|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
41-489 |
0e+00 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 906.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 41 FSGVTVPQRQFAVSGARSVSRAVQSVFAVKDGAALEGRKLRVAVIGGGPSGACAAETLAKGGVETFLLERKLDNCKPCGG 120
Cdd:PLN00093 1 LSHVSSFLPSAPSSAAKSVSRPGLRVLAAAASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKLDNAKPCGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 121 AIPLCMVEEFDLPMEIIDRRVTKMKMISPSNREVDVGKTLSETEWIGMCRREVFDDYLRNRAQKLGANIVNGLFMRSEQQ 200
Cdd:PLN00093 81 AIPLCMVGEFDLPLDIIDRKVTKMKMISPSNVAVDIGKTLKPHEYIGMVRREVLDSFLRERAQSNGATLINGLFTRIDVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 201 S-AEGPFTIHYNSYEDGSKMGKPATLEVDMIIGADGANSRIAKEIDAGEYDYAIAFQERIRIPDDKMKYYENLAEMYVGD 279
Cdd:PLN00093 161 KdPNGPYVIHYTSYDSGSGAGTPKTLEVDAVIGADGANSRVAKDIDAGDYDYAIAFQERIKIPDDKMEYYEDLAEMYVGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 280 DVSPDFYGWVFPKYDHVAVGTGTVVNKTAIKQYQQATRDRSKVKTEGGKIIRVEAHPIPEHPRPRRCKGRVALVGDAAGY 359
Cdd:PLN00093 241 DVSPDFYGWVFPKCDHVAVGTGTVVNKPAIKKYQRATRNRAKDKIAGGKIIRVEAHPIPEHPRPRRVRGRVALVGDAAGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 360 VTKCSGEGIYFAAKSGRMAAEAIVEGSANGTKMCGEDAIRVYLDKWDRKYWTTYKVLDILQKVFYRSNPAREAFVELCED 439
Cdd:PLN00093 321 VTKCSGEGIYFAAKSGRMCAEAIVEGSENGTRMVDEADLREYLRKWDKKYWPTYKVLDILQKVFYRSNPAREAFVEMCAD 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 295415666 440 SYVQKMTFDSYLYKTVVPGNPLDDVKLLVRTVSSILRSNALRSVNSKSVN 489
Cdd:PLN00093 401 EYVQKMTFDSYLYKRVVPGNPLDDIKLLVNTIGSLVRANALRREMEKLSV 450
|
|
| ChlP |
TIGR02028 |
geranylgeranyl reductase; This model represents the reductase which acts reduces the ... |
80-476 |
0e+00 |
|
geranylgeranyl reductase; This model represents the reductase which acts reduces the geranylgeranyl group to the phytyl group in the side chain of chlorophyll. It is unclear whether the enzyme has a preference for acting before or after the attachment of the side chain to chlorophyllide a by chlorophyll synthase. This clade is restricted to plants and cyanobacteria to separate it from the homologues which act in the biosynthesis of bacteriochlorophyll. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 131083 Cd Length: 398 Bit Score: 675.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 80 LRVAVIGGGPSGACAAETLAKGGVETFLLERKLDNCKPCGGAIPLCMVEEFDLPMEIIDRRVTKMKMISPSNREVDVGKT 159
Cdd:TIGR02028 1 LRVAVVGGGPAGASAAETLASAGIQTFLLERKPDNAKPCGGAIPLCMVDEFALPRDIIDRRVTKMKMISPSNIAVDIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 160 LSETEWIGMCRREVFDDYLRNRAQKLGANIVNGLFMRSEQ-QSAEGPFTIHYNSYEDGSKMGKPATLEVDMIIGADGANS 238
Cdd:TIGR02028 81 LKEHEYIGMLRREVLDSFLRRRAADAGATLINGLVTKLSLpADADDPYTLHYISSDSGGPSGTRCTLEVDAVIGADGANS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 239 RIAKEIDAGEYDYAIAFQERIRIPDDKMKYYENLAEMYVGDDVSPDFYGWVFPKYDHVAVGTGTVVNKTAIKQYQQATRD 318
