|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06834 |
PRK06834 |
hypothetical protein; Provisional |
1-485 |
1.64e-133 |
|
hypothetical protein; Provisional
Pssm-ID: 235870 [Multi-domain] Cd Length: 488 Bit Score: 394.77 E-value: 1.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVV-GAGPVGLMLAGELRLGGVDVVVYDKLPAPS-GESRGLGFTSRTAEVLDQRGLLDE-LGEFRWGQHGHFGGV 77
Cdd:PRK06834 1 MTEHAVVIaGGGPTGLMLAGELALAGVDVAIVERRPNQElVGSRAGGLHARTLEVLDQRGIADRfLAQGQVAQVTGFAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 78 RIDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVryDGPDGpGEDHAQYLIGCDGGRST 157
Cdd:PRK06834 81 RLDISDFPTRHNYGLALWQNHIERILAEWVGELGVPIYRGREVTGFAQDDTGVDV--ELSDG-RTLRAQYLVGCDGGRSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 158 VRRLAGIAFPGDEATRGMYLADVTGAdiRPRPIGERVEGGGM-VLSVGLGDGYDRIVIHEPGVRpHHGEGTLTFTEVADA 236
Cdd:PRK06834 158 VRKAAGIDFPGWDPTTSYLIAEVEMT--EEPEWGVHRDALGIhAFGRLEDEGPVRVMVTEKQVG-ATGEPTLDDLREALI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 237 WQRMTGESIHhgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLL 316
Cdd:PRK06834 235 AVYGTDYGIH--SPTWISRFTDMARQAASYRDGRVLLAGDAAHVHSPVGGQGLNTGVQDAVNLGWKLAQVVKGTSPESLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 317 DTYHAERHPLGEQLLRNVHAQSLLYLSGEEMEPLRAVMRELVRIPDAARYLAGQVSGLHIRYDVGAGeHPLLGLRLPPQR 396
Cdd:PRK06834 313 DTYHAERHPVAARVLRNTMAQVALLRPDDRTEALRDIVAELLGMDEPRKRIAAMMSGLDIHYDLGEG-HPLLGRRMPDLD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 397 vLQRADGTRvRVAELLHEARGVLIATGDPSTVhkTAADWSDRVDVV----AGTW-----AEDGGPEAVLLRPDGHVVWAA 467
Cdd:PRK06834 392 -LVTADGPR-RVFTLLHNARPVLLNLGAPGAF--DIAPWSDRVRLVdakyAGPWelpvlGAVAAPAAVLIRPDGYVAWVG 467
|
490
....*....|....*....
gi 1011218312 468 PDGGD-VTDALTRWFGAAA 485
Cdd:PRK06834 468 EGTDDgLADALTTWFGPPA 486
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
6-334 |
1.33e-79 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 251.48 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFRWGQH--GHFGGVRIDFTL 83
Cdd:pfam01494 5 LIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEgmGLAFYNTRRRAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 84 LEE--SHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGV-VVRYDGPDGPGED-HAQYLIGCDGGRSTVR 159
Cdd:pfam01494 85 LDFltSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSLEQDGDGVtAVVRDRRDGEEYTvRAKYLVGCDGGRSPVR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 160 RLAGIAFPGDEATRgMYLADVTGADIRPRP----------IGERVEGGGMVLSVGLGDGYDRIVIHEPGVRPHHGEGTLT 229
Cdd:pfam01494 165 KTLGIEFEGFEGVP-FGSLDVLFDAPDLSDpverafvhylIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEVEERPEEFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 230 FTEVADAWQRMTGESIHHGRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATING 309
Cdd:pfam01494 244 DEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRG 323
|
330 340
....*....|....*....|....*
gi 1011218312 310 WAPDGLLDTYHAERHPLGEQLLRNV 334
Cdd:pfam01494 324 QAGESLLDTYSAERLPVAWAVVDFA 348
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
5-365 |
2.91e-59 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 197.85 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGE--FRWGQ----HGHFGGVR 78
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLArgAPIRGirvrDGSDGRVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 79 IDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDgpDGpGEDHAQYLIGCDGGRSTV 158
Cdd:COG0654 86 ARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTGLEQDADGVTVTLA--DG-RTLRADLVVGADGARSAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 159 RRLAGIAFPGDEATRGMYLADVTgADIRPRpigervegggmvlsvglgdgydrivihepgvrphhgegtltFTEVADAWQ 238
Cdd:COG0654 163 RRLLGIGFTGRDYPQRALWAGVR-TELRAR-----------------------------------------LAAAGPRLG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 239 RMTgesihhgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLLDT 318
Cdd:COG0654 201 ELL-------ELSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAALAR 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1011218312 319 YHAERHPLGEQLLRNVHAQSLLYLSGEEMEPL--RAVMRELVRIPDAAR 365
Cdd:COG0654 274 YERERRPRAARVQRAADALGRLFHPDSPPLRLlrNAGLRLLDRLPPLKG 322
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
6-373 |
2.25e-15 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 77.63 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPA-----PSGESRGLGFTSRTAEVLDQRGLLDELGEFR---------WGQh 71
Cdd:TIGR01988 3 VIVGGGMVGLALALALARSGLKVALIEATPLpapadPGFDNRVSALSAASIRLLEKLGVWDKIEPARaqpirdihvSDG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 72 GHFGGVRIDFTLLEESHFGVMG----LAQSRTEQLlgdwTARLGVPVLRGREVTGFEETEDGVVVRYDGPDgpgEDHAQY 147
Cdd:TIGR01988 82 GSFGALRFDADEIGLEALGYVVenrvLQQALWERL----QELPNVTLLCPARVVELPRHSDHVELTLDDGQ---QLRARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 148 LIGCDGGRSTVRRLAGIAFPGDEATRGMYLADVTgADIRPRPIG-ERVEGGGMVLSVGLGDGYDRIVIHEPgvrPHHGEG 226
Cdd:TIGR01988 155 LVGADGANSKVRQLAGIPTTGWDYGQSAVVANVK-HERPHQGTAwERFTPTGPLALLPLPDNRSSLVWTLP---PEEAER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 227 --TLTFTEVADAWQRMTGE-----SIHHGRTRWMTALTnatgLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNL 299
Cdd:TIGR01988 231 llALSDEEFLAELQRAFGSrlgaiTLVGERHAFPLSLT----HAKRYVAPRLALIGDAAHTIHPLAGQGLNLGLRDVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 300 GWKLAATI---NGWAPDGLLDTYHAERHPLGEQLLRNVHAQSLLYLSgeEMEPLRAV----MRELVRIPDAARYLAGQVS 372
Cdd:TIGR01988 307 AEVLEDARrrgEDIGSLRVLQRYERRRRFDNAAMLGATDGLNRLFSN--DFPPLRLLrnlgLRLLNNLPPLKNFIARYAM 384
|
.
