRKKPNGKIIKCTKILADAlecdpncdvygeLEKFLNK 320
Cdd:cd08190 294 pgypvdHPHVPHGLsvaltapavfrftapACPERHLEAAELLGADTSGASDRDAGEVLADA------------LIKLMRD 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1527686801 321 LIAKKALREYGMVESQIDEFTDSTIAnQQRLLANNYVELSREEIREIF 368
Cdd:cd08190 362 IGIPNGLSALGYSEDDIPALVEGTLP-QQRLLKLNPRPVTEEDLEEIF 408
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
75-369 |
3.06e-52 |
|
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: 177.39 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 75 KKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEvSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLA 152
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAanKDGDEDLFQNG-KYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 153 VEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIvdKGEEERFNHLRD 232
Cdd:cd08181 159 NPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNL--LGDELDEEDREK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 233 FVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNGKiikcTKILADALECDpncdvYG 312
Cdd:cd08181 237 LMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKV----DKILKLLGFGS-----IE 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1527686801 313 ELEKFLNKLIAKKALreygMVESQIDEFTDstIANQQRLLANNYVELSREEIREIFA 369
Cdd:cd08181 308 EFQKFLNRLLGKKEE----LSEEELEKYAD--EAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
62-368 |
7.87e-51 |
|
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: 174.22 E-value: 7.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVPEKSID---LFEGEVSPKKVKE---LVVVPTTCGTGSEVT 135
Cdd:cd08185 67 PLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIwdyIFGGTGKGPPPEKalpIIAIPTTAGTGSEVD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 136 NVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKffVTSSV--DALIHAIESYLSPKASPFTEMYSLQAIKMIMD 213
Cdd:cd08185 147 PWAVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPR--VTAYTgfDALFHAFESYISKNANPFSDMLALEAIRLVAK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 214 GYKKIVDKGEEErfnHLRDFV-LASNYAGIAFGNAGCAAVHALSYSIGGAF-HVAHGEANYQFFTEVFKMYSRKKPNgki 291
Cdd:cd08185 225 YLPRAVKDGSDL---EAREKMaWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPE--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 292 iKCTKI----LADALECDPNCDVYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANQQRLLANNYVELSREEIREI 367
Cdd:cd08185 299 -KFAFVaraeASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETMGGLFANNPVELTEEDIVEI 377
|
.
gi 1527686801 368 F 368
Cdd:cd08185 378 Y 378
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
62-368 |
1.33e-48 |
|
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: 168.17 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL---DVPEKSIDLFEGEVSP-KKVKELVVVPTTCGTGSEVTNV 137
Cdd:cd08182 63 PDLEDLERGIELFRESGPDVIIAVGGGSVIDTAKAIAAllgSPGENLLLLRTGEKAPeENALPLIAIPTTAGTGSEVTPF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 138 A---IAELKSKHTkkgLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDG 214
Cdd:cd08182 143 AtiwDEAEGKKYS---LAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILEN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 215 YKKIVDKGEEERfnhLRDFVL-ASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNGKIIK 293
Cdd:cd08182 220 LPLLLENLPNLE---AREAMAeASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDP 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1527686801 294 CTKILADALECDPNCDVYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANqQRlLANNYVELSREEIREIF 368
Cdd:cd08182 297 RGREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTP-ER-LKNNPVRLSEEDLLRLL 369
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-368 |
1.42e-47 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 165.48 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 6 VVPKIFYFDTFKEFNEEFkIGKNDLVITNEFIYE-PYMKPL-------GIDTnLIFQEKfgTGEPSDEMIDSMTKEMKKY 77
Cdd:cd14862 5 SSPKIVFGEDALSHLEQL-SGKRALIVTDKVLVKlGLLKKVlkrllqaGFEV-EVFDEV--EPEPPLETVLKGAEAMREF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 78 NFDRIIAFGGGTIVDICK-ILAL----DVPEKSIDLFEgEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLA 152
Cdd:cd14862 81 EPDLIIALGGGSVMDAAKaAWVLyerpDLDPEDISPLD-LLGLRKKAKLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 153 VEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGE--EERFNhl 230
Cdd:cd14862 160 NPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDdlEAREK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 231 rdFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKpNGKIIKCTKILADALECDPNC-D 309
Cdd:cd14862 238 --MHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVT-DERYDLLKLLGIEARDEEEALkK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1527686801 310 VYGELEKFLNKLIAKKALREYGMVESQIDE---------FTDSTianqqrlLANNYVELSREEIREIF 368
Cdd:cd14862 315 LVEAIRELYKEVGQPLSIKDLGISEEEFEEkldelveyaMEDSC-------TITSPRPPSEEDLKKLF 375
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
61-372 |
4.66e-47 |
|
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: 164.29 E-value: 4.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 61 EPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL--DVPEKSidlFEGEVSPKKVKEL------VVVPTTCGTGS 132
Cdd:cd08179 64 DPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAAKAMWVfyEYPELT---FEDALVPFPLPELrkkarfIAIPSTSGTGS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 133 EVTNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIM 212
Cdd:cd08179 141 EVTRASVITDTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 213 DGYKKIVDKGEEERfnhLRDFVL-ASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKmYSRKKPNGKI 291
Cdd:cd08179 221 ENLPKSYNGGKDLE---AREKMHnASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIE-FNSKDPEARA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 292 IKCTKI--LADALECDPNCDVYGELEKFLNkliAKKALREYGMVE----SQIDEFTDstIANQQRLLANNYVELSREEIR 365
Cdd:cd08179 297 RYAALLigLTDEELVEDLIEAIEELNKKLG---IPLSFKEAGIDEdeffAKLDEMAE--NAMNDACTGTNPRKPTVEEMK 371
|
....*..
