|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
16-381 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 545.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 16 DLYRQRPLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELT 95
Cdd:PRK05958 18 GLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 96 GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAV-GNTLVVTDGV 174
Cdd:PRK05958 98 GAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRaGRALIVTESV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 175 FSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIEA 254
Cdd:PRK05958 178 FSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 255 LVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSR 334
Cdd:PRK05958 258 LINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAA 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490714385 335 LLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAEC 381
Cdd:PRK05958 338 ALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
16-384 |
0e+00 |
|
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: 540.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 16 DLYRQRPLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELT 95
Cdd:COG0156 16 GLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 96 GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKA--VGNTLVVTDG 173
Cdd:COG0156 96 GKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKAraARRKLIVTDG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 174 VFSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGvDDVPVLIGTLGKACGTAGAFVAGSEALIE 253
Cdd:COG0156 176 VFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELID 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 254 ALVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLS 333
Cdd:COG0156 255 YLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAERALALA 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490714385 334 RLLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAECYPQ 384
Cdd:COG0156 335 DALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
22-379 |
0e+00 |
|
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: 508.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 22 PLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRAL 101
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 102 LFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVG--NTLVVTDGVFSMDG 179
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGerRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 180 DLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 260 RPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRLLRER 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490714385 340 GLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALA 379
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
37-382 |
1.87e-158 |
|
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: 449.32 E-value: 1.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 37 QRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAITA 116
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 117 LVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAV---GNTLVVTDGVFSMDGDLADLPALADVARA 193
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrpyGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 194 RGAWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYIYTTSQPPALA 273
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEEFGGL-TDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 274 CATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSP-TPIQPIVIGDSAQALRLSRLLRERGLLVTAIRPPTVP 352
Cdd:cd06454 240 AAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319
|
330 340 350
....*....|....*....|....*....|
gi 490714385 353 AGSARLRVTLSAAHSEAQVQLLLNALAECY 382
Cdd:cd06454 320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-378 |
4.61e-44 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 155.93 E-value: 4.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 42 FCSNDYLGLAnhpeVIAAWQAGAERwgvggGASHLVVGHSTPHHQVE--EALAELTGRP--------RALLFSTGYMANL 111
Cdd:pfam00155 6 LGSNEYLGDT----LPAVAKAEKDA-----LAGGTRNLYGPTDGHPElrEALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 112 G-AITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRY-------LHNDPASLASRLDKAVGntLVVTDGVFSMDGDLAD 183
Cdd:pfam00155 77 EaLIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKPK--VVLHTSPHNPTGTVAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 184 LP---ALADVARARGAWLMVDDAHGLGTLGAQGGGIVeHFGLGVDDVPVLIGTLGKACGTAG---AFVAGSEALIEALVQ 257
Cdd:pfam00155 155 LEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 258 FARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRL-L 336
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVlL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490714385 337 RERGLLVTAIRPPTVPagsARLRVTLsAAHSEAQVQLLLNAL 378
Cdd:pfam00155 314 EEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
16-381 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 545.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 16 DLYRQRPLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELT 95
Cdd:PRK05958 18 GLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 96 GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAV-GNTLVVTDGV 174
Cdd:PRK05958 98 GAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRaGRALIVTESV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 175 FSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIEA 254