gi 1011218312 373 G 373
Cdd:TIGR01988 385 G 385
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
5-42 |
6.28e-03 |
|
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176192 [Multi-domain] Cd Length: 355 Bit Score: 38.74 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESR 42
Cdd:cd08230 176 ALVLGAGPIGLLAALLLRLRGFEVYVLNRRDPPDPKAD 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06834 |
PRK06834 |
hypothetical protein; Provisional |
1-485 |
1.64e-133 |
|
hypothetical protein; Provisional
Pssm-ID: 235870 [Multi-domain] Cd Length: 488 Bit Score: 394.77 E-value: 1.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVV-GAGPVGLMLAGELRLGGVDVVVYDKLPAPS-GESRGLGFTSRTAEVLDQRGLLDE-LGEFRWGQHGHFGGV 77
Cdd:PRK06834 1 MTEHAVVIaGGGPTGLMLAGELALAGVDVAIVERRPNQElVGSRAGGLHARTLEVLDQRGIADRfLAQGQVAQVTGFAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 78 RIDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVryDGPDGpGEDHAQYLIGCDGGRST 157
Cdd:PRK06834 81 RLDISDFPTRHNYGLALWQNHIERILAEWVGELGVPIYRGREVTGFAQDDTGVDV--ELSDG-RTLRAQYLVGCDGGRSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 158 VRRLAGIAFPGDEATRGMYLADVTGAdiRPRPIGERVEGGGM-VLSVGLGDGYDRIVIHEPGVRpHHGEGTLTFTEVADA 236
Cdd:PRK06834 158 VRKAAGIDFPGWDPTTSYLIAEVEMT--EEPEWGVHRDALGIhAFGRLEDEGPVRVMVTEKQVG-ATGEPTLDDLREALI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 237 WQRMTGESIHhgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLL 316
Cdd:PRK06834 235 AVYGTDYGIH--SPTWISRFTDMARQAASYRDGRVLLAGDAAHVHSPVGGQGLNTGVQDAVNLGWKLAQVVKGTSPESLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 317 DTYHAERHPLGEQLLRNVHAQSLLYLSGEEMEPLRAVMRELVRIPDAARYLAGQVSGLHIRYDVGAGeHPLLGLRLPPQR 396
Cdd:PRK06834 313 DTYHAERHPVAARVLRNTMAQVALLRPDDRTEALRDIVAELLGMDEPRKRIAAMMSGLDIHYDLGEG-HPLLGRRMPDLD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 397 vLQRADGTRvRVAELLHEARGVLIATGDPSTVhkTAADWSDRVDVV----AGTW-----AEDGGPEAVLLRPDGHVVWAA 467
Cdd:PRK06834 392 -LVTADGPR-RVFTLLHNARPVLLNLGAPGAF--DIAPWSDRVRLVdakyAGPWelpvlGAVAAPAAVLIRPDGYVAWVG 467
|
490
....*....|....*....
gi 1011218312 468 PDGGD-VTDALTRWFGAAA 485
Cdd:PRK06834 468 EGTDDgLADALTTWFGPPA 486
|
|
| PRK08244 |
PRK08244 |
monooxygenase; |
1-482 |
2.71e-132 |
|
monooxygenase;
Pssm-ID: 236199 [Multi-domain] Cd Length: 493 Bit Score: 391.80 E-value: 2.71e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEF-RWGQHGHFGGV-- 77
Cdd:PRK08244 1 MKYEVIIIGGGPVGLMLASELALAGVKTCVIERLKETVPYSKALTLHPRTLEILDMRGLLERFLEKgRKLPSGHFAGLdt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 78 RIDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGPDGPGEDHAQYLIGCDGGRST 157
Cdd:PRK08244 81 RLDFSALDTSSNYTLFLPQAETEKVLEEHARSLGVEIFRGAEVLAVRQDGDGVEVVVRGPDGLRTLTSSYVVGADGAGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 158 VRRLAGIAFPGDEATRGMYLADVTGADIRPRPIGERVEGGGMVLSVGLGDGYDRIVIHEPGVRPHHGEGTLTFTEVADAW 237
Cdd:PRK08244 161 VRKQAGIAFPGTDATFTAMLGDVVLKDPPPSSVLSLCTREGGVMIVPLSGGIYRVLIIDPERPQVPKDEPVTLEELKTSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 238 QRMTGESIHHGRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLLD 317
Cdd:PRK08244 241 IRICGTDFGLNDPVWMSRFGNATRQAERYRSGRIFLAGDAAHIHFPAGGQGLNVGLQDAMNLGWKLAAAIKGWAPDWLLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 318 TYHAERHPLGEQLLRNVHAQSLLYLSGEEMEPLRAVMRELVRIPDAARYLAGQVSGLHIRY--DVGAGEHPLLGLRLPPQ 395
Cdd:PRK08244 321 SYHAERHPVGTALLRNTEVQTKLFDFTRPGLALRSMLSDLLGFPEVNRYLAGQISALDVHYepDAEMPPHPLNGKRLPDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 396 RvLQRADGTRVRVAELLHEARGVLIAtgdpstVHKTAADWS--DRVDVVAGTWAEDG----GPEAVLLRPDGHVVWA--- 466
Cdd:PRK08244 401 E-LTLSDGESERLYSLLHKGTFLLLS------FGSEPQDWSryPHVRVVRASLAEGRadwnDVHTALIRPDGHVAWAvda 473
|
490
....*....|....*...
gi 1011218312 467 -APDGGD-VTDALTRWFG 482
Cdd:PRK08244 474 sDPNAEEaIAAGISRWCG 491
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
6-334 |
1.33e-79 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 251.48 E-value: 1.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFRWGQH--GHFGGVRIDFTL 83
Cdd:pfam01494 5 LIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLEDRILAEGVPHEgmGLAFYNTRRRAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 84 LEE--SHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGV-VVRYDGPDGPGED-HAQYLIGCDGGRSTVR 159
Cdd:pfam01494 85 LDFltSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSLEQDGDGVtAVVRDRRDGEEYTvRAKYLVGCDGGRSPVR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 160 RLAGIAFPGDEATRgMYLADVTGADIRPRP----------IGERVEGGGMVLSVGLGDGYDRIVIHEPGVRPHHGEGTLT 229
Cdd:pfam01494 165 KTLGIEFEGFEGVP-FGSLDVLFDAPDLSDpverafvhylIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEVEERPEEFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 230 FTEVADAWQRMTGESIHHGRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATING 309
Cdd:pfam01494 244 DEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRG 323
|
330 340
....*....|....*....|....*
gi 1011218312 310 WAPDGLLDTYHAERHPLGEQLLRNV 334
Cdd:pfam01494 324 QAGESLLDTYSAERLPVAWAVVDFA 348
|
|
| PRK06184 |
PRK06184 |
hypothetical protein; Provisional |
7-479 |
2.06e-64 |
|
hypothetical protein; Provisional
Pssm-ID: 235728 [Multi-domain] Cd Length: 502 Bit Score: 216.77 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDEL--------------GEFRWGQHG 72
Cdd:PRK06184 8 IVGAGPTGLTLAIELARRGVSFRLIEKAPEPFPGSRGKGIQPRTQEVFDDLGVLDRVvaagglyppmriyrDDGSVAESD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 73 HFGgvRIDFTLLEESHFGVMgLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGPDGPGEDHAQYLIGCD 152
Cdd:PRK06184 88 MFA--HLEPTPDEPYPLPLM-VPQWRTERILRERLAELGHRVEFGCELVGFEQDADGVTARVAGPAGEETVRARYLVGAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 153 GGRSTVRRLAGIAFPGdeATRG---MYLADV--TGADiRPRPIGERVEGGGMVLSVGLGdGYDRIVIHepGVRPHHGEGT 227
Cdd:PRK06184 165 GGRSFVRKALGIGFPG--ETLGidrMLVADVslTGLD-RDAWHQWPDGDMGMIALCPLP-GTDLFQIQ--APLPPGGEPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 228 L---TFTEVADAWQRMTGESIHhgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLA 304
Cdd:PRK06184 239 LsadGLTALLAERTGRTDIRLH--SVTWASAFRMNARLADRYRVGRVFLAGDAAHVHPPAGGQGLNTSVQDAYNLGWKLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 305 ATINGwAPDGLLDTYHAERHPLgeqllrnvhAQSLLYLSGEEmepLRAVMRELVRIPDAARYLAGQVSGLHIRYDVGAGE 384
Cdd:PRK06184 317 AVLAG-APEALLDTYEEERRPV---------AAAVLGLSTEL---LDAIKRGDMRRGRDVQQLDLGYRGSSLAVDGPERT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 385 HPLL-GLRLPPQRVLQrADGTRVRVAELLHEARGVLIATG-DPSTVHKTAA-------DWSDRVDVV--AGTWAEDGGPE 453
Cdd:PRK06184 384 GGLRaGDRAPDAPLLG-AAGQPTRLFDLFRGPHWTLLAFGaGAAAILARRGlrihrvgDAAEGGDLVddAGHFRDAYGLT 462
|
490 500 510
....*....|....*....|....*....|.
