|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 538.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 1 MSWQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVS 80
Cdd:PRK05958 1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 81 GYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLAR 160
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 161 LLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCW---LQKVKPELLVVTFGKG 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAeagLAGEPDVILVGTLGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 238 FGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSC 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMDSQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1DJ9_A 318 SAIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLHG 382
Cdd:PRK05958 319 SAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAE 383
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
24-381 |
1.92e-176 |
|
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: 495.25 E-value: 1.92e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 24 YPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRAL 103
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 104 LFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPC-PGQQMVVTEGVFSMDG 182
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRgERRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 183 DSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPE---LLVVTFGKGFGVSGAAVLCSSTVADYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 260 RHLIYSTSMPPAQAQALRASLAVIRsdEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
1DJ9_A 340 QQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:TIGR00858 319 QQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-381 |
2.15e-173 |
|
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: 488.41 E-value: 2.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 3 WQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGY 82
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 83 SVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLL 162
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 163 A-SPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPE--LLVVTFGKGFG 239
Cdd:COG0156 161 KkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 240 VSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSCSA 319
Cdd:COG0156 241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREE--PELRERLWENIAYFREGLKELGFDLGPSESP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
1DJ9_A 320 IQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:COG0156 319 IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALA 380
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
39-384 |
3.07e-151 |
|
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: 430.83 E-value: 3.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 39 RQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAA 118
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 119 MMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASP--CPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQ 196
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 197 HNGWLMVDDAHGTGVIGEQGRGSC--WLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQ 274
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEefGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 275 ALRASLAVIRSdeGDARREKLAALITRFRAGVQDLPFTLADSCS-AIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTV 353
Cdd:cd06454 241 AALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPShIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
1DJ9_A 354 PAGIARLRLTLTAAHEMQDIDRLLEVLHGNG 384
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-380 |
1.54e-63 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 206.77 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 42 LNFSSNDYLGLshhpQIIRAWQQGAEqfgIGSGGSGHVSGYSVVHQALEEELAEWLGYS--------RALLFISGFAANQ 113
Cdd:pfam00155 4 INLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 114 AVIAAMMA-KEDRIAADRLSHASLLEAASLSPSQLRRFA-------HNDVTHLARLLASPCpgqQMVVTEGVFSMDGDSA 185
Cdd:pfam00155 77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 186 PLAEIQQV---TQQHNGWLMVDDAHGTGVIGEQGRGS--CWLQKVKPELLVVTFGKGFGVSG---AAVLCSSTVADYLLQ 257
Cdd:pfam00155 154 TLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVAtrALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 258 FARHLIYSTSMPPAQAQALRASLAVIrsDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEK 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
1DJ9_A 338 LRQQ-GCWVTGIRPPTVPagiARLRLTLtAAHEMQDIDRLLEVL 380
Cdd:pfam00155 312 LLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
1-382 |
0e+00 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 538.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 1 MSWQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVS 80
Cdd:PRK05958 1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 81 GYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLAR 160
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 161 LLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCW---LQKVKPELLVVTFGKG 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAeagLAGEPDVILVGTLGKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 238 FGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSC 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMDSQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1DJ9_A 318 SAIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLHG 382
Cdd:PRK05958 319 SAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAE 383
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
24-381 |
1.92e-176 |
|
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: 495.25 E-value: 1.92e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 24 YPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRAL 103
Cdd:TIGR00858 1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 104 LFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPC-PGQQMVVTEGVFSMDG 182
