|
Name |
Accession |
Description |
Interval |
E-value |
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-383 |
7.64e-156 |
|
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: 443.72 E-value: 7.64e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 3 FDFINTHLQARQQDALLRKRHVVQHATARTITVNNKTYLNFASNDYLGF-GDVAVNLDDSQAL-----GSHSSALVTGYQ 76
Cdd:COG0156 2 LDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLaNHPRVIEAAAEALdrygtGSGGSRLVSGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 77 AQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALFQdkaaaQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHL 156
Cdd:COG0156 82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG-----RGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 157 RSRLEKS-KAQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFG 235
Cdd:COG0156 157 ERLLKKArAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 236 KAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESN 315
Cdd:COG0156 237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941936048 316 TAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLVGAIA 383
Cdd:COG0156 317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
2.87e-149 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 426.88 E-value: 2.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 1 MPFDFINTHLQARQQDALLRKRHVVQHATARTITVNNKTYLNFASNDYLGfgdvavnLDDSQAL-------------GSH 67
Cdd:PRK05958 2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLG-------LARHPRLiaaaqqaarrygaGSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 68 SSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVR 147
Cdd:PRK05958 75 GSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL-----AGKGDLIVSDKLNHASLIDGARLSRARVRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 148 FNHNDMNHLRSRLEKSKAQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLP 227
Cdd:PRK05958 150 YPHNDVDALEALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 228 D-ILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKT 306
Cdd:PRK05958 230 DvILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRA 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1941936048 307 HKIAVIESNTAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLVGAI 382
Cdd:PRK05958 310 LGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
23-378 |
6.80e-127 |
|
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: 369.29 E-value: 6.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 23 HVVQHATARTITVNNKTYLNFASNDYLGFGDVAVNLDDSQA------LGSHSSALVTGYQAQQKALEQYLCEQFGYGAGM 96
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQgaeqygAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 97 LFNSGFSANSSVIKALfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKS-KAQNKLIISEGV 175
Cdd:TIGR00858 81 LFSSGYLANVGVISAL-----VGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNrGERRKLIVTDGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 176 FSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVI-TFGKAAASSGACVLGSKQFIDY 254
Cdd:TIGR00858 156 FSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVgTLSKALGSYGAYVAGSQALIDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 255 MLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIVLGCAEQTLQAAD 334
Cdd:TIGR00858 236 LINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1941936048 335 KLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHL 378
Cdd:TIGR00858 316 ELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
38-379 |
2.94e-125 |
|
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: 364.57 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 38 KTYLNFASNDYLGFG------DVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKA 111
Cdd:cd06454 1 KKVLNFCSNDYLGLAnhpeviEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 112 LFqdkaaAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQN--KLIISEGVFSMDGDTAPLKELL 189
Cdd:cd06454 81 LA-----GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYgkKLIVTEGVYSMDGDIAPLPELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 190 ALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMS 269
Cdd:cd06454 156 DLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 270 PLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESN-TAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRP 348
Cdd:cd06454 236 PAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|.
