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Conserved domains on  [gi|542028614|gb|ERH74195|]
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8-amino-7-oxononanoate synthase [Serratia marcescens EGD-HP20]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-381 0e+00

8-amino-7-oxononanoate synthase; Reviewed


:

Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 516.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   1 MSWPQRIEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVT 80
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  81 GFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALAD 160
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 161 LLAKPCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQ---QGVRPELLVATFGKA 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEaglAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 238 FGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTA 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542028614 318 IQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-381 0e+00

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 516.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   1 MSWPQRIEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVT 80
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  81 GFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALAD 160
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 161 LLAKPCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQ---QGVRPELLVATFGKA 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEaglAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 238 FGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTA 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542028614 318 IQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 3-381 2.44e-173

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: 488.02  E-value: 2.44e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   3 WPQRIEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGF 82
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  83 SAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLL 162
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 163 AK-PCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE--LLVATFGKAFG 239
Cdd:COG0156  161 KKaRAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 240 VSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQ 319
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542028614 320 PLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:COG0156  321 PVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEV 382
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 24-379 6.83e-150

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: 427.84  E-value: 6.83e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   24 QATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRAL 103
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  104 LFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKPCD-GQRLAVTEGVFSMDG 182
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGeRRKLIVTDGVFSMDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  183 DGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE---LLVATFGKAFGVSGAAVLCDEATAEYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  260 RHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLVGDNQRALDLATRLRDR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 542028614  340 GLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLH 379
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 39-381 2.09e-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: 390.38  E-value: 2.09e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  39 RLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAA 118
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 119 LMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKP--CDGQRLAVTEGVFSMDGDGAPLAELHRLTRA 196
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 197 AGAWLMVDDAHGVGVRGEQGRGSCWQQGV--RPELLVATFGKAFGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQAC 274
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLtdDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 275 ALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDS-DTAIQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPP 353
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320

                        330       340
                 ....*....|....*....|....*...
gi 542028614 354 GGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:cd06454  321 GTARLRISLSAAHTKEDIDRLLEALKEV 348
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-378 1.03e-51

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 175.96  E-value: 1.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   42 LNFSGNDYLGLSQDARVIAAWQQGAQRygvgsggSGHVTGFSAAHQALEEQLAAWLGYP--------RALLFISGYAANQ 113
Cdd:pfam00155   4 INLGSNEYLGDTLPAVAKAEKDALAGG-------TRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  114 AVLAALMQ-KGDRILADRLSHASLLEAAAQSPAELRRF-------QHNQPQALADLLAKPCdgqRLAVTEGVFSMDGDGA 185
Cdd:pfam00155  77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  186 PLAELH---RLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQ-GVRPELLVA-TFGKAFGVSG---AAVLCDEATAEYLLQ 257
Cdd:pfam00155 154 TLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDAVATRALlAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  258 FARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLVGDNQRALDLATRLR 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVLL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 542028614  338 DR-GLWVSAIRPPTVPpggARLRITLtAAHQPQDIDRLLEVL 378
Cdd:pfam00155 314 EEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 1-381 0e+00

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 516.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   1 MSWPQRIEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVT 80
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  81 GFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALAD 160
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 161 LLAKPCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQ---QGVRPELLVATFGKA 237
Cdd:PRK05958 161 LLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEaglAGEPDVILVGTLGKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 238 FGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTA 317
Cdd:PRK05958 241 LGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542028614 318 IQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK05958 321 IQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 3-381 2.44e-173

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: 488.02  E-value: 2.44e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   3 WPQRIEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGF 82
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  83 SAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLL 162
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 163 AK-PCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE--LLVATFGKAFG 239
Cdd:COG0156  161 KKaRAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRvdIIMGTLSKALG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 240 VSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQ 319
Cdd:COG0156  241 SSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542028614 320 PLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:COG0156  321 PVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEV 382
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 24-379 6.83e-150

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: 427.84  E-value: 6.83e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   24 QATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRAL 103
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  104 LFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKPCD-GQRLAVTEGVFSMDG 182
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGeRRKLIVTDGVFSMDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  183 DGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE---LLVATFGKAFGVSGAAVLCDEATAEYLLQFA 259
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEpvdIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  260 RHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLVGDNQRALDLATRLRDR 339
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 542028614  340 GLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLH 379
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 39-381 2.09e-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: 390.38  E-value: 2.09e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  39 RLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAA 118
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 119 LMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKP--CDGQRLAVTEGVFSMDGDGAPLAELHRLTRA 196
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArrPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 197 AGAWLMVDDAHGVGVRGEQGRGSCWQQGV--RPELLVATFGKAFGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQAC 274
Cdd:cd06454  161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLtdDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 275 ALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDS-DTAIQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPP 353
Cdd:cd06454  241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320

