NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491602495|ref|WP_005460056|]
View 

8-amino-7-oxononanoate synthase [Vibrio parahaemolyticus]

Protein Classification

8-amino-7-oxononanoate synthase( domain architecture ID 10012622)

8-amino-7-oxononanoate synthase catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide in the biosynthesis of biotin

CATH:  3.40.640.10|3.90.1150.10
EC:  2.3.1.47
Gene Ontology:  GO:0030170|GO:0009102|GO:0008710|GO:0042803
PubMed:  10800595|10673430|17109392

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 2-380 0e+00

8-amino-7-oxononanoate synthase; Reviewed


:

Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 545.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   2 PAFKSRIESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVT 81
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  82 GFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLET 161
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 162 LFTN--EGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCE---LANVKPEILVVTFGKA 236
Cdd:PRK05958 161 LLAKwrAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAeagLAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 237 FGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLD-GFVETDTP 315
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGfQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491602495 316 IKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 2-380 0e+00

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 545.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   2 PAFKSRIESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVT 81
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  82 GFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLET 161
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 162 LFTN--EGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCE---LANVKPEILVVTFGKA 236
Cdd:PRK05958 161 LLAKwrAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAeagLAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 237 FGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLD-GFVETDTP 315
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGfQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491602495 316 IKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 4-380 5.22e-169

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: 477.24  E-value: 5.22e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   4 FKSRIESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGF 83
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  84 SAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETL- 162
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 163 --FTNEGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPE--ILVVTFGKAFG 238
Cdd:COG0156  161 kkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 239 MSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGF--VETDTPI 316
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFdlGPSESPI 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491602495 317 KPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:COG0156  320 VPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 29-377 5.57e-160

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: 453.26  E-value: 5.57e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   29 AGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGS 108
Cdd:TIGR00858   5 RGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  109 GFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLF---TNEGNHLVVTEGVFSMDGDCAP 185
Cdd:TIGR00858  85 GYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLeknRGERRKLIVTDGVFSMDGDIAP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  186 LKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPE---ILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHV 262
Cdd:TIGR00858 165 LPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  263 YSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLDG-FVETDTPIKPFVIGESELALQVANACRQNGIWV 341
Cdd:TIGR00858 245 FSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFtLMPSCTPIVPVIIGDNASALALAEELQQQGIFV 324

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 491602495  342 TAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALK 377
Cdd:TIGR00858 325 GAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 40-379 4.52e-135

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: 389.61  E-value: 4.52e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  40 RRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFT 119
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 120 LLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFT----NEGNHLVVTEGVFSMDGDCAPLKDIAEVARL 195
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRearrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 196 RNAWLAVDDAHGIGVLGEAGGGSCELANV--KPEILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAY 273
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLtdDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 274 ALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGFV---ETDTPIKPFVIGESELALQVANACRQNGIWVTAIRPPTVP 350
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPvggSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319

                        330       340
                 ....*....|....*....|....*....
gi 491602495 351 KGTSRLRITLTANHSTEQVKTLSIALKQA 379
Cdd:cd06454  320 RGTARLRISLSAAHTKEDIDRLLEALKEV 348
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-372 1.23e-44

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 157.47  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   43 INFSSNDYLGLANDQALVRAWQ----QGLSVYGSGSGaspmvtgfsaaHSNLEAALTEWLGF--------ERAILFGSGF 110
Cdd:pfam00155   4 INLGSNEYLGDTLPAVAKAEKDalagGTRNLYGPTDG-----------HPELREALAKFLGRspvlkldrEAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  111 SAN-QALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFK-------HNDIKHLETLFTnEGNHLVVTEGVFSMDGD 182
Cdd:pfam00155  73 GANiEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALK-EKPKVVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  183 CAP---LKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGScELANVKPE---ILVVTFGKAFGMSG---AAILCDQATGDF 253
Cdd:pfam00155 152 VATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVA-TRALLAEGpnlLVVGSFSKAFGLAGwrvGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  254 LTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLD-GFVETDTPIKPFVIGESELALQVAN 332
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGlSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 491602495  333 ACR-QNGIWVTAIRPPTVPkgtSRLRITLtANHSTEQVKTL 372
Cdd:pfam00155 311 VLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEEL 347
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 2-380 0e+00

