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Conserved domains on  [gi|1518771345|ref|WP_123614380|]
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MULTISPECIES: pyridoxal phosphate-dependent aminotransferase family protein [Duncaniella]

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

 Zoom to residue level

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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]; ...
 15-390 0e+00

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: 560.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEA 94
Cdd:COG0156    10 AALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  95 KLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVK 174
Cdd:COG0156    90 ELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKARAARRK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 175 LIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATN 254
Cdd:COG0156   170 LIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 255 KEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFK 334
Cdd:COG0156   250 KELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAER 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518771345 335 TFAITHDLLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRK 390
Cdd:COG0156   330 ALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 15-390 0e+00

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: 560.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEA 94
Cdd:COG0156    10 AALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  95 KLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVK 174
Cdd:COG0156    90 ELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKARAARRK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 175 LIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATN 254
Cdd:COG0156   170 LIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 255 KEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFK 334
Cdd:COG0156   250 KELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAER 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518771345 335 TFAITHDLLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRK 390
Cdd:COG0156   330 ALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 42-388 9.78e-147

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: 419.66  E-value: 9.78e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSC 121
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 122 LTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQK-CAPDKVKLIVSDSVFSMEGDVANIPAMVELAKK 200
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREaRRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 201 YDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTASITPASTA 280
Cdd:cd06454   161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 281 AALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEI-GNTSTPIIPLFIRDDFKTFAITHDLLEEGIFVNPVVSPAVAP 359
Cdd:cd06454   241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVgGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320

                         330       340
                  ....*....|....*....|....*....
gi 1518771345 360 TDTLIRFSLMATHTMEQVDRALETITRIF 388
Cdd:cd06454   321 GTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 15-387 1.00e-137

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 398.38  E-value: 1.00e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEA 94
Cdd:PRK05958   12 AQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  95 KLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCaPDKVK 174
Cdd:PRK05958   92 ELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKW-RAGRA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 175 LIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLI-MGTFSKSFSSLGGFIAT 253
Cdd:PRK05958  171 LIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLGKALGSSGAAVLG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 254 NKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDF 333
Cdd:PRK05958  251 SETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNE 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1518771345 334 KTFAITHDLLEEGIFVNPVVSPAVaPTDT-LIRFSLMATHTMEQVDRALETITRI 387
Cdd:PRK05958  331 RALALAAALQEQGFWVGAIRPPTV-PAGTsRLRITLTAAHTEADIDRLLEALAEA 384
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-385 1.19e-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: 397.02  E-value: 1.19e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  27 RAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVM 106
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 107 VYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVKLIVSDSVFSMEG 186
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 187 DVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLA-DDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHS 265
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 266 RSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFKTFAITHDLLEE 345
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1518771345 346 GIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETIT 385
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-384 1.74e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 160.16  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNdPRIKEAAIEATrkygtgcAGSPFLN-GTLDIHKELEAKLAEYIGKEDVM--------VYSTGF 112
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDAL-------AGGTRNLyGPTDGHPELREALAKFLGRSPVLkldreaavVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 113 -EVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYK-------HNDMESLEKQLQKcapdKVKLIVSDSVFSM 184
Cdd:pfam00155  73 gANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE----KPKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 185 EGDVANIP---AMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHyGLADDVDL-IMGTFSKSFSSLG---GFIATNKEV 257
Cdd:pfam00155 149 TGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRA-LLAEGPNLlVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 258 TNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFKTFA 337
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKE 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1518771345 338 ITHDLLEE-GIFVNPVVSPAVaptDTLIRFSlMATHTMEQVDRALETI 384
Cdd:pfam00155 308 LAQVLLEEvGVYVTPGSSPGV---PGWLRIT-VAGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 15-390 0e+00

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: 560.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEA 94
Cdd:COG0156    10 AALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  95 KLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVK 174
Cdd:COG0156    90 ELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKARAARRK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 175 LIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATN 254
Cdd:COG0156   170 LIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKALGSSGGFVAGS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 255 KEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFK 334
Cdd:COG0156   250 KELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVPVIVGDAER 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518771345 335 TFAITHDLLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRK 390
Cdd:COG0156   330 ALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 42-388 9.78e-147

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: 419.66  E-value: 9.78e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSC 121
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 122 LTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQK-CAPDKVKLIVSDSVFSMEGDVANIPAMVELAKK 200
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREaRRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 201 YDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTASITPASTA 280
Cdd:cd06454   161 YGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 281 AALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEI-GNTSTPIIPLFIRDDFKTFAITHDLLEEGIFVNPVVSPAVAP 359
Cdd:cd06454   241 AALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVgGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPR 320

                         330       340
                  ....*....|....*....|....*....
gi 1518771345 360 TDTLIRFSLMATHTMEQVDRALETITRIF 388
Cdd:cd06454   321 GTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 15-387 1.00e-137

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 398.38  E-value: 1.00e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEA 94
Cdd:PRK05958   12 AQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  95 KLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCaPDKVK 174
Cdd:PRK05958   92 ELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKW-RAGRA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 175 LIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLI-MGTFSKSFSSLGGFIAT 253
Cdd:PRK05958  171 LIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLGKALGSSGAAVLG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 254 NKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDF 333
Cdd:PRK05958  251 SETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNE 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1518771345 334 KTFAITHDLLEEGIFVNPVVSPAVaPTDT-LIRFSLMATHTMEQVDRALETITRI 387
Cdd:PRK05958  331 RALALAAALQEQGFWVGAIRPPTV-PAGTsRLRITLTAAHTEADIDRLLEALAEA 384
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-385 1.19e-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: 397.02  E-value: 1.19e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  27 RAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVM 106
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 107 VYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVKLIVSDSVFSMEG 186
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 187 DVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLA-DDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHS 265
Cdd:TIGR00858 161 DIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 266 RSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFKTFAITHDLLEE 345
Cdd:TIGR00858 241 RTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1518771345 346 GIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETIT 385
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 15-394 2.85e-136

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 394.95  E-value: 2.85e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQDPEVII-NGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELE 93
Cdd:PRK06939   14 EEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  94 AKLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKC--APD 171
Cdd:PRK06939   94 EKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAkeAGA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 172 KVKLIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFS-SLGGF 250
Cdd:PRK06939  174 RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALGgASGGY 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 251 IATNKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIR 330
Cdd:PRK06939  254 TAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLG 333

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518771345 331 DDFKTFAITHDLLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRKYDVL 394
Cdd:PRK06939  334 DAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 18-394 6.11e-119

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: 350.66  E-value: 6.11e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  18 KAAGVYPYFRAISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLA 97
Cdd:TIGR01825   9 KENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLHEELEEKLA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  98 EYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVKLIV 177
Cdd:TIGR01825  89 KFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENPSYGKKLIV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 178 SDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEV 257
Cdd:TIGR01825 169 TDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLEDKVDIQVGTLSKAIGVVGGYAAGHKEL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 258 TNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFKTFA 337
Cdd:TIGR01825 249 IEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITPVVIGDEKAAQE 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1518771345 338 ITHDLLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRKYDVL 394
Cdd:TIGR01825 329 FSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 15-390 6.10e-69

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: 222.68  E-value: 6.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  15 QEAKAAGVYPYFRAISSEQD--PEVIINGKK----VLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDI 88
Cdd:TIGR01821  12 DKLHLEGRYRVFADLERQAGefPFAQWHRPDgakdVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  89 HKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSCLTGR--EDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQ 166
Cdd:TIGR01821  92 HVELEAELADLHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 167 KCAPDKVKLIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSS 246
Cdd:TIGR01821 172 SVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAFGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 247 LGGFIATNKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEP-ER---QENLWKLTNHaldgFRSQGFEIGNTST 322
Cdd:TIGR01821 252 VGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQdLRrahQENVKRLKNL----LEALGIPVIPNPS 327

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1518771345 323 PIIPLFIRDDFKTFAITHDLLEE-GIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRK 390
Cdd:TIGR01821 328 HIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396
PLN02483 PLN02483
serine palmitoyltransferase
 40-387 1.58e-67

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 221.56  E-value: 1.58e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  40 NGKKVLMFGSNCYTGLVN-DPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGV 118
Cdd:PLN02483   98 KTRRCLNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTI 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 119 VSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCA---------PDKVKLIVSDSVFSMEGDVA 189
Cdd:PLN02483  178 IPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIaegqprthrPWKKIIVIVEGIYSMEGELC 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 190 NIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGL-ADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSY 268
Cdd:PLN02483  258 KLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAH 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 269 IFTASITPASTAAALKALEIMQTEPERQENLWKL------TNHALDGFRSQGFE-IGNTSTPIIPLFIRDDFKTFAITHD 341
Cdd:PLN02483  338 LYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLaqirenSNFFRSELQKMGFEvLGDNDSPVMPIMLYNPAKIPAFSRE 417

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1518771345 342 LLEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRI 387
Cdd:PLN02483  418 CLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEV 463
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 42-393 7.75e-67

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 217.41  E-value: 7.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSC 121
Cdd:PRK13392   46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALST 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 122 LTGRED--YILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDKVKLIVSDSVFSMEGDVANIPAMVELAK 199
Cdd:PRK13392  126 LGKLLPgcVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLAD 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 200 KYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTASITP--- 276
Cdd:PRK13392  206 RYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPava 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 277 ASTAAALKALEIMQTEPERQENLWKLTNHALDgfrSQGFEIGNTSTPIIPLFIRDDFKTFAITHDLLEE-GIFVNPVVSP 355
Cdd:PRK13392  286 AGATAAIRHLKTSQTERDAHQDRVAALKAKLN---ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYP 362

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1518771345 356 AVAPTDTLIRFSLMATHTMEQVDRALETITRIFRKYDV 393
Cdd:PRK13392  363 TVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 42-379 8.41e-63

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 209.15  E-value: 8.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVN------ 115
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANmaamva 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 116 LGVVSCLTGREDYILWDEQ--------DHASIIEGRRLSFSQQ----LKYKHNDMESLEKQLQKCAPDKvKLIVSDSVFS 183
Cdd:PLN02955  182 IGSVASLLAASGKPLKNEKvaifsdalNHASIIDGVRLAERQGnvevFVYRHCDMYHLNSLLSSCKMKR-KVVVTDSLFS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 184 MEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRH 263
Cdd:PLN02955  261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 264 HSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHaldgFRS-QGFEIGntsTPIIPLFIRDDFKTFAITHDL 342
Cdd:PLN02955  341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKE----FKAlSGVDIS---SPIISLVVGNQEKALKASRYL 413

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1518771345 343 LEEGIFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDR 379
Cdd:PLN02955  414 LKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKK 450
PLN02822 PLN02822
serine palmitoyltransferase
 28-349 4.79e-62

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 206.90  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  28 AISSEQDPEVIINGKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMV 107
Cdd:PLN02822   95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 108 YSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKC-APDKVK-----LIVSDSV 181
Cdd:PLN02822  175 YSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLtAENKRKkklrrYIVVEAI 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 182 FSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLA-DDVDLIMGTFSKSFSSLGGFIATNKEVTNY 260
Cdd:PLN02822  255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPiEKIDIITAAMGHALATEGGFCTGSARVVDH 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 261 LRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRS-QGFEIG-NTSTPIIPLFIR-------D 331
Cdd:PLN02822  335 QRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDiPGLSIGsNTLSPIVFLHLEkstgsakE 414

                         330       340
                  ....*....|....*....|
gi 1518771345 332 DFKTFAITHD--LLEEGIFV 349
Cdd:PLN02822  415 DLSLLEHIADrmLKEDSVLV 434
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
45-388 7.30e-58