Cdd:TIGR02028 161 RVAKEIDAGDYSYAIAFQERIRLPDEKMAYYDDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVAAKPEIKRLQSGIRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 319 RSKVKTEGGKIIRVEAHPIPEHPRPRRCKGRVALVGDAAGYVTKCSGEGIYFAAKSGRMAAEAIVEGSANGTKMCGEDAI 398
Cdd:TIGR02028 241 RAAGKVAGGRIIRVEAHPIPEHPRPRRVVGRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEESRLGGAVTEEGDL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295415666 399 RVYLDKWDRKYWTTYKVLDILQKVFYRSNPAREAFVELCEDSYVQKMTFDSYLYKTVVPGNPLDDVKLLVRTVSSILR 476
Cdd:TIGR02028 321 AGYLRRWDKEYRPTYRVLDLLQRVFYRSNAGREAFVEMCADEHVQKRTFDSYLYKRVAPAEPLGDLKLLWRTIGSLVR 398
|
|
| BchP-ChlP |
TIGR02023 |
geranylgeranyl reductase; This model represents a group of geranylgeranyl reductases specific ... |
80-476 |
0e+00 |
|
geranylgeranyl reductase; This model represents a group of geranylgeranyl reductases specific for the biosyntheses of bacteriochlorophyll and chlorophyll. It is unclear whether the processes of isoprenoid ligation to the chlorin ring and reduction of the geranylgeranyl chain to a phytyl chain are necessarily ordered the same way in all species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273932 Cd Length: 388 Bit Score: 536.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 80 LRVAVIGGGPSGACAAETLAKGGVETFLLERKLDNCKPCGGAIPLCMVEEFDLPMEIIDRRVTKMKMISPSNreVDVGKT 159
Cdd:TIGR02023 1 YDVAVIGGGPSGATAAETLARAGIETILLERALSNIKPCGGAIPPCLIEEFDIPDSLIDRRVTQMRMISPSR--VPIKVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 160 L-SETEWIGMCRREVFDDYLRNRAQKLGANIVNGLFMRSEQQsaEGPFTIHYNSYEDGSKMGKPaTLEVDMIIGADGANS 238
Cdd:TIGR02023 79 IpSEDGYVGMVRREVFDSYLRERAQKAGAELIHGLFLKLERD--RDGVTLTYRTPKKGAGGEKG-SVEADVVIGADGANS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 239 RIAKEIDAGE-YDYAIAFQERIRIPDDKMKYYENLAEMYVGDDVSPDFYGWVFPKYDHVAVGTGTVVNKTAIKQYQQATR 317
Cdd:TIGR02023 156 PVAKELGLPKnLPRVIAYQERIKLPDDKMAYYEELADVYYGGEVSPDFYGWVFPKGDHIAVGTGTGTHGFDAKQLQANLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 318 DRSKVktEGGKIIRVEAHPIPEHPRPRRCKGRVALVGDAAGYVTKCSGEGIYFAAKSGRMAAEAIVEGSANGTkmcgEDA 397
Cdd:TIGR02023 236 RRAGL--DGGQTIRREAAPIPMKPRPRWDFGRAMLVGDAAGLVTPASGEGIYFAMKSGQMAAQAIAEYLQNGD----ATD 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295415666 398 IRVYLDKWDRKYWTTYKVLDILQKVFYRSNPAREAFVELCEDSYVQKMTFDSYLYKTVVPGNPLDDVKLLVRTVSSILR 476
Cdd:TIGR02023 310 LRHYERKFMKLYGTTFRVLRVLQMVYYRSDRRREVFVEMCRDKDVQRLTFDSYMYKQMAPAPWLAQLKIAAKNIGSLVR 388
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
82-382 |
1.41e-55 |
|
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: 187.91 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 82 VAVIGGGPSGACAAETLAKGGVETFLLERK-LDNCKPCGGAIPLCMVEEFDLPMEIIDRRVTKMKMISPSNREVdvgKTL 160
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKsFPRYKPCGGALSPRALEELDLPGELIVNLVRGARFFSPNGDSV---EIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 161 SETEWIGMCRREVFDDYLRNRAQKLGANIVNGLFMRSEQQSAEGPFTIHynsyeDGSKmgkpATLEVDMIIGADGANSRI 240
