NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488368310|ref|WP_002437695|]
View 

MULTISPECIES: aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [Staphylococcus]

Protein Classification

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 10157841)

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme similar to Sphingomonas paucimobilis serine palmitoyltransferase (SPT) that catalyzes the condensation of L-serine and palmitoyl-CoA, the first step in the de novo sphingolipid biosynthetic pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
35-370 4.44e-144

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: 412.34  E-value: 4.44e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  35 QSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNI 114
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 115 FKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQR 194
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 195 YNAILIIDASHSLGLN---------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLY 265
Cdd:cd06454  161 YGAILFVDEAHSVGVYgphgrgveeFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 266 FIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSN-TPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQ 344
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320
                        330       340
                 ....*....|....*....|....*...
gi 488368310 345 PT--LRISLSYFHDTDDIDRLFNVMKQY 370
Cdd:cd06454  321 GTarLRISLSAAHTKEDIDRLLEALKEV 348
 
Name Accession Description Interval E-value
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
35-370 4.44e-144

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: 412.34  E-value: 4.44e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  35 QSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNI 114
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 115 FKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQR 194
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 195 YNAILIIDASHSLGLN---------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLY 265
Cdd:cd06454  161 YGAILFVDEAHSVGVYgphgrgveeFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 266 FIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSN-TPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQ 344
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320
                        330       340
                 ....*....|....*....|....*...
gi 488368310 345 PT--LRISLSYFHDTDDIDRLFNVMKQY 370
Cdd:cd06454  321 GTarLRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
3-369 2.43e-118

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: 348.19  E-value: 2.43e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   3 IKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGigqLEYQP---QNFLDFIKTYSIHLSSSRLVSGNS 79
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLG---LANHPrviEAAAEALDRYGTGSGGSRLVSGTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  80 VVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLA 159
Cdd:COG0156   82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 160 RHTnPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADIDIVTSSLSKAWG 230
Cdd:COG0156  162 KAR-AARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGvlgetgrglVEHFGLEDRVDIIMGTLSKALG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 231 AHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPlSNTPI 309
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELgFDLGP-SESPI 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488368310 310 KNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:COG0156  320 VPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTarLRITLSAAHTEEDIDRLLEALAE 381
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
2-369 1.91e-92

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 282.05  E-value: 1.91e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   2 DIKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVV 81
Cdd:PRK05958   6 RLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  82 YQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARH 161
Cdd:PRK05958  86 HEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 162 TNPdvQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADID-IVTSSLSKAWGA 231
Cdd:PRK05958 166 RAG--RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGvlgpqgrglAAEAGLAGEPDvILVGTLGKALGS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 232 HGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKN 311
Cdd:PRK05958 244 SGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQP 323
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 312 IVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PRK05958 324 LIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTsrLRITLTAAHTEADIDRLLEALAE 383
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
20-368 4.55e-84

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303 [Multi-domain]  Cd Length: 360  Bit Score: 259.89  E-value: 4.55e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   20 QPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDAL 99
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  100 IFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDvQKVIVSDSVFSTN 179
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGER-RKLIVTDGVFSMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  180 GTKADINRLVHLKQRYNAILIIDASHSLG------LNLFEY----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINK 249
Cdd:TIGR00858 160 GDIAPLPQLVALAERYGAWLMVDDAHGTGvlgedgRGTLEHfglkPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  250 GRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKNIVCDSLASAQAQYDMLFE 329
Cdd:TIGR00858 240 ARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQ 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 488368310  330 HGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMK 368
Cdd:TIGR00858 320 QGIFVGAIRPPTVPAGTsrLRLTLSAAHTPGDIDRLAEALK 360
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
38-363 1.65e-28

