|
Name |
Accession |
Description |
Interval |
E-value |
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
1-346 |
0e+00 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 610.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 1 MHLMEFPREVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEEFEVYSITVKEAHINEVERVISKIR 80
Cdd:PRK00843 5 SHWIQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIVDEATMEEVEKVEEKAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 81 DKGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRY 160
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 161 LAAGVGDIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIRDAEIIRLGQDEGIRKVVKALISSGVAMSIAGSSR 240
Cdd:PRK00843 165 LAAGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 241 PASGAEHLFSHALDMLLDKPALHGEQTGIGTIIMAYLHGINWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIAHTIRP 320
Cdd:PRK00843 245 PASGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRP 324
|
330 340
....*....|....*....|....*.
gi 1850361749 321 ERYTILGKEGITREAAEKAAKITGVI 346
Cdd:PRK00843 325 ERYTILGDRGLTREAAEKAARITGVI 350
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
6-346 |
0e+00 |
|
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: 536.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 6 FPREVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVK----EEFEVYSITVKEAhiNEVERVISKIRD 81
Cdd:cd08173 1 LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLEssgvEVVIVDIATIEEA--AEVEKVKKLIKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 82 KGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYL 161
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 162 AAGVGDIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIRDAEIIRLGQDEGIRKVVKALISSGVAMSIAGSSRP 241
Cdd:cd08173 159 AAGCGDLISNITAVKDWRLAHRLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 242 ASGAEHLFSHALDMLLDKPALHGEQTGIGTIIMAYLHGINWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIAHTIRPE 321
Cdd:cd08173 239 ASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWKEIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPE 318
|
330 340
....*....|....*....|....*
gi 1850361749 322 RYTILGKEGITREAAEKAAKITGVI 346
Cdd:cd08173 319 RYTILGDNGLTEEAAERLARITGVI 343
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
2-343 |
4.82e-121 |
|
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: 352.55 E-value: 4.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 2 HLMEFPREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGSNVEKIVKEE-FEVYSITVK-EAHINEVERVISKI 79
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADL--GKRALIITGPTALKAAGDRLEESLEDAgIEVEVEVFGgECSEEEIERLAEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 80 RDKGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIK---GLNVKTSIKAKPPIAVIADIDVIKTA 156
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYtedGAFDGYSFLAKNPDLVLVDTDIIAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 157 PKRYLAAGVGDIVSNITAVRDWKLAHK-LKGEYFSEYAASLSLMSAKMVIRDAE------IIRLGQDEGIRKVVKALISS 229
Cdd:COG0371 159 PVRLLAAGIGDALAKWYEARDWSLAHRdLAGEYYTEAAVALARLCAETLLEYGEaaikavEAGVVTPALERVVEANLLLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 230 GVAMSIaGSSRPASGAEHLFSHALDMLLD-KPALHGEQTGIGTIIMAYLHGIN--WKKIRDTLKIVGAPTTAYELGIDPE 306
Cdd:COG0371 239 GLAMGI-GSSRPGSGAAHAIHNGLTALPEtHHALHGEKVAFGTLVQLVLEGRPeeIEELLDFLRSVGLPTTLADLGLDDE 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1850361749 307 IIIEALTIAHTIRPERYTILGKE-GITREAAEKAAKIT 343
Cdd:COG0371 318 TEEELLTVAEAARPERYTILNLPfEVTPEAVEAAILAT 355
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
7-336 |
2.77e-110 |
|
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: 324.52 E-value: 2.77e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKLGSPgLVVYGPITKKIAGSNVEKIVKEEFEVysITVKEAHINEVERVISKIRDKgikw 86
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKLNLKRV-LIITGKNTKAKYCRFFYDQLKTVCDI--VYYDNIDNLEDELKKYTFYDC---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 87 AIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAGVG 166
Cdd:cd08549 74 VIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADAPIAIIADTEIIKKSPRRLLSAGIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 167 DIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIRDAEiIRLGQDEGIRKVVKALISSGVAMSIAGSSRPASGAE 246
Cdd:cd08549 154 DLVSNITAVLDWKLAHKEKGEKYSEFAAILSKTSAKELVSYVL-KASDLEEYHRVLVKALVGSGIAMAIAGSSRPASGSE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 247 HLFSHALDMLLDK----PALHGEQTGIGTIIMAYLHGI-------NWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIA 315
Cdd:cd08549 233 HLFSHALDKLKEEylniNVLHGEQVGVGTIIMSYLHEKenkklsgLHERIKMILKKVGAPTTAKQLGIDEDLIIEALTEA 312
|
330 340
....*....|....*....|.
gi 1850361749 316 HTIRPERYTILGkeGITREAA 336
Cdd:cd08549 313 HKIRPRRYTLLD--GLSREEA 331
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
7-339 |
6.04e-108 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 318.70 E-value: 6.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKLGSPG-LVVYGPITKKIAGSNVEKIVKEEFEVYsiTVKEAHINEVERVISKIR-DKGI 84
Cdd:cd08174 1 PLILKIEEGALEHLGKYLADRNQGFGKvAIVTGEGIDELLGEDILESLEEAGEIV--TVEENTDNSAEELAEKAFsLPKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 85 KWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAG 164
Cdd:cd08174 79 DAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKRKSLGAKMPYGVIVDLDVIKSAPRRLILAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 165 VGDIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIR--DAEIIrlgQDEGIRKVVKALISSGVAMSIAGSSRPA 242
Cdd:cd08174 159 IGDLISNITALYDWKLAEEKGGEPVDDFAYLLSRTAADSLLNtpGKDIK---DDEFLKELAESLVLSGIAMEIAGSSRPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 243 SGAEHLFSHALDMLLDKPALHGEQTGIGTIIMAYLHGINWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIAHTIRPER 322
Cdd:cd08174 236 SGSEHLISHALDKLFPGPALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRTGFPLNPSDLGLTKEEFIEAVKLAPSTRPGR 315
|
330
....*....|....*..
