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Conserved domains on  [gi|1232675783|gb|OYZ07310.1|]
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8-amino-7-oxononanoate synthase [Hydrogenophilales bacterium 16-64-46]

Protein Classification

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 11414994)

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme similar to 8-amino-7-oxononanoate synthase, which 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.-.-
Gene Ontology:  GO:0030170|GO:0016747
PubMed:  10800595|10673430

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 6-386 3.57e-160

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: 454.89  E-value: 3.57e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   6 LNRLELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHH 85
Cdd:COG0156     2 LDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  86 RYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLA 165
Cdd:COG0156    82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 166 KSRASD-KLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGV 243
Cdd:COG0156   162 KARAARrKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVdIIMGTLSKALGS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 244 AGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQ 323
Cdd:COG0156   242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFDLGPSESPIV 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232675783 324 PWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:COG0156   321 PVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 6-386 3.57e-160

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: 454.89  E-value: 3.57e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   6 LNRLELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHH 85
Cdd:COG0156     2 LDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  86 RYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLA 165
Cdd:COG0156    82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 166 KSRASD-KLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGV 243
Cdd:COG0156   162 KARAARrKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVdIIMGTLSKALGS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 244 AGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQ 323
Cdd:COG0156   242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFDLGPSESPIV 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232675783 324 PWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:COG0156   321 PVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 4-386 5.97e-150

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 428.81  E-value: 5.97e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   4 AALNRLELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITG 83
Cdd:PRK05958    2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  84 HHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQ 163
Cdd:PRK05958   82 NSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 164 LAKSRASDKLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDR--VIYLATLGKAA 241
Cdd:PRK05958  162 LAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEpdVILVGTLGKAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 242 GVAGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTP 321
Cdd:PRK05958  242 GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRAL-GFQLMDSQSA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232675783 322 IQPWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:PRK05958  321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 28-383 1.64e-137

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: 396.25  E-value: 1.64e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  28 LDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLF 107
Cdd:TIGR00858   3 LDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 108 STGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD-KLIVSDLVFSMDGDC 186
Cdd:TIGR00858  83 SSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERrKLIVTDGVFSMDGDI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 187 APVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRA--RASDRVIYLATLGKAAGVAGAAVAAHPVVIDWLVNTARP 264
Cdd:TIGR00858 163 APLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFglKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRART 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 265 YVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVRLSRALLARG 344
Cdd:TIGR00858 243 LIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEAL-GFTLMPSCTPIVPVIIGDNASALALAEELQQQG 321

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1232675783 345 LLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALH 383
Cdd:TIGR00858 322 IFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 43-385 1.70e-128

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: 373.05  E-value: 1.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  43 VISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALV 122
Cdd:cd06454     3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 123 KRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD--KLIVSDLVFSMDGDCAPVDALLDLAERYD 200
Cdd:cd06454    83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYgkKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 201 AWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASL 279
Cdd:cd06454   163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVdIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 280 IESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPS-STPIQPWVVGENADAVRLSRALLARGLLVPAIRTPTVPAG 358
Cdd:cd06454   243 LAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                         330       340
                  ....*....|....*....|....*..
gi 1232675783 359 TARLRITLSAAHSDADVMHLIEALHEL 385
Cdd:cd06454   322 TARLRISLSAAHTKEDIDRLLEALKEV 348
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-382 2.14e-41

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 148.99  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  43 VISFCSNDYLGLaadpVLVAAAHRALDdcgLGAGAAHLITGHHRYHHDFETAFAHFVGKP--------AALLFSTGYLAN 114
Cdd:pfam00155   3 KINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 115 LGVVSALVK-RHSEIFADRLNHASLVDAAQLSGATLTRYR-------HLDLAQLESQLAKSRasdKLIVSDLVFSMDGDC 186
Cdd:pfam00155  76 IEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 187 APVD---ALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTpRARASDR--VIYLATLGKAAGVAGAAV---AAHPVVIDWL 258
Cdd:pfam00155 153 ATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGpnLLVVGSFSKAFGLAGWRVgyiLGNAAVISQL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 259 VNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVRLSR 338
Cdd:pfam00155 232 RKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA-GLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1232675783 339 ALLAR-GLLVPAIRTPTVPagtARLRITLsAAHSDADVMHLIEAL 382
Cdd:pfam00155 311 VLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 6-386 3.57e-160