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 545.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   2 PAFKSRIESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVT 81
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  82 GFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLET 161
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 162 LFTN--EGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCE---LANVKPEILVVTFGKA 236
Cdd:PRK05958 161 LLAKwrAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAeagLAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 237 FGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLD-GFVETDTP 315
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGfQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491602495 316 IKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 4-380 5.22e-169

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: 477.24  E-value: 5.22e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   4 FKSRIESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGF 83
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  84 SAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETL- 162
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 163 --FTNEGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPE--ILVVTFGKAFG 238
Cdd:COG0156  161 kkARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 239 MSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGF--VETDTPI 316
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFdlGPSESPI 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491602495 317 KPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:COG0156  320 VPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 29-377 5.57e-160

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: 453.26  E-value: 5.57e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   29 AGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGS 108
Cdd:TIGR00858   5 RGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  109 GFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLF---TNEGNHLVVTEGVFSMDGDCAP 185
Cdd:TIGR00858  85 GYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLeknRGERRKLIVTDGVFSMDGDIAP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  186 LKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPE---ILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHV 262
Cdd:TIGR00858 165 LPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  263 YSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLDG-FVETDTPIKPFVIGESELALQVANACRQNGIWV 341
Cdd:TIGR00858 245 FSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFtLMPSCTPIVPVIIGDNASALALAEELQQQGIFV 324

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 491602495  342 TAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALK 377
Cdd:TIGR00858 325 GAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 40-379 4.52e-135

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: 389.61  E-value: 4.52e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  40 RRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFT 119
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 120 LLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFT----NEGNHLVVTEGVFSMDGDCAPLKDIAEVARL 195
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLRearrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 196 RNAWLAVDDAHGIGVLGEAGGGSCELANV--KPEILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAY 273
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLtdDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 274 ALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGFV---ETDTPIKPFVIGESELALQVANACRQNGIWVTAIRPPTVP 350
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPvggSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVP 319

                        330       340
                 ....*....|....*....|....*....
gi 491602495 351 KGTSRLRITLTANHSTEQVKTLSIALKQA 379
Cdd:cd06454  320 RGTARLRISLSAAHTKEDIDRLLEALKEV 348
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 1-369 7.53e-91

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 278.62  E-value: 7.53e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   1 MPAFKSRIESALAARKAQGLNRSMNVVFAGNQSILE-HEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPM 79
Cdd:PRK06939   2 SGAFYAQLREELEEIKAEGLYKEERVITSPQGADITvADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  80 VTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHL 159
Cdd:PRK06939  82 ICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 160 ETLF---TNEG--NHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANV--KPEILVVT 232
Cdd:PRK06939 162 EAQLkeaKEAGarHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVmdRVDIITGT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 233 FGKAF-GMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGF-- 309
Cdd:PRK06939 242 LGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAA-GFtl 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 310 VETDTPIKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQV 369
Cdd:PRK06939 321 GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQL 380
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 8-382 2.83e-83

pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.


Pssm-ID: 130884 [Multi-domain]  Cd Length: 385  Bit Score: 258.98  E-value: 2.83e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495    8 IESALAARKAQGLNRSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAH 87
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   88 SNLEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLF---T 164
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLrenP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  165 NEGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANV--KPEILVVTFGKAFGMSGA 242
Cdd:TIGR01825 161 SYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLedKVDIQVGTLSKAIGVVGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  243 AILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLdGF--VETDTPIKPFV 320
Cdd:TIGR01825 241 YAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKL-GYdtGGSETPITPVV 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491602495  321 IGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQvktlsiaLKQALGA 382
Cdd:TIGR01825 320 IGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDD-------LDQALDA 374
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 47-383 1.20e-66

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: 216.52  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   47 SNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLEK-SD 125
Cdd:TIGR01821  52 SNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIiPG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  126 VLI-QDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFTNEGNH---LVVTEGVFSMDGDCAPLKDIAEVARLRNAWLA 201
Cdd:TIGR01821 132 CVIfSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNrpkIIAFESVYSMDGDIAPIEEICDLADKYGALTY 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  202 VDDAHGIGVLGEAGGGSCELANVKPEILVV--TFGKAFGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAV 279
Cdd:TIGR01821 212 LDEVHAVGLYGPRGGGIAERDGLMHRIDIIegTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASI 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  280 SMIQEQSWRREKLVElNEVYQTNLSDLDGFVETDTP--IKPFVIGESELALQVANACRQN-GIWVTAIRPPTVPKGTSRL 356
Cdd:TIGR01821 292 RHLKESQDLRRAHQE-NVKRLKNLLEALGIPVIPNPshIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTERL 370

                         330       340
                  ....*....|....*....|....*..
gi 491602495  357 RITLTANHSTEQVKTLSIALKQALGAL 383
Cdd:TIGR01821 371 RITPTPAHTDKMIDDLVEALLLVWDRL 397
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 40-381 1.08e-63

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 211.07  E-value: 1.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  40 RRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFT 119
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 120 LLEKSDVL--------------IQDRLNHASLMEAGALS----TAKMKRFKHNDIKHLETLFTN--EGNHLVVTEGVFSM 179
Cdd:PLN02955 182 IGSVASLLaasgkplknekvaiFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSckMKRKVVVTDSLFSM 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 180 DGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPE--ILVVTFGKAFGMSGAAILCDQATGDFLTQF 257
Cdd:PLN02955 262 DGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADvdLCVGTLSKAAGCHGGFIACSKKWKQLIQSR 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 258 ARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQtnlsDLDGfVETDTPIKPFVIGESELALQVANACRQN 337
Cdd:PLN02955 342 GRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK----ALSG-VDISSPIISLVVGNQEKALKASRYLLKS 416

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 491602495 338 GIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQALG 381
Cdd:PLN02955 417 GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLD 460
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 1-383 2.23e-63

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 208.17  E-value: 2.23e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   1 MPAFKSRIESALAARKAQGLNRsmnvVFAGnqsiLEHEGRRYIN--------------FSSNDYLGLANDQALVRAWQQG 66
Cdd:PRK13392   1 MMNYDSYFDAALAQLHQEGRYR----VFAD----LEREAGRFPRardhgpdgprrvtiWCSNDYLGMGQHPDVIGAMVDA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  67 LSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTL--LEKSDVLIQDRLNHASLMEAGALS 144
Cdd:PRK13392  73 LDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 145 TAKMKRFKHNDIKHLETLFTNEGNH---LVVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCEL 221
Cdd:PRK13392 153 GAEKQVFRHNDLADLEEQLASVDPDrpkLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAER 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 222 ANVKPEILVV--TFGKAFGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVY 299
Cdd:PRK13392 233 DGLMDRIDMIqgTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAAL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 300 QTNLSDLDGFVE-TDTPIKPFVIGESELALQVANAC-RQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALK 377
Cdd:PRK13392 313 KAKLNANGIPVMpSPSHIVPVMVGDPTLCKAISDRLmSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALV 392


                 ....*.
gi 491602495 378 QALGAL 383
Cdd:PRK13392 393 AIWDRL 398
PLN02483 PLN02483
serine palmitoyltransferase
 40-378 1.07e-51

