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Conserved domains on  [gi|4758668|ref|NP_004854|]
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serine palmitoyltransferase 2 [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) ...
 67-542 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: 683.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDS 466
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758668   467 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 542
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 67-542 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 683.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDS 466
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758668   467 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 542
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 168-532 0e+00

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: 515.96  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  168 KGVINMGSYNYLGFARNtGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:cd06454   1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 327
Cdd:cd06454  80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGvVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  408 ATSLSPPVVEQIITSMKCIMGqdgtslGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREML 487
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 4758668  488 KRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVG 532
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 136-533 2.23e-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: 406.36  E-value: 2.23e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  136 RPICSVPGARVDIMERQshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDK 215
Cdd:COG0156  22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  216 HEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 295
Cdd:COG0156  84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  296 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMG 375
Cdd:COG0156 164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  376 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDgtslgkECVQQLAENTRYFRRRLKE 455
Cdd:COG0156 234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKE 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758668  456 MGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGD 533
Cdd:COG0156 308 LGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 149-537 5.48e-56

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: 193.41  E-value: 5.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQeAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:TIGR01821  26 LERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRP 306
Cdd:TIGR01821 105 KESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    307 wkKIlILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:TIGR01821 179 --KI-IAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGG 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMgqdgTSLGKECVQQlaENTRYFRRRLKEMGFIIYGNeDS 466
Cdd:TIGR01821 255 YIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIPN-PS 327

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758668    467 PVVPLMLYMPAKIGAFGrEMLKRNIGVVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 537
Cdd:TIGR01821 328 HIVPVIIGDAALCKKVS-DLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
168-528 2.44e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    168 KGVINMGSYNYLGfarntGSCQEAAAKVLEeygAGVCSTRQEIGNLDKHEELEELVARFLG--------VEAAMAYGMGF 239
Cdd:pfam00155   1 TDKINLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    240 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 311
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    312 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPTGRGVVeYFGLDPEDVDVMMGTFTKSFGASG--- 385
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    386 GYIGGKKELIDYLRTHShSAVYATSLSPPVVEQIITSmkcimGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEd 465
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSD-----PLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758668    466 SPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIIESRARFCLsAAHTKEILDTALKEI 528
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 67-542 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 683.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    67 PMLVAVLTYVGYGVLTLFGYLRDFLRywRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARV 146
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   147 DIMERQSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARF 226
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   227 LGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 306
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   307 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGG 386
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDS 466
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758668   467 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 542
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 168-532 0e+00

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: 515.96  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  168 KGVINMGSYNYLGFARNtGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:cd06454   1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 327
Cdd:cd06454  80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGvVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  408 ATSLSPPVVEQIITSMKCIMGqdgtslGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREML 487
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 4758668  488 KRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVG 532
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 136-533 2.23e-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: 406.36  E-value: 2.23e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  136 RPICSVPGARVDIMERQshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDK 215
Cdd:COG0156  22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  216 HEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 295
Cdd:COG0156  84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  296 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMG 375
Cdd:COG0156 164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  376 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDgtslgkECVQQLAENTRYFRRRLKE 455
Cdd:COG0156 234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKE 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758668  456 MGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGD 533
Cdd:COG0156 308 LGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 115-537 1.33e-102

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 314.83  E-value: 1.33e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   115 YQDFENFYTRNLyMRIRDN--WN--RPICSVPGARVDIMerqshdynwsfkyTGniiKGVINMGSYNYLGFArNTGSCQE 190
Cdd:PRK06939   2 SGAFYAQLREEL-EEIKAEglYKeeRVITSPQGADITVA-------------DG---KEVINFCANNYLGLA-NHPELIA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   191 AAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGA 270
Cdd:PRK06939  64 AAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   271 RLSGATIRIFKHNNMQSLEKLLKDAIVYGQprtrrpwKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIG 350
Cdd:PRK06939 144 RLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   351 ALGPTGRGVVEYFGLDpEDVDVMMGTFTKSF-GASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKciMGQ 429
Cdd:PRK06939 217 FVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLE--LLE 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   430 DGTSLgkecVQQLAENTRYFRRRLKEMGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRAR 509
Cdd:PRK06939 294 ESDEL----RDRLWENARYFREGMTAAGFTL-GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIR 368

                        410       420
                 ....*....|....*....|....*...
gi 4758668   510 FCLSAAHTKEILDTALKEIDEVGDLLQL 537
Cdd:PRK06939 369 TQMSAAHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 168-532 4.18e-96

