|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
1-343 |
0e+00 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 754.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 1 MGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASI 80
Cdd:PLN02955 134 MGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 81 IDGVRLAERQGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:PLN02955 214 IDGVRLAERQGNVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRR 240
Cdd:PLN02955 294 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 241 KAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLIT 320
Cdd:PLN02955 374 KAIWERVKEFKALSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLIT 453
|
330 340
....*....|....*....|...
gi 30680578 321 ALSSCLDFDNTATHIPSFLFPKL 343
Cdd:PLN02955 454 ALSSCLDFDNTATYIPSFLFPKL 476
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
2-327 |
2.80e-132 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 382.09 E-value: 2.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmvaigsVASLLaasgkplkNEKVAIFSDALNHASII 81
Cdd:COG0156 70 GSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGV------ISALA--------GRGDLIFSDELNHASII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAerqgNVEVFVYRHCDMYHLNSLLSNCKM-KRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:COG0156 136 DGARLS----GAKVVRFRHNDMDDLERLLKKARAaRRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRR 240
Cdd:COG0156 212 GETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 241 KAIWERVKEFKEL---SGVDI---SSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTED 314
Cdd:COG0156 292 ERLWENIAYFREGlkeLGFDLgpsESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEED 371
|
330
....*....|...
gi 30680578 315 VKKLITALSSCLD 327
Cdd:COG0156 372 IDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
2-323 |
2.88e-110 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 324.90 E-value: 2.88e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAamvaigsvasLLAAsgkpLKNEKVAIFSDALNHASII 81
Cdd:cd06454 34 GAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG----------VLST----LAGKGDLIISDSLNHASII 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAerqgNVEVFVYRHCDMYHLNSLLSN--CKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFV 159
Cdd:cd06454 100 DGIRLS----GAKKRIFKHNDMEDLEKLLREarRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 160 CGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWR 239
Cdd:cd06454 176 YGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQGGPER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 240 RKAIWERVKEFKEL---SGVDI----SSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTT 312
Cdd:cd06454 256 RERLQENVRYLRRGlkeLGFPVggspSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTK 335
|
330
....*....|.
gi 30680578 313 EDVKKLITALS 323
Cdd:cd06454 336 EDIDRLLEALK 346
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
2-322 |
2.01e-102 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 305.35 E-value: 2.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAigsvasllaasgkpLKNEKVAIFSDALNHASII 81
Cdd:TIGR00858 49 GSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA--------------LVGKGDLILSDALNHASLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAErqgnVEVFVYRHCDMYHL-NSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:TIGR00858 115 DGCRLSG----ARVRRYRHNDVEHLeRLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFN-CEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWR 239
Cdd:TIGR00858 191 GEDGRGTLEHFGlKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAVAAAALAALELIQEEPWR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 240 RKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 313
Cdd:TIGR00858 271 REKLLALIARLRAglealgFTLMPSCTPIVPVIIGDNASALALAEELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPG 350
|
....*....
gi 30680578 314 DVKKLITAL 322
Cdd:TIGR00858 351 DIDRLAEAL 359
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
11-322 |
2.63e-39 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 142.06 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 11 GYTTYHRL--LESSLAQLK--------KKEDCLVCPTGFAANMAAMVAIgsvasllaasgkpLKNEKVAIFSDALNHASI 80
Cdd:pfam00155 34 LYGPTDGHpeLREALAKFLgrspvlklDREAAVVFGSGAGANIEALIFL-------------LANPGDAILVPAPTYASY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 81 IDGVRLAErqgnVEVFVYR-------HCDMYHLNSLLSNckmKRKVVVTDSLFSMDGDFAPMEELSQLR---KKYGFLLV 150
Cdd:pfam00155 101 IRIARLAG----GEVVRYPlydsndfHLDFDALEAALKE---KPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 151 IDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHG---GFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAY 227
Cdd:pfam00155 174 VDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 228 AAVVVARKEIWRRKAIWERVKEF-KELSGVDIS-----SPIISLVVGNQEKALKASRYLLK-SGFHVMAIRPPTVPPnsc 300
Cdd:pfam00155 254 DPLLVASELEEMRQRIKERRDYLrDGLQAAGLSvlpsqAGFFLLTGLDPETAKELAQVLLEeVGVYVTPGSSPGVPG--- 330
|
330 340
....*....|....*....|..
