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Conserved domains on  [gi|1207114269|ref|XP_021336238|]
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serine palmitoyltransferase 3 isoform X1 [Danio rerio]

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) ...
 58-535 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: 664.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269  58 EAPMYVAVLTYMGYGIVILFGYFRDFLRAVglekcHQAQEREEQKDFVPLYQDFENFYKRNLYMRVRDNWNRPICSLPGP 137
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRAI-----LDWWKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTiENVINMGSYNYLGFAENNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAICSGQPRTH 297
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 298 RSWKKILIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGAT 377
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 378 GGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMGVDGTTEGQRRVRQLAENTHYFRSRLKEMGFIIYGNK 457
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207114269 458 DSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDYIRVKFSRH 535
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 58-535 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 664.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269  58 EAPMYVAVLTYMGYGIVILFGYFRDFLRAVglekcHQAQEREEQKDFVPLYQDFENFYKRNLYMRVRDNWNRPICSLPGP 137
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRAI-----LDWWKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTiENVINMGSYNYLGFAENNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAICSGQPRTH 297
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 298 RSWKKILIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGAT 377
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 378 GGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMGVDGTTEGQRRVRQLAENTHYFRSRLKEMGFIIYGNK 457
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207114269 458 DSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDYIRVKFSRH 535
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 161-525 1.35e-168

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: 481.68  E-value: 1.35e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIP 240
Cdd:cd06454     1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 241 ALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAIcsgqprthRSWKKILIMVEGIYSMEGSLVRL 320
Cdd:cd06454    80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIAPL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 321 PEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVtEHFGVDPKEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVY 400
Cdd:cd06454   152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 401 ATAMSPPVVEQIIRAIKCIMGvdgtteGQRRVRQLAENTHYFRSRLKEMGFIIYGNKDSPVIPLLLYQPGKVGAFSRAML 480
Cdd:cd06454   231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1207114269 481 KRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELG 525
Cdd:cd06454   305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 111-526 6.23e-137

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 402.12  E-value: 6.23e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 111 FENFYKRNLYMRVRDNWNR---PICSLPGPvfdlmervsddynwTFRLTGRTienVINMGSYNYLGFAeNNVDFLKTVAE 187
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRylrVLESPQGP--------------RVTIDGRE---VLNFSSNDYLGLA-NHPRVIEAAAE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 188 KTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSG 267
Cdd:COG0156    63 ALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 268 ATIRVFKHNNMQSLEKLLKEaicsgqprtHRSWKKILIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGP 347
Cdd:COG0156   143 AKVVRFRHNDMDDLERLLKK---------ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGE 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 348 TGRGVTEHFGVDPkEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMgvdgtTE 427
Cdd:COG0156   214 TGRGLVEHFGLED-RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILR-----EE 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 428 GQRRVRqLAENTHYFRSRLKEMGFIIyGNKDSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSA 507
Cdd:COG0156   288 PELRER-LWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSA 365

                         410
                  ....*....|....*....
gi 1207114269 508 AHTRDMLNKVLQSLDELGD 526
Cdd:COG0156   366 AHTEEDIDRLLEALAEVGK 384
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 138-526 2.68e-60

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: 204.58  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTIENVINMGSYNYLGFAENnVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:TIGR01821  22 VFADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQH-PEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGK--GCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKeaicSGQPR 295
Cdd:TIGR01821 101 DLHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ----SVDPN 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 296 THRswkkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKeIDVLMGTFTKSFG 375
Cdd:TIGR01821 177 RPK-----IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHR-IDIIEGTLAKAFG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 376 ATGGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMgvdgTTEGQRRVRQlaENTHYFRSRLKEMGFIIYG 455
Cdd:TIGR01821 251 VVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIP 324

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207114269 456 NkDSPVIPLLLYQPGKVGAFSRAML-KRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGD 526
Cdd:TIGR01821 325 N-PSHIVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWD 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
161-521 2.23e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAennvdfLKTVAEKTRQygVGVCSTRQELGNFSIHEELEHLVADFLG--------VESAMAFGMGF 232
Cdd:pfam00155   1 TDKINLGSNEYLGDT------LPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 233 ATNSMNIPALVG-KGCLILSDELNHTSLILGARLSGATIRVFK-------HNNMQSLEKLLKEAIcsgqprthrswkkIL 304
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP-------------KV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 305 IMVEGIYSMEGSLVRLPE---IIALKKKYKAYLYLDEAHSIGAVGPTGRgVTEHFGVDPKEIDVLMGTFTKSFGATG--- 378
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 379 GYIAGKKELVDYLRCHShSAVYATAMSPPVVEQIIRAIKCIMGvdgttEGQRRVRQLAENTHYFRSRLKEMGFIIYGNkD 458
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS-----ELEEMRQRIKERRDYLRDGLQAAGLSVLPS-Q 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207114269 459 SPVIPLLLYQPGKVGAFSRAMLKRKiGVVVVGFPATTITEaRARFCVsAAHTRDMLNKVLQSL 521
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEEV-GVYVTPGSSPGVPG-WLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 58-535 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 664.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269  58 EAPMYVAVLTYMGYGIVILFGYFRDFLRAVglekcHQAQEREEQKDFVPLYQDFENFYKRNLYMRVRDNWNRPICSLPGP 137
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRAI-----LDWWKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTiENVINMGSYNYLGFAENNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAICSGQPRTH 297
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 298 RSWKKILIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGAT 377
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 378 GGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMGVDGTTEGQRRVRQLAENTHYFRSRLKEMGFIIYGNK 457
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207114269 458 DSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDYIRVKFSRH 535
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 161-525 1.35e-168

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: 481.68  E-value: 1.35e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIP 240
Cdd:cd06454     1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 241 ALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAIcsgqprthRSWKKILIMVEGIYSMEGSLVRL 320
Cdd:cd06454    80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIAPL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 321 PEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVtEHFGVDPKEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVY 400
Cdd:cd06454   152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 401 ATAMSPPVVEQIIRAIKCIMGvdgtteGQRRVRQLAENTHYFRSRLKEMGFIIYGNKDSPVIPLLLYQPGKVGAFSRAML 480
Cdd:cd06454   231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1207114269 481 KRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELG 525
Cdd:cd06454   305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 111-526 6.23e-137

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 402.12  E-value: 6.23e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 111 FENFYKRNLYMRVRDNWNR---PICSLPGPvfdlmervsddynwTFRLTGRTienVINMGSYNYLGFAeNNVDFLKTVAE 187
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRylrVLESPQGP--------------RVTIDGRE---VLNFSSNDYLGLA-NHPRVIEAAAE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 188 KTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSG 267
Cdd:COG0156    63 ALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 268 ATIRVFKHNNMQSLEKLLKEaicsgqprtHRSWKKILIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGP 347
Cdd:COG0156   143 AKVVRFRHNDMDDLERLLKK---------ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGE 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 348 TGRGVTEHFGVDPkEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMgvdgtTE 427
Cdd:COG0156   214 TGRGLVEHFGLED-RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILR-----EE 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 428 GQRRVRqLAENTHYFRSRLKEMGFIIyGNKDSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSA 507
Cdd:COG0156   288 PELRER-LWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSA 365

                         410
                  ....*....|....*....
gi 1207114269 508 AHTRDMLNKVLQSLDELGD 526
Cdd:COG0156   366 AHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 161-525 3.45e-99

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 305.97  E-value: 3.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIP 240
Cdd:PRK06939   42 KEVINFCANNYLGLA-NHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 241 ALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAICSGQprthrswKKILIMVEGIYSMEGSLVRL 320
Cdd:PRK06939  121 TLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 321 PEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKeIDVLMGTFTKSF-GATGGYIAGKKELVDYLRCHSHSAV 399
Cdd:PRK06939  194 PEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDR-VDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYL 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 400 YATAMSPPVVEQIIRAIKCIMgvdgttEGQRRVRQLAENTHYFRSRLKEMGFIIyGNKDSPVIPLLLYQPGKVGAFSRAM 479
Cdd:PRK06939  273 FSNSLAPAIVAASIKVLELLE------ESDELRDRLWENARYFREGMTAAGFTL-GPGEHPIIPVMLGDAKLAQEFADRL 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1207114269 480 LKRkiGVVVVGF--PATTITEARARFCVSAAHTRDMLNKVLQSLDELG 525
Cdd:PRK06939  346 LEE--GVYVIGFsfPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVG 391
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 161-525 3.17e-94