gi 1527686801 366 EIFANLY 372
Cdd:cd08179 372 ELLKAAY 378
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
62-372 |
7.01e-47 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 163.87 E-value: 7.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSD---EMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVPE--KSIDLFEG-EVSPKKVKELVVVPTTCGTGSEVT 135
Cdd:cd14865 66 PPDssvAVVNEAAARAREAGADGIIAVGGGSVIDTAKGVNILLSEggDDLDDYGGaNRLTRPLKPLIAIPTTAGTGSEVT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 136 NVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGY 215
Cdd:cd14865 146 LVAVIKDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 216 KKIVDKG--EEERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEV--FKMYSRKKPNGKI 291
Cdd:cd14865 226 PKAVKNGkdLEARLALA----IAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVmrYNLDAAAERYAEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 292 IKCTKILADALECDPNcDVYGELEKFLNKLIAK----KALREYGMVESQIDEFTDSTIANQQrlLANNYVELSREEIREI 367
Cdd:cd14865 302 ALALAYGVTPAGRRAE-EAIEAAIDLVRRLHELcglpTRLRDVGVPEEQLEAIAELALNDGA--ILFNPREVDPEDILAI 378
|
....*
gi 1527686801 368 FANLY 372
Cdd:cd14865 379 LEAAY 383
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
58-367 |
4.00e-44 |
|
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: 156.51 E-value: 4.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 58 GTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILA--LDVPEKSIDLFEGEVSPKKVKE----LVVVPTTCGTG 131
Cdd:cd08183 58 VSGEPTVETVDAAVALAREAGCDVVIAIGGGSVIDAAKAIAalLTNEGSVLDYLEVVGKGRPLTEpplpFIAIPTTAGTG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 132 SEVT-NVAIAELKSKHtKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKM 210
Cdd:cd08183 138 SEVTkNAVLSSPEHGV-KVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 211 IMDGYKKIVDKGE--EERfnhlRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHG-----------EANYQFFTE 277
Cdd:cd08183 217 AARSLRRAYEDGEdlEAR----EDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGaicaallppvlEANLRALRE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 278 vfkmysrKKPNGKIIKCTKILADALECDPNC---DVYGELEKFLNKL-IAKkaLREYGMVESQIDEFTDStiANQQRLLA 353
Cdd:cd08183 293 -------REPDSPALARYRELAGILTGDPDAaaeDGVEWLEELCEELgIPR--LSEYGLTEEDFPEIVEK--ARGSSSMK 361
|
330
....*....|....
gi 1527686801 354 NNYVELSREEIREI 367
Cdd:cd08183 362 GNPIELSDEELLEI 375
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
62-372 |
7.94e-44 |
|
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: 155.75 E-value: 7.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVPEKS-------IDLFEGEVSPkkvkeLVVVPTTCGTGSEV 134
Cdd:cd08193 67 PPEAVVEAAVEQAREAGADGVIGFGGGSSMDVAKLVALLAGSDQplddiygVGKATGPRLP-----LILVPTTAGTGSEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 135 TNVAIAELKSkHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSP-KASPFTEMYSLQAIKMIMD 213
Cdd:cd08193 142 TPISIVTTGE-TEKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhKKNPISDALAREALRLLGA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 214 GYKKIVDKG--EEERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFK--------MYS 283
Cdd:cd08193 221 NLRRAVEDGsdLEAREAML----LGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRfnlpaaeaLYA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 284 RKKPN---GKIIKCTKILADALecdpncdvYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIAnQQRLLANNYVELS 360
Cdd:cd08193 297 ELARAllpGLAFGSDAAAAEAF--------IDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMK-QTRLLVNNPREVT 367
|
330
....*....|..