gi 1011218312 454 A---VLLRPDGHV--VWAAPDGGDVTDALTR 479
Cdd:PRK06184 463 GgtlVLVRPDGYVglIAAGDDAAALEAYLAR 493
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
5-365 |
2.91e-59 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 197.85 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGE--FRWGQ----HGHFGGVR 78
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRLLArgAPIRGirvrDGSDGRVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 79 IDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDgpDGpGEDHAQYLIGCDGGRSTV 158
Cdd:COG0654 86 ARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTEVTGLEQDADGVTVTLA--DG-RTLRADLVVGADGARSAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 159 RRLAGIAFPGDEATRGMYLADVTgADIRPRpigervegggmvlsvglgdgydrivihepgvrphhgegtltFTEVADAWQ 238
Cdd:COG0654 163 RRLLGIGFTGRDYPQRALWAGVR-TELRAR-----------------------------------------LAAAGPRLG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 239 RMTgesihhgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLLDT 318
Cdd:COG0654 201 ELL-------ELSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAALAR 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1011218312 319 YHAERHPLGEQLLRNVHAQSLLYLSGEEMEPL--RAVMRELVRIPDAAR 365
Cdd:COG0654 274 YERERRPRAARVQRAADALGRLFHPDSPPLRLlrNAGLRLLDRLPPLKG 322
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
7-486 |
8.83e-54 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 188.19 E-value: 8.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFRWGQHG-----HFGGVRIDF 81
Cdd:PRK06183 15 IVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAVGIDDEALRVLQAIGLADEVLPHTTPNHGmrfldAKGRCLAEI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 82 TLLEESHFG---VMGLAQSRTEQLLGDWTARL-GVPVLRGREVTGFEETEDGVVVRYDGPDGPGED-HAQYLIGCDGGRS 156
Cdd:PRK06183 95 ARPSTGEFGwprRNAFHQPLLEAVLRAGLARFpHVRVRFGHEVTALTQDDDGVTVTLTDADGQRETvRARYVVGCDGANS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 157 TVRRLAGIAFPGDEATRGMYLADVTgadIRPRPIGerveGGGMVL---------SVGLGDGYDRiviHEPGVRPhhGEGT 227
Cdd:PRK06183 175 FVRRTLGVPFEDLTFPERWLVVDVL---IANDPLG----GPHTYQycdparpytSVRLPHGRRR---WEFMLLP--GETE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 228 LTFTEVADAWQRMTGESIHHGRTRWM--TALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAA 305
Cdd:PRK06183 243 EQLASPENVWRLLAPWGPTPDDAELIrhAVYTFHARVADRWRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLAWKLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 306 TINGWAPDGLLDTYHAERHPlgeqllrnvHAQSLLYLSgeemEPLRAVM----RELVRIPDAARyLAGQV---------S 372
Cdd:PRK06183 323 VLRGRAGDALLDTYEQERRP---------HARAMIDLA----VRLGRVIcptdRLAAALRDAVL-PVGTLfpqprvelgG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 373 GLHIRYD--VGAGeHPLLGLRLPPQRVLqrADGTRVRVAellheARGVLIATGDPStvhkTAADWSDRVDVVAGT----- 445
Cdd:PRK06183 389 GDRGLLDdvLGPG-FAVLGWGCDPLAGL--SDEQRARWR-----ALGARFVQVVPA----VQAHTAQDDHDSDVDgalra 456
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1011218312 446 WAEDGGPEAVLLRPDGHVVwAAPDGGDVTDALTRWFGAAAV 486
Cdd:PRK06183 457 WLARHGASAVLLRPDRYVA-AAADAQTLGALLAALAALLHL 496
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
6-472 |
1.97e-47 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 172.10 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELgefrwgqhgHFGGVRIDFTL-- 83
Cdd:PRK06126 11 LIVGGGPVGLALALDLGRRGVDSILVERKDGTAFNPKANTTSARSMEHFRRLGIADEV---------RSAGLPVDYPTdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 84 ----------LEESHFGVMGLAQSRTEQLLGDW----------------------TARLGVPVLRGREVTGFEETEDGVV 131
Cdd:PRK06126 82 ayftrltgyeLARFRLPSAREAITPVGGPDGSWpspelphripqkylepillehaAAQPGVTLRYGHRLTDFEQDADGVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 132 --VRYDGPDGPGEDHAQYLIGCDGGRSTVRRLAGIAFPGDEATRgmylaDVTGADIRPRPIGERVEGGG--MVLSVGLG- 206
Cdd:PRK06126 162 atVEDLDGGESLTIRADYLVGCDGARSAVRRSLGISYEGTSGLQ-----RDLSIYIRAPGLAALVGHDPawMYWLFNPDr 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 207 -------DGYDRIVIHEpgVRPHHGEGTLTFTEVADAWQRMTGESIHHGRTRWMTALTNATgLAEQYRSGRVLLAGDAAH 279
Cdd:PRK06126 237 rgvlvaiDGRDEWLFHQ--LRGGEDEFTIDDVDARAFVRRGVGEDIDYEVLSVVPWTGRRL-VADSYRRGRVFLAGDAAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 280 DHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLLDTYHAERHPLGeqlLRNV-----HAQSLLYLSG----EEMEPL 350
Cdd:PRK06126 314 LFTPTGGYGMNTGIGDAVNLAWKLAAVLNGWAGPALLDSYEAERRPIA---ARNTdyarrNADALGSFPVppeiEDDGPA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 351 RAVMRELVRipDAARYLAGQ---VSGLHI--RYD-----VGAGEHP------------LLGLRLP--------------- 393
Cdd:PRK06126 391 GDAARRKVG--DALSEHARQefnSPGITLgyRYDgspiiVPDGTPPppddpgvyvpsaCPGGRAPhawlsdgrslydlfg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 394 PQRVLQRADGTRVRVAELLHEARgvliATGDPSTVHKTAAdwsdrvDVVAGTWAEDggpeAVLLRPDGHVVW---AAPDG 470
Cdd:PRK06126 469 PGFTLLRFGDAAVDVAPLEAAAA----ALGVPLAVVDLPG------PEAAALYEAD----LVLVRPDQHVAWrgdAAPDD 534
|
..