gi 1850361749 323 YTILGKEGITREAAEKA 339
Cdd:cd08174 316 YTILEELDLSEERLKEI 332
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
8-326 |
3.44e-97 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 291.34 E-value: 3.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 8 REVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEE-FEVYSITVKEA---HINE--VERVISKIRd 81
Cdd:cd08175 2 KEIVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAgVTVCLLIFPGEgdlIADEaaVGKVLLELE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 82 KGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYL 161
Cdd:cd08175 81 KDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQRMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 162 AAGVGDIVSNITAVRDWKLAHKLKGEYFSEYAASLSLMSAKMVIRDAEIIRLGQDEGIRKVVKALISSGVAMSIAGSSRP 241
Cdd:cd08175 161 AAGFGDLLGKYTALADWKLSHLLGGEYYCPEVADLVQEALEKCLDNAEGIAARDPEAIEALMEALILSGLAMQLVGNSRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 242 ASGAEHLFSHALDMLLD----KPALHGEQTGIGTIIMA--YLHG--INWKKIRDTLKIVGAPTTAYELGIDPEIIIEALT 313
Cdd:cd08175 241 ASGAEHHLSHYWEMEFLrlgkPPVLHGEKVGVGTLLIAalYILEqlPPPEELRELLRKAGAPTTPEDLGIDRDLLRDSLR 320
|
330
....*....|...
gi 1850361749 314 IAHTIRPeRYTIL 326
Cdd:cd08175 321 LAKEIRD-RYTVL 332
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
11-268 |
1.53e-82 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 251.07 E-value: 1.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 11 ILGKNLIQEINNVIKRLKlGSPGLVVYGPITKKIAGSNVEKIVKE---EFEVYSITVKEAHINEVERVISKIRDKGIKWA 87
Cdd:pfam13685 1 VIGPGALGRLGEYLAELG-FRRVALVADANTYAAAGRKVAESLKRagiEVETRLEVAGNADMETAEKLVGALRERDADAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 88 IAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASIKGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAGVGD 167
Cdd:pfam13685 80 VGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 168 IVSNITAVRDWKLAHKlkgeyfSEYAASLSLMSAKMVIRDAEiiRLGQDEGIRKVVKALIsSGVAMSIAGSSRPASGAEH 247
Cdd:pfam13685 160 LLAKITAVADWELAHA------EEVAAPLALLSAAMVMNFAD--RPLRDPGDIEALAELL-SALAMGGAGSSRPASGSEH 230
|
250 260
....*....|....*....|.
gi 1850361749 248 LFSHALDMLLDKPALHGEQTG 268
Cdd:pfam13685 231 LISHALDMIAPKQALHGEQVG 251
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
7-313 |
5.40e-28 |
|
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: 110.15 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGSNVEKIVKEE--FEVYSITVKEAHINEVERVISKIRDKGI 84
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRG--FDRALVVSDEGVVKGVGEKVADSLKKGlaVAIFDFVGENPTFEEVKNAVERARAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 85 KWAIAVGGGSIIDVTKLASFKM--GIPFISFPTTASHDGIASANASIKGLNVKTSIK--AKPPIAVIADIDVIKTAPKRY 160
Cdd:cd07766 79 DAVIAVGGGSTLDTAKAVAALLnrGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVgpHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 161 LAAGVGDIVSNitavrdwklahklkgeyfseyaaslslmsakMVIRDaeiirlgqdegirKVVKALISSGvamsIAGSSR 240
Cdd:cd07766 159 VASGGVDALAH-------------------------------AVELE-------------KVVEAATLAG----MGLFES 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 241 PASGAEHLFSHALDMLLDKPalHGEQTGIGTIIMAYLH-------GINWKKIRDTLKIVGAPTTAYELGI---DPEIIIE 310
Cdd:cd07766 191 PGLGLAHAIGHALTAFEGIP--HGEAVAVGLPYVLKVAndmnpepEAAIEAVFKFLEDLGLPTHLADLGVskeDIPKLAE 268
|
...
gi 1850361749 311 ALT 313
Cdd:cd07766 269 KAL 271
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
7-306 |
8.16e-26 |
|
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: 105.70 E-value: 8.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGSNVEKIVKEEFEVYSITVKEAH--INEVERVISKIRDKGI 84
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPL--GKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGEctEENIERLAEKAKEEGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 85 KWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGiASANASI----KGLNVKTSIKAKPPIAVIADIDVIKTAPKRY 160
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCA-AWSALSVlydeEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 161 LAAGVGDivsnitAVRDWKLAHKLKGEYFSEYAASLSLMSAKM-----------VIRDAEIIRLGQDegIRKVVKALI-S 228
Cdd:cd08550 158 LAAGIGD------TLAKWYEARPSSRGGPDDLALQAAVQLAKLaydllleygvqAVEDVRQGKVTPA--LEDVVDAIIlL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 229 SGVAMSIaGSSRPASGAEHLFSHALDML-LDKPALHGEQTGIGTIIMAYLHGINWKKIRDT---LKIVGAPTTAYELGID 304
Cdd:cd08550 230 AGLVGSL-GGGGCRTAAAHAIHNGLTKLpETHGTLHGEKVAFGLLVQLALEGRSEEEIEELiefLRRLGLPVTLEDLGLE 308
|
..
gi 1850361749 305 PE 306
Cdd:cd08550 309 LT 310
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
11-167 |
9.27e-22 |
|
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: 94.40 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 11 ILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGSNVEKIVKEEFEVYSITV--KEAHINEVERVISKIRDKGIKWAI 88
Cdd:cd08170 5 VQGPGALDRLGEYLAPL--GKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVfgGECSREEIERLAAIARANGADVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 89 AVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASI---KGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAGV 165
Cdd:cd08170 83 GIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIyteDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVAGM 162
|
..