gi 1527686801 361 REEIREIFANLY 372
Cdd:cd08193 368 EEDALAIYQAAL 379
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
59-372 |
1.86e-43 |
|
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: 154.61 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 59 TGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICK-ILALDVPEKSIDLFEG-EVSPKKVKELVVVPTTCGTGSEVTN 136
Cdd:cd08194 61 VSEPTDEMVEEGLALYKEGGCDFIVALGGGSPIDTAKaIAVLATNGGPIRDYMGpRKVDKPGLPLIAIPTTAGTGSEVTR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 137 VAI---AELKSKHTKKGLAVeetYADYAVLIPETVKGLPYKffVTSS--VDALIHAIESYLSPKASPFTEMYSLQAIKMI 211
Cdd:cd08194 141 FTVitdTETDVKMLLKGPAL---LPAVAIVDPELTLSMPPR--VTAAtgIDALTHAIEAYVSRKAQPLTDTLALSAIKLI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 212 MDGYKKIVDKGE--EERfnhlRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKmYSRKKPNG 289
Cdd:cd08194 216 GRNLRRAYADGDdlEAR----EAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTE-FSLPGAPE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 290 KIIKCTKILADALECDPNCDVYGELEKFLNKLIAK---KALREYGM----VESQIDEFTDSTIANQqrLLANNYVELSRE 362
Cdd:cd08194 291 RYAEIARAMGIATEGDSDEEAAEKLVEALERLCADleiPTLREYGIdeeeFEAALDKMAEDALASG--SPANNPRVPTKE 368
|
330
....*....|
gi 1527686801 363 EIREIFANLY 372
Cdd:cd08194 369 EIIELYREAW 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
6-271 |
2.22e-43 |
|
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: 153.42 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 6 VVPKIFYFDTFKEFNEEFKiGKNDLVITNEFIYE-PYMKPlgIDTNL-------IFQEKfgTGEPSDEMIDSMTKEMKKY 77
Cdd:cd08180 3 LKTKIYSGEDSLERLKELK-GKRVFIVTDPFMVKsGMVDK--VTDELdksneveIFSDV--VPDPSIEVVAKGLAKILEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 78 NFDRIIAFGGGTIVDICKilaldvpekSIDLFEGEVSP-KKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLAVEET 156
Cdd:cd08180 78 KPDTIIALGGGSAIDAAK---------AIIYFALKQKGnIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 157 YADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEEErfnHLRDFV-L 235
Cdd:cd08180 149 LPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDL---EAREKMhN 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1527686801 236 ASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd08180 226 ASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRAN 261
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
62-371 |
3.57e-43 |
|
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: 153.78 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEvspKKVKE----LVVVPTTCGTGSEVT 135
Cdd:cd08189 68 PTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIAARAanPKKSVRKLKGL---LKVRKklppLIAVPTTAGTGSEAT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 136 NVAIAELKSKHTKkglaveetYA--------DYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQA 207
Cdd:cd08189 145 IAAVITDPETHEK--------YAindpklipDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 208 IKMIMDGYKKIVDKGE--EERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSrk 285
Cdd:cd08189 217 VKLIFENLPKAYEDGSdlEARENML----LASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYG-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 286 kpnGKIIKCTKILADALECDPNCDVYGEL-EKFLNKLiakKALREYGMVESQIDEFTDS---TIANQQRLLAN-NY---V 357
Cdd:cd08189 291 ---PAAEKRLAELADAAGLGDSGESDSEKaEAFIAAI---RELNRRMGIPTTLEELKEEdipEIAKRALKEANpLYpvpR 364
|
330
....*....|....
gi 1527686801 358 ELSREEIREIFANL 371
Cdd:cd08189 365 IMDRKDCEELLRKV 378
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
58-372 |
3.36e-42 |
|
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: 151.61 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 58 GTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVP-EKSI-DLF-EGEVsPKKVKELVVVPTTCGTGSEV 134
Cdd:cd08191 62 GQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLLAhGGDPrDYYgEDRV-PGPVLPLIAVPTTAGTGSEV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 135 TNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLS-PKAS--------------PF 199
Cdd:cd08191 141 TPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTArDFPPfprldpdpvyvgknPL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 200 TEMYSLQAIKMIMDGYKKIVDKG--EEERfnhlRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTE 277
Cdd:cd08191 221 TDLLALEAIRLIGRHLPRAVRDGddLEAR----SGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 278 VFKmYSRKKPNGKIIKctkiLADALECDPNCDVYGELEKFLNKLIAKKA-------LREYGMVESQIDEFTDSTIAnQQR 350
Cdd:cd08191 297 VMR-FNRPARAAELAE----IARALGVTTAGTSEEAADRAIERVEELLArigipttLADLGVTEADLPGLAEKALS-VTR 370
|
330 340
....*....|....*....|..