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 113.94  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   38 INFTSNDYLGiGQLEYQPQNFLDfiktysIHLSSSRLVSGNSVVYQQLEQAISEHFNF--------EDALIFNSGYDANL 109
Cdd:pfam00155   4 INLGSNEYLG-DTLPAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGANI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  110 AVFN-IFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIY-------QHLNYDDLESHLARHTnpdvqKVIVSDSVFSTNG- 180
Cdd:pfam00155  77 EALIfLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKP-----KVVLHTSPHNPTGt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  181 --TKADINRLVHLKQRYNAILIIDASHS-LGLNLFEYHADI--------DIVTSSLSKAWGAHG---GVIFSSKDIKDLI 246
Cdd:pfam00155 152 vaTLEELEKLLDLAKEHNILLLVDEAYAgFVFGSPDAVATRallaegpnLLVVGSFSKAFGLAGwrvGYILGNAAVISQL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  247 INKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPLSNTPIKNIVCDSLASAQAQYD 325
Cdd:pfam00155 232 RKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAgLSVLPSQAGFFLLTGLDPETAKELAQV 311
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 488368310  326 MLFEHGIFVSYLRYPTVSqPTLRISLSYfHDTDDIDRL 363
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP-GWLRITVAG-GTEEELEEL 347
 
Name Accession Description Interval E-value
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
35-370 4.44e-144

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: 412.34  E-value: 4.44e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  35 QSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNI 114
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 115 FKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQR 194
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 195 YNAILIIDASHSLGLN---------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLY 265
Cdd:cd06454  161 YGAILFVDEAHSVGVYgphgrgveeFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 266 FIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSN-TPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQ 344
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320
                        330       340
                 ....*....|....*....|....*...
gi 488368310 345 PT--LRISLSYFHDTDDIDRLFNVMKQY 370
Cdd:cd06454  321 GTarLRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
3-369 2.43e-118

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: 348.19  E-value: 2.43e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   3 IKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGigqLEYQP---QNFLDFIKTYSIHLSSSRLVSGNS 79
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLG---LANHPrviEAAAEALDRYGTGSGGSRLVSGTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  80 VVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLA 159
Cdd:COG0156   82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 160 RHTnPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADIDIVTSSLSKAWG 230
Cdd:COG0156  162 KAR-AARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGvlgetgrglVEHFGLEDRVDIIMGTLSKALG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 231 AHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPlSNTPI 309
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELgFDLGP-SESPI 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488368310 310 KNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:COG0156  320 VPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTarLRITLSAAHTEEDIDRLLEALAE 381
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
2-369 1.91e-92

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 282.05  E-value: 1.91e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   2 DIKAQLKQIQDKVLYRELQPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVV 81
Cdd:PRK05958   6 RLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  82 YQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARH 161
Cdd:PRK05958  86 HEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 162 TNPdvQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADID-IVTSSLSKAWGA 231
Cdd:PRK05958 166 RAG--RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGvlgpqgrglAAEAGLAGEPDvILVGTLGKALGS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 232 HGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKN 311
Cdd:PRK05958 244 SGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQP 323
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 312 IVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PRK05958 324 LIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTsrLRITLTAAHTEADIDRLLEALAE 383
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
20-368 4.55e-84

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303 [Multi-domain]  Cd Length: 360  Bit Score: 259.89  E-value: 4.55e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   20 QPIQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDAL 99
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  100 IFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDvQKVIVSDSVFSTN 179
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGER-RKLIVTDGVFSMD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  180 GTKADINRLVHLKQRYNAILIIDASHSLG------LNLFEY----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINK 249
Cdd:TIGR00858 160 GDIAPLPQLVALAERYGAWLMVDDAHGTGvlgedgRGTLEHfglkPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  250 GRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMELFPDQPLSNTPIKNIVCDSLASAQAQYDMLFE 329
Cdd:TIGR00858 240 ARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQ 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 488368310  330 HGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMK 368
Cdd:TIGR00858 320 QGIFVGAIRPPTVPAGTsrLRLTLSAAHTPGDIDRLAEALK 360
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
2-362 1.96e-59

