|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
2-404 |
0e+00 |
|
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: 647.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 2 FDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGAQqDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGA 81
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAK-DVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 82 GGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIFR 161
Cdd:TIGR01821 80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 162 HNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGID 241
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 242 IVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAG 321
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 322 IPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNV 401
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
...
gi 1560964891 402 ARQ 404
Cdd:TIGR01821 400 PLS 402
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
1-408 |
0e+00 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 578.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 1 MFDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGaQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK13392 1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPDG-PRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGI 240
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 241 DIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEA 320
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNAN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 321 GIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCN 400
Cdd:PRK13392 320 GIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLE 399
|
....*...
gi 1560964891 401 VARQPAAA 408
Cdd:PRK13392 400 LPRWREAA 407
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
4-398 |
2.43e-178 |
|
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: 501.89 E-value: 2.43e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 4 YKSAFQNSVDQVRSEGRYRVFADLKRVRGqfPRAVRrreDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGG 83
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQG--PRVTI---DG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 84 TRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHN 163
Cdd:COG0156 74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 164 DLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIV 243
Cdd:COG0156 152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 244 ECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:COG0156 232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFD 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSH 398
Cdd:COG0156 312 LGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
47-396 |
3.38e-172 |
|
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: 484.76 E-value: 3.38e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLST 126
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEEL-LAAAPAAAPKLVAFESVYSMDGDIADIAGTIALA 205
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLlREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 206 KKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPAL 285
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 286 TAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVG-NPVHCKLISDMLLeEHGIYVQPINYPT 364
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRYPT 317
|
330 340 350
....*....|....*....|....*....|..
gi 1560964891 365 VPKGTERLRFTPSPDHDDAMIDKLVEAMDKLW 396
Cdd:cd06454 318 VPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
48-391 |
6.47e-73 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 231.81 E-value: 6.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 48 DVVVWCSNDYLGMgqhpVVIDAMQAEIEktgAGAGGTRNISGTTRSAVDLEAELASWH--------QKEAALLFTSGYVA 119
Cdd:pfam00155 2 DKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLqKILPGLIIFSDALNHASMIAGIRNGGGERHIFR-------HNDLEHLEELLAAAPaaapKLVAFESVYSMD 192
Cdd:pfam00155 75 NIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP----KVVLHTSPHNPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 193 GDIADIAG--TIA-LAKKYGALTYLDEVHAVGLYGETGAgVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAADAVIV 265
Cdd:pfam00155 150 GTVATLEEleKLLdLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 266 DAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLI 345
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1560964891 346 SDMLLEEHGIYVQPINYPTVPkgtERLRFTPSpDHDDAMIDKLVEA 391
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEA 350
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
2-404 |
0e+00 |
|
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: 647.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 2 FDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGAQqDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGA 81
Cdd:TIGR01821 1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAK-DVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 82 GGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIFR 161
Cdd:TIGR01821 80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 162 HNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGID 241
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 242 IVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAG 321
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 322 IPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNV 401
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
...
gi 1560964891 402 ARQ 404
Cdd:TIGR01821 400 PLS 402
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
1-408 |
0e+00 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 578.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 1 MFDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGaQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK13392 1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPDG-PRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK13392 80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGI 240
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 241 DIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEA 320
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNAN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 321 GIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCN 400
Cdd:PRK13392 320 GIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLE 399
|
....*...
gi 1560964891 401 VARQPAAA 408
Cdd:PRK13392 400 LPRWREAA 407
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
4-398 |
2.43e-178 |
|
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: 501.89 E-value: 2.43e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 4 YKSAFQNSVDQVRSEGRYRVFADLKRVRGqfPRAVRrreDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGG 83
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQG--PRVTI---DG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 84 TRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHN 163
Cdd:COG0156 74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 164 DLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIV 243
Cdd:COG0156 152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 244 ECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:COG0156 232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFD 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSH 398
Cdd:COG0156 312 LGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
47-396 |
3.38e-172 |
|
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: 484.76 E-value: 3.38e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLST 126
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEEL-LAAAPAAAPKLVAFESVYSMDGDIADIAGTIALA 205
Cdd:cd06454 81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLlREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 206 KKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPAL 285
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 286 TAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVG-NPVHCKLISDMLLeEHGIYVQPINYPT 364
Cdd:cd06454 239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRYPT 317
|
330 340 350
....*....|....*....|....*....|..