gi 1850361749 166 GD 167
Cdd:cd08170 163 GD 164
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
4-167 |
2.59e-18 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 84.87 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 4 MEFPREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGSNVEKIVKE-----EFEVYSitvKEAHINEVERVISK 78
Cdd:PRK09423 5 FISPSKYVQGKGALARLGEYLKPL--GKRALVIADEFVLGIVGDRVEASLKEagltvVFEVFN---GECSDNEIDRLVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 79 IRDKGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASHDGIASANASI---KGLNVKTSIKAKPPIAVIADIDVIKT 155
Cdd:PRK09423 80 AEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIyteEGEFERYLFLPKNPDLVLVDTAIIAK 159
|
170
....*....|..
gi 1850361749 156 APKRYLAAGVGD 167
Cdd:PRK09423 160 APARFLAAGIGD 171
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
7-312 |
1.01e-17 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 83.04 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKI-AGSNVEKIVKE---EFEVYSITVKEAHINEVERVISKIRDK 82
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRL--GARALIVTDPGSLKSgLLDKVLASLEEagiEVVVFDGVEPEPTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 83 GIKWAIAVGGGSIIDVTKLASF------------------KMGIPFISFPTTASHDGIASANA--SIKGLNVKTSIKAKP 142
Cdd:pfam00465 79 GADVIIAVGGGSVIDTAKAIALlltnpgdvwdylggkpltKPALPLIAIPTTAGTGSEVTPLAviTDTETGEKLGIFSPK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 143 --PIAVIADIDVIKTAPKRYLAAGVGDIvsnitavrdwkLAHKLKGeYFS----EYAASLSLMSAKMVIRDAEIIRL-GQ 215
Cdd:pfam00465 159 llPDLAILDPELTLTLPPRLTAATGMDA-----------LAHAVEA-YVSkganPLTDALALEAIRLIAENLPRAVAdGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 216 DEGIR-KVVKALISSGVAMSIAGssrpaSGAEHLFSHALDMLLDKPalHGEQTGigtIIMAYLHGINWKKIRDTLKIVGA 294
Cdd:pfam00465 227 DLEAReNMLLASTLAGLAFSNAG-----LGAAHALAHALGGRYGIP--HGLANA---ILLPYVLRFNAPAAPEKLAQLAR 296
|
330
....*....|....*...
gi 1850361749 295 PTTAYELGIDPEIIIEAL 312
Cdd:pfam00465 297 ALGEDSDEEAAEEAIEAL 314
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
9-312 |
1.20e-16 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 79.79 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 9 EVILGKNLIQEINNvIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEE-FEVYSITVK--EAH--INEVERVISKIRDKG 83
Cdd:cd08195 3 PILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAAgFKVEVIVIPagEKSksLETVERIYDFLLEAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 84 IK---WAIAVGGGSIIDVTKL--ASFKMGIPFISFPTT--ASHDgiasanASIKGlnvKTSI---KAK-------PPIAV 146
Cdd:cd08195 82 LDrdsLLIALGGGVVGDLAGFvaSTYMRGIPFIQVPTTllAQVD------SSIGG---KTGInlpGGKnligafyQPKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 147 IADIDVIKTAPKRYLAAGVGDIVsNITAVRDWKLAHKLKGEYFSEYAASLSLMSAkmVIRD-----AEIIRlgQDE---G 218
Cdd:cd08195 153 LIDPDFLKTLPEREFRSGLAEVI-KYGLIADKELFEFLEKNLDKILARDPEALEE--IIARsveikADIVE--EDErekG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 219 IRKVvkalissgvamsiagssrpasgaehL-----FSHALDMLLDKPALHGEQTGIGTIIMAYL---HGI----NWKKIR 286
Cdd:cd08195 228 LRAI-------------------------LnfghtFGHAIESASGYKLLHGEAVAIGMVAAARLsvkLGLlseeDLERIR 282
|
330 340
....*....|....*....|....*.
gi 1850361749 287 DTLKIVGAPTTAYElgIDPEIIIEAL 312
Cdd:cd08195 283 ALLKKLGLPTSIKD--LDPEELLEAM 306
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
9-312 |
7.04e-16 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 77.44 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 9 EVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEE-FEVYSITVK--EAH--INEVERVISKIRDKG 83
Cdd:COG0337 14 DIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAgFEVHLLVLPdgEASktLETLERILDALLEAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 84 ------IkwaIAVGGGSIIDVTKL--ASFKMGIPFISFPTT--ASHDgiasanASIKGlnvKTSI---KAK-------PP 143
Cdd:COG0337 94 ldrddlV---VALGGGVVGDLAGFaaATYLRGVPFIQVPTTllAQVD------SSVGG---KTGVnhpGGKnligafhQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 144 IAVIADIDVIKTAPKRYLAAGVGDIV---------------SNITAVRDWKLAHklkgeyfSEYAASLSLmSAKmvirdA 208
Cdd:COG0337 162 RAVLIDLDFLKTLPERELRAGLAEVIkygliadaeffewleENADALLARDPEA-------LEEAIARSC-EIK-----A 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 209 EIIrlGQDE---GIRkvvkALISSGvamsiagssrpasgaeHLFSHALDMLLDKPALHGEQTGIGTIIMAYL-HGINW-- 282
Cdd:COG0337 229 EVV--AADEresGLR----ALLNFG----------------HTFGHAIEAATGYRLLHGEAVAIGMVFAARLsARLGLls 286
|
330 340 350
....*....|....*....|....*....|....