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: 454.89  E-value: 3.57e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   6 LNRLELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHH 85
Cdd:COG0156     2 LDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  86 RYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLA 165
Cdd:COG0156    82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 166 KSRASD-KLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGV 243
Cdd:COG0156   162 KARAARrKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVdIIMGTLSKALGS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 244 AGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQ 323
Cdd:COG0156   242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKEL-GFDLGPSESPIV 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232675783 324 PWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:COG0156   321 PVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 4-386 5.97e-150

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 428.81  E-value: 5.97e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   4 AALNRLELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITG 83
Cdd:PRK05958    2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  84 HHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQ 163
Cdd:PRK05958   82 NSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 164 LAKSRASDKLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDR--VIYLATLGKAA 241
Cdd:PRK05958  162 LAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEpdVILVGTLGKAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 242 GVAGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTP 321
Cdd:PRK05958  242 GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRAL-GFQLMDSQSA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232675783 322 IQPWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:PRK05958  321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 28-383 1.64e-137

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: 396.25  E-value: 1.64e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  28 LDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLF 107
Cdd:TIGR00858   3 LDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 108 STGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD-KLIVSDLVFSMDGDC 186
Cdd:TIGR00858  83 SSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERrKLIVTDGVFSMDGDI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 187 APVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRA--RASDRVIYLATLGKAAGVAGAAVAAHPVVIDWLVNTARP 264
Cdd:TIGR00858 163 APLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFglKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRART 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 265 YVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVRLSRALLARG 344
Cdd:TIGR00858 243 LIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEAL-GFTLMPSCTPIVPVIIGDNASALALAEELQQQG 321

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1232675783 345 LLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALH 383
Cdd:TIGR00858 322 IFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 43-385 1.70e-128

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: 373.05  E-value: 1.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  43 VISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALV 122
Cdd:cd06454     3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 123 KRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD--KLIVSDLVFSMDGDCAPVDALLDLAERYD 200
Cdd:cd06454    83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPYgkKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 201 AWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAASL 279
Cdd:cd06454   163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVdIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAAA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 280 IESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPS-STPIQPWVVGENADAVRLSRALLARGLLVPAIRTPTVPAG 358
Cdd:cd06454   243 LAALEVLQGGPERRERLQENVRYLRRGLKEL-GFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                         330       340
                  ....*....|....*....|....*..
gi 1232675783 359 TARLRITLSAAHSDADVMHLIEALHEL 385
Cdd:cd06454   322 TARLRISLSAAHTKEDIDRLLEALKEV 348
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 1-381 7.62e-102

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 306.74  E-value: 7.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   1 MSSAALNRLELGLAARRADQLERRRSVLDSAQGAHIRV-DGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAH 79
Cdd:PRK06939    1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  80 LITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQ 159
Cdd:PRK06939   81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 160 LESQLAKSRASD---KLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVL-NDGRGglTPRAR-ASDRV-IY 233
Cdd:PRK06939  161 LEAQLKEAKEAGarhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVgENGRG--TVEHFgVMDRVdII 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 234 LATLGKAAGVAGAA-VAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqG 312
Cdd:PRK06939  239 TGTLGKALGGASGGyTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAA-G 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232675783 313 GHLLPSSTPIQPWVVGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEA 381
Cdd:PRK06939  318 FTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 9-386 2.43e-95