gi 1560964891 365 VPKGTERLRFTPSPDHDDAMIDKLVEAMDKLW 396
Cdd:cd06454 318 VPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
5-391 |
1.62e-115 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 342.14 E-value: 1.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 5 KSAFQNSVDQVRSEGRYRVFadlkRVRGQFPRAVRRREDgaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGT 84
Cdd:PRK05958 4 LDRLEAALAQRRAAGLYRSL----RPREGGAGRWLVVDG---RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 85 RNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHND 164
Cdd:PRK05958 77 RLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 165 LEHLEELLAAAPAAApKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVE 244
Cdd:PRK05958 155 VDALEALLAKWRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 245 C-TLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:PRK05958 234 VgTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQ 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLeEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK05958 314 LMDSQSAIQPLIVGDNERALALAAALQ-EQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
29-393 |
6.00e-109 |
|
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: 324.61 E-value: 6.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 29 RVRGQFPRAVRRREDgaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKE 108
Cdd:TIGR00858 1 RPLDRGPGPEVVRDG---RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 109 AALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPKLVAFESV 188
Cdd:TIGR00858 78 AALLFSSGYLANVGVISALVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 189 YSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVL-DGIDIVECTLGKAIGVMGGYIAADAVIVDA 267
Cdd:TIGR00858 156 FSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSYGAYVAGSQALIDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLISD 347
Cdd:TIGR00858 236 LINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1560964891 348 MLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMD 393
Cdd:TIGR00858 316 ELQQQ-GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-391 |
1.12e-97 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 297.11 E-value: 1.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 1 MFDYKSAFQNSVDQVRSEGRYRVfadlKRVRGQFPRAVRRREDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK06939 2 SGAFYAQLREELEEIKAEGLYKE----ERVITSPQGADITVADG--KEVINFCANNYLGLANHPELIAAAKAALDSHGFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLqkILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK06939 76 MASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLE--HLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLD 238
Cdd:PRK06939 154 ANNDMAdlEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 239 GIDIVECTLGKAI-GVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRL 317
Cdd:PRK06939 234 RVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGM 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560964891 318 SEAGIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
48-391 |
6.47e-73 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 231.81 E-value: 6.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 48 DVVVWCSNDYLGMgqhpVVIDAMQAEIEktgAGAGGTRNISGTTRSAVDLEAELASWH--------QKEAALLFTSGYVA 119
Cdd:pfam00155 2 DKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLqKILPGLIIFSDALNHASMIAGIRNGGGERHIFR-------HNDLEHLEELLAAAPaaapKLVAFESVYSMD 192
Cdd:pfam00155 75 NIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP----KVVLHTSPHNPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 193 GDIADIAG--TIA-LAKKYGALTYLDEVHAVGLYGETGAgVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAADAVIV 265
Cdd:pfam00155 150 GTVATLEEleKLLdLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 266 DAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLI 345
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1560964891 346 SDMLLEEHGIYVQPINYPTVPkgtERLRFTPSpDHDDAMIDKLVEA 391
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEA 350
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
44-392 |
1.91e-52 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 182.18 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 44 GAQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEAT 123
Cdd:PLN02955 99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 124 ----------LSTLQKILPG--LIIFSDALNHASMIAGIR----NGGGERHIFRHNDLEHLEELLAAAPAAApKLVAFES 187
Cdd:PLN02955 179 mvaigsvaslLAASGKPLKNekVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 188 VYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDA 267
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKrrlSEAGIPVlpsVSHIVPVHVGNPVHCKLISD 347
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDI---SSPIISLVVGNQEKALKASR 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1560964891 348 MLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAM 392
Cdd:PLN02955 412 YLLKS-GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
54-406 |
5.94e-50 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 175.72 E-value: 5.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 54 SNDYLGMGQH-----PVVIDAMQaeieKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLq 128
Cdd:PLN02483 107 SYNYLGFAAAdeyctPRVIESLK----KYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 129 kILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPK---------LVAFESVYSMDGDIADIA 199
Cdd:PLN02483 182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPrthrpwkkiIVIVEGIYSMEGELCKLP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 200 GTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVlD--GIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PLN02483 261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGV-DpaDVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 278 TTSLPPALTAGALASV----------RHLKAHPELRDahqeRAATLKRRLSEAGIPVLPSV-SHIVPVHVGNPVHCKLIS 346
Cdd:PLN02483 340 ATSMSPPAVQQVISAIkvilgedgtnRGAQKLAQIRE----NSNFFRSELQKMGFEVLGDNdSPVMPIMLYNPAKIPAFS 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 347 DMLLEEHGIYVQpINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNVARQPA 406
Cdd:PLN02483 416 RECLKQNVAVVV-VGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
45-391 |
4.84e-41 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 149.77 E-value: 4.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 45 AQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGagaggtrniSGTTRSAV---------DLEAELASWHQKEAALLFTS 115
Cdd:PRK07179 52 PGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEG---------DSLVMSAVflhddspkpQFEKKLAAFTGFESCLLCQS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 116 GYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAapkLVAFESVYSMDGDI 195
Cdd:PRK07179 123 GWAANVGLLQTIAD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 196 ADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGF 275
Cdd:PRK07179 198 APLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 276 IFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPvLPSVSHIVPVHVGNPVHCKLISDMlLEEHGI 355
Cdd:PRK07179 278 IFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYN-IRSESQIIALETGSERNTEVLRDA-LEERNV 355
|
330 340 350
....*....|....*....|....*....|....*.