Cdd:TIGR00858 81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRgERRKLIVTDGVFSMDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 183 DSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPE---LLVVTFGKGFGVSGAAVLCSSTVADYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 260 RHLIYSTSMPPAQAQALRASLAVIRsdEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
1DJ9_A 340 QQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:TIGR00858 319 QQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
3-381 |
2.15e-173 |
|
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: 488.41 E-value: 2.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 3 WQEKINAALDARGAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGY 82
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 83 SVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLL 162
Cdd:COG0156 81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 163 A-SPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPE--LLVVTFGKGFG 239
Cdd:COG0156 161 KkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 240 VSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSCSA 319
Cdd:COG0156 241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREE--PELRERLWENIAYFREGLKELGFDLGPSESP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
1DJ9_A 320 IQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:COG0156 319 IVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALA 380
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
39-384 |
3.07e-151 |
|
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: 430.83 E-value: 3.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 39 RQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAA 118
Cdd:cd06454 1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 119 MMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASP--CPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQ 196
Cdd:cd06454 81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 197 HNGWLMVDDAHGTGVIGEQGRGSC--WLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQ 274
Cdd:cd06454 161 YGAILFVDEAHSVGVYGPHGRGVEefGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 275 ALRASLAVIRSdeGDARREKLAALITRFRAGVQDLPFTLADSCS-AIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTV 353
Cdd:cd06454 241 AALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPShIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
1DJ9_A 354 PAGIARLRLTLTAAHEMQDIDRLLEVLHGNG 384
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
27-379 |
8.85e-84 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 260.51 E-value: 8.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 27 AQGAgRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFI 106
Cdd:PRK06939 31 PQGA-DITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 107 SGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHL-ARLLASPCPGQQ--MVVTEGVFSMDGD 183
Cdd:PRK06939 110 SCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLeAQLKEAKEAGARhkLIATDGVFSMDGD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 184 SAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKV--KPELLVVTFGKGF-GVSGAAVLCSSTVADYLLQFAR 260
Cdd:PRK06939 190 IAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVmdRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 261 HLIYSTSMPPAQAqalRASLAVIRS-DEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLR 339
Cdd:PRK06939 270 PYLFSNSLAPAIV---AASIKVLELlEESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLL 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
1DJ9_A 340 QQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEV 379
Cdd:PRK06939 347 EEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386
|
|
| gly_Cac_T_rel |
TIGR01825 |
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ... |
27-379 |
3.23e-80 |
|
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: 250.89 E-value: 3.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 27 AQGAgrWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFI 106
Cdd:TIGR01825 23 AQGP--RVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLAKFKKTEAALVFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 107 SGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLL-ASPCPGQQMVVTEGVFSMDGDSA 185
Cdd:TIGR01825 101 SGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLrENPSYGKKLIVTDGVFSMDGDVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 186 PLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSC---WLQKvKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHL 262
Cdd:TIGR01825 181 PLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVhhfGLED-KVDIQVGTLSKAIGVVGGYAAGHKELIEYLKNRARPF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 263 IYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQG 342
Cdd:TIGR01825 260 LFSTAQPPAVVAALAAAVDELQRS--PELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVIGDEKAAQEFSRRLFDEG 337
|
330 340 350
....*....|....*....|....*....|....*..
1DJ9_A 343 CWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEV 379
Cdd:TIGR01825 338 IFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDA 374
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-380 |
1.54e-63 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 206.77 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 42 LNFSSNDYLGLshhpQIIRAWQQGAEqfgIGSGGSGHVSGYSVVHQALEEELAEWLGYS--------RALLFISGFAANQ 113
Cdd:pfam00155 4 INLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 114 AVIAAMMA-KEDRIAADRLSHASLLEAASLSPSQLRRFA-------HNDVTHLARLLASPCpgqQMVVTEGVFSMDGDSA 185
Cdd:pfam00155 77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 186 PLAEIQQV---TQQHNGWLMVDDAHGTGVIGEQGRGS--CWLQKVKPELLVVTFGKGFGVSG---AAVLCSSTVADYLLQ 257
Cdd:pfam00155 154 TLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDAVAtrALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 258 FARHLIYSTSMPPAQAQALRASLAVIrsDEGDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEK 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
1DJ9_A 338 LRQQ-GCWVTGIRPPTVPagiARLRLTLtAAHEMQDIDRLLEVL 380
Cdd:pfam00155 312 LLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
39-380 |
2.69e-60 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 202.21 E-value: 2.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 39 RQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAA 118
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 119 MMA------------KEDRIA--ADRLSHASLLEAASLSPSQ----LRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSM 180
Cdd:PLN02955 182 IGSvasllaasgkplKNEKVAifSDALNHASIIDGVRLAERQgnveVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSM 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 181 DGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRG-----SCwlqKVKPELLVVTFGKGFGVSGAAVLCSSTVADYL 255
Cdd:PLN02955 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGvaeefNC---EADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 256 LQFARHLIYSTSMPPAQAQALRASLAVIRSDEGdaRREKLAALITRFRAgvqdlpFTLADSCSAIQPLIVGDNSRALQLA 335
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKW--RRKAIWERVKEFKA------LSGVDISSPIISLVVGNQEKALKAS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
1DJ9_A 336 EKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVL 380
Cdd:PLN02955 411 RYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
20-381 |
1.06e-58 |
|
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: 195.72 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 20 LRRRYPVAQgagrWLVADDRQYLN-FSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLG 98
Cdd:TIGR01821 29 QAGEFPFAQ----WHRPDGAKDVTvWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 99 YSRALLFISGFAANQAVIA--AMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQ-QMVVTE 175
Cdd:TIGR01821 105 KESALVFTSGYVANDATLAtlAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRpKIIAFE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 176 GVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVV--TFGKGFGVSGAAVLCSSTVAD 253
Cdd:TIGR01821 185 SVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIegTLAKAFGVVGGYIAASRKLID 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 254 YLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEgdARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQ 333
Cdd:TIGR01821 265 AIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKK 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
1DJ9_A 334 LAEKL-RQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:TIGR01821 343 VSDLLlNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALL 391
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
20-380 |
1.35e-57 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 193.15 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 20 LRRRYPVAqgagRWLVAD-DRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLG 98
Cdd:PRK13392 30 EAGRFPRA----RDHGPDgPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 99 YSRALLFISGFAANQAVIAAMMAKEDR--IAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQ-QMVVTE 175
Cdd:PRK13392 106 KESALLFTSGYVSNDAALSTLGKLLPGcvILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRpKLIAFE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 176 GVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVV--TFGKGFGVSGAAVLCSSTVAD 253
Cdd:PRK13392 186 SVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIqgTLAKAFGCLGGYIAASADLID 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 254 YLLQFARHLIYSTSMPPAQAQALRASLAVIRSDegDARREKLAALITRFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQ 333
Cdd:PRK13392 266 FVRSFAPGFIFTTALPPAVAAGATAAIRHLKTS--QTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKA 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
1DJ9_A 334 LAEKL-RQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVL 380
Cdd:PRK13392 344 ISDRLmSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAAL 391
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
39-380 |
1.13e-51 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 179.57 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 39 RQYLNFSSNDYLGLSHH-----PQIIrawqQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQ 113
Cdd:PLN02483 100 RRCLNLGSYNYLGFAAAdeyctPRVI----ESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 114 AVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQ----------MVVTEGVFSMDGD 183
Cdd:PLN02483 176 TIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrpwkkiIVIVEGIYSMEGE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 184 SAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKP---ELLVVTFGKGFGVSGAAVLCSSTVADYLLQFAR 260
Cdd:PLN02483 256 LCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPadvDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCP 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 261 HLIYSTSMPPAQAQALRASLAVIRSDEGDAR-REKLAALITR---FRAGVQDLPF-TLADSCSAIQPLIVGDNSRALQLA 335
Cdd:PLN02483 336 AHLYATSMSPPAVQQVISAIKVILGEDGTNRgAQKLAQIRENsnfFRSELQKMGFeVLGDNDSPVMPIMLYNPAKIPAFS 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
1DJ9_A 336 EKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVL 380
Cdd:PLN02483 416 RECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVI 460
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
42-381 |
3.96e-47 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 165.57 E-value: 3.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 42 LNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMA 121
Cdd:PRK07179 57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 122 KEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGqqMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWL 201
Cdd:PRK07179 137 PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG--IIVVDSVYSTTGTIAPLADIVDIAEEFGCVL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 202 MVDDAHGTGVIGEQGRGSCwlqkvkPEL--------LVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQA 273
Cdd:PRK07179 215 VVDESHSLGTHGPQGAGLV------AELgltsrvhfITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 274 QALRASLAVIRSdeGDARREKLAALITRFRAGVQDLPFTLAdSCSAIQPLIVGDNSRALQLAEKLRQQGcwVTG---IRP 350
Cdd:PRK07179 289 AGLEATLEVIES--ADDRRARLHANARFLREGLSELGYNIR-SESQIIALETGSERNTEVLRDALEERN--VFGavfCAP 363
|
330 340 350
....*....|....*....|....*....|.
1DJ9_A 351 PTvPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:PRK07179 364 AT-PKNRNLIRLSLNADLTASDLDRVLEVCR 393
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
3-381 |
2.77e-44 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 157.83 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 3 WQEKI----NAALDArgAADALRRRYPVAQGAGRWLVADD-RQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSG 77
Cdd:PRK07505 7 NNKKRinraEKFWDA--AYDEGLNGLTVGEREGILITLADgHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 78 HVSGYSVVHQALEEELAEWLGySRALLFISGFAANQAV---IAAMMAKEDR---IAADRLSHASL--LEAASLSPSQLRR 149
Cdd:PRK07505 85 RTRVRSQILKDLEEALSELFG-ASVLTFTSCSAAHLGIlplLASGHLTGGVpphMVFDKNAHASLniLKGICADETEVET 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 150 FAHNDVTHLARLlaspCPGQQMV--VTEGVFSMdGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRG---SCWLQK 224
Cdd:PRK07505 164 IDHNDLDALEDI----CKTNKTVayVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvrSELDYR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 225 VKPELLVVT-FGKGFGVSGAAVLCSST-VADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRF 302
Cdd:PRK07505 239 LNERTIIAAsLGKAFGASGGVIMLGDAeQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DJ9_A 303 RagvQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTGIRPPTVPAGIARLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:PRK07505 319 D---SLIPTEQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLK 394
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
42-380 |
1.70e-37 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 139.27 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 42 LNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMA 121
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 122 KEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLAS----------PCPGQ-QMVVTEGVFSMDGDSAPLAEI 190
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQrRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 191 QQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKP--ELLVVTFG--KGFGVSGAAVLCSSTVADYLLQFARHLIYST 266
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSleNAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 267 SMPPAQAQALRASLAVIRSDE------GDARREKLAALITR---FRAGVQDLPFTLADSCSAIQPLIVGD--NSRAL--- 332
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPqllnrlHDSIANLYSTLTNSshpYALKLRNRLVITSDPISPIIYLRLSDqeATRRTdet 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
1DJ9_A 333 ----QLAEKLRQQGCWV--TGIRPPTVPAGIAR--LRLTLTAAHEMQDIDRLLEVL 380
Cdd:PLN03227 321 lildQIAHHSLSEGVAVvsTGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTVL 376
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
42-381 |
1.51e-34 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 131.06 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 42 LNFSSNDYLGLSHHPQIIRA----WQQGAEQFGIGSGGSGHVSGYS---VVHQALEEELAEWLGYSRALLFISGFAANQA 114
Cdd:PRK05937 7 IDFVTNDFLGFSRSDTLVHEvekrYRLYCRQFPHAQLGYGGSRAILgpsSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 115 VIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLAS---PCPGQQMVVTEGVFSMDGDSAPLAEIQ 191
Cdd:PRK05937 87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEScrqRSFGRIFIFVCSVYSFKGTLAPLEQII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 192 QVTQQHNGWLMVDDAHGTGVIGEQGRGSCwlQKVKPE---LLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSM 268
Cdd:PRK05937 167 ALSKKYHAHLIVDEAHAMGIFGDDGKGFC--HSLGYEnfyAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 269 PPAQAQALRASLAVIrSDEGDARREKLAALITRFRAgvqdlPFTLADSCsAIQPLIVGDNSRALqLAEKLRQQGCWVTGI 348
Cdd:PRK05937 245 PPHLLISIQVAYDFL-SQEGELARKQLFRLKEYFAQ-----KFSSAAPG-CVQPIFLPGISEQE-LYSKLVETGIRVGVV 316
|
330 340 350
....*....|....*....|....*....|...
1DJ9_A 349 RPPTVPAgiarLRLTLTAAHEMQDIDRLLEVLH 381
Cdd:PRK05937 317 CFPTGPF----LRVNLHAFNTEDEVDILVSVLA 345
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
17-380 |
9.73e-26 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 107.90 E-value: 9.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 17 ADALRRRYPVAQGA-GRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAE 95
Cdd:PLN02822 86 TEEMRPEPPVLESAaGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 96 WLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPG------- 168
Cdd:PLN02822 166 FLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEnkrkkkl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 169 QQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPE---LLVVTFGKGFGVSGAAV 245
Cdd:PLN02822 246 RRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkidIITAAMGHALATEGGFC 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 246 LCSSTVADYLLQFARHLIYSTSMPPAQAQAlrASLAVIRSDEGDARREKLAALITRFRAGVQDLPfTLADSCSAIQPLI- 324
Cdd:PLN02822 326 TGSARVVDHQRLSSSGYVFSASLPPYLASA--AITAIDVLEDNPSVLAKLKENIALLHKGLSDIP-GLSIGSNTLSPIVf 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1DJ9_A 325 ------VGDNSRALQLAEK-----LRQQGCWVTGIRPPTV-----PAGIarlRLTLTAAHEMQDIDRLLEVL 380
Cdd:PLN02822 403 lhleksTGSAKEDLSLLEHiadrmLKEDSVLVVVSKRSTLdkcrlPVGI---RLFVSAGHTESDILKASESL 471
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
89-247 |
8.47e-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: 51.61 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 89 LEEELAEWL------GYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLL 162
Cdd:cd01494 1 KLEELEEKLarllqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 163 ASPCPGQQ------MVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHgtgVIGEQGRGSCWLQKVKPELLVVTFGK 236
Cdd:cd01494 81 VAILEELKakpnvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAAS---AGGASPAPGVLIPEGGADVVTFSLHK 157
|
170
....*....|.
1DJ9_A 237 GFGVSGAAVLC 247
Cdd:cd01494 158 NLGGEGGGVVI 168
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
86-381 |
1.47e-04 |
|
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: 43.48 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 86 HQALEEELAEWLGYSRA--------LLFISGFAANQAVIAAMMAKEDRIAADRLS---HASLLEAASLSPSQLRRFAHN- 153
Cdd:cd00609 38 LPELREAIAEWLGRRGGvdvppeeiVVTNGAQEALSLLLRALLNPGDEVLVPDPTypgYEAAARLAGAEVVPVPLDEEGg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 154 DVTHLARLLASPCPGQQMVV-------TEGVFSMDGdsapLAEIQQVTQQHNGWLMVDDAHGtGVIGEQGRGSCWLQKVK 226
Cdd:cd00609 118 FLLDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 227 PELLVV--TFGKGFGVSG---AAVLCSStvADYLLQFARHLIYSTSMPPAQAQAlrASLAVIRSDEG--DARREKLAALI 299
Cdd:cd00609 193 YERVIVlrSFSKTFGLPGlriGYLIAPP--EELLERLKKLLPYTTSGPSTLSQA--AAAAALDDGEEhlEELRERYRRRR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DJ9_A 300 TRFRAGVQDLPFTLADSCSA-----IQpliVGDNSRALQLAEKLRQQGcwvTGIRPPTV--PAGIARLRLTLTAAHEmqD 372
Cdd:cd00609 269 DALLEALKELGPLVVVKPSGgfflwLD---LPEGDDEEFLERLLLEAG---VVVRPGSAfgEGGEGFVRLSFATPEE--E 340
|
....*....
1DJ9_A 373 IDRLLEVLH 381
Cdd:cd00609 341 LEEALERLA 349
|
|
| |