gi 30680578 301 RLRVTLsAAHTTEDVKKLITAL 322
Cdd:pfam00155 331 WLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
1-343 |
0e+00 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 754.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 1 MGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASI 80
Cdd:PLN02955 134 MGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAASGKPLKNEKVAIFSDALNHASI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 81 IDGVRLAERQGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:PLN02955 214 IDGVRLAERQGNVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRR 240
Cdd:PLN02955 294 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 241 KAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLIT 320
Cdd:PLN02955 374 KAIWERVKEFKALSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLIT 453
|
330 340
....*....|....*....|...
gi 30680578 321 ALSSCLDFDNTATHIPSFLFPKL 343
Cdd:PLN02955 454 ALSSCLDFDNTATYIPSFLFPKL 476
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
2-327 |
2.80e-132 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 382.09 E-value: 2.80e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmvaigsVASLLaasgkplkNEKVAIFSDALNHASII 81
Cdd:COG0156 70 GSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGV------ISALA--------GRGDLIFSDELNHASII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAerqgNVEVFVYRHCDMYHLNSLLSNCKM-KRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:COG0156 136 DGARLS----GAKVVRFRHNDMDDLERLLKKARAaRRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRR 240
Cdd:COG0156 212 GETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 241 KAIWERVKEFKEL---SGVDI---SSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTED 314
Cdd:COG0156 292 ERLWENIAYFREGlkeLGFDLgpsESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEED 371
|
330
....*....|...
gi 30680578 315 VKKLITALSSCLD 327
Cdd:COG0156 372 IDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
2-323 |
2.88e-110 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 324.90 E-value: 2.88e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAamvaigsvasLLAAsgkpLKNEKVAIFSDALNHASII 81
Cdd:cd06454 34 GAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDG----------VLST----LAGKGDLIISDSLNHASII 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAerqgNVEVFVYRHCDMYHLNSLLSN--CKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFV 159
Cdd:cd06454 100 DGIRLS----GAKKRIFKHNDMEDLEKLLREarRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 160 CGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWR 239
Cdd:cd06454 176 YGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQGGPER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 240 RKAIWERVKEFKEL---SGVDI----SSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTT 312
Cdd:cd06454 256 RERLQENVRYLRRGlkeLGFPVggspSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTK 335
|
330
....*....|.
gi 30680578 313 EDVKKLITALS 323
Cdd:cd06454 336 EDIDRLLEALK 346
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
5-326 |
3.13e-110 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 326.34 E-value: 3.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 5 GSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLlaasgkplknekvaIFSDALNHASIIDGV 84
Cdd:PRK05958 75 GSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDL--------------IVSDKLNHASLIDGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 85 RLaerqGNVEVFVYRHCDMYHLNSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENG 164
Cdd:PRK05958 141 RL----SRARVRRYPHNDVDALEALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 165 GGVAEEFNCEADVD-LCVGTLSKAAGCHGGFIACSKKWKQ-LIQsRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKA 242
Cdd:PRK05958 217 RGLAAEAGLAGEPDvILVGTLGKALGSSGAAVLGSETLIDyLIN-RARPFIFTTALPPAQAAAARAALRILRREPERRER 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 243 IWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVK 316
Cdd:PRK05958 296 LAALIARLRAglralgFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADID 375
|
330
....*....|
gi 30680578 317 KLITALSSCL 326
Cdd:PRK05958 376 RLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
2-322 |
2.01e-102 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 305.35 E-value: 2.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAigsvasllaasgkpLKNEKVAIFSDALNHASII 81
Cdd:TIGR00858 49 GSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA--------------LVGKGDLILSDALNHASLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAErqgnVEVFVYRHCDMYHL-NSLLSNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:TIGR00858 115 DGCRLSG----ARVRRYRHNDVEHLeRLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFN-CEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWR 239
Cdd:TIGR00858 191 GEDGRGTLEHFGlKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAVAAAALAALELIQEEPWR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 240 RKAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 313
Cdd:TIGR00858 271 REKLLALIARLRAglealgFTLMPSCTPIVPVIIGDNASALALAEELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPG 350
|
....*....
gi 30680578 314 DVKKLITAL 322
Cdd:TIGR00858 351 DIDRLAEAL 359
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
2-322 |
8.37e-70 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 223.07 E-value: 8.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmvaigsvaslLAASGKPLKNekVAIFSDALNHASII 81
Cdd:TIGR01821 78 GAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDAT----------LATLAKIIPG--CVIFSDELNHASMI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVrlaeRQGNVEVFVYRHCDMYHLNSLLSNCKMKR-KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:TIGR01821 146 EGI----RHSGAEKFIFRHNDVAHLEKLLQSVDPNRpKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRR 240
Cdd:TIGR01821 222 GPRGGGIAERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 241 KAIWERVKEFKE------LSGVDISSPIISLVVGNQEKALKASRYLL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 313
Cdd:TIGR01821 302 RAHQENVKRLKNllealgIPVIPNPSHIVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGTERLRITPTPAHTDK 381
|
....*....