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 197.34  E-value: 1.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   2 DIKAQLKQIQDKVLYRELQPIQSVEKQYIYIND-QSYINFTSNDYLGIG---QLEYQPQNFLDfikTYSIHLSSSRLVSG 77
Cdd:PRK06939   8 QLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLAnhpELIAAAKAALD---SHGFGMASVRFICG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  78 NSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESH 157
Cdd:PRK06939  85 TQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 158 L-------ARHtnpdvqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG---------LNLFEYHADIDIV 221
Cdd:PRK06939 165 LkeakeagARH------KLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGfvgengrgtVEHFGVMDRVDII 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 222 TSSLSKA-WGAHGGVIFSSKDIKDLIINKGRSLIYSSSL-PSYHLYFIQVsLQHVIEDTYRREKLNVLSEYFNHQFMELF 299
Cdd:PRK06939 239 TGTLGKAlGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLaPAIVAASIKV-LELLEESDELRDRLWENARYFREGMTAAG 317
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368310 300 PDQPLSNTPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPTLRI--SLSYFHDTDDIDR 362
Cdd:PRK06939 318 FTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIrtQMSAAHTKEQLDR 382
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
42-367 4.32e-49

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: 170.29  E-value: 4.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   42 SNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVF----NIFKN 117
Cdd:TIGR01821  52 SNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLatlaKIIPG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  118 nnVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARhTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNA 197
Cdd:TIGR01821 132 --CVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQS-VDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  198 ILIIDASHSLGL---------NLFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYFIQ 268
Cdd:TIGR01821 209 LTYLDEVHAVGLygprgggiaERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  269 VSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FP--DQPLSNTPIknIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQP 345
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALgIPviPNPSHIVPV--IIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRG 366
                         330       340
                  ....*....|....*....|....
gi 488368310  346 T--LRISLSYFHDTDDIDRLFNVM 367
Cdd:TIGR01821 367 TerLRITPTPAHTDKMIDDLVEAL 390
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
42-363 7.55e-45

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 159.25  E-value: 7.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  42 SNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIF--KNNN 119
Cdd:PRK13392  53 SNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPG 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 120 VVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARhTNPDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAIL 199
Cdd:PRK13392 133 CVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLAS-VDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALT 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 200 IIDASHSLGLnlfeYHAD-------------IDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYHLYF 266
Cdd:PRK13392 212 YVDEVHAVGL----YGARgggiaerdglmdrIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAG 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 267 IQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPlSNTPIKNIVCDSLASAQAQYDMLF-EHGIFVSYLRYPTVSQ 344
Cdd:PRK13392 288 ATAAIRHLKTSQTERDAHQDRVAALKAKLNANgIPVMP-SPSHIVPVMVGDPTLCKAISDRLMsEHGIYIQPINYPTVPR 366
                        330       340
                 ....*....|....*....|.
gi 488368310 345 PT--LRISLSYFHDTDDIDRL 363
Cdd:PRK13392 367 GTerLRITPTPLHDDEDIDAL 387
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
40-363 1.03e-41

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 152.52  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  40 FTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVF------- 112
Cdd:PLN02955 107 FSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMvaigsva 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 113 -------NIFKNNNVVIFSDQQNHASIIDGIKLS---GLSKV-IYQHLNYDDLESHLARHTNPdvQKVIVSDSVFSTNGT 181
Cdd:PLN02955 187 sllaasgKPLKNEKVAIFSDALNHASIIDGVRLAerqGNVEVfVYRHCDMYHLNSLLSSCKMK--RKVVVTDSLFSMDGD 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 182 KADINRLVHLKQRYNAILIIDASHSL---GLN------LFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRS 252
Cdd:PLN02955 265 FAPMEELSQLRKKYGFLLVIDDAHGTfvcGENgggvaeEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRS 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 253 LIYSSSLPsyhLYFIQVSLQHVI---EDTYRREKL-NVLSEyfnhqFMELfPDQPLSnTPIKNIVCDSLASAQAQYDMLF 328
Cdd:PLN02955 345 FIFSTAIP---VPMAAAAYAAVVvarKEKWRRKAIwERVKE-----FKAL-SGVDIS-SPIISLVVGNQEKALKASRYLL 414
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 488368310 329 EHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRL 363
Cdd:PLN02955 415 KSGFHVMAIRPPTVPPNScrLRVTLSAAHTTEDVKKL 451
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
38-372 8.35e-35

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 131.44  E-value: 8.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  38 INFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLS-------SSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLA 110
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVHEVEKRYRLYCRQFPhaqlgygGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 111 V-FNIFKNNNVViFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTNPDVQKV-IVSDSVFSTNGTKADINRL 188
Cdd:PRK05937  87 LcAHLSSVTDYV-LWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIfIFVCSVYSFKGTLAPLEQI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL---------------NLFEyhadidiVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSL 253
Cdd:PRK05937 166 IALSKKYHAHLIVDEAHAMGIfgddgkgfchslgyeNFYA-------VLVTYSKALGSMGAALLSSSEVKQDLMLNSPPL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 254 IYSSSLPSYHLYFIQVSLQH-VIEDTYRREKLNVLSEYFNHQFMELFPD--QPLSNTPIknivcdslaSAQAQYDMLFEH 330
Cdd:PRK05937 239 RYSTGLPPHLLISIQVAYDFlSQEGELARKQLFRLKEYFAQKFSSAAPGcvQPIFLPGI---------SEQELYSKLVET 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 488368310 331 GIFVSYLRYPTvsQPTLRISLSYFHDTDDIDRLFNVMKQYDE 372
Cdd:PRK05937 310 GIRVGVVCFPT--GPFLRVNLHAFNTEDEVDILVSVLATYLE 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
38-363 1.65e-28

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 113.94  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   38 INFTSNDYLGiGQLEYQPQNFLDfiktysIHLSSSRLVSGNSVVYQQLEQAISEHFNF--------EDALIFNSGYDANL 109
Cdd:pfam00155   4 INLGSNEYLG-DTLPAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGANI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  110 AVFN-IFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIY-------QHLNYDDLESHLARHTnpdvqKVIVSDSVFSTNG- 180
Cdd:pfam00155  77 EALIfLLANPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKP-----KVVLHTSPHNPTGt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  181 --TKADINRLVHLKQRYNAILIIDASHS-LGLNLFEYHADI--------DIVTSSLSKAWGAHG---GVIFSSKDIKDLI 246
Cdd:pfam00155 152 vaTLEELEKLLDLAKEHNILLLVDEAYAgFVFGSPDAVATRallaegpnLLVVGSFSKAFGLAGwrvGYILGNAAVISQL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  247 INKGRSLIYSSSLPSYHLYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQPLSNTPIKNIVCDSLASAQAQYD 325
Cdd:pfam00155 232 RKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAgLSVLPSQAGFFLLTGLDPETAKELAQV 311
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 488368310  326 MLFEHGIFVSYLRYPTVSqPTLRISLSYfHDTDDIDRL 363
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP-GWLRITVAG-GTEEELEEL 347
PRK07505 PRK07505
hypothetical protein; Provisional
22-369 2.66e-28

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 114.31  E-value: 2.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  22 IQSVEKQYIYINDQS---YINFTSNDYLGigqLEYQPQ---NFLDFIKTY-SIHLSSSRLVSgNSVVYQQLEQAISEHFN 94
Cdd:PRK07505  30 LTVGEREGILITLADghtFVNFVSCSYLG---LDTHPAiieGAVDALKRTgSLHLSSSRTRV-RSQILKDLEEALSELFG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  95 FEdALIFNSGYDANLAVF-----NIFKNN-NVVIFSDQQNHAS--IIDGIkLSGLSKVIY-QHLNYDDLESHLARHTNPd 165
Cdd:PRK07505 106 AS-VLTFTSCSAAHLGILpllasGHLTGGvPPHMVFDKNAHASlnILKGI-CADETEVETiDHNDLDALEDICKTNKTV- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 166 vqkVIVSDSVFSTNGtKADINRLVHLKQRYNAILIIDASHSL--------GLNLFEYHADID---IVTSSLSKAWGAHGG 234
Cdd:PRK07505 183 ---AYVADGVYSMGG-IAPVKELLRLQEKYGLFLYIDDAHGLsiygkngeGYVRSELDYRLNertIIAASLGKAFGASGG 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 235 VIF-SSKDIKDLIINKGRSLIYSSSLPSYHLYFIQVSLQ-HVIED-TYRREKLNVLSEYFNhqfmELFP-DQPLSNTPIK 310
Cdd:PRK07505 259 VIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEiHLSEElDQLQQKLQNNIALFD----SLIPtEQSGSFLPIR 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488368310 311 NIVCDSLASAQAQYDMLFEHGIFVSYLRYPTVSQPT--LRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PRK07505 335 LIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRagLRIMFRASHTNDEIKRLCSLLKE 395
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
38-374 1.05e-25

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 107.02  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  38 INFTSNDYLGIGQleyQPQNFLDFIKTYSIH-----LSSSRLVSGNSVvyQQLEQAISEHFNFEDALIFNSGYDANLAVF 112
Cdd:PRK07179  57 IILQSNDYLNLSG---HPDIIKAQIAALQEEgdslvMSAVFLHDDSPK--PQFEKKLAAFTGFESCLLCQSGWAANVGLL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 113 NIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARHTnpdvQKVIVSDSVFSTNGTKADINRLVHLK 192
Cdd:PRK07179 132 QTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHG----PGIIVVDSVYSTTGTIAPLADIVDIA 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 193 QRYNAILIIDASHSLG---------LNLFEYHADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSSLPSYH 263
Cdd:PRK07179 208 EEFGCVLVVDESHSLGthgpqgaglVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHE 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 264 LYFIQVSLQHVIEDTYRREKLNVLSEYFNHQFMEL-FPDQplSNTPIKNIVCDSLASAQAQYDMLFEHGIFVSYLRYPTV 342
Cdd:PRK07179 288 IAGLEATLEVIESADDRRARLHANARFLREGLSELgYNIR--SESQIIALETGSERNTEVLRDALEERNVFGAVFCAPAT 365
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 488368310 343 SQ--PTLRISLSYFHDTDDIDRLFNVMKQ-YDEGD 374
Cdd:PRK07179 366 PKnrNLIRLSLNADLTASDLDRVLEVCREaRDEVD 400
PLN02822 PLN02822
serine palmitoyltransferase
22-369 6.72e-22

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 96.73  E-value: 6.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  22 IQSVEKQYIYINDQSYINFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIF 101
Cdd:PLN02822  96 LESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILY 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 102 NSGYDANLAVFNIFKNNNVVIFSDQQNHASIIDGIKLSgLSKVIY-QHLNYDDLESHLARHTNPD-----VQKVIVSDSV 175
Cdd:PLN02822 176 SYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLS-RSTIVYfKHNDMESLRNTLEKLTAENkrkkkLRRYIVVEAI 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 176 FSTNGTKADINRLVHLKQRYNAILIIDASHSLGL------NLFEYHA----DIDIVTSSLSKAWGAHGGVIFSSKDIKDL 245
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVlgksgrGLSEHFGvpieKIDIITAAMGHALATEGGFCTGSARVVDH 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 246 IINKGRSLIYSSSLPSYhLYFIQVSLQHVIED-----TYRREKLNVLseyfnHQFMELFPDQPLSNTPIKNIVC----DS 316
Cdd:PLN02822 335 QRLSSSGYVFSASLPPY-LASAAITAIDVLEDnpsvlAKLKENIALL-----HKGLSDIPGLSIGSNTLSPIVFlhleKS 408
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488368310 317 LASAQAQYD--------MLFEHGIFVSYLRYPTVSQ----PTLRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PLN02822 409 TGSAKEDLSllehiadrMLKEDSVLVVVSKRSTLDKcrlpVGIRLFVSAGHTESDILKASESLKR 473
PLN02483 PLN02483
serine palmitoyltransferase
38-260 8.23e-22

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 96.76  E-value: 8.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  38 INFTSNDYLGIGQL-EYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFK 116
Cdd:PLN02483 103 LNLGSYNYLGFAAAdEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALI 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 117 NNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHLARH-------TNPDVQKVIV-SDSVFSTNGTKADINRL 188
Cdd:PLN02483 183 GKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqprTHRPWKKIIViVEGIYSMEGELCKLPEI 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL------NLFEY----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSSS 258
Cdd:PLN02483 263 VAVCKKYKAYVYLDEAHSIGAvgktgrGVCELlgvdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATS 342

                 ..
gi 488368310 259 LP 260
Cdd:PLN02483 343 MS 344
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
38-369 5.07e-19

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 87.65  E-value: 5.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  38 INFTSNDYLGIGQLEYQPQNFLDFIKTYSIHLSSSRLVSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKN 117
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 118 NNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDL---------ESHLARHTNPDVQKVIVSDSVFSTNGTKADINRL 188
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 189 VHLKQRYNAILIIDASHSLGL------NLFEY-----HADIDIVTSSLSKAWGAHGGVIFSSKDIKDLIINKGRSLIYSS 257
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTlgksgrGSLEHaglkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 258 SLPSYHLYFIQVSLQHVIED-----------TYRREKLNVLSEYFNHQFMELF-----PDQP-----LSNTPIKNIVCDS 316
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGpqllnrlhdsiANLYSTLTNSSHPYALKLRNRLvitsdPISPiiylrLSDQEATRRTDET 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488368310 317 LASAQAQYDMLFEHGIFVSYLRYPT-----VSQPTLRISLSYFHDTDDIDRLFNVMKQ 369
Cdd:PLN03227 321 LILDQIAHHSLSEGVAVVSTGGHVKkflqlVPPPCLRVVANASHTREDIDKLLTVLGE 378
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
82-237 3.86e-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: 49.69  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  82 YQQLEQAISEHFN--FEDALIFNSGYDANLAVF-NIFKNNNVVIFSDQQNHASIIDGIKLSGLSKVIYQHLNYDDLESHL 158
Cdd:cd01494    2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALlALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 159 ARHTN---PDVQKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLG-------LNLFEYhadIDIVTSSLSKA 228
Cdd:cd01494   82 AILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspapgvLIPEGG---ADVVTFSLHKN 158
                        170
                 ....*....|
gi 488368310 229 WGAHG-GVIF 237
Cdd:cd01494  159 LGGEGgGVVI 168
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
82-369 2.11e-06