                        330       340
                 ....*....|....*....|....*...
gi 542028614 354 GGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:cd06454  321 GTARLRISLSAAHTKEDIDRLLEALKEV 348
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 7-383 2.38e-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: 2.38e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614    7 IEQALAERRLNAAYRRRQATEGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAH 86
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   87 QALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAK-P 165
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLREnP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  166 CDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGV--RPELLVATFGKAFGVSGA 243
Cdd:TIGR01825 161 SYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLedKVDIQVGTLSKAIGVVGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  244 AVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLV 323
Cdd:TIGR01825 241 YAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVI 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  324 GDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDVSQ 383
Cdd:TIGR01825 321 GDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGK 380
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 5-381 1.96e-79

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 249.34  E-value: 1.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   5 QRIEQALAERRLNAAYRRRQATEGGNGRQIRLGD-RLYLNFSGNDYLGLSQDARVIAAWQQGAQRYgvgsggsghvtGFS 83
Cdd:PRK06939   7 AQLREELEEIKAEGLYKEERVITSPQGADITVADgKEVINFCANNYLGLANHPELIAAAKAALDSH-----------GFG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  84 AA-----------HQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQH 152
Cdd:PRK06939  76 MAsvrficgtqdlHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 153 NQPQAL-ADLLAKPCDGQR--LAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGV--RP 227
Cdd:PRK06939 156 NDMADLeAQLKEAKEAGARhkLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVmdRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 228 ELLVATFGKAF-GVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAP 306
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTA 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542028614 307 LALTLTDSDTAIQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK06939 316 AGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKV 390
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 27-380 2.36e-57

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 194.12  E-value: 2.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  27 EGGNGRQIRLGDRL----------YLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAW 96
Cdd:PLN02955  80 IPSNGEEIFSGDALaeerkgrfkkLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  97 LGYPRALLFISGYAANQAVLAALMQ------------KGDR--ILADRLSHASLLE----AAAQSPAELRRFQHNQPQAL 158
Cdd:PLN02955 160 KKKEDCLVCPTGFAANMAAMVAIGSvasllaasgkplKNEKvaIFSDALNHASIIDgvrlAERQGNVEVFVYRHCDMYHL 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 159 ADLLAKPCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE--LLVATFGK 236
Cdd:PLN02955 240 NSLLSSCKMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADvdLCVGTLSK 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 237 AFGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRqgaaplALTLTDSDT 316
Cdd:PLN02955 320 AAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK------ALSGVDISS 393

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542028614 317 AIQPLLVGDNQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHD 380
Cdd:PLN02955 394 PIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSS 457
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 47-381 3.32e-55

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 186.98  E-value: 3.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  47 NDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQK--GD 124
Cdd:PRK13392  54 NDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGC 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 125 RILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAK-PCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMV 203
Cdd:PRK13392 134 VILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASvDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYV 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 204 DDAHGVGVRGEQGRGSCWQQGV--RPELLVATFGKAFGVSGAAVLCDEATAEYLLQFARHLIYSTAMPPAQACALQAALA 281
Cdd:PRK13392 214 DEVHAVGLYGARGGGIAERDGLmdRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIR 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 282 CIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLVGDNQRALDLATRL-RDRGLWVSAIRPPTVPPGGARLRI 360
Cdd:PRK13392 294 HLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLmSEHGIYIQPINYPTVPRGTERLRI 373

                        330       340
                 ....*....|....*....|.
gi 542028614 361 TLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK13392 374 TPTPLHDDEDIDALVAALVAI 394
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-378 1.03e-51

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 175.96  E-value: 1.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   42 LNFSGNDYLGLSQDARVIAAWQQGAQRygvgsggSGHVTGFSAAHQALEEQLAAWLGYP--------RALLFISGYAANQ 113
Cdd:pfam00155   4 INLGSNEYLGDTLPAVAKAEKDALAGG-------TRNLYGPTDGHPELREALAKFLGRSpvlkldreAAVVFGSGAGANI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  114 AVLAALMQ-KGDRILADRLSHASLLEAAAQSPAELRRF-------QHNQPQALADLLAKPCdgqRLAVTEGVFSMDGDGA 185
Cdd:pfam00155  77 EALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYplydsndFHLDFDALEAALKEKP---KVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  186 PLAELH---RLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQ-GVRPELLVA-TFGKAFGVSG---AAVLCDEATAEYLLQ 257
Cdd:pfam00155 154 TLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDAVATRALlAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  258 FARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTAIQPLLVGDNQRALDLATRLR 337
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQVLL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 542028614  338 DR-GLWVSAIRPPTVPpggARLRITLtAAHQPQDIDRLLEVL 378
Cdd:pfam00155 314 EEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 42-381 2.14e-45

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 162.62  E-value: 2.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  42 LNFSGNDYLGLSQ-----DARVIAAwqqgAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVL 116
Cdd:PLN02483 103 LNLGSYNYLGFAAadeycTPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 117 AALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKP-CDGQR---------LAVTEGVFSMDGDGAP 186
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiAEGQPrthrpwkkiIVIVEGIYSMEGELCK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 187 LAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRP---ELLVATFGKAFGVSGAAVLCDEATAEYLLQFARHLI 263
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPadvDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHL 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 264 YSTAMPPAQACALQAALACI------REGDELRARLQDNIRRFRQGAAPLAL-TLTDSDTAIQPLLVGDNQRALDLATRL 336
Cdd:PLN02483 339 YATSMSPPAVQQVISAIKVIlgedgtNRGAQKLAQIRENSNFFRSELQKMGFeVLGDNDSPVMPIMLYNPAKIPAFSREC 418

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 542028614 337 RDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PLN02483 419 LKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEV 463
PRK07505 PRK07505
hypothetical protein; Provisional
 29-381 2.45e-43

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 155.14  E-value: 2.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  29 GNGRQIRLGD-RLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGyPRALLFIS 107
Cdd:PRK07505  35 REGILITLADgHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSELFG-ASVLTFTS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 108 GYAANQAVLAAL----MQKGDRILA--DRLSHASL--LEAAAQSPAELRRFQHNQPQALADLlakpCDGQR--LAVTEGV 177
Cdd:PRK07505 114 CSAAHLGILPLLasghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDI----CKTNKtvAYVADGV 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 178 FSMdGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGScwqqgVRPEL---------LVATFGKAFGVSGAAVLCD 248
Cdd:PRK07505 190 YSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGY-----VRSELdyrlnertiIAASLGKAFGASGGVIMLG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 249 EA-TAEYLLQFARHLIYSTAM--PPAQACALQAALACIREGDELRARLQDNIRRFRQgaaPLALTLTDSDTAIQPLLVGD 325
Cdd:PRK07505 264 DAeQIELILRYAGPLAFSQSLnvAALGAILASAEIHLSEELDQLQQKLQNNIALFDS---LIPTEQSGSFLPIRLIYIGD 340

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 542028614 326 NQRALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK07505 341 EDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEI 396
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
13-381 2.73e-41

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 149.77  E-value: 2.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  13 ERRLNAAYRRRQATEGgNGRQIRLGDRL---YLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQAL 89
Cdd:PRK07179  26 EERLDKYIEERVNKNW-NGKHLVLGKTPgpdAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  90 EEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKpcDGQ 169
Cdd:PRK07179 105 EKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER--HGP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 170 RLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGV--RPELLVATFGKAFGVSGAAVLC 247
Cdd:PRK07179 183 GIIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLtsRVHFITASLAKAFAGRAGIITC 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 248 DEATAEYLLQFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTdSDTAIQPLLVGDNQ 327
Cdd:PRK07179 263 PRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIR-SESQIIALETGSER 341

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 542028614 328 RALDLATRLRDRGLWVSAIRPPTVPPGGARLRITLTAAHQPQDIDRLLEVLHDV 381
Cdd:PRK07179 342 NTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREA 395
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 42-380 2.48e-38

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 141.58  E-value: 2.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  42 LNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQ 121
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 122 KGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAK-----------PCDGQRLAVTEGVFSMDGDGAPLAEL 190
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrkPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 191 HRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRP----ELLVATFGKAFGVSGAAVLCDEATAEYLLQFARHLIYST 266
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvhaEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 267 AMPPAQACALQAALACIREGDELRARLQDNIRRFRQ----GAAPLALTL-------TDSDTAIQPLLVGDNQ--RALD-- 331
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnSSHPYALKLrnrlvitSDPISPIIYLRLSDQEatRRTDet 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 332 -----LATRLRDRGLWVSAIR------PPTVPPGGarLRITLTAAHQPQDIDRLLEVLHD 380
Cdd:PLN03227 321 lildqIAHHSLSEGVAVVSTGghvkkfLQLVPPPC--LRVVANASHTREDIDKLLTVLGE 378
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 42-383 3.73e-31

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 121.81  E-value: 3.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  42 LNFSGNDYLGLSQDARVIAAWQQGAQRYGVG-------SGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFISGYAANQA 114
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVHEVEKRYRLYCRQfphaqlgYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 115 VLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLA---KPCDGQRLAVTEGVFSMDGDGAPLAELH 191
Cdd:PRK05937  87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscrQRSFGRIFIFVCSVYSFKGTLAPLEQII 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 192 RLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRP--ELLVaTFGKAFGVSGAAVLCDEATAEYLLQFARHLIYSTAMP 269
Cdd:PRK05937 167 ALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENfyAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLP 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 270 PAQACALQAALACI-REGDELRARLQdNIRRFRQGAAPLAltltdSDTAIQPLLVGDNQRALdLATRLRDRGLWVSAIRP 348
Cdd:PRK05937 246 PHLLISIQVAYDFLsQEGELARKQLF-RLKEYFAQKFSSA-----APGCVQPIFLPGISEQE-LYSKLVETGIRVGVVCF 318