gi 1941936048 349 PTVAHNTSRLRVTLTAAHTEQDITHLVKHLV 379
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALK 346
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
38-378 |
7.71e-44 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 155.16 E-value: 7.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 38 KTYLNFASNDYLgFGDVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYG--------AGMLFNSGFSANSSVI 109
Cdd:pfam00155 1 TDKINLGSNEYL-GDTLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANIEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 110 KALFQDKAaaqnSAIFQDKLNHASLIDGALHCNAALVRFN-------HNDMNHLRSRLEKSkaqNKLIISEGVFSMDGDT 182
Cdd:pfam00155 80 IFLLANPG----DAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK---PKVVLHTSPHNPTGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 183 AP---LKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSG---ACVLGSKQFIDYML 256
Cdd:pfam00155 153 ATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 257 QFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIVLGCAEQTLQAADKL 336
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1941936048 337 -KQQGIWLTAIRPPTVahnTSRLRVTLtAAHTEQDITHLVKHL 378
Cdd:pfam00155 313 lEEVGVYVTPGSSPGV---PGWLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-383 |
7.64e-156 |
|
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: 443.72 E-value: 7.64e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 3 FDFINTHLQARQQDALLRKRHVVQHATARTITVNNKTYLNFASNDYLGF-GDVAVNLDDSQAL-----GSHSSALVTGYQ 76
Cdd:COG0156 2 LDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLaNHPRVIEAAAEALdrygtGSGGSRLVSGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 77 AQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALFQdkaaaQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHL 156
Cdd:COG0156 82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG-----RGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 157 RSRLEKS-KAQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFG 235
Cdd:COG0156 157 ERLLKKArAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 236 KAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESN 315
Cdd:COG0156 237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941936048 316 TAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLVGAIA 383
Cdd:COG0156 317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
2.87e-149 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 426.88 E-value: 2.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 1 MPFDFINTHLQARQQDALLRKRHVVQHATARTITVNNKTYLNFASNDYLGfgdvavnLDDSQAL-------------GSH 67
Cdd:PRK05958 2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLG-------LARHPRLiaaaqqaarrygaGSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 68 SSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVR 147
Cdd:PRK05958 75 GSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL-----AGKGDLIVSDKLNHASLIDGARLSRARVRR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 148 FNHNDMNHLRSRLEKSKAQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLP 227
Cdd:PRK05958 150 YPHNDVDALEALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 228 D-ILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKT 306
Cdd:PRK05958 230 DvILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRA 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1941936048 307 HKIAVIESNTAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLVGAI 382
Cdd:PRK05958 310 LGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
23-378 |
6.80e-127 |
|
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: 369.29 E-value: 6.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 23 HVVQHATARTITVNNKTYLNFASNDYLGFGDVAVNLDDSQA------LGSHSSALVTGYQAQQKALEQYLCEQFGYGAGM 96
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQgaeqygAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 97 LFNSGFSANSSVIKALfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKS-KAQNKLIISEGV 175
Cdd:TIGR00858 81 LFSSGYLANVGVISAL-----VGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNrGERRKLIVTDGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 176 FSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVI-TFGKAAASSGACVLGSKQFIDY 254
Cdd:TIGR00858 156 FSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVgTLSKALGSYGAYVAGSQALIDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 255 MLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIVLGCAEQTLQAAD 334
Cdd:TIGR00858 236 LINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1941936048 335 KLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHL 378
Cdd:TIGR00858 316 ELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
38-379 |
2.94e-125 |
|
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: 364.57 E-value: 2.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 38 KTYLNFASNDYLGFG------DVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKA 111
Cdd:cd06454 1 KKVLNFCSNDYLGLAnhpeviEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 112 LFqdkaaAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQN--KLIISEGVFSMDGDTAPLKELL 189
Cdd:cd06454 81 LA-----GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYgkKLIVTEGVYSMDGDIAPLPELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 190 ALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMS 269
Cdd:cd06454 156 DLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 270 PLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESN-TAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRP 348
Cdd:cd06454 236 PAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRY 315
|
330 340 350
....*....|....*....|....*....|.
