|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
2-439 |
0e+00 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 642.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 2 FVPLYQDFENFYTRNLYMRIRDSWNRPICSVPGAKVDMMERVSHDYNWTFMYTGRVIKdVINMGSYNYLGFAQNTGICQE 81
Cdd:PLN02483 44 YAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 82 AAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSmnfl****IPALVGKGCLILSDELNHA 161
Cdd:PLN02483 123 RVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNS------TIIPALIGKGGLIISDSLNHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 162 SLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVHGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVD 241
Cdd:PLN02483 197 SIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 242 EAHSIGALGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTYSHSAVYATSLSPPVVEQIITSMK 321
Cdd:PLN02483 277 EAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 322 CIMGEDGTTSGKECVQQLAENTRYFRRQLKKMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIV 401
Cdd:PLN02483 357 VILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLL 436
|
410 420 430
....*....|....*....|....*....|....*...
gi 557326062 402 ESRARFCVSAAHTKEMLDTALKEINEVGDLLQLKYSRH 439
Cdd:PLN02483 437 LARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
59-429 |
4.02e-179 |
|
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: 504.40 E-value: 4.02e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNtGICQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSMNfl 138
Cdd:cd06454 1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqprtRRPWKKILILVEGIYSME 218
Cdd:cd06454 78 ----LSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVvEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:cd06454 146 GDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIYGNEDSPVVPLMLYMPAKIGA 378
Cdd:cd06454 225 ARGFIFSTSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 557326062 379 FGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVG 429
Cdd:cd06454 299 FSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
59-430 |
1.94e-138 |
|
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: 402.51 E-value: 1.94e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNsmnfl 138
Cdd:COG0156 37 REVLNFSSNDYLGLANHPRV-IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAAN----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqprtrRPWKKILILVEGIYSME 218
Cdd:COG0156 111 -LGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:COG0156 181 GDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIyGNEDSPVVPLMLYMPAKIGA 378
Cdd:COG0156 260 ARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALA 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 557326062 379 FGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGD 430
Cdd:COG0156 333 LADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
59-434 |
1.16e-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: 198.03 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGICQeAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATN-SMNF 137
Cdd:TIGR01821 45 KDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 138 L****IPalvgkGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqpRTRRPwkKIlILVEGIYSM 217
Cdd:TIGR01821 124 TLAKIIP-----GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP--KI-IAFESVYSM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 218 EGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRT 297
Cdd:TIGR01821 190 DGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLM-HRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 298 YSHSAVYATSLSPPVVEQIITSMKCImgedgTTSGKECVQQlAENTRYFRRQLKKMGFIIYGNeDSPVVPLMLYMPAKIG 377
Cdd:TIGR01821 269 YAPGFIFTTSLPPAIAAGATASIRHL-----KESQDLRRAH-QENVKRLKNLLEALGIPVIPN-PSHIVPVIIGDAALCK 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 557326062 378 AFGrEMLKRNIGVVV--VGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGDLLQL 434
Cdd:TIGR01821 342 KVS-DLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
59-425 |
7.78e-47 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 165.17 E-value: 7.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFaqntgiCQEAAAKVLSRYGAGvcSTRQEMGNLDKHEDLEKLVARFLG--------VESAMAYGMGF 130
Cdd:pfam00155 1 TDKINLGSNEYLGD------TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 131 ATNSMNFL****ipALVGKGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVhgqprtrrp 203
Cdd:pfam00155 73 GANIEALIF-----LLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 204 wkkiLILVEGIYSMEGSIVRLPE---VIALKKKYKSYLYVDEAHSIGALGPTGRGVVeYFGLNPEDVDIMMGTFTKSFGA 280
Cdd:pfam00155 139 ----VVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 281 AG---GYIGGKKELIDYLRTYShSAVYATSLSPPVVEQIITSMKCIMGEdgttsGKECVQQLAENTRYFRRQLKKMGFII 357
Cdd:pfam00155 214 AGwrvGYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVASE-----LEEMRQRIKERRDYLRDGLQAAGLSV 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557326062 358 YGNEdSPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIVESRARFCVsAAHTKEMLDTALKEI 425
Cdd:pfam00155 288 LPSQ-AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
2-439 |
0e+00 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 642.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 2 FVPLYQDFENFYTRNLYMRIRDSWNRPICSVPGAKVDMMERVSHDYNWTFMYTGRVIKdVINMGSYNYLGFAQNTGICQE 81
Cdd:PLN02483 44 YAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 82 AAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSmnfl****IPALVGKGCLILSDELNHA 161
Cdd:PLN02483 123 RVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNS------TIIPALIGKGGLIISDSLNHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 162 SLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVHGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVD 241
Cdd:PLN02483 197 SIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 242 EAHSIGALGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTYSHSAVYATSLSPPVVEQIITSMK 321
Cdd:PLN02483 277 EAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 322 CIMGEDGTTSGKECVQQLAENTRYFRRQLKKMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIV 401
Cdd:PLN02483 357 VILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLL 436
|
410 420 430
....*....|....*....|....*....|....*...