gi 1011218312 471 GD 472
Cdd:PRK06126 535 AA 536
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
6-479 |
8.83e-44 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 161.96 E-value: 8.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFrwGQHGHFGGVRI------ 79
Cdd:PRK08132 27 VVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLSTGSRAICFAKRSLEIFDRLGCGERMVDK--GVSWNVGKVFLrdeevy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 80 DFTLLEES--HFGVM-GLAQSRTEQLLGDWTARLGVPVLRGR-EVTGFEETEDGVVVRYDGPDGPGEDHAQYLIGCDGGR 155
Cdd:PRK08132 105 RFDLLPEPghRRPAFiNLQQYYVEGYLVERAQALPNIDLRWKnKVTGLEQHDDGVTLTVETPDGPYTLEADWVIACDGAR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 156 STVRRLAGIAFPGdEATRGMYLAdvtgADIR---PRPIgER-------VEGGGMVL-----------SVGLGDGYDRIVI 214
Cdd:PRK08132 185 SPLREMLGLEFEG-RTFEDRFLI----ADVKmkaDFPT-ERwfwfdppFHPGQSVLlhrqpdnvwriDFQLGWDADPEAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 215 HEPG-VRPHhgegtltftevadaWQRMTGESIHHgRTRWMTALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGL 293
Cdd:PRK08132 259 KKPEnVIPR--------------VRALLGEDVPF-ELEWVSVYTFQCRRMDRFRHGRVLFAGDAAHQVSPFGARGANSGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 294 QDAVNLGWKLAATINGWAPDGLLDTYHAERhplgeqllrnVHA--QSLLY--LSGEEMEP-------LR-AVMReLVRIP 361
Cdd:PRK08132 324 QDADNLAWKLALVLRGRAPDSLLDSYASER----------EFAadENIRNstRSTDFITPkspvsrlFRdAVLR-LARDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 362 DAARYL--AGQVSgLHIRY----------DVGAGEhPLLGLRLPPQRVlqRADGTRVRVAELLHEARGVLIATGDPSTVH 429
Cdd:PRK08132 393 PFARRLvnSGRLS-VPAVYadsplntpdgDAFAGG-PVPGAPAPDAPV--RADGEPGWLLDLLGGGFTLLLFGDDAAAAA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011218312 430 KTAADWSDRVDVVAGTWAEDGGPEAV-----------------------LLRPDGHVV--WAAPDGGDVTDALTR 479
Cdd:PRK08132 469 LLQALAAAALPVRVVAVVPAGAAQAAagvledadglaaerydarpgtvyLIRPDQHVAarWRTPDAAAVRAALAR 543
|
|
| PRK07190 |
PRK07190 |
FAD-binding protein; |
6-485 |
6.84e-36 |
|
FAD-binding protein;
Pssm-ID: 235955 [Multi-domain] Cd Length: 487 Bit Score: 139.18 E-value: 6.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELgeFRWGQ---------HGHFgg 76
Cdd:PRK07190 9 VIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGPLEVGRADALNARTLQLLELVDLFDEL--YPLGKpcntssvwaNGKF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 77 VRIDFTLLEE------SHFGVMGlaQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGpdgpGED-HAQYLI 149
Cdd:PRK07190 85 ISRQSSWWEElegclhKHFLMLG--QSYVEKLLDDKLKEAGAAVKRNTSVVNIELNQAGCLTTLSN----GERiQSRYVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 150 GCDGGRSTVRRLAGIAFpgdEATRGMYLADVTGADIR------PRPIGERVEGGGMVLSVGLGDgYDRIVihepgVRPHH 223
Cdd:PRK07190 159 GADGSRSFVRNHFNVPF---EIIRPQIIWAVIDGVIDtdfpkvPEIIVFQAETSDVAWIPREGE-IDRFY-----VRMDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 224 GEGTLTftEVADAWQR-MTGESIHHGRTRWMTALTNATGLAEQYR-SGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGW 301
Cdd:PRK07190 230 KDFTLE--QAIAKINHaMQPHRLGFKEIVWFSQFSVKESVAEHFFiQDRIFLAGDACHIHSVNGGQGLNTGLADAFNLIW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 302 KLAATINGWAPDGLLDTYHAERHPLgeqllrnvhAQSLLYLSGeemeplravmrELVRIPD-------AARYL------A 368
Cdd:PRK07190 308 KLNMVIHHGASPELLQSYEAERKPV---------AQGVIETSG-----------ELVRSTKysangthAQDYVkivekrA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 369 GQVSGLHIRYdvgaGEHPLLGLRLPPQRVLQRAdgTRVRVAELLHEARGVLIATGD-------PSTVHKTAADWSDRvdv 441
Cdd:PRK07190 368 GYITGMGIRY----GEEGLCGSRLFDFEIFQGS--EKTRLYSLLDYRKFTLFIFGDcevelnvPEFVKVIHIYPQQE--- 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1011218312 442 VAGTWAEDG--GPEAVLLRPDGHVVWAAPdGGDVTDALTRWFGAAA 485
Cdd:PRK07190 439 QANFWTRNSpyAGQAILVRPDSYIEWSVP-LDQVESLFALAQLTEF 483
|
|
| PRK08294 |
PRK08294 |
phenol 2-monooxygenase; Provisional |
117-331 |
9.78e-25 |
|
phenol 2-monooxygenase; Provisional
Pssm-ID: 236223 [Multi-domain] Cd Length: 634 Bit Score: 107.77 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 117 GREVTGFEETEDG---VVVRYDGPDGPGEDH-----AQYLIGCDGGRSTVRRLAGIAFPGDEATRG---M-YLADVTGAD 184
Cdd:PRK08294 163 GREFVDLEVDEEGeypVTVTLRRTDGEHEGEeetvrAKYVVGCDGARSRVRKAIGRELRGDSANHAwgvMdVLAVTDFPD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 185 IR----------------PRpigervEGGGMV-LSVGLG--DGYDRIVIHEPGV-----------RPHhgegTLTFTEVA 234
Cdd:PRK08294 243 IRlkcaiqsasegsilliPR------EGGYLVrLYVDLGevPPDERVAVRNTTVeeviakaqrilHPY----TLDVKEVA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 235 daW-------QRMTgesihhgrTRWMTALTNATGLaeqyRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATI 307
Cdd:PRK08294 313 --WwsvyevgQRLT--------DRFDDVPAEEAGT----RLPRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVL 378
|
250 260
....*....|....*....|....
