NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370513612|ref|XP_024303146|]
View 

serine palmitoyltransferase 1 isoform X3 [Homo sapiens]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 1-317 2.83e-117

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 PLN02822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 481  Bit Score: 346.73  E-value: 2.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDqknpRKA 80
Cdd:PLN02822  167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  81 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIG 160
Cdd:PLN02822  243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 161 GFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFH 240
Cdd:PLN02822  323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 241 LQLEESTGSREQDVRLLQEIVDQCMNRS---IALTQARYLekeEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVL 317
Cdd:PLN02822  403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTL---DKCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 1-317 2.83e-117

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 346.73  E-value: 2.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDqknpRKA 80
Cdd:PLN02822  167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  81 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIG 160
Cdd:PLN02822  243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 161 GFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFH 240
Cdd:PLN02822  323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 241 LQLEESTGSREQDVRLLQEIVDQCMNRS---IALTQARYLekeEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVL 317
Cdd:PLN02822  403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTL---DKCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 2-312 7.45e-53

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: 176.98  E-value: 7.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   2 KTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEqeiedqkNPRKAR 81
Cdd:cd06454    60 GKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRE-------ARRPYG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  82 vtRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVtEHYGINIDDIDLISANMENALASIGG 161
Cdd:cd06454   133 --KKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 162 FCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIsGLKVVGESLSPAFHL 241
Cdd:cd06454   210 YIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPL 288

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370513612 242 QLEEStgsreqdvRLLQEIVDQCMNRSIALTQARY---LEKEEKclpppsIRVVVTVEQTEEELERAASTIKEV 312
Cdd:cd06454   289 IGDDP--------AKAVAFSDALLERGIYVQAIRYptvPRGTAR------LRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 1-315 1.81e-51

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: 174.08  E-value: 1.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRA--ACfaIQKGLQASRSDIKLFKHNDMADLERLLKEqeiedqknPR 78
Cdd:COG0156    95 LGKEAALLFSSGYAANLGVISALAGRGDLIFSDELnhAS--IIDGARLSGAKVVRFRHNDMDDLERLLKK--------AR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  79 KARvtRRFIVVEGLY-MnTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGInIDDIDLISANMENALA 157
Cdd:COG0156   165 AAR--RKLIVTDGVFsM-DGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 158 SIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIsGLKvVGESLSP 237
Cdd:COG0156   241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFD-LGPSESP 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 238 AFHLQLEestgsreqDVRLLQEIVDQCMNRSIALTQARYlekeekclppPS-------IRVVVTVEQTEEELERAASTIK 310
Cdd:COG0156   319 IVPVIVG--------DAERALALADALLERGIYVSAIRP----------PTvpkgtarLRITLSAAHTEEDIDRLLEALA 380


                  ....*
gi 1370513612 311 EVAQA 315
Cdd:COG0156   381 EVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
2-309 4.63e-15

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 74.65  E-value: 4.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   2 KTEEAIIYSYGFATIASAIPAYSK-RGDIVFVDRAACFAIQKGLQASRSDIKLFK-------HNDMADLERLLKEQeied 73
Cdd:pfam00155  61 DREAAVVFGSGAGANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  74 qknprkarvtRRFIVVEGLYMNTGTICPLPELVKL---KYKYKARIFLEESLSFGVLGEHGRgVTEHYGINiDDIDLISA 150
Cdd:pfam00155 137 ----------PKVVLHTSPHNPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDA-VATRALLA-EGPNLLVV 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 151 N-MENALASIG---GFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIs 226
Cdd:pfam00155 205 GsFSKAFGLAGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA- 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 227 GLKVVGeSLSPAFHLQLeestGSREQDVRLLQEIVDQCmnrSIALTQARYLEKeekclpPPSIRVVVTVeQTEEELERAA 306
Cdd:pfam00155 284 GLSVLP-SQAGFFLLTG----LDPETAKELAQVLLEEV---GVYVTPGSSPGV------PGWLRITVAG-GTEEELEELL 348


                  ...
gi 1370513612 307 STI 309
Cdd:pfam00155 349 EAI 351
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 1-317 2.83e-117

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 346.73  E-value: 2.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDqknpRKA 80
Cdd:PLN02822  167 LGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN----KRK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  81 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIG 160
Cdd:PLN02822  243 KKLRRYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEG 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 161 GFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFH 240
Cdd:PLN02822  323 GFCTGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVF 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 241 LQLEESTGSREQDVRLLQEIVDQCMNRS---IALTQARYLekeEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVL 317
Cdd:PLN02822  403 LHLEKSTGSAKEDLSLLEHIADRMLKEDsvlVVVSKRSTL---DKCRLPVGIRLFVSAGHTESDILKASESLKRVAASVL 479
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 1-317 1.69e-83