gi 30680578 314 DVKKLITAL 322
Cdd:TIGR01821 382 MIDDLVEAL 390
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
9-321 |
3.41e-69 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 221.61 E-value: 3.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 9 ICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMvaigsvasllaasgKPLKNEKVAIFSDALNHASIIDGVRL-- 86
Cdd:PRK06939 82 ICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLF--------------ETLLGKEDAIISDALNHASIIDGVRLck 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 87 AERqgnvevFVYRHCDMYHLNSLL---SNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGEN 163
Cdd:PRK06939 148 AKR------YRYANNDMADLEAQLkeaKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 164 GGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKA 242
Cdd:PRK06939 222 GRGTVEHFGVMDRVDIITGTLGKAlGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 243 IWERVKEFKE-LS--GVDI---SSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVK 316
Cdd:PRK06939 302 LWENARYFREgMTaaGFTLgpgEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLD 381
|
....*
gi 30680578 317 KLITA 321
Cdd:PRK06939 382 RAIDA 386
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
9-321 |
1.43e-68 |
|
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.
Pssm-ID: 130884 [Multi-domain] Cd Length: 385 Bit Score: 219.69 E-value: 1.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 9 ICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSvasllaasgkplKNEkvAIFSDALNHASIIDGVRLAE 88
Cdd:TIGR01825 73 IAGTLRLHEELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLR------------KGD--IVLSDELNHASIIDGLRLTK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 89 rqgnVEVFVYRHCDMYHLNSLL-SNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGV 167
Cdd:TIGR01825 139 ----ATKKIYKHADMDDLDRVLrENPSYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 168 AEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERV 247
Cdd:TIGR01825 215 VHHFGLEDKVDIQVGTLSKAIGVVGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 248 KEFK-ELS--GVDIS---SPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITA 321
Cdd:TIGR01825 295 RFFKaGLGklGYDTGgseTPITPVVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDA 374
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
2-327 |
5.00e-60 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 198.15 E-value: 5.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAmvaIGSVASLLAAsgkplknekVAIFSDALNHASII 81
Cdd:PRK13392 79 GAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAA---LSTLGKLLPG---------CVILSDALNHASMI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRL--AERQgnvevfVYRHCDMYHLNSLLSNCKMKR-KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTF 158
Cdd:PRK13392 147 EGIRRsgAEKQ------VFRHNDLADLEEQLASVDPDRpKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 159 VCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIW 238
Cdd:PRK13392 221 LYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 239 RRKAIWERVKEFK-ELSGVDI-----SSPIISLVVGNQEKALKASRYLLKS-GFHVMAIRPPTVPPNSCRLRVTLSAAHT 311
Cdd:PRK13392 301 ERDAHQDRVAALKaKLNANGIpvmpsPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHD 380
|
330
....*....|....*.
gi 30680578 312 TEDVKKLITALSSCLD 327
Cdd:PRK13392 381 DEDIDALVAALVAIWD 396
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
11-322 |
2.63e-39 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 142.06 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 11 GYTTYHRL--LESSLAQLK--------KKEDCLVCPTGFAANMAAMVAIgsvasllaasgkpLKNEKVAIFSDALNHASI 80
Cdd:pfam00155 34 LYGPTDGHpeLREALAKFLgrspvlklDREAAVVFGSGAGANIEALIFL-------------LANPGDAILVPAPTYASY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 81 IDGVRLAErqgnVEVFVYR-------HCDMYHLNSLLSNckmKRKVVVTDSLFSMDGDFAPMEELSQLR---KKYGFLLV 150
Cdd:pfam00155 101 IRIARLAG----GEVVRYPlydsndfHLDFDALEAALKE---KPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 151 IDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHG---GFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAY 227
Cdd:pfam00155 174 VDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 228 AAVVVARKEIWRRKAIWERVKEF-KELSGVDIS-----SPIISLVVGNQEKALKASRYLLK-SGFHVMAIRPPTVPPnsc 300
Cdd:pfam00155 254 DPLLVASELEEMRQRIKERRDYLrDGLQAAGLSvlpsqAGFFLLTGLDPETAKELAQVLLEeVGVYVTPGSSPGVPG--- 330
|
330 340
....*....|....*....|..