gi 1941936048 349 PTVAHNTSRLRVTLTAAHTEQDITHLVKHLV 379
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALK 346
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
3-371 |
1.97e-82 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 257.05 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 3 FDFINTHLQARQQDALLRKRHVVQHATARTITVNN-KTYLNFASNDYLGFGD------VAVNLDDSQALGSHSSALVTGY 75
Cdd:PRK06939 6 YAQLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLANhpeliaAAKAALDSHGFGMASVRFICGT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 76 QAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALFqdkaaAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNH 155
Cdd:PRK06939 86 QDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLL-----GKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 156 LRSRLEKSKAQ---NKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVI 232
Cdd:PRK06939 161 LEAQLKEAKEAgarHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 233 TFGKA-AASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAV 311
Cdd:PRK06939 241 TLGKAlGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 312 IESNTAIQPIVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDI 371
Cdd:PRK06939 321 GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQL 380
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
10-371 |
2.44e-72 |
|
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: 230.86 E-value: 2.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 10 LQARQQDALLRKRHVVQHATARTITVNNKTYLNFASNDYLGFGD------VAVNLDDSQALGSHSSALVTGYQAQQKALE 83
Cdd:TIGR01825 5 LNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADhprlkeAAAQAIQQYGVGAGAVRTIAGTLRLHEELE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 84 QYLCEQFGYGAGMLFNSGFSANSSVIKALFQdkaaaQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKS 163
Cdd:TIGR01825 85 EKLAKFKKTEAALVFQSGFNTNQGVLSALLR-----KGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLREN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 164 KAQN-KLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSG 242
Cdd:TIGR01825 160 PSYGkKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLEDKVDIQVGTLSKAIGVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 243 ACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIV 322
Cdd:TIGR01825 240 GYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVV 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1941936048 323 LGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDI 371
Cdd:TIGR01825 320 IGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDL 368
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
38-382 |
1.57e-62 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 207.99 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 38 KTYLNFASNDYLGF------GDVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSAN------ 105
Cdd:PLN02955 102 KKLLLFSGNDYLGLsshptiSNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANmaamva 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 106 -SSVIKALFQDKAAAQNS--AIFQDKLNHASLIDGAL----HCNAALVRFNHNDMNHLRSRLEKSKAQNKLIISEGVFSM 178
Cdd:PLN02955 182 iGSVASLLAASGKPLKNEkvAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSM 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 179 DGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSGACVLGSKQFIDYMLQF 258
Cdd:PLN02955 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 259 NRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKthkiavIESNTAIQPIVLGCAEQTLQAADKLKQ 338
Cdd:PLN02955 342 GRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFKALSG------VDISSPIISLVVGNQEKALKASRYLLK 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1941936048 339 QGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLVGAI 382
Cdd:PLN02955 416 SGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCL 459
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
1-379 |
3.70e-60 |
|
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: 199.57 E-value: 3.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 1 MPFD-FINTHLQARQQDALLR-----KRHV-----VQH---ATARTITVnnktylnFASNDYLGFGDVAVNLD------D 60
Cdd:TIGR01821 1 MDYDqFFNKEIDKLHLEGRYRvfadlERQAgefpfAQWhrpDGAKDVTV-------WCSNDYLGMGQHPEVLQamhetlD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 61 SQALGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALFQdkaAAQNSAIFQDKLNHASLIDGALH 140
Cdd:TIGR01821 74 KYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAK---IIPGCVIFSDELNHASMIEGIRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 141 CNAALVRFNHNDMNHLRSRLEKS-KAQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCE 219