gi 557326062 402 ESRARFCVSAAHTKEMLDTALKEINEVGDLLQLKYSRH 439
Cdd:PLN02483 437 LARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
59-429 |
4.02e-179 |
|
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: 504.40 E-value: 4.02e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNtGICQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSMNfl 138
Cdd:cd06454 1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqprtRRPWKKILILVEGIYSME 218
Cdd:cd06454 78 ----LSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVvEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:cd06454 146 GDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIYGNEDSPVVPLMLYMPAKIGA 378
Cdd:cd06454 225 ARGFIFSTSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 557326062 379 FGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVG 429
Cdd:cd06454 299 FSDALLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
59-430 |
1.94e-138 |
|
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: 402.51 E-value: 1.94e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNsmnfl 138
Cdd:COG0156 37 REVLNFSSNDYLGLANHPRV-IEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAAN----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqprtrRPWKKILILVEGIYSME 218
Cdd:COG0156 111 -LGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:COG0156 181 GDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIyGNEDSPVVPLMLYMPAKIGA 378
Cdd:COG0156 260 ARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALA 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 557326062 379 FGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGD 430
Cdd:COG0156 333 LADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
59-434 |
5.56e-100 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 304.81 E-value: 5.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNsmnfl 138
Cdd:PRK06939 42 KEVINFCANNYLGLANHPEL-IAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDAN----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVHGQprtrrpwKKILILVEGIYSME 218
Cdd:PRK06939 116 -GGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSF-GAAGGYIGGKKELIDYLRT 297
Cdd:PRK06939 188 GDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 298 YSHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIyGNEDSPVVPLMLYMPAKIG 377
Cdd:PRK06939 267 RSRPYLFSNSLAPAIVAASIKVLELLEESD------ELRDRLWENARYFREGMTAAGFTL-GPGEHPIIPVMLGDAKLAQ 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 557326062 378 AFGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGDLLQL 434
Cdd:PRK06939 340 EFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
59-429 |
1.75e-96 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 295.53 E-value: 1.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNsmnfl 138
Cdd:PRK05958 39 RRMLNFASNDYLGLARHPRL-IAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAAN----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdaivhgQPRTRRPWkkilILVEGIYSME 218
Cdd:PRK05958 113 -LAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:PRK05958 182 GDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKCIMGEDgttsgkECVQQLAENTRYFRRQLKKMGFIIyGNEDSPVVPLMLYMPAKIGA 378
Cdd:PRK05958 262 ARPFIFTTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALA 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 557326062 379 FGREMLKRniGVVVVGF--PATPIVESRARFCVSAAHTKEMLDTALKEINEVG 429
Cdd:PRK05958 335 LAAALQEQ--GFWVGAIrpPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
59-416 |
2.43e-63 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 212.29 E-value: 2.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATnsmnfl 138
Cdd:PLN02822 109 KDVVNFASANYLGLIGNEKI-KESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLST------ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaIVHGQPRTRRPWKkiLILVEGIYSME 218
Cdd:PLN02822 182 IFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAENKRKKKLRR--YIVVEAIYQNS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 219 GSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRTY 298
Cdd:PLN02822 259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 299 SHSAVYATSLSPPVVEQIITSMKcIMGEDGTTSGKecvqqLAENTRYFRRQLKKM-GFIIYGNEDSPVVPLMLYMP---- 373
Cdd:PLN02822 339 SSGYVFSASLPPYLASAAITAID-VLEDNPSVLAK-----LKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKStgsa 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 557326062 374 ----AKIGAFGREMLKRNiGVVVVGFPATPIVESRA----RFCVSAAHTKE 416
Cdd:PLN02822 413 kedlSLLEHIADRMLKED-SVLVVVSKRSTLDKCRLpvgiRLFVSAGHTES 462
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
40-434 |
1.06e-58 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 198.15 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 40 MERVSHDYNWTFMYTGRVIKDVINMGSYNYLGFAQNTGICqEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLG 119
Cdd:PRK13392 27 LEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHPDVI-GAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 120 VESAMAYGMGFATNSmnfl****IPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdAIVHGQ 197
Cdd:PRK13392 106 KESALLFTSGYVSND------AALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLA-SVDPDR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 198 PRtrrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLnPEDVDIMMGTFTKS 277
Cdd:PRK13392 179 PK--------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 278 FGAAGGYIGGKKELIDYLRTYSHSAVYATSLSPPVVEQIITSMKCImgedgTTSGKEcVQQLAENTRYFRRQLKKMGFII 357
Cdd:PRK13392 250 FGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHL-----KTSQTE-RDAHQDRVAALKAKLNANGIPV 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557326062 358 YGNeDSPVVPLMLYMPAKIGAFGrEMLKRNIGVVV--VGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGDLLQL 434
Cdd:PRK13392 324 MPS-PSHIVPVMVGDPTLCKAIS-DRLMSEHGIYIqpINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
59-434 |
1.16e-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: 198.03 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGICQeAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATN-SMNF 137
Cdd:TIGR01821 45 KDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 138 L****IPalvgkGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivhgqpRTRRPwkKIlILVEGIYSM 217
Cdd:TIGR01821 124 TLAKIIP-----GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP--KI-IAFESVYSM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 218 EGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRT 297
Cdd:TIGR01821 190 DGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLM-HRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 298 YSHSAVYATSLSPPVVEQIITSMKCImgedgTTSGKECVQQlAENTRYFRRQLKKMGFIIYGNeDSPVVPLMLYMPAKIG 377
Cdd:TIGR01821 269 YAPGFIFTTSLPPAIAAGATASIRHL-----KESQDLRRAH-QENVKRLKNLLEALGIPVIPN-PSHIVPVIIGDAALCK 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 557326062 378 AFGrEMLKRNIGVVV--VGFPATPIVESRARFCVSAAHTKEMLDTALKEINEVGDLLQL 434
Cdd:TIGR01821 342 KVS-DLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
62-436 |
1.06e-55 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 189.73 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 62 INMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSmnfl*** 141
Cdd:PLN03227 1 LNFATHDFLSTSSSPTL-RQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTS------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 142 *IPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLL-----KDAIVHGQPRTRRPWkkilILVEGIYS 216
Cdd:PLN03227 74 TVAAFAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 217 MEGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNP-EDVDIMMGTFTKSFGAAGGYIGGKKELIDYL 295
Cdd:PLN03227 150 NTGTLAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 296 RTYSHSAVYATSlSPPVVEQIitSMKCIMGEDgttSGKECVQQLAENTRYFRRQLK----------KMGFIIYGNEDSPV 365
Cdd:PLN03227 230 RLSGSGYCFSAS-APPFLAKA--DATATAGEL---AGPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 366 VPLMLYMPAKIGAF---------GREMLKRNIGVVVVGFPATPIVESRA----RFCVSAAHTKEMLDTALKEINEVGDLL 432
Cdd:PLN03227 304 IYLRLSDQEATRRTdetlildqiAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGEAVEAI 383
|
....