gi 30680578 301 RLRVTLsAAHTTEDVKKLITAL 322
Cdd:pfam00155 331 WLRITV-AGGTEEELEELLEAI 351
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
19-327 |
1.72e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 127.79 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 19 LESSLAQLKKKEdCLVCPTGFAANMAAMVAIGSvaSLLAASGKPlknekVAIFsDALNHASIIDGVRLAERQGNVEVfvy 98
Cdd:PRK07505 96 LEEALSELFGAS-VLTFTSCSAAHLGILPLLAS--GHLTGGVPP-----HMVF-DKNAHASLNILKGICADETEVET--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 99 rhCDMYHLNSLLSNCKMKRKVV-VTDSLFSMdGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEfncEADV 177
Cdd:PRK07505 164 --IDHNDLDALEDICKTNKTVAyVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVRS---ELDY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 178 DL-----CVGTLSKAAGCHGGFIAC-SKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARK-EIWRR-KAIWERVKE 249
Cdd:PRK07505 238 RLnertiIAASLGKAFGASGGVIMLgDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSeELDQLqQKLQNNIAL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 250 FKEL-----SGVdiSSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSS 324
Cdd:PRK07505 318 FDSLipteqSGS--FLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKE 395
|
...
gi 30680578 325 CLD 327
Cdd:PRK07505 396 ILD 398
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
14-327 |
1.24e-32 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 125.51 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 14 TYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSvasllaasgkplknEKVAIFSDALNHASIIDGVRLAERQgnv 93
Cdd:PRK07179 99 SPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD--------------PNTPVYIDFFAHMSLWEGVRAAGAQ--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 94 eVFVYRHCDMYHLNSLLSncKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAH--GTFvcGENGGGVAEEF 171
Cdd:PRK07179 162 -AHPFRHNDVDHLRRQIE--RHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHslGTH--GPQGAGLVAEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 172 NCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEIWRRKAIWERVKEFK 251
Cdd:PRK07179 237 GLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLR 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 252 E-LS--GVDI--SSPIISLVVGNQEKALKASRYLLKSG-FHVMAIRPPTvPPNSCRLRVTLSAAHTTEDVKKLITALSSC 325
Cdd:PRK07179 317 EgLSelGYNIrsESQIIALETGSERNTEVLRDALEERNvFGAVFCAPAT-PKNRNLIRLSLNADLTASDLDRVLEVCREA 395
|
..
gi 30680578 326 LD 327
Cdd:PRK07179 396 RD 397
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
11-327 |
3.48e-29 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 117.17 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 11 GYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLlaasgkplknekvaIFSDALNHASIIDGVRLAerq 90
Cdd:PLN02483 143 GTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGGL--------------IISDSLNHNSIVNGARGS--- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 91 gNVEVFVYRHCDMYHLNSLL----------SNCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVC 160
Cdd:PLN02483 206 -GATIRVFQHNTPSHLEEVLreqiaegqprTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 161 GENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKE--- 236
Cdd:PLN02483 285 GKTGRGVCELLGVDpADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEdgt 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 237 -IWRRK--AIWERVKEFK-ELSGV------DISSPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTL 306
Cdd:PLN02483 365 nRGAQKlaQIRENSNFFRsELQKMgfevlgDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICI 444
|
330 340
....*....|....*....|.
gi 30680578 307 SAAHTTEDVKKLITALSSCLD 327
Cdd:PLN02483 445 SASHSREDLIKALEVISEVGD 465
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
1-327 |
1.17e-19 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 88.68 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 1 MGPKGSALICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLaasgkplknekvaiFSDALNHASI 80
Cdd:PRK05937 43 LGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYV--------------LWDEQVHISV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 81 IDGVRLAERQGNVevfvYRHCDMYHLNSLLSNCKM---KRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGT 157
Cdd:PRK05937 109 VYSLSVISGWHQS----FRHNDLDHLESLLESCRQrsfGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 158 FVCGENGGGVAEEFNCEADVDLCVgTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIP--VPMAAAAYAAVVVARK 235
Cdd:PRK05937 185 GIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPphLLISIQVAYDFLSQEG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 236 EIWRRK--AIWERVKEFKELSGVDISSPIISLVVGNQEkalkASRYLLKSGFHVMAIRPPTVPpnscRLRVTLSAAHTTE 313
Cdd:PRK05937 264 ELARKQlfRLKEYFAQKFSSAAPGCVQPIFLPGISEQE----LYSKLVETGIRVGVVCFPTGP----FLRVNLHAFNTED 335
|
330
....*....|....
gi 30680578 314 DVKKLITALSSCLD 327
Cdd:PRK05937 336 EVDILVSVLATYLE 349
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
2-327 |
8.42e-16 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 77.64 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 2 GPKGsalICGYTTYHRLLESSLAQLKKKEDCLVCPTGFAANMAAMVAIGSVASLLAAsgkplknekvaifsDALNHASII 81
Cdd:PLN03227 34 GPRG---FYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKRGDLLVV--------------DRGVNEALL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 82 DGVRLAErqgnVEVFVYRHCDMYHLNSLLSNCK-----------MKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLV 150
Cdd:PLN03227 97 VGVSLSR----ANVRWFRHNDMKDLRRVLEQVRaqdvalkrkptDQRRFLVVEGLYKNTGTLAPLKELVALKEEFHYRLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 151 IDDAHGTFVCGENGGGVAEEFNCE--ADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYA 228
Cdd:PLN03227 173 LDESFSFGTLGKSGRGSLEHAGLKpmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSASAPPFLAKADAT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 229 AVVVARKEiwrrKAIWERVKE-----FKELSGVDIS----------------SPIISLVVGNQEKA---------LKASR 278
Cdd:PLN03227 253 ATAGELAG----PQLLNRLHDsianlYSTLTNSSHPyalklrnrlvitsdpiSPIIYLRLSDQEATrrtdetlilDQIAH 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 30680578 279 YLLKSGFHVMAIR------PPTVPPNScrLRVTLSAAHTTEDVKKLITALSSCLD 327
Cdd:PLN03227 329 HSLSEGVAVVSTGghvkkfLQLVPPPC--LRVVANASHTREDIDKLLTVLGEAVE 381
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
70-322 |
1.42e-12 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 68.23 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 70 IFSDALNHASIIDGVRLAERQgnveVFVYRHCDMYHLNSLLSNC-------KMKRKVVVTDSLFSMDGDFAPMEELSQLR 142
Cdd:PLN02822 196 IVADEGVHWGIQNGLYLSRST----IVYFKHNDMESLRNTLEKLtaenkrkKKLRRYIVVEAIYQNSGQIAPLDEIVRLK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 143 KKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEAD-VDLCVGTLSKAAGCHGGFIACSKKW--KQLIQSRGrsFIFSTAIP 219
Cdd:PLN02822 272 EKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkIDIITAAMGHALATEGGFCTGSARVvdHQRLSSSG--YVFSASLP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 220 ----------VPMAAAAYAAVVVARKEIwrrKAIWERVKEFKELS-GVDISSPIISLVVGNQEKALK---------ASRY 279
Cdd:PLN02822 350 pylasaaitaIDVLEDNPSVLAKLKENI---ALLHKGLSDIPGLSiGSNTLSPIVFLHLEKSTGSAKedlsllehiADRM 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30680578 280 LLKSGFHVMAIRPPTVppNSCRL----RVTLSAAHTTEDVKKLITAL 322
Cdd:PLN02822 427 LKEDSVLVVVSKRSTL--DKCRLpvgiRLFVSAGHTESDILKASESL 471
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
19-196 |
3.37e-04 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 40.83 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 19 LESSLAQL--KKKEDCLVCPTGFAANMAAMVAIgsvasllaasgkpLKNEKVAIfSDALNHASIIdgVRLAERQG-NVEV 95
Cdd:cd01494 5 LEEKLARLlqPGNDKAVFVPSGTGANEAALLAL-------------LGPGDEVI-VDANGHGSRY--WVAAELAGaKPVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 96 FVYRHCDMYHLN-SLLSNCKMKRKV--VVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFn 172
Cdd:cd01494 69 VPVDDAGYGGLDvAILEELKAKPNValIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG- 147
|
170 180
....*....|....*....|....*
gi 30680578 173 ceADVdlCVGTLSKA-AGCHGGFIA 196
Cdd:cd01494 148 --ADV--VTFSLHKNlGGEGGGVVI 168
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
135-322 |
1.37e-03 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 40.02 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 135 MEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNcEADVDLCVGTLSKAAGCHG---GFIACSKKW-KQLIQSRGR 210
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAELVYDGEPPPALALLD-AYERVIVLRSFSKTFGLPGlriGYLIAPPEElLERLKKLLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680578 211 SFIFSTAIPV-----PMAAAAYAAVVVARKEI-WRRKAIWERVKEFKELSGVDISSPIISLVVGNQEKALKASRYLLKSg 284
Cdd:cd00609 233 YTTSGPSTLSqaaaaAALDDGEEHLEELRERYrRRRDALLEALKELGPLVVVKPSGGFFLWLDLPEGDDEEFLERLLLE- 311
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30680578 285 FHVmAIRPPTVPPNSCR--LRVTLsaAHTTEDVKKLITAL 322
Cdd:cd00609 312 AGV-VVRPGSAFGEGGEgfVRLSF--ATPEEELEEALERL 348
|
|
| |