Cdd:PRK05958 178 FSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 255 LVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSR 334
Cdd:PRK05958 258 LINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAA 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490714385 335 LLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAEC 381
Cdd:PRK05958 338 ALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
16-384 |
0e+00 |
|
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: 540.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 16 DLYRQRPLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELT 95
Cdd:COG0156 16 GLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 96 GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKA--VGNTLVVTDG 173
Cdd:COG0156 96 GKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKAraARRKLIVTDG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 174 VFSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGvDDVPVLIGTLGKACGTAGAFVAGSEALIE 253
Cdd:COG0156 176 VFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELID 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 254 ALVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLS 333
Cdd:COG0156 255 YLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAERALALA 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490714385 334 RLLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAECYPQ 384
Cdd:COG0156 335 DALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
22-379 |
0e+00 |
|
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: 508.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 22 PLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRAL 101
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 102 LFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVG--NTLVVTDGVFSMDG 179
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGerRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 180 DLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 260 RPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRLLRER 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490714385 340 GLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALA 379
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
37-382 |
1.87e-158 |
|
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: 449.32 E-value: 1.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 37 QRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAITA 116
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 117 LVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAV---GNTLVVTDGVFSMDGDLADLPALADVARA 193
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrpyGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 194 RGAWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYIYTTSQPPALA 273
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEEFGGL-TDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 274 CATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSP-TPIQPIVIGDSAQALRLSRLLRERGLLVTAIRPPTVP 352
Cdd:cd06454 240 AAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319
|
330 340 350
....*....|....*....|....*....|
gi 490714385 353 AGSARLRVTLSAAHSEAQVQLLLNALAECY 382
Cdd:cd06454 320 RGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
17-380 |
1.07e-116 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 344.87 E-value: 1.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 17 LYRQRPLLESPQGPEV-VVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELT 95
Cdd:PRK06939 21 LYKEERVITSPQGADItVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 96 GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVG----NTLVVT 171
Cdd:PRK06939 101 GTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEagarHKLIAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 172 DGVFSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKACGTA-GAFVAGSEA 250
Cdd:PRK06939 181 DGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGV-MDRVDIITGTLGKALGGAsGGYTAGRKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 251 LIEALVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQAL 330
Cdd:PRK06939 260 VIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQ 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490714385 331 RLSRLLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAE 380
Cdd:PRK06939 340 EFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEK 389
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
17-377 |
3.96e-107 |
|
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: 320.23 E-value: 3.96e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 17 LYRQRPLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTG 96
Cdd:TIGR01825 13 LYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 97 RPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAV--GNTLVVTDGV 174
Cdd:TIGR01825 93 TEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENPsyGKKLIVTDGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 175 FSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGvDDVPVLIGTLGKACGTAGAFVAGSEALIEA 254
Cdd:TIGR01825 173 FSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLE-DKVDIQVGTLSKAIGVVGGYAAGHKELIEY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 255 LVQFARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSR 334
Cdd:TIGR01825 252 LKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVIGDEKAAQEFSR 331
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490714385 335 LLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNA 377