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 257.14  E-value: 1.69e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKA 80
Cdd:PLN03227   56 LGTESAILYSDGASTTSSTVAAFAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRKP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  81 RVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGIN-IDDIDLISANMENALASI 159
Cdd:PLN03227  136 TDQRRFLVVEGLYKNTGTLAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKpMVHAEIVTFSLENAFGSV 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 160 GGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIS---------GLKV 230
Cdd:PLN03227  216 GGMTVGSEEVVDHQRLSGSGYCFSASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSShpyalklrnRLVI 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 231 VGESLSPAFHLQLEESTGSREQD-VRLLQEIVDQCMNRSIALTQAR-YLEKEEKCLPPPSIRVVVTVEQTEEELERAAST 308
Cdd:PLN03227  296 TSDPISPIIYLRLSDQEATRRTDeTLILDQIAHHSLSEGVAVVSTGgHVKKFLQLVPPPCLRVVANASHTREDIDKLLTV 375


                  ....*....
gi 1370513612 309 IKEVAQAVL 317
Cdd:PLN03227  376 LGEAVEAIL 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 2-312 7.45e-53

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: 176.98  E-value: 7.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   2 KTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEqeiedqkNPRKAR 81
Cdd:cd06454    60 GKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRE-------ARRPYG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  82 vtRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVtEHYGINIDDIDLISANMENALASIGG 161
Cdd:cd06454   133 --KKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 162 FCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIsGLKVVGESLSPAFHL 241
Cdd:cd06454   210 YIAGSKELIDYLRSYARGFIFSTSLPPAVAAAALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSPSHIIPPL 288

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370513612 242 QLEEStgsreqdvRLLQEIVDQCMNRSIALTQARY---LEKEEKclpppsIRVVVTVEQTEEELERAASTIKEV 312
Cdd:cd06454   289 IGDDP--------AKAVAFSDALLERGIYVQAIRYptvPRGTAR------LRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 1-315 1.81e-51

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: 174.08  E-value: 1.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRA--ACfaIQKGLQASRSDIKLFKHNDMADLERLLKEqeiedqknPR 78
Cdd:COG0156    95 LGKEAALLFSSGYAANLGVISALAGRGDLIFSDELnhAS--IIDGARLSGAKVVRFRHNDMDDLERLLKK--------AR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  79 KARvtRRFIVVEGLY-MnTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGInIDDIDLISANMENALA 157
Cdd:COG0156   165 AAR--RKLIVTDGVFsM-DGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGL-EDRVDIIMGTLSKALG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 158 SIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIsGLKvVGESLSP 237
Cdd:COG0156   241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFD-LGPSESP 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 238 AFHLQLEestgsreqDVRLLQEIVDQCMNRSIALTQARYlekeekclppPS-------IRVVVTVEQTEEELERAASTIK 310
Cdd:COG0156   319 IVPVIVG--------DAERALALADALLERGIYVSAIRP----------PTvpkgtarLRITLSAAHTEEDIDRLLEALA 380


                  ....*
gi 1370513612 311 EVAQA 315
Cdd:COG0156   381 EVGKE 385
PLN02483 PLN02483
serine palmitoyltransferase
 4-316 2.82e-38

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 141.44  E-value: 2.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   4 EEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQknPRKARVT 83
Cdd:PLN02483  162 PAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQ--PRTHRPW 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  84 RRFIV-VEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIGGF 162
Cdd:PLN02483  240 KKIIViVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 163 CCGRSFVIDHQRLSGQGYCFSASL-PPLLAAAAIEALNIMEE---NPGifavlKEKCGQIHK-------ALQGIsGLKVV 231
Cdd:PLN02483  320 IAGSKELIQYLKRTCPAHLYATSMsPPAVQQVISAIKVILGEdgtNRG-----AQKLAQIREnsnffrsELQKM-GFEVL 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 232 GESLSPAFHLQLEESTG----SREqdvrllqeivdqCMNRSIALTQARYlekeeKCLPP--PSIRVVVTVEQTEEELERA 305
Cdd:PLN02483  394 GDNDSPVMPIMLYNPAKipafSRE------------CLKQNVAVVVVGF-----PATPLllARARICISASHSREDLIKA 456

                         330
                  ....*....|.
gi 1370513612 306 ASTIKEVAQAV 316
Cdd:PLN02483  457 LEVISEVGDLV 467
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 3-313 1.32e-27