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 179.57  E-value: 1.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  40 RRYINFSSNDYLGLAN-DQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLF 118
Cdd:PLN02483 100 RRCLNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIP 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 119 TLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFTN---EG---NH------LVVTEGVFSMDGDCAPL 186
Cdd:PLN02483 180 ALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREqiaEGqprTHrpwkkiIVIVEGIYSMEGELCKL 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 187 KDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKP---EILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVY 263
Cdd:PLN02483 260 PEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPadvDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLY 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 264 STAMPPAQAYALTHAVSMI--QEQSWR-REKLVELNE---VYQTNLSDLdGFV---ETDTPIKPFVIGESELALQVANAC 334
Cdd:PLN02483 340 ATSMSPPAVQQVISAIKVIlgEDGTNRgAQKLAQIREnsnFFRSELQKM-GFEvlgDNDSPVMPIMLYNPAKIPAFSREC 418

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 491602495 335 RQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQvktLSIALKQ 378
Cdd:PLN02483 419 LKQNVAVVVVGFPATPLLLARARICISASHSRED---LIKALEV 459
PRK07505 PRK07505
hypothetical protein; Provisional
 6-380 8.42e-45

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 158.99  E-value: 8.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   6 SRIESALAARKAQGLNrSMNVVFAGNQSILEHEGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSA 85
Cdd:PRK07505  13 NRAEKFWDAAYDEGLN-GLTVGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  86 AHSNLEAALTEWLGfERAILFGSGFSANQALLFTLLE------KSDVLIQDRLNHASL-MEAGALST-AKMKRFKHNDIK 157
Cdd:PRK07505  92 ILKDLEEALSELFG-ASVLTFTSCSAAHLGILPLLASghltggVPPHMVFDKNAHASLnILKGICADeTEVETIDHNDLD 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 158 HLETLFTNEGNHLVVTEGVFSMdGDCAPLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGG--SCELANVKPE--ILVVTF 233
Cdd:PRK07505 171 ALEDICKTNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNErtIIAASL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 234 GKAFGMSGAAILC-DQATGDFLTQFARHHVYSTAMP-PAQAYALTHAvsmiqeQSWRREKLVELNEVYQTNLSDLDGFVE 311
Cdd:PRK07505 250 GKAFGASGGVIMLgDAEQIELILRYAGPLAFSQSLNvAALGAILASA------EIHLSEELDQLQQKLQNNIALFDSLIP 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491602495 312 TD-----TPIKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:PRK07505 324 TEqsgsfLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEIL 397
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-372 1.23e-44

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 157.47  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   43 INFSSNDYLGLANDQALVRAWQ----QGLSVYGSGSGaspmvtgfsaaHSNLEAALTEWLGF--------ERAILFGSGF 110
Cdd:pfam00155   4 INLGSNEYLGDTLPAVAKAEKDalagGTRNLYGPTDG-----------HPELREALAKFLGRspvlkldrEAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  111 SAN-QALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFK-------HNDIKHLETLFTnEGNHLVVTEGVFSMDGD 182
Cdd:pfam00155  73 GANiEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALK-EKPKVVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  183 CAP---LKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGScELANVKPE---ILVVTFGKAFGMSG---AAILCDQATGDF 253
Cdd:pfam00155 152 VATleeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVA-TRALLAEGpnlLVVGSFSKAFGLAGwrvGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  254 LTQFARHHVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLD-GFVETDTPIKPFVIGESELALQVAN 332
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGlSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 491602495  333 ACR-QNGIWVTAIRPPTVPkgtSRLRITLtANHSTEQVKTL 372
Cdd:pfam00155 311 VLLeEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEEL 347
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 43-379 8.32e-37

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 137.34  E-value: 8.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  43 INFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLLE 122
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 123 KSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFT-------------NEGNHLVVTEGVFSMDGDCAPLKDI 189
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEqvraqdvalkrkpTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 190 AEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKP----EILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVYST 265
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvhaEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 266 AMPPAQAYALTHAVSMI-----------QEQSWRREKLVELNEVYQTNLSdlDGFVETDTPIKPFV------------IG 322
Cdd:PLN03227 241 SAPPFLAKADATATAGElagpqllnrlhDSIANLYSTLTNSSHPYALKLR--NRLVITSDPISPIIylrlsdqeatrrTD 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491602495 323 ESELALQVANACRQNGIWVTAIR--PPTVPKGTSR--LRITLTANHSTEQVKTLSIALKQA 379
Cdd:PLN03227 319 ETLILDQIAHHSLSEGVAVVSTGghVKKFLQLVPPpcLRVVANASHTREDIDKLLTVLGEA 379
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
43-369 3.09e-32