Cdd:TIGR02032 80 IETELAYVIDRDAFDEQLAERAQEAGAELRLGTRVLDVEIHDDRVVVIV-----RGSE----GTVTAKIVIGADGSRSIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 241 AKEIDAGEYDYAIAFQERIRIPDDKMKYYENLAEMYVGDDVSPDFYGWVFPKYD---HVAVGTGTVVNKTAIKQYQQATR 317
Cdd:TIGR02032 151 AKKLGLKKEPREYGVAARAEVEMPDEEVDEDFVEVYIDRGIVPGGYGWVFPKGDgtaNVGVGSRSAEEGEDPKKYLKDFL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295415666 318 DRSKvKTEGGKIIRVEAHPIP-EHPRPRRCKGRVALVGDAAGYVTKCSGEGIYFAAKSGRMAAEAI 382
Cdd:TIGR02032 231 ARRP-ELKDAETVEVCGALIPiGRPDEKLVRGNVLLVGDAAGHVNPLTGEGIYYAMRSGDIAAEVV 295
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
87-407 |
3.10e-51 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 175.93 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 87 GGPSGACAAETLAKGGVETFLLERK-LDNCKPCGGAIPLCMVEEFDLP--MEIIDRRVTKMKMISPSNREVDVGktlSET 163
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGsFPGDKICGGGLLPRALEELEPLglDEPLERPVRGARFYSPGGKSVELP---PGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 164 EWIGMCRREVFDDYLRNRAQKLGANIVNGlfmrseqQSAEGPftihynSYEDGS---KMGKPATLEVDMIIGADGANSRI 240
Cdd:COG0644 78 GGGYVVDRARFDRWLAEQAEEAGAEVRTG-------TRVTDV------LRDDGRvvvRTGDGEEIRADYVVDADGARSLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 241 AKEIDAGE-----YDYAIAFQERIRIPDDKMkYYENLAEMYVGDDVsPDFYGWVFPK-YDHVAVGtgtvvnktaikqyqq 314
Cdd:COG0644 145 ARKLGLKRrsdepQDYALAIKEHWELPPLEG-VDPGAVEFFFGEGA-PGGYGWVFPLgDGRVSVG--------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 315 atrdrskvkteggkiirveahpIPE-HPRPRRCKGRVALVGDAAGYVTKCSGEGIYFAAKSGRMAAEAIVEGSANGTkmC 393
Cdd:COG0644 208 ----------------------IPLgGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALEGGD--F 263
|
330
....*....|....
gi 295415666 394 GEDAIRVYLDKWDR 407
Cdd:COG0644 264 SAEALAEYERRLRE 277
|
|
| PRK11445 |
PRK11445 |
FAD-binding protein; |
82-388 |
1.88e-12 |
|
FAD-binding protein;
Pssm-ID: 183139 [Multi-domain] Cd Length: 351 Bit Score: 68.55 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 82 VAVIGGGPSGACAAETLAKGgVETFLLERKlDNC------KPCGGAIP---LCMVEEFDL--PMEII-DRRVTKMKMIsp 149
Cdd:PRK11445 4 VAIIGLGPAGSALARLLAGK-MKVIAIDKK-HQCgtegfsKPCGGLLApdaQKSFAKDGLtlPKDVIaNPQIFAVKTI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 150 snrevDVGKTLS---ETEWIGMcRREVFDDYLRNRAQKLGANIVNGLFMRSEQQsaEGPFTIHYnsYEDGSKMgkpaTLE 226
Cdd:PRK11445 80 -----DLANSLTrnyQRSYINI-DRHKFDLWLKSLIPASVEVYHNSLCRKIWRE--DDGYHVIF--RADGWEQ----HIT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 227 VDMIIGADGANSRIakeidageydyaiafqERIRIPDDKMKYYENLAEMYVGDDVSP-----------DFYGWVFPKYDH 295
Cdd:PRK11445 146 ARYLVGADGANSMV----------------RRHLYPDHQIRKYVAIQQWFAEKHPVPfyscifdneitDCYSWSISKDGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 296 VAVGTGTVVNKTAIKQYQQatrdRSKVKTEG---GKIIRVEAHPIPehpRPRR-----C-KGRVALVGDAAGYVTKCSGE 366
Cdd:PRK11445 210 FIFGGAYPMKDGRERFETL----KEKLSAFGfqfGKPVKTEACTVL---RPSRwqdfvCgKDNAFLIGEAAGFISPSSLE 282
|
330 340
....*....|....*....|..