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 297.84  E-value: 4.18e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   168 KGVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIP 247
Cdd:PRK05958  39 RRMLNFASNDYLGLARHP-RLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   248 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdaivygQPRTRRPWkkilILVEGIYSMEGSIVRL 327
Cdd:PRK05958 118 ALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAPL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   328 PEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 407
Cdd:PRK05958 188 AELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIF 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   408 ATSLSPPVVEQIITSMKCIMGQDgtslgkECVQQLAENTRYFRRRLKEMGFIIyGNEDSPVVPLMLYMPAKIGAFGREML 487
Cdd:PRK05958 268 TTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALALAAALQ 340

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 4758668   488 KRniGVVVVGF--PATPIIESRARFCLSAAHTKEILDTALKEIDEVG 532
Cdd:PRK05958 341 EQ--GFWVGAIrpPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
PLN02822 PLN02822
serine palmitoyltransferase
 166-521 2.27e-61

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 209.98  E-value: 2.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   166 IIKG--VINMGSYNYLGFA---RNTGSCQEAaakvLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA 240
Cdd:PLN02822 105 IINGkdVVNFASANYLGLIgneKIKESCTSA----LEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   241 TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaIVYGQPRTRRPWKkiLILVEGIYSM 320
Cdd:PLN02822 181 TIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAENKRKKKLRR--YIVVEAIYQN 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   321 EGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRT 400
Cdd:PLN02822 258 SGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRL 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   401 HSHSAVYATSLSPPVVEQIITSMKcIMGQDGTSLGKecvqqLAENTRYFRRRLKEM-GFIIYGNEDSPVVPLMLYMP--- 476
Cdd:PLN02822 338 SSSGYVFSASLPPYLASAAITAID-VLEDNPSVLAK-----LKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKStgs 411

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4758668   477 -----AKIGAFGREMLKRNiGVVVVGFPATPIIESRA----RFCLSAAHT-KEIL 521
Cdd:PLN02822 412 akedlSLLEHIADRMLKED-SVLVVVSKRSTLDKCRLpvgiRLFVSAGHTeSDIL 465
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 149-537 5.48e-56

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: 193.41  E-value: 5.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQeAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:TIGR01821  26 LERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQ-AMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRP 306
Cdd:TIGR01821 105 KESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    307 wkKIlILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:TIGR01821 179 --KI-IAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGG 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMgqdgTSLGKECVQQlaENTRYFRRRLKEMGFIIYGNeDS 466
Cdd:TIGR01821 255 YIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIPN-PS 327

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758668    467 PVVPLMLYMPAKIGAFGrEMLKRNIGVVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 537
Cdd:TIGR01821 328 HIVPVIIGDAALCKKVS-DLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 149-537 8.78e-56

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 193.15  E-value: 8.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   149 MERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLG 228
Cdd:PRK13392  27 LEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHP-DVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   229 VEAAMAYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdAIVYGQPRtrrp 306
Cdd:PRK13392 106 KESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLA-SVDPDRPK---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   307 wkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdPEDVDVMMGTFTKSFGASGG 386
Cdd:PRK13392 181 ----LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   387 YIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCiMGQDGTSLgkecvQQLAENTRYFRRRLKEMGFIIYGNeDS 466
Cdd:PRK13392 256 YIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRH-LKTSQTER-----DAHQDRVAALKAKLNANGIPVMPS-PS 328

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758668   467 PVVPLMLYMPAKIGAFGrEMLKRNIGVVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 537
Cdd:PRK13392 329 HIVPVMVGDPTLCKAIS-DRLMSEHGIYIqpINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 171-539 2.11e-53

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 186.26  E-value: 2.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   171 INMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALV 250
Cdd:PLN03227   1 LNFATHDFLSTSSSP-TLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   251 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLL-----KDAIVYGQPRTRRPWkkilILVEGIYSMEGSIV 325
Cdd:PLN03227  80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   326 RLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDP-EDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHS 404
Cdd:PLN03227 156 PLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   405 AVYATSlSPPVVEQIitSMKCIMGQDGtslGKECVQQLAENTRYFRRRLK----------EMGFIIYGNEDSPVVPLMLY 474
Cdd:PLN03227 236 YCFSAS-APPFLAKA--DATATAGELA---GPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLRLS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   475 MPAKIGAF---------GREMLKRNIGVVVVGfpATPIIESRA------RFCLSAAHTKEILDTALKEIDEVGDLLQLKY 539
Cdd:PLN03227 310 DQEATRRTdetlildqiAHHSLSEGVAVVSTG--GHVKKFLQLvpppclRVVANASHTREDIDKLLTVLGEAVEAILCKI 387
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
168-528 2.44e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    168 KGVINMGSYNYLGfarntGSCQEAAAKVLEeygAGVCSTRQEIGNLDKHEELEELVARFLG--------VEAAMAYGMGF 239
Cdd:pfam00155   1 TDKINLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    240 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 311
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    312 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPTGRGVVeYFGLDPEDVDVMMGTFTKSFGASG--- 385
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    386 GYIGGKKELIDYLRTHShSAVYATSLSPPVVEQIITSmkcimGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEd 465
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSD-----PLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758668    466 SPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIIESRARFCLsAAHTKEILDTALKEI 528
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
171-534 3.32e-37