gi 1560964891 356 YVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK07179 356 FGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEV 391
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
47-395 |
9.10e-37 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 139.88 E-value: 9.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGyvaneatLST 126
Cdd:PLN02822 109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYG-------LST 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LQKILP-----GLIIFSDALNHASMIAGIRNGGGERHIFRHNDLE------HLEELLAAAPAAAPKLVAFESVYSMDGDI 195
Cdd:PLN02822 182 IFSVIPafckkGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMEslrntlEKLTAENKRKKKLRRYIVVEAIYQNSGQI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 196 ADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGV-LDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASG 274
Cdd:PLN02822 262 APLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 275 FIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSeaGIPVLPSVSH----IVPVHVGNP---VHCKL--- 344
Cdd:PLN02822 342 YVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLS--DIPGLSIGSNtlspIVFLHLEKStgsAKEDLsll 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1560964891 345 --ISDMLLEEHGIYVQPINYPTV-----PKGterLRFTPSPDHDDAMIDKLVEAMDKL 395
Cdd:PLN02822 420 ehIADRMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRV 474
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
38-392 |
1.38e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 123.94 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 38 VRRREDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGagaggTRNISgTTRSAV------DLEAELASWHQKEAaL 111
Cdd:PRK07505 39 LITLADG--HTFVNFVSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGASV-L 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 112 LFTSGYVANEATLSTLQK-ILPG----LIIFsDALNHASMIA--GIRNGGGERHIFRHNDLEhleelLAAAPAAAPKLVA 184
Cdd:PRK07505 110 TFTSCSAAHLGILPLLASgHLTGgvppHMVF-DKNAHASLNIlkGICADETEVETIDHNDLD-----ALEDICKTNKTVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 185 F--ESVYSMdGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVA--ERDGVLDGIDIVECTLGKAIGVMGGYIA- 259
Cdd:PRK07505 184 YvaDGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERTIIAASLGKAFGASGGVIMl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 260 ADAVIVDAVRSWASGFIFTTSLPPALTAGALASVR-HLKahPELrDAHQERaatLKRRL---------SEAGIPvLPsvs 329
Cdd:PRK07505 263 GDAEQIELILRYAGPLAFSQSLNVAALGAILASAEiHLS--EEL-DQLQQK---LQNNIalfdsliptEQSGSF-LP--- 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560964891 330 hIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAM 392
Cdd:PRK07505 333 -IRLIYIGDEDTAIKAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
47-302 |
3.55e-27 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 111.03 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 47 QDVVVWCSNDYLGMGQHPVVIDAMQAE-----IEKTGA--GAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVA 119
Cdd:PRK05937 4 SLSIDFVTNDFLGFSRSDTLVHEVEKRyrlycRQFPHAqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLQKILPglIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPK--LVAFESVYSMDGDIAD 197
Cdd:PRK05937 84 NLGLCAHLSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 198 IAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGvLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRY 240
|
250 260
....*....|....*....|....*
gi 1560964891 278 TTSLPPALTAGALASVRHLKAHPEL 302
Cdd:PRK05937 241 STGLPPHLLISIQVAYDFLSQEGEL 265
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
50-323 |
3.78e-27 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 111.53 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 50 VVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQK 129
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 130 ilPGLIIFSDALNHASMIAGIRNGGGERHIFRHND----------LEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIA 199
Cdd:PLN03227 81 --RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDmkdlrrvleqVRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 200 GTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGV--LDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PLN03227 159 ELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCF 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1560964891 278 TTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:PLN03227 239 SASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSSHP 284
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
203-394 |