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 110.63  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   3 TEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLkeqeiedqknpRKARV 82
Cdd:PRK05958   99 AERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALL-----------AKWRA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  83 TRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGInIDDIDLIS-ANMENALASIGG 161
Cdd:PRK05958  168 GRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGL-AGEPDVILvGTLGKALGSSGA 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 162 FCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGISglKVVGESLSPAFHL 241
Cdd:PRK05958  247 AVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALG--FQLMDSQSAIQPL 324

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513612 242 QLeestGSREQDVRLLQeivdQCMNRSIALTqarylekeekCLPPPS-------IRVVVTVEQTEEELERAASTIKEVA 313
Cdd:PRK05958  325 IV----GDNERALALAA----ALQEQGFWVG----------AIRPPTvpagtsrLRITLTAAHTEADIDRLLEALAEAL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 2-188 1.49e-23

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 99.50  E-value: 1.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   2 KTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQeiedqknpRKAR 81
Cdd:PRK06939  101 GTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEA--------KEAG 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  82 VTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGInIDDIDLISANMENALA-SIG 160
Cdd:PRK06939  173 ARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGV-MDRVDIITGTLGKALGgASG 251

                         170       180
                  ....*....|....*....|....*...
gi 1370513612 161 GFCCGRSFVIDHQRLSGQGYCFSASLPP 188
Cdd:PRK06939  252 GYTAGRKEVIDWLRQRSRPYLFSNSLAP 279
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 4-188 5.47e-21

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 92.61  E-value: 5.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   4 EEAIIYSYGFATIASAIPAYSKR--GDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKnprkar 81
Cdd:PRK13392  107 ESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPK------ 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  82 vtrrFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGInIDDIDLISANMENALASIGG 161
Cdd:PRK13392  181 ----LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGG 255

                         170       180
                  ....*....|....*....|....*..
gi 1370513612 162 FCCGRSFVIDHQRLSGQGYCFSASLPP 188
Cdd:PRK13392  256 YIAASADLIDFVRSFAPGFIFTTALPP 282
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
2-309 4.63e-15

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 74.65  E-value: 4.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   2 KTEEAIIYSYGFATIASAIPAYSK-RGDIVFVDRAACFAIQKGLQASRSDIKLFK-------HNDMADLERLLKEQeied 73
Cdd:pfam00155  61 DREAAVVFGSGAGANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK---- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  74 qknprkarvtRRFIVVEGLYMNTGTICPLPELVKL---KYKYKARIFLEESLSFGVLGEHGRgVTEHYGINiDDIDLISA 150
Cdd:pfam00155 137 ----------PKVVLHTSPHNPTGTVATLEELEKLldlAKEHNILLLVDEAYAGFVFGSPDA-VATRALLA-EGPNLLVV 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 151 N-MENALASIG---GFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKEKCGQIHKALQGIs 226
Cdd:pfam00155 205 GsFSKAFGLAGwrvGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA- 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612 227 GLKVVGeSLSPAFHLQLeestGSREQDVRLLQEIVDQCmnrSIALTQARYLEKeekclpPPSIRVVVTVeQTEEELERAA 306
Cdd:pfam00155 284 GLSVLP-SQAGFFLLTG----LDPETAKELAQVLLEEV---GVYVTPGSSPGV------PGWLRITVAG-GTEEELEELL 348


                  ...
gi 1370513612 307 STI 309
Cdd:pfam00155 349 EAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
1-188 5.62e-14

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 71.96  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   1 MKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLkeqeiedqknprka 80
Cdd:PRK07179  112 TGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQI-------------- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  81 rvtRRF----IVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINiDDIDLISANMENAL 156
Cdd:PRK07179  178 ---ERHgpgiIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAF 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370513612 157 ASIGGFCCGRSFVIDHQRLSGQGYCFSASLPP 188
Cdd:PRK07179  254 AGRAGIITCPRELAEYVPFVSYPAIFSSTLLP 285
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 4-139 3.41e-12

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 66.34  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612   4 EEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQeiedqknpRKARVT 83
Cdd:PRK05937   72 PEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESC--------RQRSFG 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370513612  84 RRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYG 139
Cdd:PRK05937  144 RIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG 199
PRK07505 PRK07505
hypothetical protein; Provisional
 16-162 4.21e-10

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 59.99  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  16 IASAIPAYSKRGDIVFvDRAA--CFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEiedqknprkarvtRRFIVVEGLY 93
Cdd:PRK07505  125 LASGHLTGGVPPHMVF-DKNAhaSLNILKGICADETEVETIDHNDLDALEDICKTNK-------------TVAYVADGVY 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513612  94 mNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRG-VTEHYGINIDDIDLISANMENALASIGGF 162
Cdd:PRK07505  191 -SMGGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERTIIAASLGKAFGASGGV 259
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH