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Conserved domains on  [gi|557326062|ref|XP_006036023|]
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LOW QUALITY PROTEIN: serine palmitoyltransferase 2, partial [Alligator sinensis]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 2-439 0e+00

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).


The actual alignment was detected with superfamily member PLN02483:

Pssm-ID: 450240 [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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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