gi 1850361749 283 ----KKIRDTLKIVGAPTTAyeLGIDPEIIIEAL 312
Cdd:COG0337 287 eedvERIRALLEALGLPTRL--PALDPEALLAAM 318
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
40-341 |
6.17e-14 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 71.78 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 40 ITKKIAGSNVEKIvkeEFEVYSitvKEAHINEVERVISKIRDKGIKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTASH 119
Cdd:cd08171 41 LRAALEGSGLEIT---DFIWYG---GEATYENVEKLKANPEVQEADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 120 dgiASANASI------KGLNVKTSIKAKPPIAVIADIDVIKTAPKRYLAAGVGDIVS-----NITAvRDWKLAHklkgey 188
Cdd:cd08171 115 ---CAAVTAVsvmynpDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDTLAkyyevEFSA-RGDELDH------ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 189 FSEYAASLSLMSAKMVIR-------DAEIIRLGQDegIRKVVKA-LISSGVAmSIAGSSRPASGAEHLFSHALDML--LD 258
Cdd:cd08171 185 TNALGVAISKMCSEPLLKygvqaleDCRANKVSDA--LEQVVLDiIVTTGLV-SNLVEPDYNSSLAHALYYGLTTLpqIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 259 KPALHGEQTGIGTIIMAYLHG--INWKKIRDTLKIVGAPTTAYELGIDPEIIIEALTIA-HTIRPERYTilgkEGITREA 335
Cdd:cd08171 262 EEHLHGEVVSYGVLVLLTVDGqfEELEKVYAFNKSIGLPTCLADLGLTVEDLEKVLDKAlKTKDLRHSP----YPITKEM 337
|
....*.
gi 1850361749 336 AEKAAK 341
Cdd:cd08171 338 FEEAIK 343
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
7-339 |
1.98e-13 |
|
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: 70.24 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKLGSPgLVVYGPITKKIAgsnvEKIVKEEFEVYSITVK---EAHINEVERVISKIRDKG 83
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFGIKRP-LIIHGEKSWQAA----KPYLPKLFEIEYPVLRydgECSYEEIDRLAEEAKEHQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 84 IKWAIAVGGGSIIDVTKLASFKMGIPFISFPTTAS------------HDGiasanasikGLNVKTSIKAKPPIAVIADID 151
Cdd:cd08172 76 ADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASncaawtplsviyDED---------GEFIGYDYFPRSAYLVLVDPR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 152 VIKTAPKRYLAAGVGD-------IVSNITAVRDWKLAHKLkgeyfSEYAASLS----LMSAKMVIRDAEIIRLGQDegIR 220
Cdd:cd08172 147 LLLDSPKDYFVAGIGDtlakwyeADAILRQLEELPAFLQL-----ARQAAKLCrdilLKDSEQALADLEAGKLTPA--FI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 221 KVVKALIS-SGVAMSIAGSSRPASGAeHLFSHALDMLLD-KPALHGEQTGIGTIIMAYLHGiNW---KKIRDTLKIVGAP 295
Cdd:cd08172 220 KVVETIIAlAGMVGGFGDEYGRSAGA-HAIHNGLTKLPEtHHFLHGEKVAYGILVQLALEG-KWdeiKKLLPFYRRLGLP 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1850361749 296 TTAYELGIDPEIIIEALTIA-HTIRPERYTILGKEGITREAAEKA 339
Cdd:cd08172 298 TSLADLGLTDDTEEALQKIAaFAASPEESIHLLPPDVTAEEVLQA 342
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
80-313 |
1.10e-12 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 67.14 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 80 RDKGIkwaIAVGGGSIIDVTKL--ASFKMGIPFISFPTTAshdgIASANASIKGlnvKTSI---KAK-------PPIAVI 147
Cdd:pfam01761 30 RSSLL---IALGGGVIGDLAGFvaATYMRGIRFIQVPTTL----LAQVDSSVGG---KTGInhpLGKnligafyQPKAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 148 ADIDVIKTAPKRYLAAGVGDIVsNITAVRDWKLAHKLKGEYFSEYAASLSLMsAKMVIRDAEIIR--LGQDE---GIRkv 222
Cdd:pfam01761 100 IDLDFLKTLPDREFRAGLAEVI-KYGLIADAEFFEWLEENAEALLNLDPDAL-EEAIARSCEVKAdvVAQDEkesGLR-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 223 vkALISSGvamsiagssrpasgaeHLFSHALDMLLDKPA-LHGEQTGIGTI---IMAYLHGI----NWKKIRDTLKIVGA 294
Cdd:pfam01761 176 --ALLNLG----------------HTFGHAIEALSGYGAlLHGEAVAIGMVlaaRLSERLGLldeaDVERIRALLKKYGL 237
|
250
....*....|....*....