Cdd:TIGR01821 151 SGAEKFIFRHNDVAHLEKLLQSVdPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 220 AFITQTLPDILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIAL 299
Cdd:TIGR01821 231 RDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 300 FKQLAKTHKIAVIESNTAIQPIVLGCAEQTLQAADKL-KQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHL 378
Cdd:TIGR01821 311 LKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLlNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEAL 390
|
.
gi 1941936048 379 V 379
Cdd:TIGR01821 391 L 391
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
18-379 |
4.35e-53 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 181.21 E-value: 4.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 18 LLRKRHVVQHA------TARTITVnnktylnFASNDYLGFG---DV---AVNLDDSQALGSHSSALVTGYQAQQKALEQY 85
Cdd:PRK13392 27 LEREAGRFPRArdhgpdGPRRVTI-------WCSNDYLGMGqhpDVigaMVDALDRYGAGAGGTRNISGTSHPHVLLERE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 86 LCEQFGYGAGMLFNSGFSANSSVIKALfqdKAAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKS-K 164
Cdd:PRK13392 100 LADLHGKESALLFTSGYVSNDAALSTL---GKLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVdP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 165 AQNKLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSGAC 244
Cdd:PRK13392 177 DRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 245 VLGSKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIVLG 324
Cdd:PRK13392 257 IAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVG 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1941936048 325 CAEQTLQAADKL-KQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLV 379
Cdd:PRK13392 337 DPTLCKAISDRLmSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALV 392
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
38-378 |
7.71e-44 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 155.16 E-value: 7.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 38 KTYLNFASNDYLgFGDVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYG--------AGMLFNSGFSANSSVI 109
Cdd:pfam00155 1 TDKINLGSNEYL-GDTLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANIEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 110 KALFQDKAaaqnSAIFQDKLNHASLIDGALHCNAALVRFN-------HNDMNHLRSRLEKSkaqNKLIISEGVFSMDGDT 182
Cdd:pfam00155 80 IFLLANPG----DAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK---PKVVLHTSPHNPTGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 183 AP---LKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSG---ACVLGSKQFIDYML 256
Cdd:pfam00155 153 ATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 257 QFNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIESNTAIQPIVLGCAEQTLQAADKL 336
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1941936048 337 -KQQGIWLTAIRPPTVahnTSRLRVTLtAAHTEQDITHLVKHL 378
Cdd:pfam00155 313 lEEVGVYVTPGSSPGV---PGWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
36-371 |
3.61e-43 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 156.85 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 36 NNKTY---------LNFASNDYLGFGD--------VAVNLDDSQAlGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLF 98
Cdd:PLN02483 89 NNKTLkrttktrrcLNLGSYNYLGFAAadeyctprVIESLKKYSA-STCSSRVDGGTTKLHRELEELVARFVGKPAAIVF 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 99 NSGFSANSSVIKALFqdkaaAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQ---------NKL 169
Cdd:PLN02483 168 GMGYATNSTIIPALI-----GKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEgqprthrpwKKI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 170 I-ISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLP-DILVITFGKAAASSGACVLG 247
Cdd:PLN02483 243 IvIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADvDIMMGTFTKSFGSCGGYIAG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 248 SKQFIDYMLQFNRDYTYSTAMSPLMVSHTLARIKSI------KIADDKRDKLNANIALFKQLAKTHKIAVIESN-TAIQP 320
Cdd:PLN02483 323 SKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVIlgedgtNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNdSPVMP 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1941936048 321 IVLGCAEQTLQAADKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDI 371
Cdd:PLN02483 403 IMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDL 453
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
37-379 |