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 142.46  E-value: 3.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   171 INMGSYNYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALV 250
Cdd:PRK07179  57 IILQSNDYLNLSGHP-DIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   251 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaivYGQPrtrrpwkkiLILVEGIYSMEGSIVRLPEV 330
Cdd:PRK07179 136 DPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPG---------IIVVDSVYSTTGTIAPLADI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   331 IALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATS 410
Cdd:PRK07179 204 VDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSST 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   411 LSPPVVEQIITSMKCIMGQDgtslgkECVQQLAENTRYFRRRLKEMGFIIYGNedSPVVPLMLYMPAKIGAFGREMLKRN 490
Cdd:PRK07179 283 LLPHEIAGLEATLEVIESAD------DRRARLHANARFLREGLSELGYNIRSE--SQIIALETGSERNTEVLRDALEERN 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 4758668   491 IGVVVVGFPATPIIESRARFCLSAAHTKEILD---TALKEIDEVGDL 534
Cdd:PRK07179 355 VFGAVFCAPATPKNRNLIRLSLNADLTASDLDrvlEVCREARDEVDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 177-519 6.71e-31

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 125.94  E-value: 6.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   177 NYLGFARNTgSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCL- 255
Cdd:PLN02955 111 DYLGLSSHP-TISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLl 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   256 -------------ILSDELNHASLVLGARLS----GATIRIFKHNNMQSLEKLLKDAIVygqprtrrpwKKILILVEGIY 318
Cdd:PLN02955 190 aasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KRKVVVTDSLF 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   319 SMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYL 398
Cdd:PLN02955 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   399 RTHSHSAVYATSLSPPVVEQIITSMkcIMGQdgtslgKECVQQLAENTRYfrRRLKEMGFIIYGnedSPVVPLMLYMPAK 478
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMAAAAYAAV--VVAR------KEKWRRKAIWERV--KEFKALSGVDIS---SPIISLVVGNQEK 405

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 4758668   479 IGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKE 519
Cdd:PLN02955 406 ALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 170-413 4.14e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 104.09  E-value: 4.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   170 VINMGSYNYLGFARNTGSCQEAAAKV---LEEYG---AGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNs 243
Cdd:PRK05937   6 SIDFVTNDFLGFSRSDTLVHEVEKRYrlyCRQFPhaqLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   244 MNIPALVGKGC-LILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLkdaivygQPRTRRPWKKILILVEGIYSMEG 322
Cdd:PRK05937  85 LGLCAHLSSVTdYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL-------ESCRQRSFGRIFIFVCSVYSFKG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   323 SIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLdpEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHS 402
Cdd:PRK05937 158 TLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY--ENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNS 235

                        250
                 ....*....|.
gi 4758668   403 HSAVYATSLSP 413
Cdd:PRK05937 236 PPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 170-528 1.06e-21

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 97.36  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   170 VINMGSYNYLGFaRNTGSCQEAAAKVLEEYGA-GVCSTRQEIgNLDKHEELEELVARFLGVEAAMayGMGFATNSMNIPA 248
Cdd:PRK07505  48 FVNFVSCSYLGL-DTHPAIIEGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALSELFGASVLT--FTSCSAAHLGILP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   249 LVGKGCL-------ILSDELNHASL-VLGARLS--GATIRIfKHNNMQSLEKLLKdaivygqpRTRRPwkkiLILVEGIY 318
Cdd:PRK07505 124 LLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDALEDICK--------TNKTV----AYVADGVY 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   319 SMeGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV--EYFGLDPEDVdVMMGTFTKSFGASGGYIG-GKKELI 395
Cdd:PRK07505 191 SM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERT-IIAASLGKAFGASGGVIMlGDAEQI 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668   396 DYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGkecvQQLAENTRYF--------RRRLKEMGFIIYGNEDSP 467
Cdd:PRK07505 269 ELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQ----QKLQNNIALFdslipteqSGSFLPIRLIYIGDEDTA 344

