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Conserved domains on  [gi|636856242|ref|WP_024375463|]
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alpha-hydroxyketone-type quorum-sensing autoinducer synthase [Vibrio fluvialis]

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) ...
 1-392 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 PRK07179:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 407  Bit Score: 655.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   1 MKTDAKNNRLPEFIQDRLNFFVRDLIQSNNNGKHLVLGKRPSQGDIVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMS 80
Cdd:PRK07179  12 MKEKHKNPPLPDFIEERLDKYIEERVNKNWNGKHLVLGKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  81 AIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCD 160
Cdd:PRK07179  92 AVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 161 HLLKQIKRHGPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAK 240
Cdd:PRK07179 172 HLRRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAK 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 241 TFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINIRSQSQ 320
Cdd:PRK07179 252 AFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636856242 321 IIALETGDERNTEKVRDYLEDNGIFGAVFCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNRSDLYF 392
Cdd:PRK07179 332 IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
 
Name Accession Description Interval E-value
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
1-392 0e+00

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 655.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   1 MKTDAKNNRLPEFIQDRLNFFVRDLIQSNNNGKHLVLGKRPSQGDIVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMS 80
Cdd:PRK07179  12 MKEKHKNPPLPDFIEERLDKYIEERVNKNWNGKHLVLGKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  81 AIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCD 160
Cdd:PRK07179  92 AVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 161 HLLKQIKRHGPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAK 240
Cdd:PRK07179 172 HLRRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAK 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 241 TFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINIRSQSQ 320
Cdd:PRK07179 252 AFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636856242 321 IIALETGDERNTEKVRDYLEDNGIFGAVFCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNRSDLYF 392
Cdd:PRK07179 332 IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 10-387 7.95e-109

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


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 324.70  E-value: 7.95e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  10 LPEFIQDRLN-------FFVRDLIQSNNnGKHLVLGKRPSqgdIVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAI 82
Cdd:COG0156    1 LLDRLEAELAalkaaglYRYLRVLESPQ-GPRVTIDGREV---LNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  83 FLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHL 162
Cdd:COG0156   77 VSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 163 LKQIKRH---GPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLA 239
Cdd:COG0156  157 ERLLKKAraaRRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 240 KTFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINI-RSQ 318
Cdd:COG0156  237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLgPSE 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636856242 319 SQIIALETGDERNTEKVRDYLEDNGIFGAVFCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNR 387
Cdd:COG0156  317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 46-382 2.51e-107

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: 319.51  E-value: 2.51e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  46 IVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICA 125
Cdd:cd06454    4 LNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 126 PGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLKQIKR----HGPGIIVVDSIYSTIGTIAPLAELVAIAKETGS 201
Cdd:cd06454   84 KGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREarrpYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 202 AILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAKTFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALE 281
Cdd:cd06454  164 ILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAAL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 282 ATLDVIKSADERRERLFHNTHILSTGLNRLGINIR-SQSQIIALE-TGDERNTEKVRDYLEDNGIFgAVFCR-PATSKTK 358
Cdd:cd06454  244 AALEVLQGGPERRERLQENVRYLRRGLKELGFPVGgSPSHIIPPLiGDDPAKAVAFSDALLERGIY-VQAIRyPTVPRGT 322

                        330       340
                 ....*....|....*....|....
gi 636856242 359 NIIRLSLTSSVTAEQIDRILSVCQ 382
Cdd:cd06454  323 ARLRISLSAAHTKEDIDRLLEALK 346
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
46-379 8.29e-26