gi 557326062 433 QLKY 436
Cdd:PLN03227 384 LCKI 387
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
59-425 |
7.78e-47 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 165.17 E-value: 7.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFaqntgiCQEAAAKVLSRYGAGvcSTRQEMGNLDKHEDLEKLVARFLG--------VESAMAYGMGF 130
Cdd:pfam00155 1 TDKINLGSNEYLGD------TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 131 ATNSMNFL****ipALVGKGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVhgqprtrrp 203
Cdd:pfam00155 73 GANIEALIF-----LLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 204 wkkiLILVEGIYSMEGSIVRLPE---VIALKKKYKSYLYVDEAHSIGALGPTGRGVVeYFGLNPEDVDIMMGTFTKSFGA 280
Cdd:pfam00155 139 ----VVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 281 AG---GYIGGKKELIDYLRTYShSAVYATSLSPPVVEQIITSMKCIMGEdgttsGKECVQQLAENTRYFRRQLKKMGFII 357
Cdd:pfam00155 214 AGwrvGYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVASE-----LEEMRQRIKERRDYLRDGLQAAGLSV 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557326062 358 YGNEdSPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIVESRARFCVsAAHTKEMLDTALKEI 425
Cdd:pfam00155 288 LPSQ-AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
60-431 |
5.38e-40 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 148.23 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 60 DVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNS--MNF 137
Cdd:PRK07179 55 DAIILQSNDYLNLSGHPDI-IKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVglLQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 138 L****IPALVgkgclilsDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaivHGQPrtrrpwkkiLILVEGIYSM 217
Cdd:PRK07179 134 IADPNTPVYI--------DFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPG---------IIVVDSVYST 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 218 EGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIGGKKELIDYLRT 297
Cdd:PRK07179 194 TGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITCPRELAEYVPF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 298 YSHSAVYATSLSPPVVEQIITSMKCImgedgtTSGKECVQQLAENTRYFRRQLKKMGFIIYGNedSPVVPLMLYMPAKIG 377
Cdd:PRK07179 273 VSYPAIFSSTLLPHEIAGLEATLEVI------ESADDRRARLHANARFLREGLSELGYNIRSE--SQIIALETGSERNTE 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 557326062 378 AFGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKEMLD---TALKEINEVGDL 431
Cdd:PRK07179 345 VLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDrvlEVCREARDEVDL 401
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
59-424 |
3.10e-31 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 125.17 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGIcQEAAAKVLSRYGAGVCSTRQEMGNLDKHEDLEKLVARFLGVESAMAYGMGFATNSMNFL 138
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTI-SNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 139 ****IPALVG--------KGCLILSDELNHASLVLGARLS----GATIRIFKHNNMQSLEKLLKDAIVhgqprtrrpwKK 206
Cdd:PLN02955 181 AIGSVASLLAasgkplknEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 207 ILILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLNpEDVDIMMGTFTKSFGAAGGYIG 286
Cdd:PLN02955 251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 287 GKKELIDYLRTYSHSAVYATSLSPPVVEQIITSMkcimgedgTTSGKECVQQLAENTRYfrRQLKKMGFIIYGnedSPVV 366
Cdd:PLN02955 330 CSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAV--------VVARKEKWRRKAIWERV--KEFKALSGVDIS---SPII 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557326062 367 PLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIVESRARFCVSAAHTKE---MLDTALKE 424
Cdd:PLN02955 397 SLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEdvkKLITALSS 457
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
52-310 |
4.85e-25 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 106.02 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 52 MYTGRVIKDVINmgsyNYLGFAQNTGICQEaaakVLSRYGA----------GVCSTRQEMGNLDKHEDLEKLVARFLGVE 121