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 194.07  E-value: 7.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  45 LMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSP-FLNGTLDIHKeLEAKLAEYIGKEDVMVYSTGFEVNLGVVSCLT 123
Cdd:PRK07179   57 IILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAvFLHDDSPKPQ-FEKKLAAFTGFESCLLCQSGWAANVGLLQTIA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 124 GREDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEKQLQKCAPDkvkLIVSDSVFSMEGDVANIPAMVELAKKYDA 203
Cdd:PRK07179  136 DPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFGC 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 204 SLMIDEAHGIGVFGEGGRGLVHHYGLADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTASITPASTAAAL 283
Cdd:PRK07179  213 VLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLE 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 284 KALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTpIIPLFIRDDFKTFAITHDLLEEGIFVNPVVSPAVAPTDTL 363
Cdd:PRK07179  293 ATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNL 371

                         330       340
                  ....*....|....*....|....*
gi 1518771345 364 IRFSLMATHTMEQVDRALETITRIF 388
Cdd:PRK07179  372 IRLSLNADLTASDLDRVLEVCREAR 396
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 45-381 8.19e-48

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 167.39  E-value: 8.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  45 LMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSCLTG 124
Cdd:PLN03227    1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 125 REDYILWDEQDHASIIEGRRLSFSQQLKYKHNDMESLEK----------QLQKCAPDKVKLIVSDSVFSMEGDVANIPAM 194
Cdd:PLN03227   81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRvleqvraqdvALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 195 VELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGL--ADDVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTA 272
Cdd:PLN03227  161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 273 SITPASTAAALKALEIMQTEPERQENLW--------KLTN--HALDGFRSQGFEI-GNTSTPIIPLFIRDDFKT------ 335
Cdd:PLN03227  241 SAPPFLAKADATATAGELAGPQLLNRLHdsianlysTLTNssHPYALKLRNRLVItSDPISPIIYLRLSDQEATrrtdet 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1518771345 336 ---FAITHDLLEEGIFV-----NPVVSPAVAPTDTLiRFSLMATHTMEQVDRAL 381
Cdd:PLN03227  321 lilDQIAHHSLSEGVAVvstggHVKKFLQLVPPPCL-RVVANASHTREDIDKLL 373
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-384 1.74e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 160.16  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  42 KKVLMFGSNCYTGLVNdPRIKEAAIEATrkygtgcAGSPFLN-GTLDIHKELEAKLAEYIGKEDVM--------VYSTGF 112
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDAL-------AGGTRNLyGPTDGHPELREALAKFLGRSPVLkldreaavVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 113 -EVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYK-------HNDMESLEKQLQKcapdKVKLIVSDSVFSM 184
Cdd:pfam00155  73 gANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE----KPKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 185 EGDVANIP---AMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHyGLADDVDL-IMGTFSKSFSSLG---GFIATNKEV 257
Cdd:pfam00155 149 TGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRA-LLAEGPNLlVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 258 TNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPERQENLWKLTNHALDGFRSQGFEIGNTSTPIIPLFIRDDFKTFA 337
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKE 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1518771345 338 ITHDLLEE-GIFVNPVVSPAVaptDTLIRFSlMATHTMEQVDRALETI 384
Cdd:pfam00155 308 LAQVLLEEvGVYVTPGSSPGV---PGWLRIT-VAGGTEEELEELLEAI 351
PRK07505 PRK07505
hypothetical protein; Provisional
 41-391 5.98e-42