Cdd:TIGR01825 332 RLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDA 374
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
35-378 |
3.27e-79 |
|
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: 249.26 E-value: 3.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 35 DGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAI 114
Cdd:TIGR01821 43 GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 115 TAL--VGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVGNT--LVVTDGVFSMDGDLADLPALADV 190
Cdd:TIGR01821 123 ATLakIIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRpkIIAFESVYSMDGDIAPIEEICDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 191 ARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYIYTTSQPP 270
Cdd:TIGR01821 203 ADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 271 ALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRLLRERGLL-VTAIRPP 349
Cdd:TIGR01821 282 AIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIyVQPINYP 361
|
330 340
....*....|....*....|....*....
gi 490714385 350 TVPAGSARLRVTLSAAHSEAQVQLLLNAL 378
Cdd:TIGR01821 362 TVPRGTERLRITPTPAHTDKMIDDLVEAL 390
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
37-386 |
6.55e-72 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 230.51 E-value: 6.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 37 QRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAITA 116
Cdd:PRK13392 46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALST 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 117 LVG--QGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVGN--TLVVTDGVFSMDGDLADLPALADVAR 192
Cdd:PRK13392 126 LGKllPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDrpKLIAFESVYSMDGDIAPIEAICDLAD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 193 ARGAWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYIYTTSQPPAL 272
Cdd:PRK13392 206 RYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 273 ACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRLLRERGLL-VTAIRPPTV 351
Cdd:PRK13392 285 AAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIyIQPINYPTV 364
|
330 340 350
....*....|....*....|....*....|....*
gi 490714385 352 PAGSARLRVTLSAAHSEAQVQLLLNALAECYPQLE 386
Cdd:PRK13392 365 PRGTERLRITPTPLHDDEDIDALVAALVAIWDRLE 399
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
37-381 |
2.90e-71 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 230.72 E-value: 2.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 37 QRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAITA 116
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 117 --------------LVGQGDTVLQDRLNHASLLDGGLLSGARFNR----YLHNDPASLASRLDK-AVGNTLVVTDGVFSM 177
Cdd:PLN02955 182 igsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAERQGNVevfvYRHCDMYHLNSLLSScKMKRKVVVTDSLFSM 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 178 DGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDdVPVLIGTLGKACGTAGAFVAGSEALIEALVQ 257
Cdd:PLN02955 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEAD-VDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 258 FARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREgaqqlgLQLMDSPTPIQPIVIGDSAQALRLSRLLR 337
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKA------LSGVDISSPIISLVVGNQEKALKASRYLL 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490714385 338 ERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAEC 381
Cdd:PLN02955 415 KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSC 458
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
38-380 |
3.58e-57 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 194.21 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 38 RLLAFCSNDYLGLANH-----PEVIAAWQagaeRWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLG 112
Cdd:PLN02483 101 RCLNLGSYNYLGFAAAdeyctPRVIESLK----KYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNST 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 113 AITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDKAVG-----------NTLVVTDGVFSMDGDL 181
Cdd:PLN02483 177 IIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAegqprthrpwkKIIVIVEGIYSMEGEL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 182 ADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHfgLGVD--DVPVLIGTLGKACGTAGAFVAGSEALIEALVQFA 259
Cdd:PLN02483 257 CKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCEL--LGVDpaDVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTC 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 260 RPYIYTTSQPPALACATLKSLELLRRE--TWRREHLAALIRQ----FREGAQQLGLQ-LMDSPTPIQPIVIGDSAQALRL 332
Cdd:PLN02483 335 PAHLYATSMSPPAVQQVISAIKVILGEdgTNRGAQKLAQIREnsnfFRSELQKMGFEvLGDNDSPVMPIMLYNPAKIPAF 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490714385 333 SRLLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAE 380
Cdd:PLN02483 415 SRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISE 462
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
36-386 |
2.11e-44 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 158.25 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 36 GQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAIT 115
Cdd:PRK07179 53 GPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 116 ALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLaSRLDKAVGNTLVVTDGVFSMDGDLADLPALADVARARG 195
Cdd:PRK07179 133 TIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHL-RRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 196 AWLMVDDAHGLGTLGAQGGGIVEHFGLgVDDVPVLIGTLGKA-CGTAGaFVAGSEALIEALVQFARPYIYTTSQPPALAC 274