gi 1527686801 351 LLANNYVELSREEIREIFANLY 372
Cdd:cd08191 371 LIANNPRPPTEEDLLRILRAAF 392
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
5-347 |
3.20e-39 |
|
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: 143.87 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 5 RVVPKIFY-FDTFKEFNEEFKIGKNDLVITNEFIYE--------PYMKPLGIDTNLIFQEkfgTGEPSDEMIDSMTKEMK 75
Cdd:cd08178 1 KVPPKIYFePGCLPYLLLELPGVKRAFIVTDRVLYKlgyvdkvlDVLEARGVETEVFSDV---EPDPTLSTVRKGLEAMN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 76 KYNFDRIIAFGGGTIVDICKILAL----------DVPEKSIDL----FEGEVSPKKVKeLVVVPTTCGTGSEVTNVAIAE 141
Cdd:cd08178 78 AFKPDVIIALGGGSAMDAAKIMWLfyehpetkfeDLAQRFMDIrkrvYKFPKLGKKAK-LVAIPTTSGTGSEVTPFAVIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 142 LKSKHTKKGLAveeTYA---DYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKI 218
Cdd:cd08178 157 DDKTGKKYPLA---DYAltpDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 219 VDKGEEERfnhLRDFVL-ASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKmYSRKKPNGKIIKCTKI 297
Cdd:cd08178 234 YNNGNDIE---AREKMHnAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIR-YNATDPPTKQAAFPQY 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1527686801 298 -----------LADALECDPNCDVYG------ELEKFLNKLIAKKALREYGMVESQ----IDE-----FTD-STIAN 347
Cdd:cd08178 310 kyyvakeryaeIADLLGLGGKTPEEKveslikAIEDLKKDLGIPTSIREAGIDEADflaaVDKlaedaFDDqCTGAN 386
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
62-271 |
1.27e-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: 136.52 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGeVSPKKVKE--LVVVPTTCGTGSEVTNV 137
Cdd:cd08176 69 PTIENVMAGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVanPGADVRSLEG-VAPTKNPAvpIIAVPTTAGTGSEVTIN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 138 AIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKK 217
Cdd:cd08176 148 YVITDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRK 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1527686801 218 IVDKGE--EERFNhlrdFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd08176 228 AVANPNnvEAREN----MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVAN 279
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
80-271 |
1.25e-34 |
|
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: 130.74 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 80 DRIIAFGGGTIVDICK-ILALDVPEKSIDLFEG--EVS----PkkvkeLVVVPTTCGTGSEVTNVAIAELKSKHTKKGLA 152
Cdd:cd17814 85 DGIVAVGGGSPIDCAKgIGIVVSNGGHILDYEGvdKVRrplpP-----LICIPTTAGSSADVSQFAIITDTERRVKMAII 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 153 VEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDkgEEERFNHLRD 232
Cdd:cd17814 160 SKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVA--DPDDLEAREK 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 1527686801 233 FVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd17814 238 MMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECN 276
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
60-286 |
1.30e-33 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 128.61 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 60 GEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNV 137
Cdd:PRK15454 88 GEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVtnPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 138 AIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKK 217
Cdd:PRK15454 168 TVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPK 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1527686801 218 IVDKGEE--ERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVF---KMYSRKK 286
Cdd:PRK15454 248 AVGYGHDlaARESML----LASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMefnRMVCRER 317
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
59-370 |
2.21e-33 |
|
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: 127.77 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 59 TGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILA--LDVPEKSI-DLFEGEVSPKKVKELVVVPTTCGTGSEVT 135
Cdd:cd08186 62 TPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVAvlLAYGGKTArDLYGFRFAPERALPLVAINLTHGTGSEVD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 136 NVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGY 215
Cdd:cd08186 142 RFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 216 KKIVDKGE--EERFNHLrdfvLASNYAGIAFGNAGCAAVHALSYSIGGAF-HVAHGEANYQFFTEVFKMYSRKKPngkii 292
Cdd:cd08186 222 PRALANPKdlEARYWLL----YASMIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVP----- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 293 kctKILADALEC-DPN-----CD---VYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANQ--QRLLANNYVELSR 361
Cdd:cd08186 293 ---ETLADILRPiVPGlkgtpDEaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPslDLLLSLAPVEVTE 369
|
....*....