gi 295415666 367 GIYFAAKSGRMAAEAIVEGSAN 388
Cdd:PRK11445 283 GISYALDSARILSEVLNKQPEK 304
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
78-357 |
9.14e-10 |
|
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: 59.95 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 78 RKLRVAVIGGGPSGACAAETLAKGGVETFLLERKLDNCK-PCGGAIP---LCMVEEFDLpMEIIDRR---VTKMKMISPS 150
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPdGRGIALSprsLELLRRLGL-WDRLLARgapIRGIRVRDGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 151 N----REVDVGKTLSETEWigMCRREVFDDYLRNRAQKLGANIVNGLFMRSEQQSAEGPfTIHYnsyEDGSkmgkpaTLE 226
Cdd:COG0654 81 DgrvlARFDAAETGLPAGL--VVPRADLERALLEAARALGVELRFGTEVTGLEQDADGV-TVTL---ADGR------TLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 227 VDMIIGADGANSRIAKEIDAGeydyaiafqeriripddkmkyyenlaemyvgddvspdFYGWVFPkyDHVAVGTgtvVNK 306
Cdd:COG0654 149 ADLVVGADGARSAVRRLLGIG-------------------------------------FTGRDYP--QRALWAG---VRT 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 295415666 307 TAIKQYQQATRDRSKVKTeggkIIRVEAHPIPEHPRPRRCKGRVALVGDAA 357
Cdd:COG0654 187 ELRARLAAAGPRLGELLE----LSPRSAFPLRRRRAERWRRGRVVLLGDAA 233
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
79-387 |
3.29e-09 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 58.83 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 79 KLRVAVIGGGPSGACAAETLAKGGVETFLLER-KLDNCKPCGGAIPLCMVEEFDLP----MEIIDRRVTKMKM------- 146
Cdd:PRK10015 5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERgDSAGCKNMTGGRLYAHTLEAIIPgfaaSAPVERKVTREKIsfltees 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 147 ---ISPSNREVDVGKTLSETewigmCRREVFDDYLRNRAQKLGANIVNGLfmRSEQQSAEGPFTIHYNSYEDgskmgkpa 223
Cdd:PRK10015 85 avtLDFHREQPDVPQHASYT-----VLRNRLDPWLMEQAEQAGAQFIPGV--RVDALVREGNKVTGVQAGDD-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 224 TLEVDMIIGADGANSRIAKEID----AGEYDYAIAFQERIRIPDDKMKYYENLAE------MYVGddvSPD----FYGWV 289
Cdd:PRK10015 150 ILEANVVILADGVNSMLGRSLGmvpaSDPHHYAVGVKEVIGLTPEQINDRFNITGeegaawLFAG---SPSdglmGGGFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 290 FPKYDHVAVG--TGTVVNKTAIKQYQQATRDRSKVKT-----EGGKIIRVEAHPIPE---HPRPRRCKGRVALVGDAAGY 359
Cdd:PRK10015 227 YTNKDSISLGlvCGLGDIAHAQKSVPQMLEDFKQHPAirpliSGGKLLEYSAHMVPEgglAMVPQLVNDGVMIVGDAAGF 306
|
330 340 350
....*....|....*....|....*....|
gi 295415666 360 VTKC--SGEGIYFAAKSGRMAAEAIVEGSA 387
Cdd:PRK10015 307 CLNLgfTVRGMDLAIASAQAAATTVIAAKE 336
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
69-161 |
2.12e-06 |
|
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: 50.13 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 69 VKDGAALEGRKLRVAVIGGGPSG-ACAAEtLAKGGVETFLLERkLDncKPcGG----AIPlcmveEFDLPMEIIDRRVTK 143
Cdd:COG0493 111 VKPPPPAPRTGKKVAVVGSGPAGlAAAYQ-LARAGHEVTVFEA-LD--KP-GGllryGIP-----EFRLPKDVLDREIEL 180
|
90 100
....*....|....*....|....*
gi 295415666 144 MKmispsnRE-------VDVGKTLS 161
Cdd:COG0493 181 IE------ALgvefrtnVEVGKDIT 199
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
81-145 |
3.06e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 49.78 E-value: 3.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLERkldNCKPcGG----AIPlcmveEFDLPMEIIDRRVTKMK 145
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFER---ADRI-GGllryGIP-----DFKLEKEVIDRRIELME 204
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
78-161 |
8.77e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.25 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 78 RKLRVAVIGGGPSGACAAETLAKGGVETFLLERkLDncKPcGG----AIPlcmveEFDLPMEIIDRRVTKMKM----ISP 149
Cdd:PRK11749 139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEA-RD--KA-GGllryGIP-----EFRLPKDIVDREVERLLKlgveIRT 209
|
90
....*....|..