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: 289.80  E-value: 2.43e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783   9 LELGLAARRADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYH 88
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  89 HDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSR 168
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 169 ASD-KLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLND-GRGGLTPRARASDRVIYLATLGKAAGVAGA 246
Cdd:TIGR01825 161 SYGkKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEaGRGTVHHFGLEDKVDIQVGTLSKAIGVVGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 247 AVAAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWV 326
Cdd:TIGR01825 241 YAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKL-GYDTGGSETPITPVV 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 327 VGENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:TIGR01825 320 IGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVG 379
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 21-385 7.94e-76

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: 240.40  E-value: 7.94e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  21 LERRRSVLDSAQgaHIRVDG-QAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFV 99
Cdd:TIGR01821  26 LERQAGEFPFAQ--WHRPDGaKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLH 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 100 GKPAALLFSTGYLANLGVVSALVKR--HSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRAS-DKLIVS 176
Cdd:TIGR01821 104 GKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNrPKIIAF 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 177 DLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGVAGAAVAAHPVVI 255
Cdd:TIGR01821 184 ESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIdIIEGTLAKAFGVVGGYIAASRKLI 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 256 DWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVR 335
Cdd:TIGR01821 264 DAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEAL-GIPVIPNPSHIVPVIIGDAALCKK 342

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1232675783 336 LSRALLAR-GLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHEL 385
Cdd:TIGR01821 343 VSDLLLNKhGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLV 393
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 43-385 4.37e-66

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 215.49  E-value: 4.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  43 VISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALV 122
Cdd:PRK13392   48 VTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 123 KRHSE--IFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD-KLIVSDLVFSMDGDCAPVDALLDLAERY 199
Cdd:PRK13392  128 KLLPGcvILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRpKLIAFESVYSMDGDIAPIEAICDLADRY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 200 DAWLHLDDAHGFGVLNDGRGGLTPRARASDRV-IYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYVYTTASPPVLAAS 278
Cdd:PRK13392  208 NALTYVDEVHAVGLYGARGGGIAERDGLMDRIdMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 279 LIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVRLSRALLAR-GLLVPAIRTPTVPA 357
Cdd:PRK13392  288 ATAAIRHLKTSQTERDAHQDRVAALKAKLNAN-GIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPR 366

                         330       340
                  ....*....|....*....|....*...
gi 1232675783 358 GTARLRITLSAAHSDADVMHLIEALHEL 385
Cdd:PRK13392  367 GTERLRITPTPLHDDEDIDALVAALVAI 394
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 46-382 2.01e-55

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 189.12  E-value: 2.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  46 FCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLAN------LGVVS 119
Cdd:PLN02955  107 FSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANmaamvaIGSVA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 120 ALVKRHSE--------IFADRLNHASLVDAAQLS----GATLTRYRHLDLAQLESQLAKSRASDKLIVSDLVFSMDGDCA 187
Cdd:PLN02955  187 SLLAASGKplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDSLFSMDGDFA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 188 PVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARA-SDRVIYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYV 266
Cdd:PLN02955  267 PMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCeADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFI 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 267 YTTASP-PVLAASLIeslrQIEVGSARRARLAAHVTRLRAgLSDLQGghlLPSSTPIQPWVVGENADAVRLSRALLARGL 345
Cdd:PLN02955  347 FSTAIPvPMAAAAYA----AVVVARKEKWRRKAIWERVKE-FKALSG---VDISSPIISLVVGNQEKALKASRYLLKSGF 418

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1232675783 346 LVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEAL 382
Cdd:PLN02955  419 HVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
43-382 2.14e-41

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 148.99  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  43 VISFCSNDYLGLaadpVLVAAAHRALDdcgLGAGAAHLITGHHRYHHDFETAFAHFVGKP--------AALLFSTGYLAN 114
Cdd:pfam00155   3 KINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 115 LGVVSALVK-RHSEIFADRLNHASLVDAAQLSGATLTRYR-------HLDLAQLESQLAKSRasdKLIVSDLVFSMDGDC 186
Cdd:pfam00155  76 IEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP---KVVLHTSPHNPTGTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 187 APVD---ALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTpRARASDR--VIYLATLGKAAGVAGAAV---AAHPVVIDWL 258
Cdd:pfam00155 153 ATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGpnLLVVGSFSKAFGLAGWRVgyiLGNAAVISQL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 259 VNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqGGHLLPSSTPIQPWVVGENADAVRLSR 338
Cdd:pfam00155 232 RKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA-GLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1232675783 339 ALLAR-GLLVPAIRTPTVPagtARLRITLsAAHSDADVMHLIEAL 382
Cdd:pfam00155 311 VLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 48-385 7.51e-39