gi 1850361749 295 PTTAYELgiDPEIIIEALT 313
Cdd:pfam01761 238 PTSLPDL--DVEQLLAAMA 254
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-323 |
1.55e-12 |
|
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: 67.60 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKlGSPGLVVYGP------ITKKIAGSNVEKIVKeefeVYSITVKEAHINEVERVISKIR 80
Cdd:cd08196 6 PVKIIFGEGILKELPDIIKELG-GKRGLLVTDPsfiksgLAKRIVESLKGRIVA----VFSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 81 DKGIKWAIAVGGGSIIDVTKLAS-------------------FKMGIPFISFPTTAshdGIAS--ANASI---KGLNVKT 136
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAAclaktdgsiedylegkkkiPKKGLPLIAIPTTA---GTGSevTPVAVltdKEKGKKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 137 SIKAKPPIAVIADIDVIKT--APKRYLAAgvgdivSNITAvrdwkLAHKLKGeYFSEYAASLS----LMSAKMVIRDAEI 210
Cdd:cd08196 158 PLVSPGFYPDIAIVDPELTysMPPKVTAS------TGIDA-----LCHAIEA-YWSINHQPISdalaLEAAKLVLENLEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 211 -IRLGQDEGIR-KVVKALISSGVAMSIagssrPASGAEHLFSHALDMLLDKPalHGEQTGIgTI--------------IM 274
Cdd:cd08196 226 aYNNPNDKEAReKMALASLLAGLAFSQ-----TRTTASHACSYPLTSHFGIP--HGEACAL-TLpsfirlnaealpgrLD 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1850361749 275 AYLHGINWK-------KIRDTLKIVGAPTTAYELGIDPEIIieALTIAHTIRPERY 323
Cdd:cd08196 298 ELAKQLGFKdaeeladKIEELKKRIGLRTRLSELGITEEDL--EEIVEESFHPNRA 351
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
56-312 |
5.24e-12 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 66.01 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 56 EFEVYSITVKEAH--INEVERVISKIRDKGIKW---AIAVGGGSIIDVTKLA--SFKMGIPFISFPTTAshdgIASANAS 128
Cdd:cd08199 55 EATILVLPGGEANktMETVLRIVDALDDFGLDRrepVIAIGGGVLLDVVGFAasLYRRGVPYIRVPTTL----LGLVDAG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 129 IkglNVKTSI---KAK-------PPIAVIADIDVIKTAPKRYLAAGVGDIVsnitavrdwKLAhklkgeyfseyaaslsl 198
Cdd:cd08199 131 V---GIKTGVnfgGHKnrlgayyPPVATLLDRSFLKTLPRRHIRNGLAEII---------KMA----------------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 199 msakmVIRDAEIIRLGQDEGIRKVVKALISSGVAMSIAGSS------------------RP-ASGaeHLFSHALDMLLDK 259
Cdd:cd08199 182 -----LVKDAELFELLEEHGAALVETRFFQDEVADEIIRRAiqgmleelapnlwehdleRLvDFG--HTFSPILEMAAAP 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 260 PALHGEQTGIGTIIMAYL-HGINW------KKIRDTLKIVGAPTtaYELGIDPEIIIEAL 312
Cdd:cd08199 255 ELLHGEAVAIDMALSAVLaYRRGLlseeelDRILRLMRRLGLPV--WHPLCTPDLLWRAL 312
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
88-312 |
9.48e-12 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 65.12 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 88 IAVGGGSIIDVTKLASFKM--GIPFISFPTTashdgIASANASikGLNVKTSIKAK----------PPIAVIADIDVIKT 155
Cdd:cd08169 88 VAVGGGATGDVVGFAAATYfrGIAFIRVPTT-----LLAQSDS--SVGIKVGINTRggknllgafyPPRAVFADFSFLKT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 156 APKRYLAAGVGDIVSNitAVrdwkLAHKLKGEYFSEYAASLSLMSAKMVirdaeiirlgqDEGIRKVVKALISSGVA-MS 234
Cdd:cd08169 161 LPFRQVRAGMAELVKM--AL----IADNDFFEFLEDKANSATVYSPEQL-----------EKLINKCISLKLDVVVAdED 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 235 IAGSSRPASGAeHLFSHALDMLLDKPALHGEQTGIGTII-------MAYLHGINWKKIRDTLKIVGAPTTaYELGIDPEI 307
Cdd:cd08169 224 EQGKRRGLNYG-HTFGHALELASGYKIPHGEAVAVGMAYaakianrLGLLPEHDVSRIIWLLNKLGLPLD-HPLALDPDS 301
|
....*
gi 1850361749 308 IIEAL 312
Cdd:cd08169 302 LYEYL 306
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
75-297 |
5.12e-11 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 63.25 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 75 VISKIRDKGIKWA-------IAVGGGSIIDVTKLA--SFKMGIPFISFPTTAshdgIASANASIKGlnvKTSIK---AK- 141
Cdd:PLN02834 148 TLMKVFDKALESRldrrctfVALGGGVIGDMCGFAaaSYQRGVNFVQIPTTV----MAQVDSSVGG---KTGVNhplGKn 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 142 ------PPIAVIADIDVIKTAPKRYLAAGVGDIVsNITAVRDwklahklkGEYFSEYAASLslmsAKMVIRDAEIIRLGQ 215
Cdd:PLN02834 221 migafyQPQCVLIDTDTLATLPDRELASGIAEVV-KYGLIRD--------AEFFEWQEANM----EKLLARDPGALAYAI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 216 DEGIR---KVVKA-LISSGVamsiagssRPASGAEHLFSHALDMLLDKPA-LHGEQTGIGTII---MAYLHGinW----- 282
Cdd:PLN02834 288 KRSCEnkaEVVSLdEKESGL--------RATLNLGHTFGHAIETGPGYGEwLHGEAVAAGTVMaadMSYRLG--Widmsl 357
|
250
....*....|....*.
gi 1850361749 283 -KKIRDTLKIVGAPTT 297
Cdd:PLN02834 358 vNRIFALLKRAKLPTN 373
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
7-163 |
4.71e-10 |
|
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: 60.15 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKLGSPgLVVYGPITKKI-AGSNVEKIVKE---EFEVYSITVKEAHINEVERVISKIRDK 82
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKV-LLVTDPGLVKAgLLDKVLESLKAagiEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 83 GIKWAIAVGGGSIIDVTKLASFKM------------------GIPFISFPTTA---SHdgiASANA--SIKGLNVKTSI- 138
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAgtgSE---VTPNAviTDPETGRKMGIv 156
|
170 180
....*....|....*....|....*..
gi 1850361749 139 --KAKPPIAVIaDIDVIKTAPKRYLAA 163
Cdd:cd08551 157 spYLLPDVAIL-DPELTLSLPPSVTAA 182
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-163 |
6.28e-10 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 59.75 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 1 MHLMEFPREVILGKNLIQEINNVIKRLKLGSPgLVVYGPITKKIAgsNVEKIVKE------EFEVYSITVKEAHINEVER 74
Cdd:COG1454 2 MFTFRLPTRIVFGAGALAELGEELKRLGAKRA-LIVTDPGLAKLG--LLDRVLDAleaagiEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 75 VISKIRDKGIKWAIAVGGGSIIDVTKLASF------------------KMGIPFISFPTTAshdGIAS---ANA--SIKG 131
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALlatnpgdledylgikkvpGPPLPLIAIPTTA---GTGSevtPFAviTDPE 155
|
170 180 190
....*....|....*....|....*....|....
gi 1850361749 132 LNVKTSIKAKP--PIAVIADIDVIKTAPKRYLAA 163
Cdd:COG1454 156 TGVKKGIADPEllPDVAILDPELTLTLPPSLTAA 189
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
8-312 |
7.73e-08 |
|
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway.