gi 1527686801 362 EEIREIFAN 370
Cdd:cd08186 370 EVVREIYEE 378
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
62-271 |
8.67e-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: 126.09 E-value: 8.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICK---ILALDvpEKSIDLFEG-EVSPKKVKELVVVPTTCGTGSEVTNV 137
Cdd:cd08188 69 PTVTNVNEGLELFKENGCDFIISVGGGSAHDCAKaigILATN--GGEIEDYEGvDKSKKPGLPLIAINTTAGTASEVTRF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 138 AIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKffVTSS--VDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGY 215
Cdd:cd08188 147 AVITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPS--LTAAtgMDALTHAIEAYVSTGATPLTDALALEAIRLIAENL 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1527686801 216 KKIVDKGEEERfnhLRD-FVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd08188 225 PKAVANGKDLE---AREnMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCN 278
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
61-271 |
4.78e-32 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 127.61 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 61 EPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL--DVPEKSidlFEGEVS---------------PKKVKeLVV 123
Cdd:PRK13805 522 DPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLfyEHPETD---FEDLAQkfmdirkriykfpklGKKAK-LVA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 124 VPTTCGTGSEVTNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMY 203
Cdd:PRK13805 598 IPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGL 677
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1527686801 204 SLQAIKMIMDGYKKIVDKGEE-----ERFNHlrdfvlASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:PRK13805 678 ALQAIKLVFEYLPRSYKNGAKdpearEKMHN------ASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRAN 744
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
59-370 |
5.15e-32 |
|
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: 123.78 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 59 TGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL------DVPEKSIDLFEGEVSPKKVKELVVVPTTCGTGS 132
Cdd:cd14861 63 PPNPTEADVEAGVAAYREGGCDGIIALGGGSAIDAAKAIALmathpgPLWDYEDGEGGPAAITPAVPPLIAIPTTAGTGS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 133 EVTNVAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIM 212
Cdd:cd14861 143 EVGRAAVITDDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLIS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 213 DGYKKIVDKGE--EERFNHLrdfvLASNYAGIAFGNaGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKmYSRKKPNGK 290
Cdd:cd14861 223 EWLPRAVADGSdlEARGEMM----MAALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLR-FNRPAVEDK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 291 IIKctkiLADALE---CDPNcDVYGELEKFLNKLIAKKALREYGMVESQIDE-----FTDSTIanqqrllANNYVELSRE 362
Cdd:cd14861 297 LAR----LARALGlglGGFD-DFIAWVEDLNERLGLPATLSELGVTEDDLDElaelaLADPCH-------ATNPRPVTAE 364
|
....*...
gi 1527686801 363 EIREIFAN 370
Cdd:cd14861 365 DYRALLRE 372
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
75-368 |
1.61e-30 |
|
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: 119.85 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 75 KKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLA 152
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAkyDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 153 VEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLS-PKASPFTEMYSLQAIKMIMDGYKKIVDKGE--EERFNh 229
Cdd:cd08187 163 SPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLLRTVIENGPKALKDPDdyEARAN- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 230 lrdFVLASNYA--GI-AFGNAGCAAVHALSYSIGGAFHVAHGE---------ANY----------QFFTEVFKMYSRKKP 287
Cdd:cd08187 242 ---LMWAATLAlnGLlGAGRGGDWATHAIEHELSALYDITHGAglaivfpawMRYvlkkkperfaQFARRVFGIDPGGDD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 288 ngkiikcTKILADALECdpncdvygeLEKFLNKLIAKKALREYGMVESQIDEFTDSTIANqqRLLANNYVELSREEIREI 367
Cdd:cd08187 319 -------EETALEGIEA---------LEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRG--GGLGGGFKPLTREDIEEI 380
|
.