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 292.83  E-value: 3.17e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIP 240
Cdd:PRK05958   39 RRMLNFASNDYLGLA-RHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 241 ALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEaicsgqprthRSWKKILIMVEGIYSMEGSLVRL 320
Cdd:PRK05958  118 ALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK----------WRAGRALIVTESVFSMDGDLAPL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 321 PEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVY 400
Cdd:PRK05958  188 AELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIF 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 401 ATAMSPPVVEQIIRAIKCImgvdgTTEGQRRVRqLAENTHYFRSRLKEMGFIIyGNKDSPVIPLLLYQPGKVGAFSRAML 480
Cdd:PRK05958  268 TTALPPAQAAAARAALRIL-----RREPERRER-LAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALALAAALQ 340

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207114269 481 KRkiGVVVVGF-----PATTiteARARFCVSAAHTRDMLNKVLQSLDELG 525
Cdd:PRK05958  341 EQ--GFWVGAIrpptvPAGT---SRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 138-526 2.68e-60

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: 204.58  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTIENVINMGSYNYLGFAENnVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:TIGR01821  22 VFADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMGQH-PEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGK--GCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKeaicSGQPR 295
Cdd:TIGR01821 101 DLHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ----SVDPN 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 296 THRswkkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKeIDVLMGTFTKSFG 375
Cdd:TIGR01821 177 RPK-----IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHR-IDIIEGTLAKAFG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 376 ATGGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCIMgvdgTTEGQRRVRQlaENTHYFRSRLKEMGFIIYG 455
Cdd:TIGR01821 251 VVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIP 324

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207114269 456 NkDSPVIPLLLYQPGKVGAFSRAML-KRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGD 526
Cdd:TIGR01821 325 N-PSHIVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWD 395
PLN02822 PLN02822
serine palmitoyltransferase
 163-521 1.22e-57

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 199.97  E-value: 1.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 163 VINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIPAL 242
Cdd:PLN02822  111 VVNFASANYLGLI-GNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAF 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 243 VGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEaICSGQPRThrswKKI--LIMVEGIYSMEGSLVRL 320
Cdd:PLN02822  190 CKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAENKRK----KKLrrYIVVEAIYQNSGQIAPL 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 321 PEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGATGGYIAGKKELVDYLRCHSHSAVY 400
Cdd:PLN02822  265 DEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVF 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 401 ATAMSPPVVEQIIRAIKCImgvdgtTEGQRRVRQLAENTHYFRSRLKEM-GFIIYGNKDSPVIPLLLYQPgkVGAFSR-- 477
Cdd:PLN02822  345 SASLPPYLASAAITAIDVL------EDNPSVLAKLKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKS--TGSAKEdl 416

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207114269 478 --------AMLKRKiGVVVVGFPATTITEARA----RFCVSAAHTRDMLNKVLQSL 521
Cdd:PLN02822  417 sllehiadRMLKED-SVLVVVSKRSTLDKCRLpvgiRLFVSAGHTESDILKASESL 471
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 138-536 1.32e-57

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 197.77  E-value: 1.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 138 VFDLMERVSDDYNWTFRLTGRTIENVINMGSYNYLGFAENNvDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVA 217
Cdd:PRK13392   23 VFADLEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHP-DVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 218 DFLGVESAMAFGMGFATNSMNIPALVGK--GCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLkEAICSGQPR 295
Cdd:PRK13392  102 DLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQL-ASVDPDRPK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 296 thrswkkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDPKeIDVLMGTFTKSFG 375
Cdd:PRK13392  181 --------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR-IDMIQGTLAKAFG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 376 ATGGYIAGKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKCImgvdgTTEGQRRvRQLAENTHYFRSRLKEMGFIIYG 455
Cdd:PRK13392  252 CLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHL-----KTSQTER-DAHQDRVAALKAKLNANGIPVMP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 456 NkDSPVIPLLLYQPGKVGAFS-RAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDyiRVKFSR 534
Cdd:PRK13392  326 S-PSHIVPVMVGDPTLCKAISdRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD--RLELPR 402


                  ..
gi 1207114269 535 HR 536
Cdd:PRK13392  403 WR 404
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 164-532 1.60e-55