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 106.62  E-value: 8.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   46 IVLQSNDYLSLanhPLIRArlKKAIDDTHDsvFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQ--------SGWNAN- 116
Cdd:pfam00155   4 INLGSNEYLGD---TLPAV--AKAEKDALA--GGTRNLYGPTDGHPELREALAKFLGRSPVLKLDreaavvfgSGAGANi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  117 TALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPF-------MHNNCDHLLKQIKRhGPGIIVVDSIYSTIGTIAPL 189
Cdd:pfam00155  77 EALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKE-KPKVVLHTSPHNPTGTVATL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  190 AELVAIA---KETGSAILVDESHSLGTHGKNGAGLLAeLGLSDQVDFMTA-SLAKTFA---YRAGVIWANNNVNQCVPFV 262
Cdd:pfam00155 156 EELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATR-ALLAEGPNLLVVgSFSKAFGlagWRVGYILGNAAVISQLRKL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  263 GYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGIN-IRSQSQIIALETGDERNTEKVRDYLED 341
Cdd:pfam00155 235 ARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSvLPSQAGFFLLTGLDPETAKELAQVLLE 314

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 636856242  342 NgifGAVFCRPATSKT-KNIIRLSLTsSVTAEQIDRILS 379
Cdd:pfam00155 315 E---VGVYVTPGSSPGvPGWLRITVA-GGTEEELEELLE 349
 
Name Accession Description Interval E-value
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
1-392 0e+00

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 655.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   1 MKTDAKNNRLPEFIQDRLNFFVRDLIQSNNNGKHLVLGKRPSQGDIVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMS 80
Cdd:PRK07179  12 MKEKHKNPPLPDFIEERLDKYIEERVNKNWNGKHLVLGKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  81 AIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCD 160
Cdd:PRK07179  92 AVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 161 HLLKQIKRHGPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAK 240
Cdd:PRK07179 172 HLRRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAK 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 241 TFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINIRSQSQ 320
Cdd:PRK07179 252 AFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636856242 321 IIALETGDERNTEKVRDYLEDNGIFGAVFCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNRSDLYF 392
Cdd:PRK07179 332 IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 10-387 7.95e-109

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


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 324.70  E-value: 7.95e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  10 LPEFIQDRLN-------FFVRDLIQSNNnGKHLVLGKRPSqgdIVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAI 82
Cdd:COG0156    1 LLDRLEAELAalkaaglYRYLRVLESPQ-GPRVTIDGREV---LNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  83 FLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHL 162
Cdd:COG0156   77 VSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 163 LKQIKRH---GPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLA 239
Cdd:COG0156  157 ERLLKKAraaRRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 240 KTFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINI-RSQ 318
Cdd:COG0156  237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLgPSE 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636856242 319 SQIIALETGDERNTEKVRDYLEDNGIFGAVFCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNR 387
Cdd:COG0156  317 SPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 46-382 2.51e-107

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: 319.51  E-value: 2.51e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  46 IVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICA 125
Cdd:cd06454    4 LNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 126 PGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLKQIKR----HGPGIIVVDSIYSTIGTIAPLAELVAIAKETGS 201
Cdd:cd06454   84 KGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREarrpYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 202 AILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAKTFAYRAGVIWANNNVNQCVPFVGYPAIFSSTILPYEIAALE 281
Cdd:cd06454  164 ILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAAL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 282 ATLDVIKSADERRERLFHNTHILSTGLNRLGINIR-SQSQIIALE-TGDERNTEKVRDYLEDNGIFgAVFCR-PATSKTK 358
Cdd:cd06454  244 AALEVLQGGPERRERLQENVRYLRRGLKELGFPVGgSPSHIIPPLiGDDPAKAVAFSDALLERGIY-VQAIRyPTVPRGT 322

                        330       340
                 ....*....|....*....|....
gi 636856242 359 NIIRLSLTSSVTAEQIDRILSVCQ 382
Cdd:cd06454  323 ARLRISLSAAHTKEDIDRLLEALK 346
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 31-380 3.07e-61

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 202.31  E-value: 3.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  31 NGKHLVLGKRPSqgdIVLQSNDYLSLANHPLIRARLKKAID----------------DTHDSvfmsaiflqddeskpsLE 94
Cdd:PRK05958  30 AGRWLVVDGRRM---LNFASNDYLGLARHPRLIAAAQQAARrygagsggsrlvtgnsPAHEA----------------LE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  95 HQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLKQIK--RHGPG 172
Cdd:PRK05958  91 EELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAkwRAGRA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 173 IIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVD-FMTASLAKTFAYRAGVIWA 251
Cdd:PRK05958 171 LIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDvILVGTLGKALGSSGAAVLG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 252 NNN-----VNQCVPFvgypaIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINI-RSQSQIIALE 325
Cdd:PRK05958 251 SETlidylINRARPF-----IFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLmDSQSAIQPLI 325

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636856242 326 TGDERNTEKVRDYLEDNGIF-GAVfcRP-----ATSKtkniIRLSLTSSVTAEQIDRILSV 380
Cdd:PRK05958 326 VGDNERALALAAALQEQGFWvGAI--RPptvpaGTSR----LRITLTAAHTEADIDRLLEA 380
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 50-376 3.56e-45

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 160.36  E-value: 3.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  50 SNDYLSLANHPLIRARLKKAIDDthDSVFMSAI-FL---QDDESKpsLEHQLAEFAHFDSCLLSQSGWNANTALLQTICA 125
Cdd:PRK06939  49 ANNYLGLANHPELIAAAKAALDS--HGFGMASVrFIcgtQDLHKE--LEEKLAKFLGTEDAILYSSCFDANGGLFETLLG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 126 PGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLKQIK-------RHGpgIIVVDSIYSTIGTIAPLAELVAIAKE 198
Cdd:PRK06939 125 KEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKeakeagaRHK--LIATDGVFSMDGDIAPLPEICDLADK 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 199 TGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAKTFA-----YRAG----VIWANNNvnqcvpfvGYPAIFS 269
Cdd:PRK06939 203 YDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALGgasggYTAGrkevIDWLRQR--------SRPYLFS 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 270 STILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINI-RSQSQIIALETGDERNTEKVRDYLEDNGIFGAV 348
Cdd:PRK06939 275 NSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLgPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIG 354

                        330       340
                 ....*....|....*....|....*...
gi 636856242 349 FCRPATSKTKNIIRLSLTSSVTAEQIDR 376
Cdd:PRK06939 355 FSFPVVPKGQARIRTQMSAAHTKEQLDR 382
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 50-390 1.28e-35

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 134.98  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  50 SNDYLSLANHPLIRARLKKAID--------------DTHDSVFmsaiflqddeskpsLEHQLAEFAHFDSCLLSQSGWNA 115
Cdd:PRK13392  53 SNDYLGMGQHPDVIGAMVDALDrygagaggtrnisgTSHPHVL--------------LERELADLHGKESALLFTSGYVS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 116 NTALLQTICA--PGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLKQIKR---HGPGIIVVDSIYSTIGTIAPLA 190
Cdd:PRK13392 119 NDAALSTLGKllPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASvdpDRPKLIAFESVYSMDGDIAPIE 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 191 ELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAKTFAYRAGVIWANNNVNQCVPFVGYPAIFSS 270
Cdd:PRK13392 199 AICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTT 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 271 TILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINIR-SQSQIIALETGDERNTEKVRDYL-EDNGIFGAV 348
Cdd:PRK13392 279 ALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMpSPSHIVPVMVGDPTLCKAISDRLmSEHGIYIQP 358

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 636856242 349 FCRPATSKTKNIIRLSLTSSVTAEQIDRILSVCQNAVNRSDL 390
Cdd:PRK13392 359 INYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 46-381 1.67e-26

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 110.53  E-value: 1.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  46 IVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICA 125
Cdd:PLN02955 105 LLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGS 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 126 PGS--------------NVYIDFFAHMSMWEGARYA--NATIHPFMHNNCD--HLLK-----QIKRHgpgIIVVDSIYST 182
Cdd:PLN02955 185 VASllaasgkplknekvAIFSDALNHASIIDGVRLAerQGNVEVFVYRHCDmyHLNSllsscKMKRK---VVVTDSLFSM 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 183 IGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVDFMTASLAKTFAYRAGVIWANNNVNQCVPFV 262
Cdd:PLN02955 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSR 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 263 GYPAIFSSTI-LPYEIAALEATLdVIKSADERRERLFHNTHILSTglnRLGINIrsQSQIIALETGDERNTEKVRDYLED 341
Cdd:PLN02955 342 GRSFIFSTAIpVPMAAAAYAAVV-VARKEKWRRKAIWERVKEFKA---LSGVDI--SSPIISLVVGNQEKALKASRYLLK 415

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 636856242 342 NGiFGAVFCRPATSKTKNI-IRLSLTSSVTAEQIDRI---LSVC 381
Cdd:PLN02955 416 SG-FHVMAIRPPTVPPNSCrLRVTLSAAHTTEDVKKLitaLSSC 458
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
46-379 8.29e-26

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 106.62  E-value: 8.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   46 IVLQSNDYLSLanhPLIRArlKKAIDDTHDsvFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQ--------SGWNAN- 116
Cdd:pfam00155   4 INLGSNEYLGD---TLPAV--AKAEKDALA--GGTRNLYGPTDGHPELREALAKFLGRSPVLKLDreaavvfgSGAGANi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  117 TALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPF-------MHNNCDHLLKQIKRhGPGIIVVDSIYSTIGTIAPL 189
Cdd:pfam00155  77 EALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKE-KPKVVLHTSPHNPTGTVATL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  190 AELVAIA---KETGSAILVDESHSLGTHGKNGAGLLAeLGLSDQVDFMTA-SLAKTFA---YRAGVIWANNNVNQCVPFV 262
Cdd:pfam00155 156 EELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATR-ALLAEGPNLLVVgSFSKAFGlagWRVGYILGNAAVISQLRKL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  263 GYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGIN-IRSQSQIIALETGDERNTEKVRDYLED 341
Cdd:pfam00155 235 ARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSvLPSQAGFFLLTGLDPETAKELAQVLLE 314

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 636856242  342 NgifGAVFCRPATSKT-KNIIRLSLTsSVTAEQIDRILS 379
Cdd:pfam00155 315 E---VGVYVTPGSSPGvPGWLRITVA-GGTEEELEELLE 349
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 46-385 1.65e-23

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 100.75  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  46 IVLQSNDYLSLANHPLIRARLKKAIDDTHDSVFMSAIFLQDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICA 125
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 126 PGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLK----------QIKRHGPG---IIVVDSIYSTIGTIAPLAEL 192
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRvleqvraqdvALKRKPTDqrrFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 193 VAIAKETGSAILVDESHSLGTHGKNGAGLLAELGL--SDQVDFMTASLAKTFAYRAGVIWANNNVNQCVPFVGYPAIFSS 270
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 271 TILPY-------EIAALEATLDVIK----SADERRERLFHNTHILSTGL-NRLGINIRSQSQIIALETGDERNTEkvrdY 338
Cdd:PLN03227 241 SAPPFlakadatATAGELAGPQLLNrlhdSIANLYSTLTNSSHPYALKLrNRLVITSDPISPIIYLRLSDQEATR----R 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636856242 339 LEDNGI------------FGAVFCRPATSKTKNI-----IRLSLTSSVTAEQIDRILSVCQNAV 385
Cdd:PLN03227 317 TDETLIldqiahhslsegVAVVSTGGHVKKFLQLvpppcLRVVANASHTREDIDKLLTVLGEAV 380
PLN02483 PLN02483
serine palmitoyltransferase
 28-315 6.36e-20

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 91.36  E-value: 6.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  28 SNNNGKHLvlgKRPSQGD--IVLQSNDYLSLAN-HPLIRARLKKAIDDTHDSVFMSAIFLQDDESKPSLEHQLAEFAHFD 104
Cdd:PLN02483  86 SNDNNKTL---KRTTKTRrcLNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 105 SCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLK---------QIKRHGPG--- 172
Cdd:PLN02483 163 AAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEvlreqiaegQPRTHRPWkki 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 173 IIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGL-SDQVDFMTASLAKTFAYRAGVIWA 251
Cdd:PLN02483 243 IVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSFGSCGGYIAG 322

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 252 NNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSAD------ERRERLFHNTHILSTGLNRLGINI 315
Cdd:PLN02483 323 SKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDgtnrgaQKLAQIRENSNFFRSELQKMGFEV 392
PRK07505 PRK07505
hypothetical protein; Provisional
 53-376 7.88e-19

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 87.34  E-value: 7.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  53 YLSLANHPLIRARLKKAIDDT---HDSVFMSAIFLQddeSKPSLEHQLAEfaHFDS-CLLSQSGWNANTALLQTIC---- 124
Cdd:PRK07505  56 YLGLDTHPAIIEGAVDALKRTgslHLSSSRTRVRSQ---ILKDLEEALSE--LFGAsVLTFTSCSAAHLGILPLLAsghl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 125 APGSNVY--IDFFAHMSMwegaRYANATIHPFM------HNNCDHLLKQIKRHGPGIIVVDSIYSTiGTIAPLAELVAIA 196
Cdd:PRK07505 131 TGGVPPHmvFDKNAHASL----NILKGICADETevetidHNDLDALEDICKTNKTVAYVADGVYSM-GGIAPVKELLRLQ 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 197 KETGSAILVDESHSLGTHGKNGAGL-LAELG--LSDQVdFMTASLAKTFAYRAGVIWANNnvNQCVPFV---GYPAIFSS 270
Cdd:PRK07505 206 EKYGLFLYIDDAHGLSIYGKNGEGYvRSELDyrLNERT-IIAASLGKAFGASGGVIMLGD--AEQIELIlryAGPLAFSQ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 271 TILPYEIAALEATLDVIKSA--DERRERLFHNTHILSTGLNrlGINIRSQSQIIALETGDERNTEKVRDYLEDNGIFGAV 348
Cdd:PRK07505 283 SLNVAALGAILASAEIHLSEelDQLQQKLQNNIALFDSLIP--TEQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSP 360

                        330       340
                 ....*....|....*....|....*...
gi 636856242 349 FCRPATSKTKNIIRLSLTSSVTAEQIDR 376
Cdd:PRK07505 361 VFFPVVAKGRAGLRIMFRASHTNDEIKR 388
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 93-298 1.19e-17

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 83.68  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  93 LEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLLK-----QIK 167
Cdd:PRK05937  61 LEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESllescRQR 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 168 RHGPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLsDQVDFMTASLAKTFAYRAG 247
Cdd:PRK05937 141 SFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY-ENFYAVLVTYSKALGSMGA 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 636856242 248 VIWANNNVNQCVPFVGYPAIFSSTILPYEIAALEATLDVIKSADER-RERLF 298
Cdd:PRK05937 220 ALLSSSEVKQDLMLNSPPLRYSTGLPPHLLISIQVAYDFLSQEGELaRKQLF 271
PLN02822 PLN02822
serine palmitoyltransferase
 32-385 1.06e-16

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 81.33  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  32 GKHLVLGKRpsqgDIV-LQSNDYLSLANHplirarlKKAIDDTHDSV------------FMSAIFLQDDeskpsLEHQLA 98
Cdd:PLN02822 101 GPHTIINGK----DVVnFASANYLGLIGN-------EKIKESCTSALekygvgscgprgFYGTIDVHLD-----CETKIA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  99 EFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEGARYANATIHPFMHNNCDHLL-------------KQ 165
Cdd:PLN02822 165 KFLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRntlekltaenkrkKK 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 166 IKRHgpgiIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLS-DQVDFMTASLAKTFAY 244
Cdd:PLN02822 245 LRRY----IVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPiEKIDIITAAMGHALAT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 245 RAGVIWANNNV--NQCVPFVGYpaIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLN-----RLGINIRS 317
Cdd:PLN02822 321 EGGFCTGSARVvdHQRLSSSGY--VFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSdipglSIGSNTLS 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 318 QSQIIALE------TGDERNTEKVRDY-LEDNGIFGAV-------FCRPATSktkniIRLSLTSSVTAEQIDRILSVCQN 383
Cdd:PLN02822 399 PIVFLHLEkstgsaKEDLSLLEHIADRmLKEDSVLVVVskrstldKCRLPVG-----IRLFVSAGHTESDILKASESLKR 473