gi 295415666 150 SnreVDVGKTLS 161
Cdd:PRK11749 210 N---TEVGRDIT 218
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
82-244 |
1.29e-04 |
|
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: 44.24 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 82 VAVIGGGPSGACAAETLAKGGVETFLLERKldnckpcGGAIPL---CMVEefDLPMEIIDRRVTKMKMISPSNREVDVGK 158
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVERH-------ATTSVLpraHGLN--QRTMELLRQAGLEDRILAEGVPHEGMGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 159 TLSETEwigmcRREVFDD-----------------YLRNRAQKLGANIVNGLFMRSEQQSAEGPFTIHYnsyedGSKMGK 221
Cdd:pfam01494 75 AFYNTR-----RRADLDFltspprvtvypqtelepILVEHAEARGAQVRFGTEVLSLEQDGDGVTAVVR-----DRRDGE 144
|
170 180
....*....|....*....|...
gi 295415666 222 PATLEVDMIIGADGANSRIAKEI 244
Cdd:pfam01494 145 EYTVRAKYLVGCDGGRSPVRKTL 167
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
81-244 |
2.88e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 42.94 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLERKLDNCkPCGGAIplcmveefdlpmeiidrrvtkmkmISPSN-----REVD 155
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWR-VYGAGI------------------------TLQGNalralRELG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 156 VGKTLSE----TEWIGMCR--------------------------REVFDDYLRNRAQKLGANIVNGLFMRSEQQSAEGp 205
Cdd:PRK06847 61 VLDECLEagfgFDGVDLFDpdgtllaelptprlagddlpggggimRPALARILADAARAAGADVRLGTTVTAIEQDDDG- 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 295415666 206 FTIhynSYEDGSKMgkpatlEVDMIIGADGANSRIAKEI 244
Cdd:PRK06847 140 VTV---TFSDGTTG------RYDLVVGADGLYSKVRSLV 169
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
81-161 |
4.86e-04 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 43.01 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLERkldnCKPCGGAIPLCmVEEFDLPMEIIDRRVTKMKMIS---PSNREvdVG 157
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEA----LHVVGGVLQYG-IPSFRLPRDIIDREVQRLVDIGvkiETNKV--IG 504
|
....
gi 295415666 158 KTLS 161
Cdd:PRK12775 505 KTFT 508
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
75-175 |
5.23e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.81 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 75 LEGRKLRVAVIGGGPSGACAAETLAKGGVETFLLERkldnCKPCGG----AIPlcmveEFDLPMEIIDRRVTK-MKMISP 149
Cdd:PRK12778 427 AEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEA----LHEIGGvlkyGIP-----EFRLPKKIVDVEIENlKKLGVK 497
|
90 100
....*....|....*....|....*.
gi 295415666 150 SNREVDVGKTLSetewIGMCRREVFD 175
Cdd:PRK12778 498 FETDVIVGKTIT----IEELEEEGFK 519
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
81-111 |
5.54e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 42.18 E-value: 5.54e-04
10 20 30
....*....|....*....|....*....|.
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLERK 111
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKG 32
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
81-111 |
1.09e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.38 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|.
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLERK 111
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKE 172
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
79-110 |
1.14e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 41.36 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|..
gi 295415666 79 KLRVAVIGGGPSGACAAETLAKGGVETFLLER 110
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEA 32
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
74-161 |
1.79e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.77 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295415666 74 ALEGRKLRVAVIGGGPSGACAAETLAKGGVETFLLErKLDncKPcGG----AIPlcmveEFDLPME-IIDRRVTKMKMIS 148
Cdd:PRK12831 135 TEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFE-ALH--EP-GGvlvyGIP-----EFRLPKEtVVKKEIENIKKLG 205
|
90
....*....|....
gi 295415666 149 PS-NREVDVGKTLS 161
Cdd:PRK12831 206 VKiETNVVVGKTVT 219
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
84-110 |
3.59e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.97 E-value: 3.59e-03
10 20
....*....|....*....|....*..
gi 295415666 84 VIGGGPSGACAAETLAKGGVETFLLER 110
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
71-139 |
3.73e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 39.85 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295415666 71 DGAALEGRKLRVAVIGGGPSGACAAETLAKGGVETFLLErklDNCKPCGGAIPLCMVEEfdlPMEIIDR 139
Cdd:PRK08132 15 DQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLD---DDDTLSTGSRAICFAKR---SLEIFDR 77
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
81-110 |
4.09e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.50 E-value: 4.09e-03
10 20 30
....*....|....*....|....*....|
gi 295415666 81 RVAVIGGGPSGACAAETLAKGGVETFLLER 110
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLER 33
|
|
| |