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 191.66  E-value: 1.60e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 164 INMGSYNYLGFAENNVdFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIPALV 243
Cdd:PLN03227    1 LNFATHDFLSTSSSPT-LRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 244 GKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEAICSGQP-RTHRSWKKILIMVEGIYSMEGSLVRLPE 322
Cdd:PLN03227   80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVAlKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 323 IIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDP-KEIDVLMGTFTKSFGATGGYIAGKKELVDYLRChSHSAVYA 401
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRL-SGSGYCF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 402 TAMSPPVVeqiirAIKCIMGVDGTTEGQRRVRQLAENTHYFRSRLK----------EMGFIIYGNKDSPVIPLLLY-QPG 470
Cdd:PLN03227  239 SASAPPFL-----AKADATATAGELAGPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLRLSdQEA 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207114269 471 K--------VGAFSRAMLKRKIGVVVVGFPATTITEARA----RFCVSAAHTRDMLNKVLQSLDELGDYIRVKF 532
Cdd:PLN03227  314 TrrtdetliLDQIAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGEAVEAILCKI 387
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
161-521 2.23e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAennvdfLKTVAEKTRQygVGVCSTRQELGNFSIHEELEHLVADFLG--------VESAMAFGMGF 232
Cdd:pfam00155   1 TDKINLGSNEYLGDT------LPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 233 ATNSMNIPALVG-KGCLILSDELNHTSLILGARLSGATIRVFK-------HNNMQSLEKLLKEAIcsgqprthrswkkIL 304
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP-------------KV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 305 IMVEGIYSMEGSLVRLPE---IIALKKKYKAYLYLDEAHSIGAVGPTGRgVTEHFGVDPKEIDVLMGTFTKSFGATG--- 378
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 379 GYIAGKKELVDYLRCHShSAVYATAMSPPVVEQIIRAIKCIMGvdgttEGQRRVRQLAENTHYFRSRLKEMGFIIYGNkD 458
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS-----ELEEMRQRIKERRDYLRDGLQAAGLSVLPS-Q 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207114269 459 SPVIPLLLYQPGKVGAFSRAMLKRKiGVVVVGFPATTITEaRARFCVsAAHTRDMLNKVLQSL 521
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEEV-GVYVTPGSSPGVPG-WLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
142-532 1.77e-35

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 137.45  E-value: 1.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 142 MERVSDDYNWTFRLTGRTI-ENVINMGSYNYLGFAeNNVDFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFL 220
Cdd:PRK07179   34 EERVNKNWNGKHLVLGKTPgPDAIILQSNDYLNLS-GHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 221 GVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLKEaicSGQPrthrsw 300
Cdd:PRK07179  113 GFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPG------ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 301 kkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDpKEIDVLMGTFTKSFGATGGY 380
Cdd:PRK07179  184 ---IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 381 IAGKKELVDYLRCHSHSAVYATAMSPpvveqiiraiKCIMGVDGTTE----GQRRVRQLAENTHYFRSRLKEMGFIIYGN 456
Cdd:PRK07179  260 ITCPRELAEYVPFVSYPAIFSSTLLP----------HEIAGLEATLEviesADDRRARLHANARFLREGLSELGYNIRSE 329

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207114269 457 kdSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDYIRVKF 532
Cdd:PRK07179  330 --SQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 170-531 1.82e-31

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 127.48  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 170 NYLGFAENNVdFLKTVAEKTRQYGVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFATNSMNIPALVGKGCL- 248
Cdd:PLN02955  111 DYLGLSSHPT-ISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLl 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 249 -------------ILSDELNHTSLILGARLS----GATIRVFKHNNMQSLEKLLKEAicsgqprthrSWKKILIMVEGIY 311
Cdd:PLN02955  190 aasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSC----------KMKRKVVVTDSLF 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 312 SMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDpKEIDVLMGTFTKSFGATGGYIAGKKELVDYL 391
Cdd:PLN02955  260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 392 RCHSHSAVYATAMSPPVVEQIIRAIkcimgVDGTTEGQRRVRqlaenthyFRSRLKEMGFIIYGNKDSPVIPLLLYQPGK 471
Cdd:PLN02955  339 QSRGRSFIFSTAIPVPMAAAAYAAV-----VVARKEKWRRKA--------IWERVKEFKALSGVDISSPIISLVVGNQEK 405

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 472 VGAFSRAMLKRKIGVVVVGFPATTITEARARFCVSAAHTRDMLNKVLQSLDELGDYIRVK 531
Cdd:PLN02955  406 ALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTA 465
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 161-406 4.58e-26