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: 49.26  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  82 YQQLEQAISEHFNF--------EDALIFNSGYDANLAVFNIFKNNN-VVIFSDQqNHASIIDGIKLSGLsKVIYQHLNYD 152
Cdd:cd00609   38 LPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGdEVLVPDP-TYPGYEAAARLAGA-EVVPVPLDEE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 153 ----DLESHLARHTNPDVqKVIV-------SDSVFStngtKADINRLVHLKQRYNAILIIDASHS--------LGLNLFE 213
Cdd:cd00609  116 ggflLDLELLEAAKTPKT-KLLYlnnpnnpTGAVLS----EEELEELAELAKKHGILIISDEAYAelvydgepPPALALL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 214 YHADIDIVTSSLSKAWGAHG---G-VIFSSKDIKDLIINKGRSLIYSSSLPSYHL--YFIQVSLQHVIE--DTY--RREK 283
Cdd:cd00609  191 DAYERVIVLRSFSKTFGLPGlriGyLIAPPEELLERLKKLLPYTTSGPSTLSQAAaaAALDDGEEHLEElrERYrrRRDA 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 284 L-NVLSEYFNHQFME------LFPDqplsntpiknivCDSLASAQAQYDMLFEHGIFVSYLR-YPTVSQPTLRISLSYfh 355
Cdd:cd00609  271 LlEALKELGPLVVVKpsggffLWLD------------LPEGDDEEFLERLLLEAGVVVRPGSaFGEGGEGFVRLSFAT-- 336
                        330
                 ....*....|....
gi 488368310 356 DTDDIDRLFNVMKQ 369
Cdd:cd00609  337 PEEELEEALERLAE 350
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
32-231 2.01e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 46.29  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  32 INDQSYINFtsnDYLGIGQLeyqPQNFLDFIKTY------SIHLSSSRLVSGNSVVYQQLEQAISEHFN--FEDALIFNS 103
Cdd:COG0520   11 VLGKPLVYL---DNAATGQK---PRPVIDAIRDYyepynaNVHRGAHELSAEATDAYEAAREKVARFIGaaSPDEIIFTR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 104 GydA----NLAV--FNIFKNNNVVIFSDQQNHASII--------DGIKLsglsKVIY----QHLNYDDLESHLARHTnpd 165
Cdd:COG0520   85 G--TteaiNLVAygLGRLKPGDEILITEMEHHSNIVpwqelaerTGAEV----RVIPldedGELDLEALEALLTPRT--- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488368310 166 vqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLGlnlfeyHADIDIvtsslsKAWGA 231
Cdd:COG0520  156 --KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP------HLPVDV------QALGC 207
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
85-253 3.78e-03

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 39.11  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  85 LEQAISEHFNFEDALIFNSGYDANLAVFNIFKN--NNVVIFSD--QQNHASIIDGIKLSGLS-KVIYQhLNYDDLESHLA 159
Cdd:cd00614   45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagDHVVASDDlyGGTYRLFERLLPKLGIEvTFVDP-DDPEALEAAIK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310 160 RHTnpdvqKVIVSDSVFSTNGTKADINRLVHLKQRYNAILIIDASHSLGLNL--FEYHADIdiVTSSLSKAWGAHGGVIF 237
Cdd:cd00614  124 PET-----KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQrpLELGADI--VVHSATKYIGGHSDVIA 196
                        170       180
                 ....*....|....*....|.
gi 488368310 238 -----SSKDIKDLIINKGRSL 253
Cdd:cd00614  197 gvvvgSGEALIQRLRFLRLAL 217
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
75-241 6.35e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 37.97  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310   75 VSGNSVVYQQLEQAISEHFNFEDALIFNSGYDANLAVFNIFKNNNVVIFSDQQNH--------ASIIDGIKLSGlskVIY 146
Cdd:pfam01212  27 VYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHihfdetggHAELGGVQPRP---LDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488368310  147 QHLNY---DDLESHLAR---HTNPDVQKVIVSDSVFSTNGT---KADINRLVHLKQRYNAILIID------ASHSLGLNL 211
Cdd:pfam01212 104 DEAGNmdlEDLEAAIREvgaDIFPPTGLISLENTHNSAGGQvvsLENLREIAALAREHGIPVHLDgarfanAAVALGVIV 183
                         170       180       190
                  ....*....|....*....|....*....|.
gi 488368310  212 FEYHADIDIVTSSLSKAWGAH-GGVIFSSKD 241
Cdd:pfam01212 184 KEITSYADSVTMCLSKGLGAPvGSVLAGSDD 214
 
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
HHS Vulnerability Disclosure