gi 1527686801 368 F 368
Cdd:cd08187 381 L 381
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
59-367 |
2.13e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 113.94 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 59 TGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDV--PEKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTN 136
Cdd:cd14864 63 PASATSDTIDEAAELARKAGADGIIAVGGGKVLDTAKAVAILAnnDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 137 VAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDG-- 214
Cdd:cd14864 143 RFPVVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENld 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 215 --YKKIVDKGEEERfnhlrdFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNgKII 292
Cdd:cd14864 223 gaLADPKNTPAEEL------LAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPD-KYA 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1527686801 293 KCTKIL-ADALECDPN---CDVYGELEKFLNKLIAKKALREYGmVESQIDEFtdSTIANQQRLLANNYVELSREEIREI 367
Cdd:cd14864 296 KIARALgEDVEGASPEeaaIAAVEGVRRLIAQLNLPTRLKDLD-LASSLEQL--AAIAEDAPKLNGLPRSMSSDDIFDI 371
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
62-271 |
4.46e-24 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 101.95 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALdVPEKSIDL--FEG-EVSPKKVKELVVVPTTCGTGSEVTNVA 138
Cdd:PRK09860 72 PTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL-VAANGGDIrdYEGvDRSAKPQLPMIAINTTAGTASEMTRFC 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 139 IAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKI 218
Cdd:PRK09860 151 IITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLA 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1527686801 219 VDKGEEERFNHLRDFvlASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:PRK09860 231 VEDGSNAKAREAMAY--AQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCN 281
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
80-271 |
1.95e-23 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 100.07 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 80 DRIIAFGGGTIVDICKILALDV--PE----KSIdlfEGeVSPKKVKEL--VVVPTTCGTGSEVT-NVAIAELKSKhtKKG 150
Cdd:PRK10624 89 DYLIAIGGGSPQDTCKAIGIISnnPEfadvRSL---EG-VAPTKKPSVpiIAIPTTAGTAAEVTiNYVITDEEKR--RKF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 151 LAVE-ETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEEERfnh 229
Cdd:PRK10624 163 VCVDpHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDKEAG--- 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1527686801 230 lRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:PRK10624 240 -EGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVAN 280
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
65-372 |
2.89e-22 |
|
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: 96.03 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 65 EMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILAL--DVPeksidlfegevspkkvkeLVVVPTTCgTGSEVTNV-AIAE 141
Cdd:cd08177 63 EVAERALAAAREAGADGLVAIGGGSAIGLAKAIALrtGLP------------------IVAVPTTY-AGSEMTPIwGETE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 142 LKSKHTKKGLAVeetyadyavlIPETV-------KGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDG 214
Cdd:cd08177 124 DGVKTTGRDPRV----------LPRTViydpdltLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 215 YKKIVDKGEEERFNhlRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNGkiikc 294
Cdd:cd08177 194 LPRLVADPSDLEAR--SDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDA----- 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1527686801 295 TKILADALECDpncDVYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANQqrllANNYVELSREEIREIFANLY 372
Cdd:cd08177 267 MARLARALGGG---DAAGGLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANP----YPNPRPVERDALRALLERAW 337
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
7-368 |
8.52e-21 |
|
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: 91.95 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 7 VPK-IFYFDTFKEFNE---EFKIGKNDLVItneFIYEPYMKPLGIDTNLIFQEKF------GTGEPSDEMIDSMTKEMKK 76
Cdd:cd08184 1 VPKyLFGRGSFDQLGEllaERRKSNNDYVV---FFIDDVFKGKPLLDRLPLQNGDllifvdTTDEPKTDQIDALRAQIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 77 YNF---DRIIAFGGGTIVDICKILALDV--PEKSIDlFEG-EVSPKKVKELVVVPTTCGTGSEVTNVAIaeLKSKHTKKG 150
Cdd:cd08184 78 ENDklpAAVVGIGGGSTMDIAKAVSNMLtnPGSAAD-YQGwDLVKNPGIYKIGVPTLSGTGAEASRTAV--LTGPEKKLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 151 LAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMImdgyKKIVDKGEEERFNHL 230
Cdd:cd08184 155 INSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELC----RDVFLSDDMMSPENR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 231 RDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEANyqfftevfkmysrkkpngkiikCtkILADALEcdpncDV 310