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 109.87  E-value: 4.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 161 ENVINMGSYNYLGFAENNVdFLKTVAEKTRQY-------GVGVCSTRQELGNFSIHEELEHLVADFLGVESAMAFGMGFA 233
Cdd:PRK05937    4 SLSIDFVTNDFLGFSRSDT-LVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 234 TNSMNIPALVGKGCLILSDELNHTSLILGARLSGATIRVFKHNNMQSLEKLLkeaicsgQPRTHRSWKKILIMVEGIYSM 313
Cdd:PRK05937   83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL-------ESCRQRSFGRIFIFVCSVYSF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 314 EGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGPTGRGVTEHFGVDpkEIDVLMGTFTKSFGATGGYIAGKKELVDYLRC 393
Cdd:PRK05937  156 KGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYE--NFYAVLVTYSKALGSMGAALLSSSEVKQDLML 233

                         250
                  ....*....|...
gi 1207114269 394 HSHSAVYATAMSP 406
Cdd:PRK05937  234 NSPPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 124-526 4.59e-26

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 110.45  E-value: 4.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 124 RDNWNRPICSLPGPVFDLME-------RVSDDYNWTFRLT-GRTienVINMGSYNYLGFaENNVDFLKTVAEKTRQYGV- 194
Cdd:PRK07505    4 KYRNNKKRINRAEKFWDAAYdeglnglTVGEREGILITLAdGHT---FVNFVSCSYLGL-DTHPAIIEGAVDALKRTGSl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 195 GVCSTRQELgNFSIHEELEHLVADFLGVESAMafGMGFATNSMNIPALVGKGCL-------ILSDELNHTSL-ILGARLS 266
Cdd:PRK07505   80 HLSSSRTRV-RSQILKDLEEALSELFGASVLT--FTSCSAAHLGILPLLASGHLtggvpphMVFDKNAHASLnILKGICA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 267 GAT-IRVFKHNNMQSLEkllkeAICSGQPRthrswkkILIMVEGIYSMeGSLVRLPEIIALKKKYKAYLYLDEAHSIGAV 345
Cdd:PRK07505  157 DETeVETIDHNDLDALE-----DICKTNKT-------VAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 346 GPTGRG-VTEHFGVDPKEIDVLMGTFTKSFGATGGYIA-GKKELVDYLRCHSHSAVYATAMSPPVVEQIIRAIKcimgVD 423
Cdd:PRK07505  224 GKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAE----IH 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 424 GTTEGQRRVRQLAENTHYFRSrlkEMGFIIYGNkDSPVIPLLLYQPGKVGAFSRAMLKRKIGVVVVGFPatTITEARA-- 501
Cdd:PRK07505  300 LSEELDQLQQKLQNNIALFDS---LIPTEQSGS-FLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFP--VVAKGRAgl 373

                         410       420
                  ....*....|....*....|....*
gi 1207114269 502 RFCVSAAHTRDMLNKVLQSLDELGD 526
Cdd:PRK07505  374 RIMFRASHTNDEIKRLCSLLKEILD 398
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 209-384 5.71e-11

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


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 61.24  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 209 HEELEHLVADFL--GVESAMAFGMGFATNSMNIPALVGKGCLILSDELNHTS-LILGARLSGATIRVFK-------HNNM 278
Cdd:cd01494     2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPvddagygGLDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 279 QSLEKLLKeaicsgQPRTHrswkkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGAVGptGRGVTEHFGV 358
Cdd:cd01494    82 AILEELKA------KPNVA------LIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASP--APGVLIPEGG 147

                         170       180
                  ....*....|....*....|....*..
gi 1207114269 359 dpkeIDVLMGTFTKSFGATG-GYIAGK 384
Cdd:cd01494   148 ----ADVVTFSLHKNLGGEGgGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 263-523 4.88e-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: 58.12  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 263 ARLSGATIR---VFKHNNMQSLEKLLKEAIcsgQPRThrswkKILIMV-----EG-IYSMEgslvRLPEIIALKKKYKAY 333
Cdd:cd00609   100 ARLAGAEVVpvpLDEEGGFLLDLELLEAAK---TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGIL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 334 LYLDEAHSigAVGPTGRGVTEHFGVDPKEIDVLMGTFTKSFGATG---GYIAGKKELVDYLRCHSHSAVYATAmSPPVVE 410
Cdd:cd00609   168 IISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLPYTTSGP-STLSQA 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 411 QIIRAIKcimgvDGTTEGQRRVRQLAENTHYFRSRLKEMGFIIygnKDSPVIPLLLY---QPGKVGAFSRAMLKRKIGVV 487
Cdd:cd00609   245 AAAAALD-----DGEEHLEELRERYRRRRDALLEALKELGPLV---VVKPSGGFFLWldlPEGDDEEFLERLLLEAGVVV 316