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 125.51  E-value: 3.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  43 INFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFSANQALLFTLL- 121
Cdd:PRK07179  57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAd 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 122 EKSDVLIqDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLFTNEGNHLVVTEGVFSMDGDCAPLKDIAEVARLRNAWLA 201
Cdd:PRK07179 137 PNTPVYI-DFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLV 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 202 VDDAHGIGVLGEAGGG---SCELANvKPEILVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVYSTAMPPAQAYALTHA 278
Cdd:PRK07179 216 VDESHSLGTHGPQGAGlvaELGLTS-RVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEAT 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 279 VSMIQEQSWRREKLVELNEVYQTNLSDLDGFVETDTPIKPFVIGESELALQVANACRQNGIWVTAIRPPTVPKGTSRLRI 358
Cdd:PRK07179 295 LEVIESADDRRARLHANARFLREGLSELGYNIRSESQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRL 374

                        330
                 ....*....|.
gi 491602495 359 TLTANHSTEQV 369
Cdd:PRK07179 375 SLNADLTASDL 385
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 39-380 1.04e-31

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 123.35  E-value: 1.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  39 GRRYINFSSNDYLGLANDQALVRAWQQGLSVYGS-------GSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGSGFS 111
Cdd:PRK05937   3 ESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYCRqfphaqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 112 ANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLF-----TNEGNHLVVTEGVFSMDGDCAPL 186
Cdd:PRK05937  83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLescrqRSFGRIFIFVCSVYSFKGTLAPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 187 KDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCE---LANVKPeiLVVTFGKAFGMSGAAILCDQATGDFLTQFARHHVY 263
Cdd:PRK05937 163 EQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHslgYENFYA--VLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 264 STAMPPAQAYALTHAVS-MIQEQSWRREKLVELNEVYQTNLS-DLDGFVEtdtPIKPFVIGESELALQVANAcrqnGIWV 341
Cdd:PRK05937 241 STGLPPHLLISIQVAYDfLSQEGELARKQLFRLKEYFAQKFSsAAPGCVQ---PIFLPGISEQELYSKLVET----GIRV 313

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 491602495 342 TAIRPPTVPKgtsrLRITLTANHSTEQVKTLSIALKQAL 380
Cdd:PRK05937 314 GVVCFPTGPF----LRVNLHAFNTEDEVDILVSVLATYL 348
PLN02822 PLN02822
serine palmitoyltransferase
 29-379 9.35e-31

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 122.54  E-value: 9.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  29 AGNQSILEheGRRYINFSSNDYLGLANDQALVRAWQQGLSVYGSGSGASPMVTGFSAAHSNLEAALTEWLGFERAILFGS 108
Cdd:PLN02822 100 AGPHTIIN--GKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 109 GFSANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTAKMKRFKHNDIKHLETLF---TNEGNH------LVVTEGVFSM 179
Cdd:PLN02822 178 GLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLeklTAENKRkkklrrYIVVEAIYQN 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 180 DGDCAPLKdiaEVARLRNAW---LAVDDAHGIGVLGEAGGGSCELANVKPE---ILVVTFGKAFGMSGAaiLCdqaTGDf 253
Cdd:PLN02822 258 SGQIAPLD---EIVRLKEKYrfrVLLDESNSFGVLGKSGRGLSEHFGVPIEkidIITAAMGHALATEGG--FC---TGS- 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 254 lTQFARH-------HVYSTAMPPAQAYALTHAVSMIQEQSWRREKLVELNEVYQTNLSDLDGFVETDTPIKPFVI----- 321
Cdd:PLN02822 329 -ARVVDHqrlsssgYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFlhlek 407