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 144.90  E-value: 7.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  48 SNDYLGLAA-DPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVKRHS 126
Cdd:PLN02483  107 SYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIGKGG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 127 EIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKS---------RASDKLIV-SDLVFSMDGDCAPVDALLDLA 196
Cdd:PLN02483  187 LIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqprthRPWKKIIViVEGIYSMEGELCKLPEIVAVC 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 197 ERYDAWLHLDDAHGFGVLN-DGRG-----GLTPraraSDRVIYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYVYTTA 270
Cdd:PLN02483  267 KKYKAYVYLDEAHSIGAVGkTGRGvcellGVDP----ADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 271 SPPVLAASLIESLRQI------EVGSARRARLAAHVTRLRAGLSDLqGGHLLPSS-TPIQPWVVGENADAVRLSRALLAR 343
Cdd:PLN02483  343 MSPPAVQQVISAIKVIlgedgtNRGAQKLAQIRENSNFFRSELQKM-GFEVLGDNdSPVMPIMLYNPAKIPAFSRECLKQ 421

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1232675783 344 GLLVPAIRTPTVPAGTARLRITLSAAHSDADvmhLIEALHEL 385
Cdd:PLN02483  422 NVAVVVVGFPATPLLLARARICISASHSRED---LIKALEVI 460
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
32-386 6.20e-38

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 140.91  E-value: 6.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  32 QGAHI---RVDGQAVISFCSNDYLGLAADPVLVAAAHRAL--DDCGLGAGAAHLITGHhrYHHDFETAFAHFVGKPAALL 106
Cdd:PRK07179   42 NGKHLvlgKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALqeEGDSLVMSAVFLHDDS--PKPQFEKKLAAFTGFESCLL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 107 FSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAksRASDKLIVSDLVFSMDGDC 186
Cdd:PRK07179  120 CQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIE--RHGPGIIVVDSVYSTTGTI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 187 APVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARASDRVIYL-ATLGKAAGVAGAAVAAHPVVIDWLVNTARPY 265
Cdd:PRK07179  198 APLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFItASLAKAFAGRAGIITCPRELAEYVPFVSYPA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 266 VYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLqgGHLLPSSTPIQPWVVGENADAVRLSRALLARGL 345
Cdd:PRK07179  278 IFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSEL--GYNIRSESQIIALETGSERNTEVLRDALEERNV 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1232675783 346 LVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHELA 386
Cdd:PRK07179  356 FGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREAR 396
PLN02822 PLN02822
serine palmitoyltransferase
 18-386 2.36e-36

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 137.95  E-value: 2.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  18 ADQLERRRSVLDSAQGAHIRVDGQAVISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAH 97
Cdd:PLN02822   86 TEEMRPEPPVLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  98 FVGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASDK----- 172
Cdd:PLN02822  166 FLGTPDSILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKrkkkl 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 173 --LIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGRGGLTPRARAS-DRV-IYLATLGKAAGVAGAAV 248
Cdd:PLN02822  246 rrYIVVEAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPiEKIdIITAAMGHALATEGGFC 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 249 AAHPVVIDWLVNTARPYVYTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSDLQGghLLPSSTPIQPWV-- 326
Cdd:PLN02822  326 TGSARVVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPG--LSIGSNTLSPIVfl 403

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232675783 327 -----VGENADAVRL-----SRALLARGLLVPAIRTPTV-----PAGtarLRITLSAAHSDADVMHLIEALHELA 386
Cdd:PLN02822  404 hleksTGSAKEDLSLlehiaDRMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRVA 475
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 44-386 1.41e-27