                 ..
gi 636856242 384 AV 385
Cdd:PLN02822 474 VA 475
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 115-378 1.33e-09

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 59.28  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 115 ANTALLQTICAPGSNVYID---FFAHMSMwegARYANATIHP------FMHNNCDHLLKQIKRHGPGIIVVDSIYSTIGT 185
Cdd:cd00609   71 ALSLLLRALLNPGDEVLVPdptYPGYEAA---ARLAGAEVVPvpldeeGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 186 IAP---LAELVAIAKETGSAILVDESHSLGTHGKNGAGLLAELGLSDQVdFMTASLAKTFA---YRAGVIWANNNVNQCV 259
Cdd:cd00609  148 VLSeeeLEELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERV-IVLRSFSKTFGlpgLRIGYLIAPPEELLER 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 260 PFVGYPAIFSSTILPYEIAALEATLDVIKSADERRERLFHNTHILSTGLNRLGINIRSQSQI---IALETGDERNTEKVR 336
Cdd:cd00609  227 LKKLLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSGgffLWLDLPEGDDEEFLE 306

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 636856242 337 DYLEDNGIFgAVFCRPATSKTKNIIRLSLTSSVtaEQIDRIL 378
Cdd:cd00609  307 RLLLEAGVV-VRPGSAFGEGGEGFVRLSFATPE--EELEEAL 345
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 93-252 6.63e-07

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: 48.92  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  93 LEHQLAEFAH--FDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMS-MWEGARYANATIHPF-------MHNNCDHL 162
Cdd:cd01494    5 LEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVpvddagyGGLDVAIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 163 LKQIKRHGPGIIVVDSIYSTIGTIAPLAELVAIAKETGSAILVDESHSLGthgknGAGLLAELGLSDQVDFMTASLAKTF 242
Cdd:cd01494   85 EELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLHKNL 159

                        170
                 ....*....|.
gi 636856242 243 -AYRAGVIWAN 252
Cdd:cd01494  160 gGEGGGVVIVK 170
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 157-380 2.08e-06

Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.


Pssm-ID: 99735 [Multi-domain]  Cd Length: 413  Bit Score: 49.49  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 157 NNCDHLLKQIKRHGPGI--IVVDSIYSTIGTIAP----LAELVAIAKETGSAILVDESHS-LGTHGKNGAGLLAELglsd 229
Cdd:cd00610  176 DDLEALEEALEEHPEEVaaVIVEPIQGEGGVIVPppgyLKALRELCRKHGILLIADEVQTgFGRTGKMFAFEHFGV---- 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 230 QVDFMTasLAKTFA--YRAGVIWANNNVNQCVPFVgyPAIFSSTIL--PYEIAALEATLDVIKSADERrERLFHNTHILS 305
Cdd:cd00610  252 EPDIVT--LGKGLGggLPLGAVLGREEIMDAFPAG--PGLHGGTFGgnPLACAAALAVLEVLEEEGLL-ENAAELGEYLR 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 306 TGLNRLG------INIRSQSQIIALETGDERNT--------EKVRDYLEDNGifgaVFCRPATSktkNIIRLSLTSSVTA 371
Cdd:cd00610  327 ERLRELAekhplvGDVRGRGLMIGIELVKDRATkppdkelaAKIIKAALERG----LLLRPSGG---NVIRLLPPLIITE 399


                 ....*....
gi 636856242 372 EQIDRILSV 380
Cdd:cd00610  400 EEIDEGLDA 408
Aminotran_3 pfam00202
Aminotransferase class-III;
174-379 4.32e-05

Aminotransferase class-III;


Pssm-ID: 395148 [Multi-domain]  Cd Length: 397  Bit Score: 45.40  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  174 IVVDSIYSTIGTIAP----LAELVAIAKETGSAILVDESHS-LGTHGKngagLLAELGLSDQVDFMTASLAKTFAYRAGV 248
Cdd:pfam00202 189 VIVEPIQGEGGVNPPspgfLAGLRAICKKHGVLLIADEVQTgFGRTGK----LFAHEHWGVPPDIMTFAKALTGGFPLAA 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  249 IWANNNVNQCVPFVGYPAIFSSTilPYEIAALEATLDVIKsaderRERLFHNTH----ILSTGLNRLGI------NIRSQ 318
Cdd:pfam00202 265 TLGRAEVMQAFAPGSHGGTFGGN--PLACAAALATLEIIE-----DEDLLQNAArlgaYLKEGLEDLQKkyevikDVRGK 337