gi 1011218312 308 NGWAPDGLLDTYHAERHPLGEQLL 331
Cdd:PRK08294 379 SGRSPPELLHTYSAERQAIAQELI 402
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
7-297 |
2.08e-19 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 89.92 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFRWGQ----HGHFGGVRI--- 79
Cdd:PRK06185 11 IVGGGPAGMMLGLLLARAGVDVTVLEKHADFLRDFRGDTVHPSTLELMDELGLLERFLELPHQKvrtlRFEIGGRTVtla 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 80 DFTLLEESH-FGVMgLAQSRTEQLLGDWTARL-GVPVLRGREVTGFEETEDGVV-VRYDGPDGPGEDHAQYLIGCDGGRS 156
Cdd:PRK06185 91 DFSRLPTPYpYIAM-MPQWDFLDFLAEEASAYpNFTLRMGAEVTGLIEEGGRVTgVRARTPDGPGEIRADLVVGADGRHS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 157 TVRRLAGIAfpgdeatrgmylADVTGADI------------RPRPIGERVEGGGMVLSVGLGD-----------GYDRiv 213
Cdd:PRK06185 170 RVRALAGLE------------VREFGAPMdvlwfrlprepdDPESLMGRFGPGQGLIMIDRGDywqcgyvipkgGYAA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 214 IHEPGVRPHHGEGTLTFTEVAD------AWQRMTGESIHHGR-TRWmtaltnatglaeqYRSGrVLLAGDAAHDHAPLGA 286
Cdd:PRK06185 236 LRAAGLEAFRERVAELAPELADrvaelkSWDDVKLLDVRVDRlRRW-------------HRPG-LLCIGDAAHAMSPVGG 301
|
330
....*....|.
gi 1011218312 287 QGVSVGLQDAV 297
Cdd:PRK06185 302 VGINLAIQDAV 312
|
|
| Ubi-OHases |
TIGR01988 |
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ... |
6-373 |
2.25e-15 |
|
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273913 [Multi-domain] Cd Length: 385 Bit Score: 77.63 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPA-----PSGESRGLGFTSRTAEVLDQRGLLDELGEFR---------WGQh 71
Cdd:TIGR01988 3 VIVGGGMVGLALALALARSGLKVALIEATPLpapadPGFDNRVSALSAASIRLLEKLGVWDKIEPARaqpirdihvSDG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 72 GHFGGVRIDFTLLEESHFGVMG----LAQSRTEQLlgdwTARLGVPVLRGREVTGFEETEDGVVVRYDGPDgpgEDHAQY 147
Cdd:TIGR01988 82 GSFGALRFDADEIGLEALGYVVenrvLQQALWERL----QELPNVTLLCPARVVELPRHSDHVELTLDDGQ---QLRARL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 148 LIGCDGGRSTVRRLAGIAFPGDEATRGMYLADVTgADIRPRPIG-ERVEGGGMVLSVGLGDGYDRIVIHEPgvrPHHGEG 226
Cdd:TIGR01988 155 LVGADGANSKVRQLAGIPTTGWDYGQSAVVANVK-HERPHQGTAwERFTPTGPLALLPLPDNRSSLVWTLP---PEEAER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 227 --TLTFTEVADAWQRMTGE-----SIHHGRTRWMTALTnatgLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNL 299
Cdd:TIGR01988 231 llALSDEEFLAELQRAFGSrlgaiTLVGERHAFPLSLT----HAKRYVAPRLALIGDAAHTIHPLAGQGLNLGLRDVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 300 GWKLAATI---NGWAPDGLLDTYHAERHPLGEQLLRNVHAQSLLYLSgeEMEPLRAV----MRELVRIPDAARYLAGQVS 372
Cdd:TIGR01988 307 AEVLEDARrrgEDIGSLRVLQRYERRRRFDNAAMLGATDGLNRLFSN--DFPPLRLLrnlgLRLLNNLPPLKNFIARYAM 384
|
.
gi 1011218312 373 G 373
Cdd:TIGR01988 385 G 385
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
10-170 |
2.62e-11 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 64.22 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 10 AGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLDELGEFRWGQHGHF-GGVRIDFtllEESH 88
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLERPVRGARFYSpGGKSVEL---PPGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 89 FGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGPDgpgEDHAQYLIGCDGGRSTVRRLAGIAFPG 168
Cdd:COG0644 78 GGGYVVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGE---EIRADYVVDADGARSLLARKLGLKRRS 154
|
..
gi 1011218312 169 DE 170
Cdd:COG0644 155 DE 156
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
1-325 |
7.55e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 63.74 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVVGAGPVGLMLAGELRLGGVDVVVYDKlpAPSGESRGLGFT--SRTAEVLDQRGLLDELGE--FRWGQ------ 70
Cdd:PRK06847 3 AVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEI--DPEWRVYGAGITlqGNALRALRELGVLDECLEagFGFDGvdlfdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 71 HGHFGGVRIDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDgpDGpGEDHAQYLIG 150
Cdd:PRK06847 81 DGTLLAELPTPRLAGDDLPGGGGIMRPALARILADAARAAGADVRLGTTVTAIEQDDDGVTVTFS--DG-TTGRYDLVVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 151 CDGGRSTVRRLagiafpgdeatrgmyladVTGADIRPRPIG--------ERVEG-------GGMVLSVG---LGD--GYD 210
Cdd:PRK06847 158 ADGLYSKVRSL------------------VFPDEPEPEYTGqgvwravlPRPAEvdrslmyLGPTTKAGvvpLSEdlMYL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 211 RIVIHEPGvRPHHGEGTLtFTEVADAWQRMTGESI----------HHGRTRWMTALTnatgLAEQYRSGRVLLAGDAAHD 280
Cdd:PRK06847 220 FVTEPRPD-NPRIEPDTL-AALLRELLAPFGGPVLqelreqitddAQVVYRPLETLL----VPAPWHRGRVVLIGDAAHA 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1011218312 281 HAPLGAQGVSVGLQDAVNLGWKLAatiNGWAPDGLLDTYHAERHP 325
Cdd:PRK06847 294 TTPHLAQGAGMAIEDAIVLAEELA---RHDSLEAALQAYYARRWE 335
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
5-325 |
1.46e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 62.99 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPapsgESRGLG----FTSRTAEVLDQRGLLDELGEF-----RWGQHGHFG 75
Cdd:PRK07538 3 VLIAGGGIGGLTLALTLHQRGIEVVVFEAAP----ELRPLGvginLLPHAVRELAELGLLDALDAIgirtrELAYFNRHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 76 --------GVRIDFTLLEES-HFGvmglaqsRTEQLLGD-WTARLGVPVLR-GREVTGFEETEDGVVVRYDGPDG--PGE 142
Cdd:PRK07538 79 qriwseprGLAAGYDWPQYSiHRG-------ELQMLLLDaVRERLGPDAVRtGHRVVGFEQDADVTVVFLGDRAGgdLVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 143 DHAQYLIGCDGGRSTVRRLAgiaFPGDEATRG----MYLADVTGADIRPrpigerveGGGMVlsvGLGDGYDRIVIHePG 218
Cdd:PRK07538 152 VRGDVLIGADGIHSAVRAQL---YPDEGPPRWngvmMWRGVTEAPPFLT--------GRSMV---MAGHLDGKLVVY-PI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 219 VRPHHGEGTLTFTEVADA------------WQRM--TGESIHH-GRTRW----MTALTNATGLAEQY-----------RS 268
Cdd:PRK07538 217 SEPVDADGRQLINWVAEVrvddagaprredWNRPgdLEDFLPHfADWRFdwldVPALIRAAEAIYEYpmvdrdplprwTR 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1011218312 269 GRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATingWAPDGLLDTYHAERHP 325
Cdd:PRK07538 297 GRVTLLGDAAHPMYPVGSNGASQAILDARALADALAAH---GDPEAALAAYEAERRP 350
|
|
| PRK08773 |
PRK08773 |
UbiH/UbiF family hydroxylase; |
120-299 |
3.59e-07 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181552 [Multi-domain] Cd Length: 392 Bit Score: 52.17 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 120 VTGFEETEDGVVVRYDgpDGPGEDhAQYLIGCDGGRSTVRRLAGIAFPG-DEATRGMyLADVTGADIRPRPIGERVEGGG 198
Cdd:PRK08773 136 VVALEQDADRVRLRLD--DGRRLE-AALAIAADGAASTLRELAGLPVSRhDYAQRGV-VAFVDTEHPHQATAWQRFLPTG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 199 MVLSVGLGDGYDRIVIHEPGVrphHGEGTLTFTEVADAWQRMTGESIHHGRTRWM---TALTNATGLAEQYRSGRVLLAG 275
Cdd:PRK08773 212 PLALLPFADGRSSIVWTLPDA---EAERVLALDEAAFSRELTQAFAARLGEVRVAsprTAFPLRRQLVQQYVSGRVLTLG 288
|
170 180
....*....|....*....|....
