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Conserved domains on  [gi|767982054|ref|XP_011535686|]
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serine palmitoyltransferase 2 isoform X1 [Homo sapiens]

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) ...
 67-435 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: 527.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 767982054 387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLG 435
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRG 367
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 67-435 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 527.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 767982054 387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLG 435
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRG 367
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 168-430 1.32e-133

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: 389.23  E-value: 1.32e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 168 KGVINMGSYNYLGFARNtGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:cd06454    1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 327
Cdd:cd06454   80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGvVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                        250       260
                 ....*....|....*....|...
gi 767982054 408 ATSLSPPVVEQIITSMKCIMGQD 430
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQGGP 253
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 136-430 5.53e-109

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: 327.78  E-value: 5.53e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 136 RPICSVPGARVDIMERQshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDK 215
Cdd:COG0156   22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 216 HEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 295
Cdd:COG0156   84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 296 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMG 375
Cdd:COG0156  164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767982054 376 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQD 430
Cdd:COG0156  234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP 288
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 149-416 1.46e-48

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: 171.45  E-value: 1.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQeAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:TIGR01821  26 LERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRP 306
Cdd:TIGR01821 105 KESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  307 wkKIlILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:TIGR01821 179 --KI-IAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGG 254

                         250       260       270
                  ....*....|....*....|....*....|
gi 767982054  387 YIGGKKELIDYLRTHSHSAVYATSLsPPVV 416
Cdd:TIGR01821 255 YIAASRKLIDAIRSYAPGFIFTTSL-PPAI 283
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
168-420 1.07e-33

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 130.12  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  168 KGVINMGSYNYLGfarntGSCQEAAAKVLEeygAGVCSTRQEIGNLDKHEELEELVARFLG--------VEAAMAYGMGF 239
Cdd:pfam00155   1 TDKINLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  240 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 311
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  312 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPTGRGVVeYFGLDPEDVDVMMGTFTKSFGASG--- 385
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767982054  386 GYIGGKKELIDYLRTHShSAVYATSLSPPVVEQII 420
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAAL 252
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 67-435 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 527.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 767982054 387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLG 435
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRG 367
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 168-430 1.32e-133

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: 389.23  E-value: 1.32e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 168 KGVINMGSYNYLGFARNtGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:cd06454    1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 327
Cdd:cd06454   80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGvVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                        250       260
                 ....*....|....*....|...
gi 767982054 408 ATSLSPPVVEQIITSMKCIMGQD 430
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQGGP 253
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 136-430 5.53e-109

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: 327.78  E-value: 5.53e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 136 RPICSVPGARVDIMERQshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDK 215
Cdd:COG0156   22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 216 HEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 295
Cdd:COG0156   84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 296 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMG 375
Cdd:COG0156  164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767982054 376 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQD 430
Cdd:COG0156  234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP 288
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 168-416 8.70e-83

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 260.48  E-value: 8.70e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 168 KGVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:PRK05958  39 RRMLNFASNDYLGLARHP-RLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdaivygQPRTRRPWkkilILVEGIYSMEGSIVRL 327
Cdd:PRK05958 118 ALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAPL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:PRK05958 188 AELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIF 267


                 ....*....
gi 767982054 408 ATSLSPPVV 416
Cdd:PRK05958 268 TTALPPAQA 276
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 115-434 3.38e-75

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 241.25  E-value: 3.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 115 YQDFENFYTRNLyMRIRDN--WN--RPICSVPGARVDIMerqshdynwsfkyTGniiKGVINMGSYNYLGFArNTGSCQE 190
Cdd:PRK06939   2 SGAFYAQLREEL-EEIKAEglYKeeRVITSPQGADITVA-------------DG---KEVINFCANNYLGLA-NHPELIA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 191 AAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGA 270
Cdd:PRK06939  64 AAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 271 RLSGATIRIFKHNNMQSLEKLLKDAIVYGQprtrrpwKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIG 350
Cdd:PRK06939 144 RLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 351 ALGPTGRGVVEYFGLDpEDVDVMMGTFTKSF-GASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKciMGQ 429
Cdd:PRK06939 217 FVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLE--LLE 293


                 ....*
gi 767982054 430 DGTSL 434
Cdd:PRK06939 294 ESDEL 298
PLN02822 PLN02822
serine palmitoyltransferase
 166-424 5.47e-57

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 196.12  E-value: 5.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 166 IIKG--VINMGSYNYLGFA---RNTGSCQEAaakvLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA 240
Cdd:PLN02822 105 IINGkdVVNFASANYLGLIgneKIKESCTSA----LEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 241 TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaIVYGQPRTRRPWKkiLILVEGIYSM 320
Cdd:PLN02822 181 TIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAENKRKKKLRR--YIVVEAIYQN 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 321 EGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRT 400
Cdd:PLN02822 258 SGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRL 337

                        250       260
                 ....*....|....*....|....
gi 767982054 401 HSHSAVYATSLSPPVVEQIITSMK 424
Cdd:PLN02822 338 SSSGYVFSASLPPYLASAAITAID 361
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 149-424 5.14e-51

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 178.12  E-value: 5.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:PRK13392  27 LEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHP-DVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdAIVYGQPRtrrp 306
Cdd:PRK13392 106 KESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLA-SVDPDRPK---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 307 wkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:PRK13392 181 ----LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGG 255

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 767982054 387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMK 424
Cdd:PRK13392 256 YIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIR 293
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 149-416 1.46e-48

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: 171.45  E-value: 1.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQeAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:TIGR01821  26 LERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRP 306
Cdd:TIGR01821 105 KESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  307 wkKIlILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:TIGR01821 179 --KI-IAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGG 254

                         250       260       270
                  ....*....|....*....|....*....|
gi 767982054  387 YIGGKKELIDYLRTHSHSAVYATSLsPPVV 416
Cdd:TIGR01821 255 YIAASRKLIDAIRSYAPGFIFTTSL-PPAI 283
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 171-413 2.45e-46

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 165.46  E-value: 2.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 171 INMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALV 250
Cdd:PLN03227   1 LNFATHDFLSTSSSP-TLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 251 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLL-----KDAIVYGQPRTRRPWkkilILVEGIYSMEGSIV 325
Cdd:PLN03227  80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 326 RLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDP-EDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHS 404
Cdd:PLN03227 156 PLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSG 235


                 ....*....
gi 767982054 405 AVYATSLSP 413
Cdd:PLN03227 236 YCFSASAPP 244
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
168-420 1.07e-33

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 130.12  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  168 KGVINMGSYNYLGfarntGSCQEAAAKVLEeygAGVCSTRQEIGNLDKHEELEELVARFLG--------VEAAMAYGMGF 239
Cdd:pfam00155   1 TDKINLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  240 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 311
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  312 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPTGRGVVeYFGLDPEDVDVMMGTFTKSFGASG--- 385
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767982054  386 GYIGGKKELIDYLRTHShSAVYATSLSPPVVEQII 420
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAAL 252
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
171-413 1.31e-27

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 113.95  E-value: 1.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 171 INMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALV 250
Cdd:PRK07179  57 IILQSNDYLNLSGHP-DIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 251 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaivYGQPrtrrpwkkiLILVEGIYSMEGSIVRLPEV 330
Cdd:PRK07179 136 DPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPG---------IIVVDSVYSTTGTIAPLADI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 331 IALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATS 410
Cdd:PRK07179 204 VDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSST 282


                 ...
gi 767982054 411 LSP 413
Cdd:PRK07179 283 LLP 285
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 177-416 6.03e-26

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 110.15  E-value: 6.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 177 NYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCL- 255
Cdd:PLN02955 111 DYLGLSSHP-TISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLl 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 256 -------------ILSDELNHASLVLGARLS----GATIRIFKHNNMQSLEKLLKDAIVygqprtrrpwKKILILVEGIY 318
Cdd:PLN02955 190 aasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KRKVVVTDSLF 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 319 SMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYL 398
Cdd:PLN02955 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338

                        250
                 ....*....|....*...
gi 767982054 399 RTHSHSAVYATSLSPPVV 416
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMA 356
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 170-413 4.15e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 103.32  E-value: 4.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 170 VINMGSYNYLGFARNTGSCQEAAAKV---LEEYG---AGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNS 243
Cdd:PRK05937   6 SIDFVTNDFLGFSRSDTLVHEVEKRYrlyCRQFPhaqLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 244 MNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLkdaivygQPRTRRPWKKILILVEGIYSMEGS 323
Cdd:PRK05937  86 GLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL-------ESCRQRSFGRIFIFVCSVYSFKGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 324 IVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdpEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSH 403
Cdd:PRK05937 159 LAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY--ENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSP 236

                        250
                 ....*....|
gi 767982054 404 SAVYATSLSP 413
Cdd:PRK05937 237 PLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 170-422 8.50e-18

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 85.03  E-value: 8.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 170 VINMGSYNYLGFaRNTGSCQEAAAKVLEEYGA-GVCSTRQEIgNLDKHEELEELVARFLGVEAAMayGMGFATNSMNIPA 248
Cdd:PRK07505  48 FVNFVSCSYLGL-DTHPAIIEGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALSELFGASVLT--FTSCSAAHLGILP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 249 LVGKGCL-------ILSDELNHASL-VLGARLS--GATIRIfKHNNMQSLEKLLKdaivygqpRTRRPwkkiLILVEGIY 318
Cdd:PRK07505 124 LLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDALEDICK--------TNKTV----AYVADGVY 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 319 SMeGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV--EYFGLDPEDVdVMMGTFTKSFGASGGYIG-GKKELI 395
Cdd:PRK07505 191 SM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERT-IIAASLGKAFGASGGVIMlGDAEQI 268