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 542028614 349 PTVPpggaRLRITLTAAHQPQDIDRLLEVLHDVSQ 383
Cdd:PRK05937 319 PTGP----FLRVNLHAFNTEDEVDILVSVLATYLE 349
PLN02822 PLN02822
serine palmitoyltransferase
 27-382 1.50e-20

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 92.88  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  27 EGGNGRQIRLGDRLYLNFSGNDYLGLSQDARVIAAWQQGAQRYGVGSGGSGHVTGFSAAHQALEEQLAAWLGYPRALLFI 106
Cdd:PLN02822  97 ESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYS 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 107 SGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSPAELRRFQHNQPQALADLLAKPCDG-------QRLAVTEGVFS 179
Cdd:PLN02822 177 YGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEnkrkkklRRYIVVEAIYQ 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 180 MDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQQGVRPE---LLVATFGKAFGVSGAAVLCDEATAEYLL 256
Cdd:PLN02822 257 NSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEkidIITAAMGHALATEGGFCTGSARVVDHQR 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 257 QFARHLIYSTAMPPAQACALQAALACIREGDELRARLQDNIRRFRQGAAPLALTLTDSDTaIQPLL-------VGDNQRA 329
Cdd:PLN02822 337 LSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIPGLSIGSNT-LSPIVflhleksTGSAKED 415

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542028614 330 LDLATRLRDR-----GLWVSAIRPPTV-----PPGgarLRITLTAAHQPQDIDRLLEVLHDVS 382
Cdd:PLN02822 416 LSLLEHIADRmlkedSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRVA 475
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 86-247 1.58e-13

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: 68.18  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614  86 HQALEEQLAAWL--GYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAQSP-AELRRFQ-------HNQP 155
Cdd:cd01494    2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAgAKPVPVPvddagygGLDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614 156 QALADLLAKPCDgqRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVGVRGEQGRGSCWQqgvRPELLVATFG 235
Cdd:cd01494   82 AILEELKAKPNV--ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG---GADVVTFSLH 156

                        170
                 ....*....|..
gi 542028614 236 KAFGVSGAAVLC 247
Cdd:cd01494  157 KNLGGEGGGVVI 168
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 86-130 4.08e-04

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 41.96  E-value: 4.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 542028614  86 HQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADR 130
Cdd:COG0626   60 RRALEEALAALEGGEAALAFASGMAAISAVLLALLKAGDHVVASD 104
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
87-151 7.17e-04

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 41.05  E-value: 7.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542028614   87 QALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAAqsPAELRRFQ 151
Cdd:pfam01212  35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGG--HAELGGVQ 97
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 82-210 1.71e-03

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 39.92  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542028614   82 FSAAHQALEEQLAAWLG--YPRALLFISGYA-ANQAVLAALM---QKGDRILADRLSHASLL----EAAAQSPAELRRF- 150
Cdd:pfam00266  41 ATQAYEEAREKVAEFINapSNDEIIFTSGTTeAINLVALSLGrslKPGDEIVITEMEHHANLvpwqELAKRTGARVRVLp 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542028614  151 -QHNQPQALADLLAKPCDGQRLAVTEGVFSMDGDGAPLAELHRLTRAAGAWLMVDDAHGVG 210
Cdd:pfam00266 121 lDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 87-141 2.68e-03

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 39.24  E-value: 2.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 542028614  87 QALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADRLSHASLLEAAA 141
Cdd:cd06502   35 AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDEAGA 89
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 86-128 4.30e-03

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


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 38.72  E-value: 4.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 542028614  86 HQALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILA 128
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVA 84
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 87-127 4.40e-03

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 38.86  E-value: 4.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 542028614  87 QALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRIL 127
Cdd:PRK07811  64 TALEEQLAALEGGAYGRAFSSGMAATDCLLRAVLRPGDHIV 104
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 106-133 5.66e-03

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 38.52  E-value: 5.66e-03
                         10        20
                 ....*....|....*....|....*...
gi 542028614 106 ISGYAANQAVLAALMQKGDRILADRLSH 133
Cdd:PRK00011  94 HSGSQANAAVYFALLKPGDTILGMDLAH 121
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 88-130 9.50e-03

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 37.77  E-value: 9.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 542028614  88 ALEEQLAAWLGYPRALLFISGYAANQAVLAALMQKGDRILADR 130
Cdd:PRK05994  67 VLEERVAALEGGTAALAVASGHAAQFLVFHTLLQPGDEFIAAR 109
 
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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