gi 1011218312 276 DAAHDHAPLGAQGVSVGLQDAVNL 299
Cdd:PRK08773 289 DAAHVVHPLAGQGVNLGLRDVAAL 312
|
|
| PRK08163 |
PRK08163 |
3-hydroxybenzoate 6-monooxygenase; |
120-325 |
7.58e-06 |
|
3-hydroxybenzoate 6-monooxygenase;
Pssm-ID: 181262 [Multi-domain] Cd Length: 396 Bit Score: 48.11 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 120 VTGFEETEDGVVVRydgpDGPGEDH-AQYLIGCDGGRSTVRRlagiAFPGDEATrgmyladVTG-----ADIRPRPIGER 193
Cdd:PRK08163 133 VVGIEQDGDGVTVF----DQQGNRWtGDALIGCDGVKSVVRQ----SLVGDAPR-------VTGhvvyrAVIDVDDMPED 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 194 VEGGGMVLSVGL-----------GDGYDRIVI------HEPGVRPHHGEGTLT-FTEVADAWQRMtgesIHHGRT--RWM 253
Cdd:PRK08163 198 LRINAPVLWAGPhchlvhyplrgGEQYNLVVTfhsreqEEWGVKDGSKEEVLSyFEGIHPRPRQM----LDKPTSwkRWA 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011218312 254 TALTNATglaEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWApdGLLDTYHAERHP 325
Cdd:PRK08163 274 TADREPV---AKWSTGRVTLLGDAAHPMTQYMAQGACMALEDAVTLGKALEGCDGDAE--AAFALYESVRIP 340
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
7-160 |
1.08e-05 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 47.49 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYdklpapsgESRglgftSRT-------AEVLDQRG--LLDELG------------- 64
Cdd:PRK08243 7 IIGAGPAGLLLGQLLHLAGIDSVVL--------ERR-----SREyvegrirAGVLEQGTvdLLREAGvgermdreglvhd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 65 --EFRWGQHGHfggvRIDFTLLEESHFgVMGLAQsrTEqLLGDWTA---RLGVPVLRG-REVTGFEETEDGVVVRYDGPD 138
Cdd:PRK08243 74 giELRFDGRRH----RIDLTELTGGRA-VTVYGQ--TE-VTRDLMAarlAAGGPIRFEaSDVALHDFDSDRPYVTYEKDG 145
|
170 180
....*....|....*....|..
gi 1011218312 139 GPGEDHAQYLIGCDGGRSTVRR 160
Cdd:PRK08243 146 EEHRLDCDFIAGCDGFHGVSRA 167
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
7-39 |
4.34e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 45.75 E-value: 4.34e-05
10 20 30
....*....|....*....|....*....|...
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSG 39
Cdd:PRK12770 23 IIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGG 55
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
7-39 |
5.09e-05 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 45.51 E-value: 5.09e-05
10 20 30
....*....|....*....|....*....|...
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSG 39
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
7-39 |
5.13e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.56 E-value: 5.13e-05
10 20 30
....*....|....*....|....*....|...
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSG 39
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| COQ6 |
TIGR01989 |
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ... |
263-341 |
5.87e-05 |
|
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone
Pssm-ID: 273914 [Multi-domain] Cd Length: 437 Bit Score: 45.52 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 263 AEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDG---LLDTYHAERHPLGEQLLRNVHAQSL 339
Cdd:TIGR01989 327 ADEYVTKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADIGsisSLKPYERERYAKNVVLLGLVDKLHK 406
|
..
gi 1011218312 340 LY 341
Cdd:TIGR01989 407 LY 408
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
6-156 |
8.15e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 44.66 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAP------SGESRgLGFTSRTAevldqrglLDELGEFRwGQHGHFggVR- 78
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVgrkiliSGGGR-CNFTNSEP--------LPEFLNYY-GGNPHF--LKs 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 79 ----------IDF------TLLEESH---FGVMGLAQsrteQLLGDWTARL---GVPVLRGREVTGFEETEDGVVVRydG 136
Cdd:COG2081 69 alsrftpedlIAFfeglgiETKEESSgrvFPDSSKAS----DILRALLAELreaGVEIRLRTRVTGIEKEDGGFGVE--T 142
|
170 180
....*....|....*....|
gi 1011218312 137 PDGPgEDHAQYLIGCDGGRS 156
Cdd:COG2081 143 PDGE-TVRADAVVLATGGLS 161
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
6-299 |
9.08e-05 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 44.62 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGF--TSRTAEVLDQRG----LLDELGEFRWGQ---HGHFGG 76
Cdd:PRK07364 22 AIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAAKGQAYalSLLSARIFEGIGvwekILPQIGKFRQIRlsdADYPGV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 77 VRIDFTLLEESHFGVMGLAQSRTEQLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGPDGPGEDHAQYLIGCDGGRS 156
Cdd:PRK07364 102 VKFQPTDLGTEALGYVGEHQVLLEALQEFLQSCPNITWLCPAEVVSVEYQQDAATVTLEIEGKQQTLQSKLVVAADGARS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 157 TVRRLAGIAFPGDEATRGMYLADVTGADIRPRPIGERVEGGGMVLSVGLGDGYDRIVihepGVRPHHGEGTLTFTEVADA 236