6.24e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 129.71 E-value: 6.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 37 NKTYLNFASNDYLGF-GDVAVNLDDSQALGS-----HSSALVTGYQAQQKALEQYLCEQFGyGAGMLFNSGFSANSSVIK 110
Cdd:PRK07505 45 GHTFVNFVSCSYLGLdTHPAIIEGAVDALKRtgslhLSSSRTRVRSQILKDLEEALSELFG-ASVLTFTSCSAAHLGILP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 111 -----ALFQDKAAAQnsaIFqDKLNHASL--IDGALHCNAALVRFNHNDMNhlrsRLEKSKAQNK--LIISEGVFSMdGD 181
Cdd:PRK07505 124 llasgHLTGGVPPHM---VF-DKNAHASLniLKGICADETEVETIDHNDLD----ALEDICKTNKtvAYVADGVYSM-GG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 182 TAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPD--ILVITFGKA-AASSGACVLGSKQFIDYMLQF 258
Cdd:PRK07505 195 IAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVRSELDYRLNErtIIAASLGKAfGASGGVIMLGDAEQIELILRY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 259 NRDYTYStamSPLMVSHTLARIKSIKI-----ADDKRDKLNANIALFKQLAKTHKIaviESNTAIQPIVLGCAEQTLQAA 333
Cdd:PRK07505 275 AGPLAFS---QSLNVAALGAILASAEIhlseeLDQLQQKLQNNIALFDSLIPTEQS---GSFLPIRLIYIGDEDTAIKAA 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1941936048 334 DKLKQQGIWLTAIRPPTVAHNTSRLRVTLTAAHTEQDITHLVKHLV 379
Cdd:PRK07505 349 KQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLK 394
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
24-378 |
2.27e-32 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 126.78 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 24 VVQHATARTITVNNKTYLNFASNDYLGFGDVAVNLDDSQA------LGSHSSALVTGYQAQQKALEQYLCEQFGYGAGML 97
Cdd:PLN02822 95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSalekygVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 98 FNSGFSANSSVIKALfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQNK-------LI 170
Cdd:PLN02822 175 YSYGLSTIFSVIPAF-----CKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKrkkklrrYI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 171 ISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFitqTLP----DILVITFGKAAASSGACVL 246
Cdd:PLN02822 250 VVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHF---GVPiekiDIITAAMGHALATEGGFCT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 247 GSKQFIDYMLQFNRDYTYSTAMSPLMVShtlARIKSIKIADDKRD---KLNANIALF-KQLAKTHKIAvIESNTaIQPIV 322
Cdd:PLN02822 327 GSARVVDHQRLSSSGYVFSASLPPYLAS---AAITAIDVLEDNPSvlaKLKENIALLhKGLSDIPGLS-IGSNT-LSPIV 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1941936048 323 L-------GCAE---QTLQA-ADK-LKQQGIWLTA--------IRPPTvahntsRLRVTLTAAHTEQDITHLVKHL 378
Cdd:PLN02822 402 FlhlekstGSAKedlSLLEHiADRmLKEDSVLVVVskrstldkCRLPV------GIRLFVSAGHTESDILKASESL 471
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
41-378 |
7.78e-32 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 123.86 E-value: 7.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 41 LNFASNDYLGFG------DVAVNLDDSQALGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSSVIKALfq 114
Cdd:PLN03227 1 LNFATHDFLSTSssptlrQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 115 dkaAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQN-----------KLIISEGVFSMDGDTA 183
Cdd:PLN03227 79 ---AKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDvalkrkptdqrRFLVVEGLYKNTGTLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 184 PLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFG--KAAASSGACVLGSKQFIDYMLQFNRD 261
Cdd:PLN03227 156 PLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPMVHAEIVTFSleNAFGSVGGMTVGSEEVVDHQRLSGSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 262 YTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIA-LFKQLA--------KTHKIAVIESNtAIQPIVL--------- 323
Cdd:PLN03227 236 YCFSASAPPFLAKADATATAGELAGPQLLNRLHDSIAnLYSTLTnsshpyalKLRNRLVITSD-PISPIIYlrlsdqeat 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941936048 324 GCAEQTL---QAADKLKQQGIWLTAIRPPTVAHNTSR----LRVTLTAAHTEQDITHLVKHL 378
Cdd:PLN03227 315 RRTDETLildQIAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTVL 376
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
41-376 |
3.01e-30 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 119.73 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 41 LNFASNDYLGfgdVAVNLDDSQA----LGSHSSALVTGYQAQQ-----KALEQYLCEQFGYGAGMLFNSGFSANSSVIKA 111
Cdd:PRK07179 57 IILQSNDYLN---LSGHPDIIKAqiaaLQEEGDSLVMSAVFLHddspkPQFEKKLAAFTGFESCLLCQSGWAANVGLLQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 112 LfqdkaAAQNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAqnKLIISEGVFSMDGDTAPLKELLAL 191