                        250       260
                 ....*....|....*....|....*..
gi 767982054 396 DYLRTHSHSAVYATSLSPPVVEQIITS 422
Cdd:PRK07505 269 ELILRYAGPLAFSQSLNVAALGAILAS 295
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 215-391 2.35e-13

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 67.79  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 215 KHEELEELVARFL--GVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHAS-LVLGARLSGATIRIFKHNNmqslekl 291
Cdd:cd01494    1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDD------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 292 LKDAIVYGQPRTRRPWKKI--LILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGAlgptgRGVVEYFGLDpED 369
Cdd:cd01494   74 AGYGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGA-----SPAPGVLIPE-GG 147

                        170       180
                 ....*....|....*....|...
gi 767982054 370 VDVMMGTFTKSFGASG-GYIGGK 391
Cdd:cd01494  148 ADVVTFSLHKNLGGEGgGVVIVK 170
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
218-397 3.49e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 48.75  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  218 ELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLG---ARLSGA---TIRIFKHNNM--QSLE 289
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELGGVqprPLDGDEAGNMdlEDLE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  290 KLLKDAIVYGQPRTRrpwkkiLILVE--------GIYSMEgsivRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVE 361
Cdd:pfam01212 116 AAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIPVHLDGARFANAAVALGVIVKE 185

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767982054  362 YFgldpEDVDVMMGTFTKSFGAS-GGYIGGKKELIDY 397
Cdd:pfam01212 186 IT----SYADSVTMCLSKGLGAPvGSVLAGSDDFIAK 218
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 214-360 7.29e-06

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: 48.01  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  214 DKHEELEELVARFLGveAAMAYGMGF---ATNSMNI------PALVGKGCLILSDELNHASLVLGARLS---GATIRIFK 281
Cdd:pfam00266  43 QAYEEAREKVAEFIN--APSNDEIIFtsgTTEAINLvalslgRSLKPGDEIVITEMEHHANLVPWQELAkrtGARVRVLP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054  282 HNNMQSLE-KLLKDAIvygQPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGA--------- 351
Cdd:pfam00266 121 LDEDGLLDlDELEKLI---TPKTK------LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHrpidvqklg 191

                         170       180
                  ....*....|....*....|
gi 767982054  352 -----------LGPTGRGVV 360
Cdd:pfam00266 192 vdflafsghklYGPTGIGVL 211
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 270-420 2.59e-05

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: 46.18  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 270 ARLSGATIRIF--KHNNMQSLEKLLKDAIVygQPRTrrpwkKILILV-----EG-IYSMEgsivRLPEVIALKKKYKAYL 341
Cdd:cd00609  100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 342 YLDEAHSigALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASG---GY-IGGKKELIDYLRthshSAVYATSLSPPVVE 417
Cdd:cd00609  169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLK----KLLPYTTSGPSTLS 242


                 ...
gi 767982054 418 QII 420
Cdd:cd00609  243 QAA 245
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 217-399 7.34e-05

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 44.63  E-value: 7.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 217 EELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLV-LGA--RLSGATIRIFKHNNMQSLEKLLK 293
Cdd:cd06502   35 AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENGKLTPEDLE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 294 DAIVYGQ----PRTRrpwkkiLILVEGiySMEGSIVRLPEVI----ALKKKYKAYLYLDEAHSIGALGPTGRGVVEYfgl 365
Cdd:cd06502  115 AAIRPRDdihfPPPS------LVSLEN--TTEGGTVYPLDELkaisALAKENGLPLHLDGARLANAAAALGVALKTY--- 183

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767982054 366 dPEDVDVMMGTFTKSFGASGGYI-GGKKELI---DYLR 399
Cdd:cd06502  184 -KSGVDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRR 220
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
199-399 8.72e-03

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 38.20  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 199 YGAGVCSTRQEignlDKHEELEELVARFLGVEAA--MAYGMGfATNSMNIPA----LVGKGCLILSDELNHASLVLG--- 269
Cdd:COG0520   48 RGAHELSAEAT----DAYEAAREKVARFIGAASPdeIIFTRG-TTEAINLVAyglgRLKPGDEILITEMEHHSNIVPwqe 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767982054 270 -ARLSGATIRIFKHN-----NMQSLEKLLKdaivygqPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYL 343
Cdd:COG0520  123 lAERTGAEVRVIPLDedgelDLEALEALLT-------PRTK------LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLV 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767982054 344 DEAHSIGalgptgrgvveYFGLD--PEDVDVMMGTFTKSFGASGgyIG---GKKELIDYLR 399
Cdd:COG0520  190 DGAQSVP-----------HLPVDvqALGCDFYAFSGHKLYGPTG--IGvlyGKRELLEALP 237
 
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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