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636856242  319 SQIIALET-GDERNTEKVRDYLEDNGifgaVFCRPATsktKNIIRLSLTSSVTAEQIDRILS 379
Cdd:pfam00202 338 GLMIGIELkEDVTVNPPILLAALEAG----VLILPCG---DNVIRLLPPLTITDEQIDEGLE 392
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
184-378 2.28e-04

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.82  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 184 GTIAPLAELVAIAKETGSAILVDESHSLGTHGKNgaglLAELGlsdqVDFMTASLAKTFAYR-AGVIWANNNV-NQCVPF 261
Cdd:COG0520  168 GTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVD----VQALG----CDFYAFSGHKLYGPTgIGVLYGKRELlEALPPF 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 262 -VGYPAI----FSSTI---LPY----------EIAALEATLDVIKS--ADERRERLFHNTHILSTGLNRL-GINIRSQSQ 320
Cdd:COG0520  240 lGGGGMIewvsFDGTTyadLPRrfeagtpniaGAIGLGAAIDYLEAigMEAIEARERELTAYALEGLAAIpGVRILGPAD 319

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636856242 321 ------IIALeTGDERNTEKVRDYLEDNGIfgAV----FCRPATSKTKNI---IRLSLTSSVTAEQIDRIL 378
Cdd:COG0520  320 pedrsgIVSF-NVDGVHPHDVAALLDDEGI--AVraghHCAQPLMRRLGVpgtVRASFHLYNTEEEIDRLV 387
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 158-204 4.40e-03

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 38.67  E-value: 4.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 158 NCDHLLKQIKRHGPGIIVVDSIySTI---------GTIAPL----AELVAIAKETGSAIL 204
Cdd:cd01121  146 NLEAILAEIEELKPSLVVIDSI-QTVyspeltsspGSVSQVrecaAELLRLAKETGIPVF 204
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 295-380 6.36e-03

Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 38.47  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242 295 ERLFHNTHILSTGLNRLGINIRSQSQI---IALETGDerNTEKVRDYLEDNGIFGAVfcrPATSKTKNIIRLSLTSSVTA 371
Cdd:COG0403  356 ERIHQKAHYLAERLAALGVEVPFNGPFfdeFVVRLPK--PAAEINAALLEKGILGGL---NLRRVDDDTLLVAVTETTTK 430


                 ....*....
gi 636856242 372 EQIDRILSV 380
Cdd:COG0403  431 EDIDALVEA 439
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 86-206 7.51e-03

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: 38.08  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  86 DDESKPSLEHQLAEfaHFDSC--LLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEG---ARYANATIHPFMHNNCD 160
Cdd:cd06502   30 EDPTTAKLEARAAE--LFGKEaaLFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDEAgapEFLSGVKLLPVPGENGK 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636856242 161 HLLKQIKRHgpgIIVVDSIYST------------IGTIAPLAELVAI---AKETGSAILVD 206
Cdd:cd06502  108 LTPEDLEAA---IRPRDDIHFPppslvslentteGGTVYPLDELKAIsalAKENGLPLHLD 165
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
85-206 9.64e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.58  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242   85 QDDESKPSLEHQLAEFAHFDSCLLSQSGWNANTALLQTICAPGSNVYIDFFAHMSMWEG---ARYANATIHPFMHNNC-- 159
Cdd:pfam01212  29 GGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELGGVQPRPLDGDEAgn 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 636856242  160 ---DHLLKQIKRHG-------PGIIVVDSIYSTIGTIAPLAEL---VAIAKETGSAILVD 206
Cdd:pfam01212 109 mdlEDLEAAIREVGadifpptGLISLENTHNSAGGQVVSLENLreiAALAREHGIPVHLD 168
 
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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