Cdd:PRK07364 182 PIRQAAGIKTKGWKYWQSCVTATVKHEAPHNDIAYERFWPSGPFAILPLPGNRCQIV----WTAPHAQAKALLALPEAEF 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 237 WQRMTGesiHHGRTRWMTALTNATGL-------AEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNL 299
Cdd:PRK07364 258 LAELQQ---RYGDQLGKLELLGDRFLfpvqlmqSDRYVQHRLALVGDAAHCCHPVGGQGLNLGIRDAAAL 324
|
|
| PRK07333 |
PRK07333 |
ubiquinone biosynthesis hydroxylase; |
4-299 |
9.40e-05 |
|
ubiquinone biosynthesis hydroxylase;
Pssm-ID: 180935 [Multi-domain] Cd Length: 403 Bit Score: 44.59 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 4 GAIVVGAGPVGLMLAGELRLGG--VDVVVYDKLPA--PSGESRGLGFTSRTAEVLDQRGLLDELGEfrwgqhghfggvri 79
Cdd:PRK07333 3 DVVIAGGGYVGLALAVALKQAAphLPVTVVDAAPAgaWSRDPRASAIAAAARRMLEALGVWDEIAP-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 80 dftllEESHFGVMGLAQSRTE------------------------------QLLGDWTARLGVPVLRGREVTGFEETEDG 129
Cdd:PRK07333 69 -----EAQPITDMVITDSRTSdpvrpvfltfegevepgepfahmvenrvliNALRKRAEALGIDLREATSVTDFETRDEG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 130 VVVRYDgpDGPGEDhAQYLIGCDGGRSTVRRLAGIAFPGdeatrgmyladvtgadirpRPIGErvegGGMVLSVGlgdgy 209
Cdd:PRK07333 144 VTVTLS--DGSVLE-ARLLVAADGARSKLRELAGIKTVG-------------------WDYGQ----SGIVCTVE----- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 210 driviHEpgvRPHHGEG--------------------TLTFTE-VADAwQRMTGES-------------IHHGRTRWMT- 254
Cdd:PRK07333 193 -----HE---RPHGGRAeehflpagpfailplkgnrsSLVWTErTADA-ERLVALDdlvfeaeleqrfgHRLGELKVLGk 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1011218312 255 --ALTNATGLAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNL 299
Cdd:PRK07333 264 rrAFPLGLTLARSFVAPRFALVGDAAHGIHPIAGQGLNLGLKDVAAL 310
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
6-293 |
9.97e-05 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 44.23 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESRGLGFTSRTAEVLDQRGLLdELGEFRWGQ-HGHFGGVRIDFTLL 84
Cdd:TIGR02032 4 VVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGALSPRALEELDLPGEL-IVNLVRGARfFSPNGDSVEIPIET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 85 EESHfgvmglAQSRTE--QLLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDGpdGPGEDHAQYLIGCDGGRSTVRR-- 160
Cdd:TIGR02032 83 ELAY------VIDRDAfdEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIVRG--SEGTVTAKIVIGADGSRSIVAKkl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 161 ----------LAGIAFpgDEATRGMYLADVT----GADIRPRPIGERVEGGGMVLSVGLGdgyDRIVIHEPGVRPHHGEG 226
Cdd:TIGR02032 155 glkkepreygVAARAE--VEMPDEEVDEDFVevyiDRGIVPGGYGWVFPKGDGTANVGVG---SRSAEEGEDPKKYLKDF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011218312 227 TLTFTEVADAwqrMTGESIHHGRTRWMTALTNATglaeqyrsGRVLLAGDAAHDHAPLGAQGVSVGL 293
Cdd:TIGR02032 230 LARRPELKDA---ETVEVCGALIPIGRPDEKLVR--------GNVLLVGDAAGHVNPLTGEGIYYAM 285
|
|
| PRK07236 |
PRK07236 |
hypothetical protein; Provisional |
5-160 |
2.32e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235980 [Multi-domain] Cd Length: 386 Bit Score: 43.37 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSgESRGLGftsrtaeVLDQRGLLDELgEFRWGQHGHFGGVRIDFTLL 84
Cdd:PRK07236 9 AVVIGGSLGGLFAALLLRRAGWDVDVFERSPTEL-DGRGAG-------IVLQPELLRAL-AEAGVALPADIGVPSRERIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 85 EESHFGVmgLAQSRTEQLLGDWT-------ARLGVPVLR-GREVTGFEETEDGVVVRY-DGpdgpGEDHAQYLIGCDGGR 155
Cdd:PRK07236 80 LDRDGRV--VQRRPMPQTQTSWNvlyralrAAFPAERYHlGETLVGFEQDGDRVTARFaDG----RRETADLLVGADGGR 153
|
....*
gi 1011218312 156 STVRR 160
Cdd:PRK07236 154 STVRA 158
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
1-306 |
2.94e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 43.02 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVVGAGPVGLMLAGELRLGGVDVVVYD----KLPAPSG-ESRGLGFTSRTAEVLDQRGLLDELGEFRWGQ----- 70
Cdd:PRK07608 4 MKFDVVVVGGGLVGASLALALAQSGLRVALLAprapPRPADDAwDSRVYAISPSSQAFLERLGVWQALDAARLAPvydmr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 71 -HGHFGGvRIDFTLLEEshfGVMGLA---QSRTEQLLGDWTARLG--VPVLRGReVTGFEETEDGVVVRYDgpDGpGEDH 144
Cdd:PRK07608 84 vFGDAHA-RLHFSAYQA---GVPQLAwivESSLIERALWAALRFQpnLTWFPAR-AQGLEVDPDAATLTLA--DG-QVLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 145 AQYLIGCDGGRSTVRRLAGIafpgdeatrgmyladvtGADIRP-RPIGervegggmvlsvglgdgydrIVIHEPGVRPHH 223
Cdd:PRK07608 156 ADLVVGADGAHSWVRSQAGI-----------------KAERRPyRQTG--------------------VVANFKAERPHR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 224 G--------EGTL---------------TFTEVADAWQRMTGESI-------HHGRTRWMTALTNATGL------AEQYR 267
Cdd:PRK07608 199 GtayqwfrdDGILallplpdghvsmvwsARTAHADELLALSPEALaarveraSGGRLGRLECVTPAAGFplrlqrVDRLV 278
|
330 340 350
....*....|....*....|....*....|....*....