Cdd:PRK05937 1 MKESLSIDFVTN----DFLGFSRSDTLVHE----VEKRYRLycrqfphaqlGYGGSRAILGPSSLLDDLEHKIAHFHGAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 122 SAMAYGMGFATNsmnfl****IPALVGKGC-LILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLkdaIVHGQprt 200
Cdd:PRK05937 73 EAFIVPSGYMAN-------LGLCAHLSSVTdYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL---ESCRQ--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 201 rRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVVEYFGLnpEDVDIMMGTFTKSFGA 280
Cdd:PRK05937 140 -RSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY--ENFYAVLVTYSKALGS 216
|
250 260 270
....*....|....*....|....*....|
gi 557326062 281 AGGYIGGKKELIDYLRTYSHSAVYATSLSP 310
Cdd:PRK05937 217 MGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
59-430 |
1.97e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 95.82 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 59 KDVINMGSYNYLGFAQNTGICqEAAAKVLSRYGA-GVCSTRQEMgNLDKHEDLEKLV-----ARFLGVESAMAYGMGfat 132
Cdd:PRK07505 46 HTFVNFVSCSYLGLDTHPAII-EGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALselfgASVLTFTSCSAAHLG--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 133 nsmnfl****IPaLVGKGCL-------ILSDELNHASL-VLGARLS--GATIRIfKHNNMQSLEKLLKdaivhgqpRTRR 202
Cdd:PRK07505 121 ---------ILP-LLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDALEDICK--------TNKT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 203 PwkkiLILVEGIYSMeGSIVRLPEVIALKKKYKSYLYVDEAHSIGALGPTGRGVV--EYFGLNPEDVdIMMGTFTKSFGA 280
Cdd:PRK07505 182 V----AYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERT-IIAASLGKAFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 281 AGGYIG-GKKELIDYLRTYSHSAVYATSLSPPVVEQIITSMKCIMGEDGTtsgkECVQQLAENTRYF--------RRQLK 351
Cdd:PRK07505 256 SGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELD----QLQQKLQNNIALFdslipteqSGSFL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 352 KMGFIIYGNEDSPVvplmlympakigAFGREMLKRNIGVVVVGFPATPivESRA--RFCVSAAHTKEMLDTALKEINEVG 429
Cdd:PRK07505 332 PIRLIYIGDEDTAI------------KAAKQLLDRGFYTSPVFFPVVA--KGRAglRIMFRASHTNDEIKRLCSLLKEIL 397
|
.
gi 557326062 430 D 430
Cdd:PRK07505 398 D 398
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
106-288 |
4.26e-11 |
|
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: 61.24 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 106 KHEDLEKLVARFL--GVESAMAYGMGFATNSMNFL****ipALVGKGCLILSDELNHAS-LVLGARLSGATIRIFKHNNm 182
Cdd:cd01494 1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALL------ALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 183 qsleklLKDAIVHGQPRTRRPWKKI--LILVEGIYSMEGSIVRLPEVIALKKKYKSYLYVDEAHSIGAlgptgRGVVEYF 260
Cdd:cd01494 74 ------AGYGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGA-----SPAPGVL 142
|
170 180
....*....|....*....|....*....
gi 557326062 261 GLNpEDVDIMMGTFTKSFGAAG-GYIGGK 288
Cdd:cd01494 143 IPE-GGADVVTFSLHKNLGGEGgGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
167-427 |
1.55e-09 |
|
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: 59.28 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 167 ARLSGATIRIF--KHNNMQSLEKLLKDAIVhgQPRTrrpwkKILILV-----EG-IYSMEgsivRLPEVIALKKKYKSYL 238
Cdd:cd00609 100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 239 YVDEAHSigALGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAAG---GY-IGGKKELIDYLRtyshSAVYATSLSPPVVE 314
Cdd:cd00609 169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLK----KLLPYTTSGPSTLS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 315 QIITSmkcIMGEDGTTSGKECVQQLAENTRYFRRQLKKMGFIIygnedsPVVP-----LMLYMPAKIGA-FGREMLKRNI 388
Cdd:cd00609 243 QAAAA---AALDDGEEHLEELRERYRRRRDALLEALKELGPLV------VVKPsggffLWLDLPEGDDEeFLERLLLEAG 313
|
250 260 270
....*....|....*....|....*....|....*....