Pssm-ID: 341476 Cd Length: 355 Bit Score: 53.36 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 8 REVILGKNLIQEINNVIKRLKlGSPGLVVYGPITKKIAGSNV-EKIVKEEFEVYSITV--KEAH--INEVERVISKIRDK 82
Cdd:cd08197 2 TDIYLGRGILESLLSILEELK-ADRHFLVTDSNVNDLYGDRLlEGLKKAGIPVELLVVpaGESNktLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 83 GI---KWAIAVGGGSIIDVTKLASFKM--GIPFISFPTT--ASHDGIASANASIKGLNVKTSIKA-KPPIAVIADIDVIK 154
Cdd:cd08197 81 GItrrSVIIALGGGVVGNIAGLLAGLLyrGIRLVHVPTTllAQSDSVLSLKQAVNGKSGKNLVGSyYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 155 TAPKRYLAAGVGDIVSN-ITAVRDWKlahklkgEYFSEYAASLSLMSakmvirdaeiirlgqDEGIRKVVKALISSGVAM 233
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNaLIQDPEFL-------DYLEDYLNSDLDYD---------------PEFLEKVIDLSIEAKLEV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 234 sIAGSSRPASGA---E--HLFSHALDMLLDKPALHGEQTGIGTIIMA---YLHGINWKKIRDT----LKIVGAPtTAYEL 301
Cdd:cd08197 219 -LSNDPYEKKEGlilEygHTVGHAIELLSGGELSHGEAVAIGMCVAAeisHLLGLLSEEDVDKhyelLEKIGLP-TIIPD 296
|
330
....*....|.
gi 1850361749 302 GIDPEIIIEAL 312
Cdd:cd08197 297 GISVEAILEVI 307
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
6-170 |
1.57e-07 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 52.38 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 6 FPREVILGKNLIQEINNVIKrlKLGSPGLVVYGpitkkiAGSnVEKI-----VKEEFEVYSITVKE-------AHINEVE 73
Cdd:COG1979 8 NPTKIIFGKGQIAKLGEEIP--KYGKKVLLVYG------GGS-IKKNglydqVKAALKEAGIEVVEfggvepnPRLETVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 74 RVISKIRDKGIKWAIAVGGGSIIDVTKL------------------ASFKMGIPFISFPT---TASHdgiASANASI--K 130
Cdd:COG1979 79 KGVELCKEEGIDFILAVGGGSVIDGAKAiaagakydgdpwdiltgkAPVEKALPLGTVLTlpaTGSE---MNSGSVItnE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1850361749 131 GLNVKTSIKA---KPPIAVIaDIDVIKTAPKRYLAAGVGDIVS 170
Cdd:COG1979 156 ETKEKLGFGSplvFPKFSIL-DPELTYTLPKRQTANGIVDIFS 197
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-163 |
3.91e-07 |
|
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: 51.39 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 10 VILGKNLIQEINNVIKRLKLGSPGLVVygpiTKKIAGSNVEKIVKE-------EFEVYSITVKEAHINEVERVISKIRDK 82
Cdd:cd08190 4 IRFGPGATRELGMDLKRLGAKKVLVVT----DPGLAKLGLVERVLEslekagiEVVVYDGVRVEPTDESFEEAIEFAKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 83 GIKWAIAVGGGSIIDVTKLASFKM-----------------------GIPFISFPTTAshdGIAS-----ANASIKGLNV 134
Cdd:cd08190 80 DFDAFVAVGGGSVIDTAKAANLYAthpgdfldyvnapigkgkpvpgpLKPLIAIPTTA---GTGSettgvAIFDLEELKV 156
|
170 180 190
....*....|....*....|....*....|..