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 151.67  E-value: 5.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  41 GKKVLMFGSNCYTGLVNDPRIKEAAIEATRKYGTGCAGSPFLNGTLDIHKELEAKLAEYIGKEdVMVYSTGFEVNLGVVS 120
Cdd:PRK07505   45 GHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSELFGAS-VLTFTSCSAAHLGILP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 121 CLT------GREDYILWDEQDHAS--IIEGRRLSFSQQLKYKHNDMESLEkqlQKCAPDKVKLIVSDSVFSMeGDVANIP 192
Cdd:PRK07505  124 LLAsghltgGVPPHMVFDKNAHASlnILKGICADETEVETIDHNDLDALE---DICKTNKTVAYVADGVYSM-GGIAPVK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 193 AMVELAKKYDASLMIDEAHGIGVFGEGGRGLV--HHYGLADDVDLIMGTFSKSFSSLGGFIATN-KEVTNYLRHHSRSYI 269
Cdd:PRK07505  200 ELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERTIIAASLGKAFGASGGVIMLGdAEQIELILRYAGPLA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 270 FTASITPASTAAALKALEIMQTE--PERQENLWklTNHALdgFRSQ-GFEIGNTSTPIIPLFIRDDFKTFAITHDLLEEG 346
Cdd:PRK07505  280 FSQSLNVAALGAILASAEIHLSEelDQLQQKLQ--NNIAL--FDSLiPTEQSGSFLPIRLIYIGDEDTAIKAAKQLLDRG 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1518771345 347 IFVNPVVSPAVAPTDTLIRFSLMATHTMEQVDRALETITRIFRKY 391
Cdd:PRK07505  356 FYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEG 400
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 75-378 1.43e-36

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 136.83  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  75 GCAGSPFLNGTLDIHKELEAKLAEYIGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIEGRRLSFSQQLKYK 154
Cdd:PRK05937   44 GYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 155 HNDMESLEKQLQKC---APDKVKLIVSdSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIGVFGEGGRGLVHHYGLaD 231
Cdd:PRK05937  124 HNDLDHLESLLESCrqrSFGRIFIFVC-SVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY-E 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 232 DVDLIMGTFSKSFSSLGGFIATNKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEPER-QENLWKLTNHALDGF 310
Cdd:PRK05937  202 NFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPHLLISIQVAYDFLSQEGELaRKQLFRLKEYFAQKF 281

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 311 --RSQGFeigntstpIIPLFIRdDFKTFAITHDLLEEGIFVNpVVSPAVAPtdtLIRFSLMATHTMEQVD 378
Cdd:PRK05937  282 ssAAPGC--------VQPIFLP-GISEQELYSKLVETGIRVG-VVCFPTGP---FLRVNLHAFNTEDEVD 338
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 156-388 8.56e-13

Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.


Pssm-ID: 99735 [Multi-domain]  Cd Length: 413  Bit Score: 69.13  E-value: 8.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 156 NDMESLEKQLQKcAPDKVKLIVSDSVFSmEGDVaNIP------AMVELAKKYDASLMIDEAH-GIGVFGEGGRglVHHYG 228
Cdd:cd00610   176 DDLEALEEALEE-HPEEVAAVIVEPIQG-EGGV-IVPppgylkALRELCRKHGILLIADEVQtGFGRTGKMFA--FEHFG 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 229 LADDvdlIMgTFSKSFSslGGF----IATNKEVTNYLRHHSRSYIFTASITPASTAAALKALEIMQTEpERQENLWKLTN 304
Cdd:cd00610   251 VEPD---IV-TLGKGLG--GGLplgaVLGREEIMDAFPAGPGLHGGTFGGNPLACAAALAVLEVLEEE-GLLENAAELGE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 305 HALDGFRS-----------------QGFEIGNTSTPIIPlfirDDFKTFAITHDLLEEGIFVNPVvspavapTDTLIRFS 367
Cdd:cd00610   324 YLRERLRElaekhplvgdvrgrglmIGIELVKDRATKPP----DKELAAKIIKAALERGLLLRPS-------GGNVIRLL 392

                         250       260
                  ....*....|....*....|.
gi 1518771345 368 LMATHTMEQVDRALETITRIF 388
Cdd:cd00610   393 PPLIITEEEIDEGLDALDEAL 413
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 59-384 3.94e-11