Cdd:cd08184 231 EKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN----------------------C--IVFNVLE-----EF 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1527686801 311 YGE--------LEKflNKLIAKKALrEYGMVESQIDEFTDSTIANqQRLLANNYVE-----LSREEIREIF 368
Cdd:cd08184 282 YPEgvkefremLEK--QNITLPKGI-CKDLTDEQYEKMVAVTLIH-EKPLTNALGPdwkdiLTPEKVTKLF 348
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
67-367 |
4.87e-20 |
|
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: 90.39 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 67 IDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVPEKSID------LFEGEVSPKKVK----ELVVVPTTCgTGSEVTN 136
Cdd:cd08192 68 VLEAARAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDvdqldaLEDGKRIDPNVTgptlPHIAIPTTL-SGAEFTA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 137 VAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGyK 216
Cdd:cd08192 147 GAGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEG-L 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 217 KIVDKGEEERFNHLRDFvLASNYAGIAFGN-AGCAAVHALSYSIGGAFHVAHGEANYQFFTEVFKMYSRKKPNGKIIKCT 295
Cdd:cd08192 226 PRSKADPEDLEARLKCQ-LAAWLSLFGLGSgVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIAR 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1527686801 296 KILADALECD-PNCDVYGELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANQQrLLANNYVELSREEIREI 367
Cdd:cd08192 305 ALGLVTGGLGrEAADAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVW-CRTNPRPITDKDDVLEI 376
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
75-368 |
1.48e-18 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 85.89 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 75 KKYNFDRIIAFGGGTIVDICKILALDVP--EKSIDLFEGEVSPKKVKELVVVPTTCGTGSEVTNVAIAELKSKHTKKGLA 152
Cdd:COG1979 85 KEEGIDFILAVGGGSVIDGAKAIAAGAKydGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 153 VEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLS-PKASPFTEMYSLQAIKMIMDGYKKIVDKGE--EERFNh 229
Cdd:COG1979 165 SPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTyPVDAPLQDRFAEGLLRTLIEEGPKALKDPEdyDARAN- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 230 lrdFVLASNYA--G-IAFGNAGCAAVHALSYSIGGAFHVAHG---------------EAN----YQFFTEVF--KMYSRK 285
Cdd:COG1979 244 ---LMWAATLAlnGlIGAGVPQDWATHMIEHELSALYDIDHGaglaivlpawmryvlEEKpekfAQYAERVWgiTEGDDE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 286 KpngkiikctKILAdALEcdpncdvygELEKFLNKLIAKKALREYGMVESQIDEFTDSTIANQQRLLAnNYVELSREEIR 365
Cdd:COG1979 321 E---------RALE-GIE---------ATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALG-EFKDLTPEDVR 380
|
...
gi 1527686801 366 EIF 368
Cdd:COG1979 381 EIL 383
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
80-271 |
3.58e-14 |
|
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: 73.03 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 80 DRIIAFGGGTIVDICKILAL------DVPEKSIDLFEG--EVSPKKVKEL---VVVPTTCGTGSEVTNVAIAELKSKHtK 148
Cdd:cd14866 85 DAVVAVGGGSAIVTARAASIllaedrDVRELCTRRAEDglMVSPRLDAPKlpiFVVPTTPTTADVKAGSAVTDPPAGQ-R 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 149 KGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEEERfn 228
Cdd:cd14866 164 LALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDPAA-- 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1527686801 229 hLRDFVLASNYAGIAFGNAGCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd14866 242 -RADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVH 283
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
57-271 |
5.41e-12 |
|
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: 65.46 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 57 FGTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILALDVPEKsidlfegevspkkvKELVVVPTTCGTGSEVTN 136
Cdd:cd07766 56 FVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAALLNRG--------------IPFIIVPTTASTDSEVSP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 137 VAIAELKSKHTKKGLAveETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIEsylspkaspftemyslqaikmimdgyk 216
Cdd:cd07766 122 KSVITDKGGKNKQVGP--HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1527686801 217 kivdkgeeerfnhLRDFVLASNYAGIAFGNA-GCAAVHALSYSIGGAFHVAHGEAN 271
Cdd:cd07766 173 -------------LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAV 215
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
24-269 |
1.13e-08 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 55.94 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 24 KIGKNDLVITNEFIYE---PYMKPLGIDTNL-IFQEKFGtGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILA- 98
Cdd:COG0371 25 DLGKRALIITGPTALKaagDRLEESLEDAGIeVEVEVFG-GECSEEEIERLAEEAKEQGADVIIGVGGGKALDTAKAVAy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 99 -LDVPeksidlfegevspkkvkeLVVVPT---TCGTGSevtnvAIAELKS-KHTKKGLAVEETYADyAVLI-PETVKGLP 172