Cdd:PRK07179 134 I-----ADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGP--GIIVVDSVYSTTGTIAPLADIVDI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 192 AKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILVITFGKAAASSGACVLGSKQFIDYMLQFNRDYTYSTAMSPL 271
Cdd:PRK07179 207 AEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPH 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 272 MVSHTLARIKSIKIADDKRDKLNAN-----IALfKQLAKThkiavIESNTAIQPIVLGCAEQTLQAADKLKQQGIWLTAI 346
Cdd:PRK07179 287 EIAGLEATLEVIESADDRRARLHANarflrEGL-SELGYN-----IRSESQIIALETGSERNTEVLRDALEERNVFGAVF 360
|
330 340 350
....*....|....*....|....*....|
gi 1941936048 347 RPPTVAHNTSRLRVTLTAAHTEQDITHLVK 376
Cdd:PRK07179 361 CAPATPKNRNLIRLSLNADLTASDLDRVLE 390
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
41-378 |
1.03e-25 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 106.79 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 41 LNFASNDYLGFGDVAVNLDDSQA-------------LGSHSSALVTGYQAQQKALEQYLCEQFGYGAGMLFNSGFSANSS 107
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLVHEVEKryrlycrqfphaqLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 108 VIKALFQDkaaaqNSAIFQDKLNHASLIDGALHCNAALVRFNHNDMNHLRSRLEKSKAQNK---LIISEGVFSMDGDTAP 184
Cdd:PRK05937 87 LCAHLSSV-----TDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFgriFIFVCSVYSFKGTLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 185 LKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFITQTLPDILViTFGKAAASSGACVLGSKQFIDYMLQFNRDYTY 264
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 265 STAMSPlmvsHTLARIKS-----IKIADDKRDKLNANIALFKQLAKTHkiavieSNTAIQPIVL-GCAEQTLQAadKLKQ 338
Cdd:PRK05937 241 STGLPP----HLLISIQVaydflSQEGELARKQLFRLKEYFAQKFSSA------APGCVQPIFLpGISEQELYS--KLVE 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1941936048 339 QGIWLTAIRPPtvahNTSRLRVTLTAAHTEQDITHLVKHL 378
Cdd:PRK05937 309 TGIRVGVVCFP----TGPFLRVNLHAFNTEDEVDILVSVL 344
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
79-249 |
9.82e-08 |
|
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: 51.23 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 79 QKALEQYLCEQFGYGA--GMLFNSGFSANSSVIKALFQDKAAAQNSAifqdkLNHAS---LIDGALHCNAALVRFNHNDM 153
Cdd:cd01494 2 LEELEEKLARLLQPGNdkAVFVPSGTGANEAALLALLGPGDEVIVDA-----NGHGSrywVAAELAGAKPVPVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 154 NHLRSR-LEKSKAQN--KLIISEGVFSMDGDTAPLKELLALAKQHNAWLMIDDAHGFGALGKTGLGSCEAFItqtlpDIL 230
Cdd:cd01494 77 GGLDVAiLEELKAKPnvALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA-----DVV 151
|
170
....*....|....*....
gi 1941936048 231 VITFGKAAASSGACVLGSK 249
Cdd:cd01494 152 TFSLHKNLGGEGGGVVIVK 170
|
|
| PTZ00125 |
PTZ00125 |
ornithine aminotransferase-like protein; Provisional |
35-259 |
8.95e-04 |
|
ornithine aminotransferase-like protein; Provisional
Pssm-ID: 240281 [Multi-domain] Cd Length: 400 Bit Score: 41.20 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 35 VNNKTYLNFASndylgfGDVAVNLDDSqalgsH---SSALVTgyQAQQKAL-------------EQYLCEQFGYGAGMLF 98
Cdd:PTZ00125 28 VEGKKYYDFLS------AYSAVNQGHC-----HpkiLAALIN--QAQKLTLtsrafyndvlglaEKYITDLFGYDKVLPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 99 NSGFSANSSVIKAL----FQDKAAAQNSAI---FQDKLNHASLidGALHCNAALVRFN-------------HNDMNHLRS 158
Cdd:PTZ00125 95 NSGAEAGETALKFArkwgYEVKGIPENQAKiifCNGNFSGRTI--GACSASTDPKCYNnfgpfvpgfelvdYNDVEALEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 159 RLEKSKAQNKLIisEGVFSMDGDTAP----LKELLALAKQHNAWLMIDDAHgfGALGKTG-LGSCEAFitQTLPDIlvIT 233
Cdd:PTZ00125 173 LLQDPNVAAFIV--EPIQGEAGVIVPddgyLKQVYELCKKYNVLLIVDEIQ--TGLGRTGkLLAHDHE--GVKPDI--VL 244
|
250 260 270
....*....|....*....|....*....|
gi 1941936048 234 FGKaAASSG----ACVLGSKqfiDYMLQFN 259
Cdd:PTZ00125 245 LGK-ALSGGlypiSAVLAND---DVMLVIK 270
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
185-378 |
7.21e-03 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 38.09 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 185 LKELLALAKQHNAWLMIDDAHG---FGALGKTGLGSCEAFitqtlPDILVI-TFGKAAASSG---ACVLGSKQFIDYMLQ 257
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAelvYDGEPPPALALLDAY-----ERVIVLrSFSKTFGLPGlriGYLIAPPEELLERLK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941936048 258 FNRDYTYSTAMSPLMVSHTLARIKSIKIADDKRDKLNANIALFKQLAKTHKIAVIesntaIQP-----IVLGCAEQT--L 330
Cdd:cd00609 229 KLLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVV-----VKPsggffLWLDLPEGDdeE 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1941936048 331 QAADKLKQQGIwltAIRPPTVAHNT--SRLRVTLtaAHTEQDITHLVKHL 378
Cdd:cd00609 304 FLERLLLEAGV---VVRPGSAFGEGgeGFVRLSF--ATPEEELEEALERL 348
|
|
| |