gi 1850361749 135 KTSI---KAKPPIAVIaDIDVIKTAPKRYLAA 163
Cdd:cd08190 157 KTGIssrYLRPTLAIV-DPLLTLTLPPRVTAS 187
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-312 |
1.81e-06 |
|
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: 49.15 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 6 FPREVILGKNLIQEINNVIKRlklgsPGLVVYGPITKKIAGsnVEKIVKE------EFEVYSITVKEAHINEVERVISKI 79
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSGK-----RALIVTDKVLVKLGL--LKKVLKRllqagfEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 80 RDKGIKWAIAVGGGSIIDVTKLASFKMGIP--------------------FISFPTTASHDGIASANA--SIKGLNVKTS 137
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkakLIAIPTTSGTGSEATWAIvlTDTEEPRKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 138 I---KAKPPIAVIaDIDVIKTAPKRyLAAGVGdivsnITAvrdwkLAHKLKGeYFS----EYAASLSLMSAKMVIRD-AE 209
Cdd:cd14862 158 VanpELVPDVAIL-DPEFVLGMPPK-LTAGTG-----LDA-----LAHAVEA-YLStwsnDFSDALALKAIELIFKYlPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 210 IIRLGQDEGIR-KVVKALISSGVAMSIAGssrpaSGAEHLFSHALDMLLDKPalHGEQTGI--------------GTIIM 274
Cdd:cd14862 225 AYKDGDDLEAReKMHNAATIAGLAFGNSQ-----AGLAHALGHSLGAVFHVP--HGIAVGLflpyviefyakvtdERYDL 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1850361749 275 AYLHGIN-----------WKKIRDTLKIVGAPTTAYELGIDPEIIIEAL 312
Cdd:cd14862 298 LKLLGIEardeeealkklVEAIRELYKEVGQPLSIKDLGISEEEFEEKL 346
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
7-338 |
1.97e-06 |
|
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: 48.97 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKrlKLGSPGLVVYGpitkkiaGSNVEKI-----VKEEFEVYSITVKE-------AHINEVER 74
Cdd:cd08187 7 PTKIIFGKGAIEELGEEIK--KYGKKVLLVYG-------GGSIKKNglydrVVASLKEAGIEVVEfggvepnPRLETVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 75 VISKIRDKGIKWAIAVGGGSIIDVTKLASF------------------KMGIPFISFPT---TASHdgiASANA--SIKG 131
Cdd:cd08187 78 GIELAREENVDFILAVGGGSVIDAAKAIAAgakydgdvwdfftgkappEKALPVGTVLTlaaTGSE---MNGGAviTNEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 132 LNVKTSIKAKP--PIAVIADIDVIKTAPKRYLAAGVGDIVSNI-----TAVRDWKLAhklkgEYFSEyaaslSLMsaKMV 204
Cdd:cd08187 155 TKEKLGFGSPLlrPKFSILDPELTYTLPKYQTAAGIVDIFSHVleqyfTGTEDAPLQ-----DRLAE-----GLL--RTV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 205 IRDAEI-IRLGQDEGIRkvvkALI--SSGVAMS-IAGSSRPASGAEHLFSHALDMLLDKPalHGEqtGIGTIIMAYLH-- 278
Cdd:cd08187 223 IENGPKaLKDPDDYEAR----ANLmwAATLALNgLLGAGRGGDWATHAIEHELSALYDIT--HGA--GLAIVFPAWMRyv 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 279 ------------------------------GInwKKIRDTLKIVGAPTTAYELGIDPEIIIEaltIAHTIRPERYTILGK 328
Cdd:cd08187 295 lkkkperfaqfarrvfgidpggddeetaleGI--EALEEFFKSIGLPTTLSELGIDEEDIEE---MAEKAVRGGGLGGGF 369
|
410
....*....|
gi 1850361749 329 EGITREAAEK 338
Cdd:cd08187 370 KPLTREDIEE 379
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-163 |
2.34e-06 |
|
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: 48.65 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLklGSPGLVVYG--PITKKIAGSNVEKIVKEEFEVYSITVK-EAHINEVERVISKIRDKG 83
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAEL--GKRALLVTGrsSLRSGRLARLLEALEAAGIEVALFSVSgEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 84 IKWAIAVGGGSIIDVTKLAS----------------------FKMGIPFISFPTTASHDGIASANA--SIKGLNVKTSIK 139
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAalltnegsvldylevvgkgrplTEPPLPFIAIPTTAGTGSEVTKNAvlSSPEHGVKVSLR 158
|
170 180
....*....|....*....|....*..
gi 1850361749 140 AK---PPIAVIaDIDVIKTAPKRYLAA 163
Cdd:cd08183 159 SPsmlPDVALV-DPELTLSLPPEVTAA 184
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
7-117 |
8.54e-06 |
|
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: 47.22 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLKLGSPGLVVYGPITKKIAGSNVEKIVKEEFEVYSITVKEAH--INEVERVISKIRDKGI 84
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNpdLEDLERGIELFRESGP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1850361749 85 KWAIAVGGGSIIDVTKLASFKMG--------------------IPFISFPTTA 117
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGspgenllllrtgekapeenaLPLIAIPTTA 133
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-163 |
1.94e-05 |
|
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: 45.99 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLkLGSPGLVVYGPITKKIAgsNVEKIVKE------EFEVYSITVKEAHINEVERVISKIR 80
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASL-GGKRALIVTDKVMVKLG--LVDKVTQLlaeagiAYAVFDDVVSEPTDEMVEEGLALYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 81 DKGIKWAIAVGGGSIIDVTK-----------LASF-------KMGIPFISFPTTASHDGIASANASIK--GLNVKTSIKA 140
Cdd:cd08194 78 EGGCDFIVALGGGSPIDTAKaiavlatnggpIRDYmgprkvdKPGLPLIAIPTTAGTGSEVTRFTVITdtETDVKMLLKG 157
|
170 180
....*....|....*....|....*
gi 1850361749 141 KP--PIAVIADIDVIKTAPKRYLAA 163
Cdd:cd08194 158 PAllPAVAIVDPELTLSMPPRVTAA 182
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
12-103 |
3.81e-05 |
|
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: 44.95 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 12 LGKNLIQEINNVIKRLKLGSPgLVVYGPITKKIAG--SNVEKIVKE---EFEVYSITVKEAHINEVERVISKIRDKGIKW 86
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKV-IIVTGRSSYKKSGawDDVEKALEEngiEYVVYDKVTPNPTVDQADEAAKLARDFGADA 84
|
90
....*....|....*..
gi 1850361749 87 AIAVGGGSIIDVTKLAS 103
Cdd:cd08186 85 VIAIGGGSPIDTAKSVA 101
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
7-100 |
1.33e-04 |
|
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: 43.33 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEInnviKRLKlGSPGLVVYGPITKKIAGS--NVEKIVKE---EFEVYSITVKEAHINEVERVISKIRD 81
Cdd:cd08179 5 PRDIYFGEGALEYL----KTLK-GKRAFIVTGGGSMKRNGFldKVEDYLKEagmEVKVFEGVEPDPSVETVEKGAEAMRE 79
|
90
....*....|....*....