Cdd:COG0371 104 rLGLP------------------VVSVPTiasTDAPAS-----PLSVIYTeDGAFDGYSFLAKNPD-LVLVdTDIIAKAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 173 YKFFVTSSVDAL--IHAIESYLSPKASPFTEMYSLQAIKMIMDGYKKIVDKGEE-----ERFNHLRDF--VLASN--YAG 241
Cdd:COG0371 160 VRLLAAGIGDALakWYEARDWSLAHRDLAGEYYTEAAVALARLCAETLLEYGEAaikavEAGVVTPALerVVEANllLSG 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1527686801 242 IAFG----NAGCAAVHALSYS---IGGAFHVAHGE 269
Cdd:COG0371 240 LAMGigssRPGSGAAHAIHNGltaLPETHHALHGE 274
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
24-130 |
4.05e-07 |
|
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: 51.26 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 24 KIGKNDLVITNEFIY-------EPYMKPLGIDtnlIFQEKFGtGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKI 96
Cdd:cd08170 20 PLGKKALVIADPFVLdlvgerlEESLEKAGLE---VVFEVFG-GECSREEIERLAAIARANGADVVIGIGGGKTIDTAKA 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1527686801 97 LA--LDVPeksidlfegevspkkvkeLVVVPTTCGT 130
Cdd:cd08170 96 VAdyLGLP------------------VVIVPTIAST 113
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
62-193 |
8.15e-06 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 47.48 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 62 PSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILA--LDVPEKSIDLFEGEVSPKKVKELV---VVPTTCGTGSEVTN 136
Cdd:PRK15138 69 PTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAaaANYPENIDPWHILETGGKEIKSAIpmgSVLTLPATGSESNA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1527686801 137 VAIAELKSKHTKKGLAVEETYADYAVLIPETVKGLPYKFFVTSSVDALIHAIESYLS 193
Cdd:PRK15138 149 GAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVT 205
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
50-269 |
3.91e-05 |
|
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: 45.22 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 50 NLIFQEKFGTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDICKILA--LDVPeksidlfegevspkkvkeLVVVPT- 126
Cdd:cd08550 49 GIDYEVEVFGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKAVAdrLGLP------------------VVTVPTi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 127 --TCGTGSEVTNVaiaelkskHTKKGLAVEETYADY---AVLI-PETVKGLPYKFFVTSSVDALI--HAIESYLSPKASP 198
Cdd:cd08550 111 aaTCAAWSALSVL--------YDEEGEFLGYSLLKRspdLVLVdTDIIAAAPVRYLAAGIGDTLAkwYEARPSSRGGPDD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 199 FTEMYSLQAIKMIMDGYKK-----IVDKGEEERFNHLRDFVLASNY-AGIA--FGNAGC--AAVHALSYS---IGGAFHV 265
Cdd:cd08550 183 LALQAAVQLAKLAYDLLLEygvqaVEDVRQGKVTPALEDVVDAIILlAGLVgsLGGGGCrtAAAHAIHNGltkLPETHGT 262
|
....
gi 1527686801 266 AHGE 269
Cdd:cd08550 263 LHGE 266
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-106 |
1.72e-04 |
|
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: 42.93 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 14 DTFKEFNEEFKIGKNDLVITNEFIYEPYMKPLGIDTNLIFQEKFGTGEPSDE---MIDSMTKEMKKYNFDRIIAFGGGTI 90
Cdd:cd08173 13 NKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEeaaEVEKVKKLIKESKADFIIGVGGGKV 92
|
90
....*....|....*...
gi 1527686801 91 VDICKILA--LDVPEKSI 106
Cdd:cd08173 93 IDVAKYAAykLNLPFISI 110
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
18-128 |
2.91e-04 |
|
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: 42.50 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 18 EFNEEFKIgKNDLVITNEFIYE---PYMKPLgidTNLIFQEKFGTGEPSDEMIDSMTKEMKKYNFDRIIAFGGGTIVDIC 94
Cdd:cd08172 16 ELLSEFGI-KRPLIIHGEKSWQaakPYLPKL---FEIEYPVLRYDGECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTA 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 1527686801 95 KILA--LDVPeksidlfegevspkkvkeLVVVPT---TC 128
Cdd:cd08172 92 KAVAdkLNIP------------------LILIPTlasNC 112
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
27-267 |
6.93e-03 |
|
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: 37.93 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 27 KNDLVITNEFIYEPYMKPL--GIDTNLIFQekfgtgepSDEMIDSMTKEMKKYNF-DRIIAFGGGTIVDICKILALdvpe 103
Cdd:cd08549 24 KRVLIITGKNTKAKYCRFFydQLKTVCDIV--------YYDNIDNLEDELKKYTFyDCVIGIGGGRSIDTGKYLAY---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 104 ksidlfegevspKKVKELVVVPTTC---GTGSEVTNVAI-AELKSKHTKKGLAVeetYADYAVLipetvKGLPYKfFVTS 179
Cdd:cd08549 92 ------------KLKIPFISVPTSAsndGIASPIVSLRIpGVKKTFMADAPIAI---IADTEII-----KKSPRR-LLSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686801 180 SVDALIHAIESYL---------SPKASPFTEMYSLQAIKMIMDGYKKIVDKgeEERFNHLRDFVLASnyaGIAFGNAGCa 250
Cdd:cd08549 151 GIGDLVSNITAVLdwklahkekGEKYSEFAAILSKTSAKELVSYVLKASDL--EEYHRVLVKALVGS---GIAMAIAGS- 224
|
250
....*....|....*...
gi 1527686801 251 avhalSYSIGGAFH-VAH 267
Cdd:cd08549 225 -----SRPASGSEHlFSH 237
|
|
| |