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 63.90  E-value: 3.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  59 PRIKEAAIEATRKygtgcagSPFLNGTLDI-HKELEAKLAEYIGK--------EDVMVYSTGFEVNLGVVSCLTGREDYI 129
Cdd:cd00609    14 PEVLEALAAAALR-------AGLLGYYPDPgLPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 130 L-----WDEQDHASIIEGRRLSFSQqLKYKHNDMESLEkQLQKCAPDKVKLIV-------SDSVFSMEgdvaNIPAMVEL 197
Cdd:cd00609    87 LvpdptYPGYEAAARLAGAEVVPVP-LDEEGGFLLDLE-LLEAAKTPKTKLLYlnnpnnpTGAVLSEE----ELEELAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 198 AKKYDASLMIDEAHGIgvFGEGGRGLVHHYGLADDVDLI-MGTFSKSFSS----LGGFIATNKEVTNYLRHHSRSYIFTA 272
Cdd:cd00609   161 AKKHGILIISDEAYAE--LVYDGEPPPALALLDAYERVIvLRSFSKTFGLpglrIGYLIAPPEELLERLKKLLPYTTSGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 273 SitPASTAAALKALEIMQTE-PERQENLWKLTNHALDGFRSQGFEIgntstPIIP-----LFIR--DDFKTFAITHDLLE 344
Cdd:cd00609   239 S--TLSQAAAAAALDDGEEHlEELRERYRRRRDALLEALKELGPLV-----VVKPsggffLWLDlpEGDDEEFLERLLLE 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1518771345 345 EGIFVNPVVSPAVAPTDTlIRFSLmaTHTMEQVDRALETI 384
Cdd:cd00609   312 AGVVVRPGSAFGEGGEGF-VRLSF--ATPEEELEEALERL 348
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 89-254 4.75e-09

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 55.08  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  89 HKELEAKLAEY--IGKEDVMVYSTGFEVNLGVVSCLTGREDYILWDEQDHASIIE------GRRLSFSQQLKYKHNDMES 160
Cdd:cd01494     2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWvaaelaGAKPVPVPVDDAGYGGLDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 161 LEKQLQKcAPDKVKLIVSDSVFSMEGDVANIPAMVELAKKYDASLMIDEAHGIgvfgeGGRGLVHHYGLADDVDLIMGTF 240
Cdd:cd01494    82 AILEELK-AKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG-----GASPAPGVLIPEGGADVVTFSL 155

                         170
                  ....*....|....*
gi 1518771345 241 SKSFS-SLGGFIATN 254
Cdd:cd01494   156 HKNLGgEGGGVVIVK 170
Aminotran_3 pfam00202
Aminotransferase class-III;
187-387 3.68e-05

Aminotransferase class-III;


Pssm-ID: 395148 [Multi-domain]  Cd Length: 397  Bit Score: 45.40  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 187 DVANIPAMVELAKKYDASLMIDE-AHGigvFGEGGRGLVH-HYGLADDvdlIMgTFSKSFSslGGF----IATNKEVtnY 260
Cdd:pfam00202 204 SPGFLAGLRAICKKHGVLLIADEvQTG---FGRTGKLFAHeHWGVPPD---IM-TFAKALT--GGFplaaTLGRAEV--M 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 261 LRHHSRSYIFTASITPASTAAALKALEIMQTEPeRQENLWKLTNHALDGFRSQGF------EIGNTSTPIIPLFIRDDFK 334
Cdd:pfam00202 273 QAFAPGSHGGTFGGNPLACAAALATLEIIEDED-LLQNAARLGAYLKEGLEDLQKkyevikDVRGKGLMIGIELKEDVTV 351

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1518771345 335 TFAITHDLLEEGIFVNPVvspavapTDTLIRFSLMATHTMEQVDRALETITRI 387
Cdd:pfam00202 352 NPPILLAALEAGVLILPC-------GDNVIRLLPPLTITDEQIDEGLEIISKA 397
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 202-387 5.07e-05

Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439849 [Multi-domain]  Cd Length: 341  Bit Score: 44.74  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 202 DASLMIDEAhgigvFGEGGRGLVHHYGLADDVD--LIMGTFSKSFsSLG----GFIATNKEVTNYLRHHSRSYiftaSIT 275
Cdd:COG0079   168 DGLVVVDEA-----YAEFVPEEDSALPLLARYPnlVVLRTFSKAY-GLAglrlGYAIASPELIAALRRVRGPW----NVN 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 276 PASTAAALKALEimqtEPERQENLWKLTNHALD----GFRSQGFEIGNTSTPIIplFIRDDFKTFAITHDLLEEGIFVNP 351
Cdd:COG0079   238 SLAQAAALAALE----DRAYLEETRARLRAERErlaaALRALGLTVYPSQANFV--LVRVPEDAAELFEALLERGILVRD 311

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1518771345 352 VVSPavaPTDTLIRFSLmatHTMEQVDRALETITRI 387
Cdd:COG0079   312 FSSF---GLPDYLRITV---GTPEENDRLLAALKEI 341
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 88-212 3.83e-04

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


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 41.85  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345  88 IHKELEAKLAEYIGKEDVMVYSTGFEV-NLGVVSCLTGREDYILWDEQDHASIIEGrrLSFSQQ----LKYKHN------ 156
Cdd:cd00615    60 PIKEAQELAARAFGAKHTFFLVNGTSSsNKAVILAVCGPGDKILIDRNCHKSVING--LVLSGAvpvyLKPERNpyygia 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1518771345 157 ---DMESLEKQLQKcAPDKVKLIVSDSVFsmEGDVANIPAMVELAKKYDASLMIDEAHG 212
Cdd:cd00615   138 ggiPPETFKKALIE-HPDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
PRK07036 PRK07036
aminotransferase;
161-315 8.02e-04

aminotransferase;


Pssm-ID: 235913 [Multi-domain]  Cd Length: 466  Bit Score: 41.21  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 161 LEKQLQKCAPDKVKLIVSDSVFSmEGDVANIPA-----MVELAKKYDASLMIDEAhgIGVFGEGGrglvhHYGLADDV-- 233
Cdd:PRK07036  209 FEDKILSLGADNIAAFIAEPILG-SGGVIVPPPgyharMREICRRYDILYISDEV--VTGFGRLG-----HFFASEAVfg 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 234 ---DLImgTFSKSFSS----LGGFIATNK--EVTNYLRHHSRSYI--FTASITPASTAAALKALEIMQTE---------- 292
Cdd:PRK07036  281 iqpDII--TFAKGLTSgyqpLGAVIISERllDVISGPNAKGNVFThgFTYSGHPVACAAALKNIEIMEREglcehvrevg 358

                         170       180
                  ....*....|....*....|....
gi 1518771345 293 PERQENLWKLTNHALDG-FRSQGF 315
Cdd:PRK07036  359 PYFEERLASLRELPLVGdVRGDHL 382
PRK07678 PRK07678
aminotransferase; Validated
 196-318 8.39e-04

aminotransferase; Validated


Pssm-ID: 181078 [Multi-domain]  Cd Length: 451  Bit Score: 41.15  E-value: 8.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 196 ELAKKYDASLMIDEAhgIGVFGEGGRGLVH-HYGLADDVDlimgTFSKSFSSlgGFI-----ATNKEV---------TNY 260
Cdd:PRK07678  241 EICQKHGALLISDEV--ICGFGRTGKAFGFmNYGVKPDII----TMAKGITS--AYLplsatAVKKEIyeafkgkgeYEH 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518771345 261 LRHhsrsyIFTASITPASTAAALKALEIMQTEP--ERQENLWKLTNHALDGF----------RSQGFEIG 318
Cdd:PRK07678  313 FRH-----VNTFGGNPAACALALKNLEIMENENliERSAQLGELLLEQLKEElgehplvgdiRGKGLLVG 377
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 157-208 6.82e-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: 38.34  E-value: 6.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1518771345 157 DMESLEKQLQKcapdKVKLIVSDSVFSMEGDVANIPAMVELAKKYDASLMID 208
Cdd:cd00614   114 DPEALEAAIKP----ETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
 
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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