gi 1850361749 82 KGIKWAIAVGGGSIIDVTK 100
Cdd:cd08179 80 FEPDWIIAIGGGSVIDAAK 98
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-117 |
1.50e-04 |
|
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: 43.30 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 4 MEF--PREVILGKNLIQEINNVIKRLKLGSPGLVvygpITKKIAGSNVEKIVK-------EEFEVYSITVKEAHINEVER 74
Cdd:cd14865 1 FEFfnPTKIVSGAGALENLPAELARLGARRPLIV----TDKGLAAAGLLKKVEdalgdaiEIVGVFDDVPPDSSVAVVNE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1850361749 75 VISKIRDKGIKWAIAVGGGSIIDVTKLA--SFKMG-----------------IPFISFPTTA 117
Cdd:cd14865 77 AAARAREAGADGIIAVGGGSVIDTAKGVniLLSEGgddlddygganrltrplKPLIAIPTTA 138
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-117 |
1.74e-04 |
|
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: 42.91 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 4 MEFPREVILGKNLIQEINNVIKRLKLGSPgLVVYGPITKKIAGsnVEKIVK------EEFEVYSITVKEAHINEVERVIS 77
Cdd:cd14863 2 YSQLTPVIFGAGAVEQIGELLKELGCKKV-LLVTDKGLKKAGI--VDKIIDlleeagIEVVVFDDVEPDPPDEIVDEAAE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1850361749 78 KIRDKGIKWAIAVGGGSIIDVTKLAS-------------------FKMGIPFISFPTTA 117
Cdd:cd14863 79 IAREEGADGVIGIGGGSVLDTAKAIAvlltnpgpiidyalagppvPKPGIPLIAIPTTA 137
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
1-163 |
2.88e-04 |
|
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: 42.15 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 1 MHLMEfprEVILGKNLIQEINNVIKRLKL------GSPGLVVYGpITKKIagsnvEKIVKE---EFEVYSITVKEAHINE 71
Cdd:cd08176 3 FVLNP---TSYFGWGAIEEIGEEAKKRGFkkalivTDKGLVKFG-IVDKV-----TDVLKEagiAYTVFDEVKPNPTIEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 72 VERVISKIRDKGIKWAIAVGGGSIIDVTK------------LASF-------KMGIPFISFPTTAshdGIAS---ANASI 129
Cdd:cd08176 74 VMAGVAAYKESGADGIIAVGGGSSIDTAKaigiivanpgadVRSLegvaptkNPAVPIIAVPTTA---GTGSevtINYVI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1850361749 130 kglnVKTSIKAK--------PPIAVIADIDVIKTAPKRYLAA 163
Cdd:cd08176 151 ----TDTEKKRKfvcvdphdIPTVAIVDPDLMSSMPKGLTAA 188
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-117 |
9.12e-04 |
|
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: 40.67 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 7 PREVILGKNLIQEINNVIKRLklGSPGLVVYGPITKKIAGsnVEKIVKE------EFEVYSITVKEAHINEVERVISKIR 80
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARL--GSRVLIVTDPRLASTPL--VAELLAAltaagvAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1850361749 81 DKGIKWAIAVGGGSIIDVTKLAS---------------FKM---GIPFISFPTTA 117
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVAlllahggdprdyygeDRVpgpVLPLIAVPTTA 134
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
10-277 |
3.76e-03 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 38.79 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 10 VILGKNLIQEINNVIKRLKLGSPGLVVY--------GPITKKIAgsnvekiVKEEFEVYSI-TVKEAHINEVERVISKIR 80
Cdd:cd08184 4 YLFGRGSFDQLGELLAERRKSNNDYVVFfiddvfkgKPLLDRLP-------LQNGDLLIFVdTTDEPKTDQIDALRAQIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 81 DKGIKWAIAV---GGGSIIDVTKLAS-----------------------FKMGIPFISfPTTAShdgiASANASIKGLNV 134
Cdd:cd08184 77 AENDKLPAAVvgiGGGSTMDIAKAVSnmltnpgsaadyqgwdlvknpgiYKIGVPTLS-GTGAE----ASRTAVLTGPEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 135 KTSIKAK--PPIAVIADIDVIKTAPK-RYLAAGVGDIVSNITAvrdwklahkLKGEYFSEYAASLSLMSAKMvIRDaeiI 211
Cdd:cd08184 152 KLGINSDytVFDQVILDPELIATVPRdQYFYTGMDCYIHCVES---------LNGTYRNAFGDAYAEKALEL-CRD---V 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1850361749 212 RLGQDEGIR----KVVKALISSGvaMSIAGSSrpaSGAEHLFSHALDMLLdkpalhGEQTGIG-TIIMAYL 277
Cdd:cd08184 219 FLSDDMMSPenreKLMVASYLGG--SSIANSQ---VGVCHALSYGLSVVL------GTHHGVAnCIVFNVL 278
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
72-109 |
4.50e-03 |
|
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: 38.74 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1850361749 72 VERVISKIRDKGIKWAIAVGGGSIIDVTKLASFKMGIP 109
Cdd:cd14860 67 VEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISP 104
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-163 |
6.30e-03 |
|
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: 38.05 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 6 FPREVILGKNLIQEINNVIKrlKLGSPGLVVYGPITKkiaGSNVEKIVKEEFEVYSITV-------KEAHINEVERVISK 78
Cdd:cd14864 3 IPPNIVFGADSLERIGEEVK--EYGSRFLLITDPVLK---ESGLADKIVSSLEKAGISVivfdeipASATSDTIDEAAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850361749 79 IRDKGIKWAIAVGGGSIIDVTKLAS-----------FKMG-------IPFISFPTTAsHDG---------IASANASIKG 131
Cdd:cd14864 78 ARKAGADGIIAVGGGKVLDTAKAVAilanndggaydFLEGakpkkkpLPLIAVPTTP-RSGfefsdrfpvVDSRSREVKL 156
|
170 180 190
....*....|....*....|....*....|..
gi 1850361749 132 LNvktsIKAKPPIAVIADIDVIKTAPKRYLAA 163
Cdd:cd14864 157 LK----AQPGLPKAVIVDPNLMASLTGNQTAA 184
|
|
| |