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758668   468 VvplmlympakigAFGREMLKRNIGVVVVGFPATPiiESRA--RFCLSAAHTKEILDT---ALKEI 528
Cdd:PRK07505 345 I------------KAAKQLLDRGFYTSPVFFPVVA--KGRAglRIMFRASHTNDEIKRlcsLLKEI 396
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 215-391 2.44e-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: 68.18  E-value: 2.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  215 KHEELEELVARFL--GVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHAS-LVLGARLSGATIRIFKHNNmqslekl 291
Cdd:cd01494   1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDD------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  292 LKDAIVYGQPRTRRPWKKI--LILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGAlgptgRGVVEYFGLDpED 369
Cdd:cd01494  74 AGYGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGA-----SPAPGVLIPE-GG 147

                       170       180
                ....*....|....*....|...
gi 4758668  370 VDVMMGTFTKSFGASG-GYIGGK 391
Cdd:cd01494 148 ADVVTFSLHKNLGGEGgGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 270-530 1.28e-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: 60.05  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  270 ARLSGATIRIF--KHNNMQSLEKLLKDAIVygQPRTrrpwkKILILV-----EG-IYSMEgsivRLPEVIALKKKYKAYL 341
Cdd:cd00609 100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  342 YLDEAHSigALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASG---GY-IGGKKELIDYLRthshSAVYATSLSPPVVE 417
Cdd:cd00609 169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLK----KLLPYTTSGPSTLS 242

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  418 QIITSmkcIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIygnedsPVVP-----LMLYMPAKIGA-FGREMLKRNI 491
Cdd:cd00609 243 QAAAA---AALDDGEEHLEELRERYRRRRDALLEALKELGPLV------VVKPsggffLWLDLPEGDDEeFLERLLLEAG 313

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 4758668  492 GVVVVGFPATPIIESRARFCLsaAHTKEILDTALKEIDE 530
Cdd:cd00609 314 VVVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 217-531 1.03e-06

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: 50.79  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  217 EELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLV-LGA--RLSGATIRIFKHNNMQSLEKLLK 293
Cdd:cd06502  35 AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENGKLTPEDLE 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  294 DAIVYGQ----PRTRrpwkkiLILVEGiySMEGSIVRLPEVI----ALKKKYKAYLYLDEAHSIGALGPTGRGVVEYfgl 365
Cdd:cd06502 115 AAIRPRDdihfPPPS------LVSLEN--TTEGGTVYPLDELkaisALAKENGLPLHLDGARLANAAAALGVALKTY--- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  366 dPEDVDVMMGTFTKSFGASGGYI-GGKKELI---DYLRTHshsavyatslsppvVEQIITSMKCIMGQDGTSLGKECVQQ 441
Cdd:cd06502 184 -KSGVDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQ--------------AGGGMRQSGFLAAAGLAALENDLWLR 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  442 LAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEIL 521
Cdd:cd06502 249 RLRHDHEMARRLAEALEELGGLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEEDV 328

                       330
                ....*....|
gi 4758668  522 DTALKEIDEV 531
Cdd:cd06502 329 DELLSALKAV 338
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
218-397 6.69e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 47.98  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    218 ELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLG---ARLSGA---TIRIFKHNNM--QSLE 289
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELGGVqprPLDGDEAGNMdlEDLE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    290 KLLKDAIVYGQPRTRrpwkkiLILVE--------GIYSMEgsivRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVE 361
Cdd:pfam01212 116 AAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIPVHLDGARFANAAVALGVIVKE 185

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 4758668    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 8.56e-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: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    214 DKHEELEELVARFLGveAAMAYGMGF---ATNSMNI------PALVGKGCLILSDELNHASLVLGARLS---GATIRIFK 281
Cdd:pfam00266  43 QAYEEAREKVAEFIN--APSNDEIIFtsgTTEAINLvalslgRSLKPGDEIVITEMEHHANLVPWQELAkrtGARVRVLP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    282 HNNMQSLE-KLLKDAIvygQPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGA--------- 351
Cdd:pfam00266 121 LDEDGLLDlDELEKLI---TPKTK------LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHrpidvqklg 191