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 112.31  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  44 ISFCSNDYLGLAADPVLVAAAHRALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSALVK 123
Cdd:PLN03227    1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 124 RHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASD-----------KLIVSDLVFSMDGDCAPVDAL 192
Cdd:PLN03227   81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDvalkrkptdqrRFLVVEGLYKNTGTLAPLKEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 193 LDLAERYDAWLHLDDAHGFGVLND-GRG-----GLTPrarASDRVIYLATLGKAAGVAGAAVAAHPVVIDWLVNTARPYV 266
Cdd:PLN03227  161 VALKEEFHYRLILDESFSFGTLGKsGRGslehaGLKP---MVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYC 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 267 YTTASPPVLAASLIESLRQIEVGSARRARLAAHVTRLRAGLSD--------LQGGhLLPSSTPIQPWVVGENADAV---- 334
Cdd:PLN03227  238 FSASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNsshpyalkLRNR-LVITSDPISPIIYLRLSDQEatrr 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232675783 335 --------RLSRALLARGLLVPAIRTPTVPAGTAR----LRITLSAAHSDADVMHLIEALHELA 386
Cdd:PLN03227  317 tdetlildQIAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTVLGEAV 380
PRK07505 PRK07505
hypothetical protein; Provisional
 39-385 2.03e-22

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 97.74  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  39 DGQAVISFCSNDYLGLAADPVLVAAAHRALddcgLGAGAAHLITGHHRYHH----DFETAFAHFVGkPAALLFSTGYLAN 114
Cdd:PRK07505   44 DGHTFVNFVSCSYLGLDTHPAIIEGAVDAL----KRTGSLHLSSSRTRVRSqilkDLEEALSELFG-ASVLTFTSCSAAH 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 115 LGVVSAL--------VKRHSeIFaDRLNHASLvdaAQLSG-----ATLTRYRHLDLAQLEsQLAKSRASdKLIVSDLVFS 181
Cdd:PRK07505  119 LGILPLLasghltggVPPHM-VF-DKNAHASL---NILKGicadeTEVETIDHNDLDALE-DICKTNKT-VAYVADGVYS 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 182 MdGDCAPVDALLDLAERYDAWLHLDDAHGFGVLND-GRGGLTPR--ARASDRVIYLATLGKAAGVagaavaaHPVVIdwL 258
Cdd:PRK07505  192 M-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKnGEGYVRSEldYRLNERTIIAASLGKAFGA-------SGGVI--M 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 259 VNTAR--PYVYTTASPPVLAASLieSLRQIEVGSAR-RARLAAHVTRLRAGLSD-------LQGGHLLPSSTPIQPWVVG 328
Cdd:PRK07505  262 LGDAEqiELILRYAGPLAFSQSL--NVAALGAILASaEIHLSEELDQLQQKLQNnialfdsLIPTEQSGSFLPIRLIYIG 339

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1232675783 329 ENADAVRLSRALLARGLLVPAIRTPTVPAGTARLRITLSAAHSDADVMHLIEALHEL 385
Cdd:PRK07505  340 DEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEI 396
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 40-219 8.36e-22

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 95.62  E-value: 8.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  40 GQAVISFCSNDYLGLAADPVLVAAAHR-------ALDDCGLGAGAAHLITGHHRYHHDFETAFAHFVGKPAALLFSTGYL 112
Cdd:PRK05937    3 ESLSIDFVTNDFLGFSRSDTLVHEVEKryrlycrQFPHAQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 113 ANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLTRYRHLDLAQLESQLAKSRASDK---LIVSDLVFSMDGDCAPV 189
Cdd:PRK05937   83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFgriFIFVCSVYSFKGTLAPL 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1232675783 190 DALLDLAERYDAWLHLDDAHGFGVL-NDGRG 219
Cdd:PRK05937  163 EQIIALSKKYHAHLIVDEAHAMGIFgDDGKG 193
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 88-212 6.78e-08