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGL-TSRVHFITASLAKAfAGRAG-IITCPRELAEYVPFVSYPAIFSSTLLPHEIA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 275 ATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLmDSPTPIQPIVIGDSAQALRLSRLLRERGLLVTAIRPPTVPAG 354
Cdd:PRK07179 290 GLEATLEVIESADDRRARLHANARFLREGLSELGYNI-RSESQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKN 368
|
330 340 350
....*....|....*....|....*....|..
gi 490714385 355 SARLRVTLSAAHSEAQVQLLLNALAECYPQLE 386
Cdd:PRK07179 369 RNLIRLSLNADLTASDLDRVLEVCREARDEVD 400
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-378 |
4.61e-44 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 155.93 E-value: 4.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 42 FCSNDYLGLAnhpeVIAAWQAGAERwgvggGASHLVVGHSTPHHQVE--EALAELTGRP--------RALLFSTGYMANL 111
Cdd:pfam00155 6 LGSNEYLGDT----LPAVAKAEKDA-----LAGGTRNLYGPTDGHPElrEALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 112 G-AITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRY-------LHNDPASLASRLDKAVGntLVVTDGVFSMDGDLAD 183
Cdd:pfam00155 77 EaLIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKPK--VVLHTSPHNPTGTVAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 184 LP---ALADVARARGAWLMVDDAHGLGTLGAQGGGIVeHFGLGVDDVPVLIGTLGKACGTAG---AFVAGSEALIEALVQ 257
Cdd:pfam00155 155 LEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 258 FARPYIYTTSQPPALACATLKSLELLRRETWRREHLAALIRQFREGAQQLGLQLMDSPTPIQPIVIGDSAQALRLSRL-L 336
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVlL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490714385 337 RERGLLVTAIRPPTVPagsARLRVTLsAAHSEAQVQLLLNAL 378
Cdd:pfam00155 314 EEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
22-283 |
5.55e-37 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 139.88 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 22 PLLESPQGPEVVVDGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRAL 101
Cdd:PLN02822 94 PVLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 102 LFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASLASRLDK-AVGNT-------LVVTDG 173
Cdd:PLN02822 174 LYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKlTAENKrkkklrrYIVVEA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 174 VFSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIE 253
Cdd:PLN02822 254 IYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVD 333
|
250 260 270
....*....|....*....|....*....|
gi 490714385 254 ALVQFARPYIYTTSQPPALACATLKSLELL 283
Cdd:PLN02822 334 HQRLSSSGYVFSASLPPYLASAAITAIDVL 363
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
35-380 |
1.49e-35 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 134.34 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 35 DGQRLLAFCSNDYLGLANHPEVIAAWQAGAERWGVgggaSHLVVGHSTPHHQV----EEALAELTGrPRALLFSTGYMAN 110
Cdd:PRK07505 44 DGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGS----LHLSSSRTRVRSQIlkdlEEALSELFG-ASVLTFTSCSAAH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 111 LGAItALVGQG---DTV----LQDRLNHASL--LDGGLLSGARFNRYLHNDPASL--ASRLDKAVgntLVVTDGVFSMdG 179
Cdd:PRK07505 119 LGIL-PLLASGhltGGVpphmVFDKNAHASLniLKGICADETEVETIDHNDLDALedICKTNKTV---AYVADGVYSM-G 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 180 DLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIV-EHFGLGVDDVPVLIGTLGKACGTAGAFVA-GSEALIEALVQ 257
Cdd:PRK07505 194 GIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 258 FARPYIYttSQPPALAC--ATLKSLELLRRE--TWRREHLAALIRQFRE--GAQQLGlqlmdSPTPIQPIVIGDSAQALR 331
Cdd:PRK07505 274 YAGPLAF--SQSLNVAAlgAILASAEIHLSEelDQLQQKLQNNIALFDSliPTEQSG-----SFLPIRLIYIGDEDTAIK 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490714385 332 LSRLLRERGLLVTAIRPPTVPAGSARLRVTLSAAHSEAQVQLLLNALAE 380
Cdd:PRK07505 347 AAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKE 395
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
40-322 |
1.77e-30 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 120.39 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 40 LAFCSNDYLGLANHPEVIAAWQAGAERWGVGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYMANLGAITALVG 119
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 120 QGDTVLQDRLNHASLLDGGLLSGARFNRYLHNDPASL------------ASRLDKAVGNTLVVTDGVFSMDGDLADLPAL 187
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqdvALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 188 ADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLG-VDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYIYTT 266
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490714385 267 SQPPALACATLKSLELLRRETWRREHLAALIRQFREG--------AQQLGLQLMDSPTPIQPIV 322
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTltnsshpyALKLRNRLVITSDPISPII 304
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
36-379 |
3.25e-24 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 102.55 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 36 GQRLLAFCSNDYLGLANHP----EVIAAWQAGAERWG---VGGGASHLVVGHSTPHHQVEEALAELTGRPRALLFSTGYM 108
Cdd:PRK05937 3 ESLSIDFVTNDFLGFSRSDtlvhEVEKRYRLYCRQFPhaqLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 109 ANLGAITALVGQGDTVLQDRLNHASLLDG-GLLSGaRFNRYLHNDPASLASRLD----KAVGNTLVVTDGVFSMDGDLAD 183
Cdd:PRK05937 83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSlSVISG-WHQSFRHNDLDHLESLLEscrqRSFGRIFIFVCSVYSFKGTLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 184 LPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEhfGLGVDDVPVLIGTLGKACGTAGAFVAGSEALIEALVQFARPYI 263