                         170       180
                  ....*....|....*....|
gi 4758668    352 -----------LGPTGRGVV 360
Cdd:pfam00266 192 vdflafsghklYGPTGIGVL 211
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
199-531 6.83e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 45.52  E-value: 6.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  199 YGAGVCSTRQEignlDKHEELEELVARFLGVEAA--MAYGMGfATNSMNIPA----LVGKGCLILSDELNHASLVLG--- 269
Cdd:COG0520  48 RGAHELSAEAT----DAYEAAREKVARFIGAASPdeIIFTRG-TTEAINLVAyglgRLKPGDEILITEMEHHSNIVPwqe 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  270 -ARLSGATIRIFKHN-----NMQSLEKLLKdaivygqPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYL 343
Cdd:COG0520 123 lAERTGAEVRVIPLDedgelDLEALEALLT-------PRTK------LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLV 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  344 DEAHSIGalgptgrgvveYFGLD--PEDVDVMMGTFTKSFGASGgyIG---GKKELIDYL-------RTHSHSAVYATSL 411
Cdd:COG0520 190 DGAQSVP-----------HLPVDvqALGCDFYAFSGHKLYGPTG--IGvlyGKRELLEALppflgggGMIEWVSFDGTTY 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  412 SP---------PVVEQIITSMKCI--MgqdgTSLGKECVQQ-LAENTRYFRRRLKEM-GFIIYGNED----SPVVPLML- 473
Cdd:COG0520 257 ADlprrfeagtPNIAGAIGLGAAIdyL----EAIGMEAIEArERELTAYALEGLAAIpGVRILGPADpedrSGIVSFNVd 332

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758668  474 -YMPAKIGAFgreMLKRNIGVVVVGFPATPI-----IESRARFCLSAAHTKEILDTALKEIDEV 531
Cdd:COG0520 333 gVHPHDVAAL---LDDEGIAVRAGHHCAQPLmrrlgVPGTVRASFHLYNTEEEIDRLVEALKKL 393
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 209-455 9.41e-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: 9.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  209 EIGNLDKHE----ELEELVARFLGVEAAMaygmgFATN---SMN---IPALVGKGCLILSDELNHASLVLGARLSGAT-- 276
Cdd:cd00615  50 GLDDLLDPTgpikEAQELAARAFGAKHTF-----FLVNgtsSSNkavILAVCGPGDKILIDRNCHKSVINGLVLSGAVpv 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  277 ---------IRIFKHNNMQSLEKLLKDAivygqprtrrPWKKILILVEGIYsmEGSIVRLPEVIALKKKYKAYLYLDEAH 347
Cdd:cd00615 125 ylkpernpyYGIAGGIPPETFKKALIEH----------PDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668  348 siGAlgptgrgvveYFGLDPE----------DVDV-----MMGTFTKsfgasGGYIGGKKELID------YLRTHshsav 406
Cdd:cd00615 193 --GA----------HFRFHPIlpssaamagaDIVVqsthkTLPALTQ-----GSMIHVKGDLVNpdrvneALNLH----- 250

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 4758668  407 yaTSLSPPVveQIITSMKCIMGQDGTSlGKECVQQLAENTRYFRRRLKE 455
Cdd:cd00615 251 --QSTSPSY--LILASLDVARAMMALE-GKELVEELIELALYARQEINK 294
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
201-447 1.39e-03

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 41.33  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    201 AGVCSTRQEIGNLDKHE----ELEELVARFLGveAAMAYGMGFATNSMN---IPALVGKGCLILSDELNHASLVLGARLS 273
Cdd:pfam01276  49 IDVCIEDVELGDLLDHEgaikEAQKYAARVFG--ADKSYFVVNGTSGSNktvGMAVCTPGDTILIDRNCHKSIHHALMLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    274 GAT------------------IRIFKHnnmQSLEKLLKDAivygqPRTRrpWKKILILVEGIYsmEGSIVRLPEVIALKK 335
Cdd:pfam01276 127 GATpvylepsrnaygiiggipLHEFQE---ETLKEAIAEV-----PDAK--GPRLAVITNPTY--DGVLYNAKEIVDTLH 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758668    336 KYKAYLYLDEAHS---------IGALGPTGRGVVEYFGLDPEDVDVMMGTFTKS--FGASGGYIGGKKELIDYLRTHShs 404
Cdd:pfam01276 195 HLSDPILFDSAWVgyeqfipiyADASPMGGENENGPGIFVTQSVHKLLAALSQAsyIHKKEGHIVNHDRFNEAFMMHA-- 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 4758668    405 avyATSLSPPVVEQIITSMKCIMGQDGTSLGKECVqQLAENTR 447
Cdd:pfam01276 273 ---TTSPSYPIFASLDVAAKMLEGNSGRRLWNECV-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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