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: 51.61  E-value: 6.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  88 HHDFETAFAHF--VGKPAALLFSTGYLANLGVVSALVKRHSEIFADRLNHAS-LVDAAQLSGATLTRYR-------HLDL 157
Cdd:cd01494     2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPvddagygGLDV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1232675783 158 AQLESQLAKSRAsdKLIVSDLVFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFG 212
Cdd:cd01494    82 AILEELKAKPNV--ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG 134
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 80-218 4.27e-05

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 44.97  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  80 LITGhhRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSAL-VKRHSEIFADRLNHASLVDAAQLSGAT------LTRY 152
Cdd:pfam01041  20 LTTG--PYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALgVGPGDEVITPSFTFVATANAALRLGAKpvfvdiDPDT 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232675783 153 RHLDLAQLESQLAKSRasdKLIVSdlvFSMDGDCAPVDALLDLAERYDAWLHLDDAHGFGVLNDGR 218
Cdd:pfam01041  98 YNIDPEAIEAAITPRT---KAIIP---VHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGK 157
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
62-344 6.57e-04

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 41.59  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783  62 AAAHRALDDCglgagaaHLITGhhRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSAL-VKRHSEI------FAdrln 134
Cdd:COG0399    15 AAVVEVLRSG-------WLTLG--PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALgIGPGDEVitpaftFV---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 135 hASlVDAAQLSGATL------TRYRHLDLAQLESQL-AKSRAsdkLIVSDLvFsmdGDCAPVDALLDLAERYDAWLHLDD 207
Cdd:COG0399    82 -AT-ANAILYVGATPvfvdidPDTYNIDPEALEAAItPRTKA---IIPVHL-Y---GQPADMDAIMAIAKKHGLKVIEDA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 208 AHGFGVLNDGR-----------------------GG--LTPRARASDRVIYLATLGKaagvagaavaahpvvidwlvNTA 262
Cdd:COG0399   153 AQALGATYKGKkvgtfgdagcfsfyptknlttgeGGavVTNDEELAERARSLRNHGR--------------------DRD 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 263 RPYVYTTAS-----PPVLAASLIESLRQIEVGSARRARLAAhvtRLRAGLSDLQGGHLLPSSTPIQ------PWVVGENA 331
Cdd:COG0399   213 AKYEHVELGynyrmDELQAAIGLAQLKRLDEFIARRRAIAA---RYREALADLPGLTLPKVPPGAEhvyhlyVIRLDEGE 289

                         330
                  ....*....|...
gi 1232675783 332 DAVRLSRALLARG 344
Cdd:COG0399   290 DRDELIAALKARG 302
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 113-210 4.79e-03

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: 38.38  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 113 ANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGATLT-------RYRHLDLAQLESQLAKS--RASD-KLIVSDLVfSM 182
Cdd:cd00615    87 SNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVylkpernPYYGIAGGIPPETFKKAliEHPDaKAAVITNP-TY 165

                          90       100
                  ....*....|....*....|....*...
gi 1232675783 183 DGDCAPVDALLDLAERYDAWLHLDDAHG 210
Cdd:cd00615   166 YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
113-210 5.69e-03

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 38.64  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232675783 113 ANLGVVSALVKRHSEIFADRLNHASLVDAAQLSGAT------------------LTRYRHLDLAQLESQLAKSRASDKLI 174
Cdd:pfam01276  94 SNKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATpvylepsrnaygiiggipLHEFQEETLKEAIAEVPDAKGPRLAV 173

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232675783 175 VSDLVFsmDGDCAPVDALLDLAERYDAWLHLDDAHG 210
Cdd:pfam01276 174 ITNPTY--DGVLYNAKEIVDTLHHLSDPILFDSAWV 207
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 80-121 9.72e-03

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 37.94  E-value: 9.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1232675783  80 LITGhhRYHHDFETAFAHFVGKPAALLFSTGYLANLGVVSAL 121
Cdd:PRK15407   59 LTTG--RFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSAL 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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