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1207114269 488 VVGFPATTITEARARFCVsaAHTRDMLNKVLQSLDE 523
Cdd:cd00609   317 RPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
210-524 1.84e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 53.60  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 210 EELEHLVADFLGVESA--MAFGMGfATNSMNIPA----LVGKGCLILSDELNHTSLILG----ARLSGATIRVFKHN--- 276
Cdd:COG0520    62 EAAREKVARFIGAASPdeIIFTRG-TTEAINLVAyglgRLKPGDEILITEMEHHSNIVPwqelAERTGAEVRVIPLDedg 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 277 --NMQSLEKLLKE-----AIcsgqprTHRSWkkilimVEGIysmegslvRLP--EIIALKKKYKAYLYLDEAHSIGavgp 347
Cdd:COG0520   141 elDLEALEALLTPrtklvAV------THVSN------VTGT--------VNPvkEIAALAHAHGALVLVDGAQSVP---- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 348 tgrgvteHFGVDPKEIDV--LMGTFTKSFGATG-GYIAGKKELVDYLR-----------CHSHSAVYAT------AMSPP 407
Cdd:COG0520   197 -------HLPVDVQALGCdfYAFSGHKLYGPTGiGVLYGKRELLEALPpflggggmiewVSFDGTTYADlprrfeAGTPN 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 408 VVeQIIRAIKCI-----MGVDgttEGQRRVRQLAEnthYFRSRLKEM-GFIIYGNKD----SPVIPLLL--YQPGKVGAF 475
Cdd:COG0520   270 IA-GAIGLGAAIdyleaIGME---AIEARERELTA---YALEGLAAIpGVRILGPADpedrSGIVSFNVdgVHPHDVAAL 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207114269 476 sraMLKRKIGVVVVGFPATTITEAR-----ARFCVSAAHTRDMLNKVLQSLDEL 524
Cdd:COG0520   343 ---LDDEGIAVRAGHHCAQPLMRRLgvpgtVRASFHLYNTEEEIDRLVEALKKL 393
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 208-387 1.02e-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: 51.09  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 208 IHEELEHLVADFLGVESA--MAFGMGfATNSMNIPAL-----VGKGCLILSDELNHTSLILG----ARLSGATIRVFKHN 276
Cdd:pfam00266  44 AYEEAREKVAEFINAPSNdeIIFTSG-TTEAINLVALslgrsLKPGDEIVITEMEHHANLVPwqelAKRTGARVRVLPLD 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 277 NMQSLE-KLLKEAIcsgQPRTHrswkkiLIMVEGIYSMEGSLVRLPEIIALKKKYKAYLYLDEAHSIGavgptgrgvteH 355
Cdd:pfam00266 123 EDGLLDlDELEKLI---TPKTK------LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG-----------H 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207114269 356 FGVDPKEIDVLMGTFT--KSFGATG-GYIAGKKEL 387
Cdd:pfam00266 183 RPIDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDL 217
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 322-453 4.30e-05

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 45.89  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 322 EIIALKKKYKAYLYLDEA-----------HSIGAVGptgrgvtehfgvDPKEIDVLMGTFTKSFGATG---GYIAGKKEL 387
Cdd:COG0436   187 ALAELAREHDLLVISDEIyeelvydgaehVSILSLP------------GLKDRTIVINSFSKSYAMTGwriGYAVGPPEL 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207114269 388 VDYL-RCHSHsavyaTAMSPPVVEQIIrAIKCIMGVDGTTEGQRRVrqLAENTHYFRSRLKEMGFII 453
Cdd:COG0436   255 IAALlKLQSN-----LTSCAPTPAQYA-AAAALEGPQDYVEEMRAE--YRRRRDLLVEGLNEIGLSV 313
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 412-524 8.22e-04

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 41.81  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114269 412 IIRAIKC-----IMGVDGTTEGQRRVRQLAentHYFRSRLKEM-GFIIYGNKDSPVIPLLLYQPGKVG----AFSRAMLK 481
Cdd:cd06450   228 LVRALKLwatlrRFGRDGYGEHIDRIVDLA---KYLAELIRADpGFELLGEPNLSLVCFRLKPSVKLDelnyDLSDRLNE 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207114269 482 RKIGVVvvgfPATTITEARA-RFCVSAAH-TRDMLNKVLQSLDEL 524
Cdd:cd06450   305 RGGWHV----PATTLGGPNVlRFVVTNPLtTRDDADALLEDIERA 345
 
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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