6.24e-09 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 57.58 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 203 ALAKKYGALTYLDEVhAVGLyGETGAGVA-ERDGVLdgIDIVecTLGKAIG---VMGGYIAADAviVDAVRSWASGFIFT 278
Cdd:cd00610 219 ELCRKHGILLIADEV-QTGF-GRTGKMFAfEHFGVE--PDIV--TLGKGLGgglPLGAVLGREE--IMDAFPAGPGLHGG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 279 T--SLPPALTAGaLASVRHLKAHPELRDAhQERAATLKRRLSEAgIPVLPSVSHI-----------VPVHVGNPVHCKLI 345
Cdd:cd00610 291 TfgGNPLACAAA-LAVLEVLEEEGLLENA-AELGEYLRERLREL-AEKHPLVGDVrgrglmigielVKDRATKPPDKELA 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1560964891 346 SDMLLE--EHGIYVQPInyptvpkGTERLRFTPSPDHDDAMIDKLVEAMDK 394
Cdd:cd00610 368 AKIIKAalERGLLLRPS-------GGNVIRLLPPLIITEEEIDEGLDALDE 411
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
187-390 |
1.23e-08 |
|
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: 56.20 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 187 SVYSMDgDIADIAgtiALAKKYGALTYLDEVHavGLYGETGAGVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAA-D 261
Cdd:cd00609 147 AVLSEE-ELEELA---ELAKKHGILIISDEAY--AELVYDGEPPPALALLDAYERVIVLrSFSKTFGLPGlriGYLIApP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 262 AVIVDAVRSWASgfiFTTSLPPALTAGALASV-----RHLKahpELRDAHQERAATLKRRLSEAGIPVLPSVS---HIVp 333
Cdd:cd00609 221 EELLERLKKLLP---YTTSGPSTLSQAAAAAAlddgeEHLE---ELRERYRRRRDALLEALKELGPLVVVKPSggfFLW- 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1560964891 334 VHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVE 390
Cdd:cd00609 294 LDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFVRLSFATPEEELEEALERLAE 350
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
106-256 |
1.58e-07 |
|
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: 50.84 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 106 QKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRN-GGGERHIFRHNDLEHLEELLAAA----PAAAP 180
Cdd:cd01494 16 GNDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAElAGAKPVPVPVDDAGYGGLDVAILeelkAKPNV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560964891 181 KLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGlygetGAGVAERDGVLDGIDIVECTLGKAIGVMGG 256
Cdd:cd01494 94 ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLHKNLGGEGG 164
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
91-331 |
6.20e-04 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 41.80 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 91 TRSAvdLEAELASWHQKEAALLFTSGYVANEATLSTLQK----ILPGLIIFSDALNHASMIAgiRNGGGERHIFRHNDLE 166
Cdd:cd00614 41 TVDA--LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERLL--PKLGIEVTFVDPDDPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 167 hleeLLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYgetgagvaeRDGVLDGIDIVECT 246
Cdd:cd00614 117 ----ALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYL---------QRPLELGADIVVHS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 247 LGKAIG----VMGGYIAA-DAVIVDAVRSWasGFIFTTSLPPALTAGALASVRHLkahpELR-DAHQERAATLKRRLSEa 320
Cdd:cd00614 184 ATKYIGghsdVIAGVVVGsGEALIQRLRFL--RLALGTILSPFDAWLLLRGLKTL----PLRmERHSENALKVAEFLEK- 256
|
250
....*....|.
gi 1560964891 321 gipvLPSVSHI 331
Cdd:cd00614 257 ----HPKVERV 263
|
|
| Aminotran_3 |
pfam00202 |
Aminotransferase class-III; |
63-394 |
9.14e-04 |
|
Aminotransferase class-III;
Pssm-ID: 395148 [Multi-domain] Cd Length: 397 Bit Score: 41.16 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 63 HPVVIDAMQAEIEKTGAGAGGTRnisgTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKIL--------PGL 134
Cdd:pfam00202 45 HPALVAAVKTQADKLSHVSFGAF----TNEPALDLAEKLLKLTPGDRVFLMNSGSEANETAVKLARKWYrekgatgrTKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 135 IIFSDALN---HASM-----IAGIRNGGG----ERHIFRHNDLEHLEELLAAAPAAAPKLVA--------FESVYSMDGD 194
Cdd:pfam00202 121 IAFSGAFHgrtMGALsvtgsKPKYKTGFGpflpGFPRLPYPDPEFLKEQRCLEELEALIAVKddevaaviVEPIQGEGGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 195 IAD----IAGTIALAKKYGALTYLDEVhAVGLyGETGAGVA-ERDGVLDgiDIVecTLGKAIGvmGGYIAAdAVIVDA-- 267
Cdd:pfam00202 201 NPPspgfLAGLRAICKKHGVLLIADEV-QTGF-GRTGKLFAhEHWGVPP--DIM--TFAKALT--GGFPLA-ATLGRAev 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLP-PALTAGALASVRHLKAHPELRDAhQERAATLKRRLSEAG-----IPVLPSVSHIVPVHVGNPVH 341
Cdd:pfam00202 272 MQAFAPGSHGGTFGGnPLACAAALATLEIIEDEDLLQNA-ARLGAYLKEGLEDLQkkyevIKDVRGKGLMIGIELKEDVT 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1560964891 342 CKLISDMLLEEHGIYVQPINYPTVpkgterlRFTPSPDHDDAMIDKLVEAMDK 394
Cdd:pfam00202 351 VNPPILLAALEAGVLILPCGDNVI-------RLLPPLTITDEQIDEGLEIISK 396
|
|
|