gi 1011218312 268 SGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAAT 306
Cdd:PRK07608 279 APRVALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAGR 317
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
262-325 |
4.28e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 42.58 E-value: 4.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011218312 262 LAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDGLLDTYHAERHP 325
Cdd:PRK07494 273 VAHRFAAGRTALVGEAAHVFPPIGAQGLNLGLRDVATLVEIVEDRPEDPGSAAVLAAYDRARRP 336
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
7-122 |
4.73e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 42.46 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 7 VVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESR-GL-GFTSrTAEVLDQR-GLLDELG-EFRWGQHghfGGVRIDFT 82
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERADRIGGLLRyGIpDFKL-EKEVIDRRiELMEAEGiEFRTNVE---VGKDITAE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1011218312 83 LLEESHFGV---MGLAQSRteqllgdwtaRLGVPvlrGREVTG 122
Cdd:PRK12810 224 ELLAEYDAVflgTGAYKPR----------DLGIP---GRDLDG 253
|
|
| PRK07045 |
PRK07045 |
putative monooxygenase; Reviewed |
264-341 |
8.49e-04 |
|
putative monooxygenase; Reviewed
Pssm-ID: 136171 [Multi-domain] Cd Length: 388 Bit Score: 41.43 E-value: 8.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011218312 264 EQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGW-APDGLLDTYHAERHPLGEQLLRNVHAQSLLY 341
Cdd:PRK07045 280 DRYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQiALADALERFERIRRPVNEAVISYGHALATTY 358
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
6-165 |
1.49e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 40.90 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGEL-RLGGVDVVVYDKLPAPSGESrglgfTSRTAEVL---------------------------DQR 57
Cdd:COG0579 8 VIIGAGIVGLALARELsRYEDLKVLVLEKEDDVAQES-----SGNNSGVIhaglyytpgslkarlcvegnelfyelcREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 58 GL-------------------LDELgeFRWGQHGHFGGVR-IDFTLLEE-----SHFGVMGLaQSR----------TEQL 102
Cdd:COG0579 83 GIpfkrcgklvvatgeeevafLEKL--YERGKANGVPGLEiLDREELRElepllSDEGVAAL-YSPstgivdpgalTRAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011218312 103 LGDWTARlGVPVLRGREVTGFEETEDGVVVRYDGpdgpGEDHAQYLIGCDGGRS-TVRRLAGIA 165
Cdd:COG0579 160 AENAEAN-GVELLLNTEVTGIEREGDGWEVTTNG----GTIRARFVINAAGLYAdRLAQMAGIG 218
|
|
| PRK08849 |
PRK08849 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
263-325 |
1.49e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 181564 [Multi-domain] Cd Length: 384 Bit Score: 40.91 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011218312 263 AEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLgwkLAAT-INGWAPDGLLDTYHAERHP 325
Cdd:PRK08849 273 AQQYVKNNCVLLGDAAHTINPLAGQGVNLGFKDVDVL---LAETeKQGVLNDASFARYERRRRP 333
|
|
| PRK08850 |
PRK08850 |
2-octaprenyl-6-methoxyphenol hydroxylase; Validated |
270-306 |
2.03e-03 |
|
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
Pssm-ID: 236341 [Multi-domain] Cd Length: 405 Bit Score: 40.52 E-value: 2.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1011218312 270 RVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAAT 306
Cdd:PRK08850 283 RVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILAL 319
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-156 |
2.49e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.26 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAP------SGESRgLGFTSRTAEvldqrglLDELGEfRWGQHGHFggVR 78
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLgrkiliSGGGR-CNVTNLSEE-------PDNFLS-RYPGNPKF--LK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 79 -----------IDF------TLLEESHfGVMGLAQSRTEQLLGDWTARL---GVPVLRGREVTGFEETEDGV-VVRYDGp 137
Cdd:pfam03486 72 salsrftpwdfIAFfeslgvPLKEEDH-GRLFPDSDKASDIVDALLNELkelGVKIRLRTRVLSVEKDDDGRfRVKTGG- 149
|
170
....*....|....*....
gi 1011218312 138 dgpGEDHAQYLIGCDGGRS 156
Cdd:pfam03486 150 ---EELEADSLVLATGGLS 165
|
|
| PRK05868 |
PRK05868 |
FAD-binding protein; |
262-329 |
2.96e-03 |
|
FAD-binding protein;
Pssm-ID: 180297 [Multi-domain] Cd Length: 372 Bit Score: 39.97 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011218312 262 LAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDAVNLGWKLAATINGWAPDglLDTYHAERHPLGEQ 329
Cdd:PRK05868 275 LMDRWSRGRVALVGDAGYCCSPLSGQGTSVALLGAYILAGELKAAGDDYQLG--FANYHAEFHGFVER 340
|
|
| PRK05714 |
PRK05714 |
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional |
1-325 |
2.99e-03 |
|
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
Pssm-ID: 168201 [Multi-domain] Cd Length: 405 Bit Score: 39.81 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 1 MAKGAIVVGAGPVGLMLAGELRLGGVDVVVYDKLP---------APSgESRGLGFTSRTAEVLDQRGLLDELGEFRWGQH 71
Cdd:PRK05714 1 MRADLLIVGAGMVGSALALALQGSGLEVLLLDGGPlsvkpfdpqAPF-EPRVSALSAASQRILERLGAWDGIAARRASPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 72 GHF------GGVRIDFTLlEESHFGVMG-LAQSRTEQ-LLGDWTARLGVPVLRGREVTGFEETEDGVVVRYDgpDGPgED 143
Cdd:PRK05714 80 SEMqvwdgsGTGQIHFSA-ASVHAEVLGhIVENRVVQdALLERLHDSDIGLLANARLEQMRRSGDDWLLTLA--DGR-QL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 144 HAQYLIGCDGGRSTVRRLAGIAFPGDEATRGMYLADVTGADIRPRPIGERVEGGGMVLSVGL-GDGYDRIVIHEPGVRPH 222
Cdd:PRK05714 156 RAPLVVAADGANSAVRRLAGCATREWDYLHHAIVTSVRCSEPHRATAWQRFTDDGPLAFLPLeRDGDEHWCSIVWSTTPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 223 HGEGTLTFTEVA------DAWQRMTGESIHHGRtRWMTALTNATglAEQYRSGRVLLAGDAAHDHAPLGAQGVSVGLQDA 296
Cdd:PRK05714 236 EAERLMALDDDAfcaaleRAFEGRLGEVLSADP-RLCVPLRQRH--AKRYVEPGLALIGDAAHTIHPLAGQGVNLGFLDA 312
|
330 340 350
....*....|....*....|....*....|..
gi 1011218312 297 VNLGWKL-AATING--WAPDGLLDTYHAERHP 325
Cdd:PRK05714 313 AVLAEVLlHAAERGerLADVRVLSRFERRRMP 344
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
6-165 |
3.13e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.92 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 6 IVVGAGPVGLMLAGELRLGGVDVVVYDKLPA-----PSGESRGLGFTSRTAEVLDQRGLLDELGEfrwgqhghfggvrID 80
Cdd:PRK09126 7 VVVGAGPAGLSFARSLAGSGLKVTLIERQPLaaladPAFDGREIALTHASREILQRLGAWDRIPE-------------DE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011218312 81 FTLLEESH-------FGVMGLAQSRTEQLLGD-----------WTA---RLGVPVLRGREVTGFEETEDGVVVRYDgpdg 139
Cdd:PRK09126 74 ISPLRDAKvlngrspFALTFDARGRGADALGYlvpnhlirraaYEAvsqQDGIELLTGTRVTAVRTDDDGAQVTLA---- 149
|
170 180
....*....|....*....|....*..
gi 1011218312 140 PGED-HAQYLIGCDGGRSTVRRLAGIA 165
Cdd:PRK09126 150 NGRRlTARLLVAADSRFSATRRQLGIG 176
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1-55 |
3.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 39.87 E-value: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011218312 1 MAKGAIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESR------------GLGFTSRTAEVLD 55
Cdd:PRK07208 3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRtvtykgnrfdigGHRFFSKSPEVMD 69
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
5-42 |
6.28e-03 |
|
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176192 [Multi-domain] Cd Length: 355 Bit Score: 38.74 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1011218312 5 AIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESR 42
Cdd:cd08230 176 ALVLGAGPIGLLAALLLRLRGFEVYVLNRRDPPDPKAD 213
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
3-42 |
8.29e-03 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 38.56 E-value: 8.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1011218312 3 KGAIVVGAGPVGLMLAGELRLGGVDVVVYDKLPAPSGESR 42
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMR 233
|
|
| |