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCH--SLGYENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 264 YTTSQPPALACATLKSLELLRRETwrrEHLAALIRQFREG-AQQLGLQlmdSPTPIQPIVIGDSAQaLRLSRLLRERGLL 342
Cdd:PRK05937 240 YSTGLPPHLLISIQVAYDFLSQEG---ELARKQLFRLKEYfAQKFSSA---APGCVQPIFLPGISE-QELYSKLVETGIR 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 490714385 343 VTAIRPPTVPAgsarLRVTLSAAHSEAQVQLLLNALA 379
Cdd:PRK05937 313 VGVVCFPTGPF----LRVNLHAFNTEDEVDILVSVLA 345
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
83-243 |
2.48e-13 |
|
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: 67.41 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 83 PHHQVEEALAELT--GRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHAS-LLDGGLLSGARFNRYLHND----PAS 155
Cdd:cd01494 1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDagygGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 156 LASRLD-KAVGNT-LVVTDGVFSMDGDLADLPALADVARARGAWLMVDDAHGLGTLGAQGGGIVEHFGLgvddvpVLIGT 233
Cdd:cd01494 81 VAILEElKAKPNVaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGAD------VVTFS 154
|
170
....*....|
gi 490714385 234 LGKACGTAGA 243
Cdd:cd01494 155 LHKNLGGEGG 164
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
80-205 |
4.11e-08 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 54.18 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 80 HSTPHHQVEEALAELTGRPRALLF---STGymANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGAR-------FNRYL 149
Cdd:cd00615 57 PTGPIKEAQELAARAFGAKHTFFLvngTSS--SNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVpvylkpeRNPYY 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490714385 150 H---------NDPASLASRLDKAVgntlVVTDGVFsmDGDLADLPALADVARARGAWLMVDDAHG 205
Cdd:cd00615 135 GiaggippetFKKALIEHPDAKAA----VITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
80-201 |
5.45e-08 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 54.28 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 80 HSTP-HHQVEEALAELTGRPRALLFSTGyMAnlgAITA----LVGQGDTVL-QDRLNHAS--LLDGGLlsgARFN---RY 148
Cdd:COG0626 55 YGNPtRRALEEALAALEGGEAALAFASG-MA---AISAvllaLLKAGDHVVaSDDLYGGTrrLLDKVL---ARFGievTF 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490714385 149 LH-NDPASLASRLDKAvgntlvvTDGVF-----SMDGDLADLPALADVARARGAWLMVD 201
Cdd:COG0626 128 VDpTDLAAVEAAIRPN-------TKLVFletpsNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
42-380 |
1.32e-06 |
|
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: 49.65 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 42 FCSNDYLgLANHPEVIAAWQAGAERwgvgggASHLVVGHSTPHHQVEEALAELTGR-------PRALLFSTG-YMANLGA 113
Cdd:cd00609 3 LSIGEPD-FPPPPEVLEALAAAALR------AGLLGYYPDPGLPELREAIAEWLGRrggvdvpPEEIVVTNGaQEALSLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 114 ITALVGQGDTVLQDRLNHASLLDGGLLSGARFNRYL-----HNDPASLASRLDKAVGNTLVV-------TDGVFSMDgdl 181
Cdd:cd00609 76 LRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPldeegGFLLDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 182 aDLPALADVARARGAWLMVDDAHGLgtLGAQGGGIVEHFGLGVDDVPVLIGTLGKACGTAG---AFVAGSEALIEALVQF 258
Cdd:cd00609 153 -ELEELAELAKKHGILIISDEAYAE--LVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 259 ARPYIY-TTSQPPALACAtlkslELLRRetwRREHLAALIRQFREGAQQL--GLQLMDSPTPIQP-----IVIGDSAQAL 330
Cdd:cd00609 230 LLPYTTsGPSTLSQAAAA-----AALDD---GEEHLEELRERYRRRRDALleALKELGPLVVVKPsggffLWLDLPEGDD 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490714385 331 RLSRLLRERGLLVtAIRPPTV--PAGSARLRVTLsaAHSEAQVQLLLNALAE 380
Cdd:cd00609 302 EEFLERLLLEAGV-VVRPGSAfgEGGEGFVRLSF--ATPEEELEEALERLAE 350
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
80-205 |
4.81e-06 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 48.27 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 80 HSTPHHQVEEALAELTGRPRALLFSTGY-MANLGAITALVGQGDTVLQDRLNHASLLDGGLLSGARfNRYLHND------ 152
Cdd:pfam01276 64 HEGAIKEAQKYAARVFGADKSYFVVNGTsGSNKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGAT-PVYLEPSrnaygi 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490714385 153 ----------PASLASRLdKAVGNT-----LVVTDGVFsmDGDLADLPALADVARARGAWLMVDDAHG 205
Cdd:pfam01276 143 iggiplhefqEETLKEAI-AEVPDAkgprlAVITNPTY--DGVLYNAKEIVDTLHHLSDPILFDSAWV 207
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
87-201 |
1.21e-05 |
|
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: 46.81 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 87 VEEALAELTGRPRALLFSTGYMANLGAITALVGQGDTVLqdrlnHASLLDGGllSGARFNRYLHN--------DPASLAS 158
Cdd:cd00614 45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVV-----ASDDLYGG--TYRLFERLLPKlgievtfvDPDDPEA 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 490714385 159 rLDKAVGNTlvvTDGVF-----SMDGDLADLPALADVARARGAWLMVD 201
Cdd:cd00614 118 -LEAAIKPE---TKLVYvesptNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
87-260 |
8.42e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 37.58 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 87 VEEALAELTGRPRALLFSTGYMANLGAITALVGQGDTVLQDRLNHASLLDGG---LLSGARFNRYLHN-----DPASLAS 158
Cdd:pfam01212 37 LEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGghaELGGVQPRPLDGDeagnmDLEDLEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490714385 159 RLDK------------AVGNTLVVTDG-VFSMDgdlaDLPALADVARARGAWLMVDDAHgLGTLGAQGGGIVEHFGLGVD 225
Cdd:pfam01212 117 AIREvgadifpptgliSLENTHNSAGGqVVSLE----NLREIAALAREHGIPVHLDGAR-FANAAVALGVIVKEITSYAD 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 490714385 226 DVPVligTLGKACGT-AGAFVAGSEALIEALVQFAR 260
Cdd:pfam01212 192 SVTM---CLSKGLGApVGSVLAGSDDFIAKAIRQRK 224
|
|
| |