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 322 ------GESELALQVAN-ACRQNGIWVTAIRPPTV-----PKGtsrLRITLTANHSTEQVKTLSIALKQA 379
Cdd:PLN02822 408 stgsakEDLSLLEHIADrMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRV 474
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 99-246 7.13e-09

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: 54.70  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  99 GFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHAS-LMEAGALSTAKMKRFK-------HNDIKHLETLFTNEGNHL 170
Cdd:cd01494   16 GNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPvddagygGLDVAILEELKAKPNVAL 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491602495 171 VVTEGVFSMDGDCAPLKDIAEVARLRNAWLAVDDAHGIgvlGEAGGGSCELANVKPEILVVTFGKAFGMSGAAILC 246
Cdd:cd01494   96 IVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVVI 168
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 43-378 7.68e-08

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: 53.50  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495  43 INFSSNDY---LGLANDQALVR-AWQQGLSVYGSGSGASPmvtgfsaahsnLEAALTEWLGFERA-------ILFGSGFS 111
Cdd:cd00609    1 IDLSIGEPdfpPPPEVLEALAAaALRAGLLGYYPDPGLPE-----------LREAIAEWLGRRGGvdvppeeIVVTNGAQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 112 -ANQALLFTLLEKSD-VLIQDR--LNHASLME-AGA-LSTAKMKR-FKHNDIKHLETLFTNEGNHLVV-------TEGVF 177
Cdd:cd00609   70 eALSLLLRALLNPGDeVLVPDPtyPGYEAAARlAGAeVVPVPLDEeGGFLLDLELLEAAKTPKTKLLYlnnpnnpTGAVL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 178 SMDGdcapLKDIAEVARLRNAWLAVDDAHGIGVLGEAGGGSCELANVKPEILVV-TFGKAFGMSG---AAILCDQAtgDF 253
Cdd:cd00609  150 SEEE----LEELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLrSFSKTFGLPGlriGYLIAPPE--EL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 254 LTQFARHHVYSTAMPP-AQAYALTHAVSmiQEQSW---RREKLVELNEVYQTNLSDLDGFVETDTPIKPFV---IGESEL 326
Cdd:cd00609  224 LERLKKLLPYTTSGPStLSQAAAAAALD--DGEEHleeLRERYRRRRDALLEALKELGPLVVVKPSGGFFLwldLPEGDD 301

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491602495 327 ALQVANACRQNGIWVtaiRPPTV--PKGTSRLRITLTAnhSTEQVKTLSIALKQ 378
Cdd:cd00609  302 EEFLERLLLEAGVVV---RPGSAfgEGGEGFVRLSFAT--PEEELEEALERLAE 350
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 111-207 6.71e-04

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 41.08  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495 111 SANQALLFTLLEKSDVLIQDRLNHASLMEAGALSTA-----KMKRFKHNDIKHLETLFTNE--------GNHLVVTEGVF 177
Cdd:cd00615   86 SSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAvpvylKPERNPYYGIAGGIPPETFKkaliehpdAKAAVITNPTY 165

                         90       100       110
                 ....*....|....*....|....*....|
gi 491602495 178 smDGDCAPLKDIAEVARLRNAWLAVDDAHG 207
Cdd:cd00615  166 --YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
90-210 2.17e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 39.51  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491602495   90 LEAALTEWLGFERAILFGSGFSANQALLFTLLEKSDVLIQDRLNHASLMEAGA---LSTAKMKRFKHN-----DIKHLET 161
Cdd:pfam01212  37 LEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGhaeLGGVQPRPLDGDeagnmDLEDLEA 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491602495  162 LFTNEGNH-------LVVTEGVFSMDGDCAPLKDIAEVArlrnawlAVDDAHGIGV 210
Cdd:pfam01212 117 AIREVGADifpptglISLENTHNSAGGQVVSLENLREIA-------ALAREHGIPV 165
 
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