gi 557326062 389 GVVVVGFPATPIVESRARFCVsaAHTKEMLDTALKEINE 427
Cdd:cd00609 314 VVVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
81-257 |
6.56e-07 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 51.09 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 81 EAAAKVLSRYGAGVCSTRQEMGNL--DKHEDLEKLVARFLGVESAmaYGMGF---ATNSMNFL****IPALVGKGCLILS 155
Cdd:pfam00266 17 DAIQEYYTDYNGNVHRGVHTLGKEatQAYEEAREKVAEFINAPSN--DEIIFtsgTTEAINLVALSLGRSLKPGDEIVIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 156 DELNHASLVLGARLS---GATIRIFKHNNMQSLE-KLLKDAIvhgQPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALK 231
Cdd:pfam00266 95 EMEHHANLVPWQELAkrtGARVRVLPLDEDGLLDlDELEKLI---TPKTK------LVAITHVSNVTGTIQPVPEIGKLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 557326062 232 KKYKSYLYVDEAHSIGA--------------------LGPTGRGVV 257
Cdd:pfam00266 166 HQYGALVLVDAAQAIGHrpidvqklgvdflafsghklYGPTGIGVL 211
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
100-352 |
6.71e-04 |
|
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: 41.47 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 100 EMGNLDKHE----DLEKLVARFLGVESAMaygmgFATNSMNFL****IPALVGKGCLILSDELNHASLVLGARLSGAT-- 173
Cdd:cd00615 50 GLDDLLDPTgpikEAQELAARAFGAKHTF-----FLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVpv 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 174 ---------IRIFKHNNMQSLEKLLKDAivhgqprtrrPWKKILILVEGIYsmEGSIVRLPEVIALKKKYKSYLYVDEAH 244
Cdd:cd00615 125 ylkpernpyYGIAGGIPPETFKKALIEH----------PDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 245 siGAlgptgrgvveYFGLNPE--------DVDI-------MMGTFTKsfgaaGGYIGGKKELIDYLRtYSHSAVYATSLS 309
Cdd:cd00615 193 --GA----------HFRFHPIlpssaamaGADIvvqsthkTLPALTQ-----GSMIHVKGDLVNPDR-VNEALNLHQSTS 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 557326062 310 PPVveQIITSMKC---IMGEdgttSGKECVQQLAENTRYFRRQLKK 352
Cdd:cd00615 255 PSY--LILASLDVaraMMAL----EGKELVEELIELALYARQEINK 294
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
92-344 |
1.51e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 40.95 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 92 AGVCSTRQEMGNLDKHE----DLEKLVARFLGVESAMaygmgFATNSMNFL****IPALVGKGCLILSDELNHASLVLGA 167
Cdd:pfam01276 49 IDVCIEDVELGDLLDHEgaikEAQKYAARVFGADKSY-----FVVNGTSGSNKTVGMAVCTPGDTILIDRNCHKSIHHAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 168 RLSGAT------------------IRIFKHnnmQSLEKLLKDAivhgqPRTRrpWKKILILVEGIYsmEGSIVRLPEVIA 229
Cdd:pfam01276 124 MLSGATpvylepsrnaygiiggipLHEFQE---ETLKEAIAEV-----PDAK--GPRLAVITNPTY--DGVLYNAKEIVD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557326062 230 LKKKYKSYLYVDEAHSIGA-LGPTGRGVVEYFGLNPEDVDIMMGTFTKSFGAA---GGYIGGKKELIdylrtYSHSAV-- 303
Cdd:pfam01276 192 TLHHLSDPILFDSAWVGYEqFIPIYADASPMGGENENGPGIFVTQSVHKLLAAlsqASYIHKKEGHI-----VNHDRFne 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 557326062 304 -----YATSLSPPVVEQIITSMKCIMGEDGTTSGKECVqQLAENTR 344
Cdd:pfam01276 267 afmmhATTSPSYPIFASLDVAAKMLEGNSGRRLWNECV-ERAIEFR 311
|
|
|