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Conserved domains on  [gi|311907994|gb|ADQ18435|]
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2-amino-3-ketobutyrate coenzyme A ligase [Leadbetterella byssophila DSM 17132]

Protein Classification

PLP-dependent aspartate aminotransferase family protein( domain architecture ID 10012856)

PLP-dependent aspartate aminotransferase family protein similar to 8-amino-7-oxononanoate synthase (EC 2.3.1.47) and glycine C-acetyltransferase (EC2.3.1.29)

EC:  2.3.1.-
Gene Ontology:  GO:0030170|GO:0009058|GO:0016740
PubMed:  10800595
SCOP:  4000675

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 3-397 0e+00

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


:

Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 759.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   3 NTSFLSHLQNTLQEIENDGLYKRERIITSSQSAEIE-ANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRF 81
Cdd:PRK06939   2 SGAFYAQLREELEEIKAEGLYKEERVITSPQGADITvADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  82 ICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDL 161
Cdd:PRK06939  82 ICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 162 EAQLIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITST 241
Cdd:PRK06939 162 EAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 242 LGKALGGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIP 321
Cdd:PRK06939 242 LGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLG 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311907994 322 DGDAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGII 397
Cdd:PRK06939 322 PGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
 
Name Accession Description Interval E-value
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 3-397 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 759.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   3 NTSFLSHLQNTLQEIENDGLYKRERIITSSQSAEIE-ANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRF 81
Cdd:PRK06939   2 SGAFYAQLREELEEIKAEGLYKEERVITSPQGADITvADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  82 ICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDL 161
Cdd:PRK06939  82 ICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 162 EAQLIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITST 241
Cdd:PRK06939 162 EAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 242 LGKALGGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIP 321
Cdd:PRK06939 242 LGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLG 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311907994 322 DGDAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGII 397
Cdd:PRK06939 322 PGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 6-397 0e+00

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130881 [Multi-domain]  Cd Length: 393  Bit Score: 637.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994    6 FLSHLQNTLQEIENDGLYKRERIITSSQSAEIE-ANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICG 84
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRvADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   85 TQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQ 164
Cdd:TIGR01822  81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  165 LIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGK 244
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  245 ALGGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGD 324
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311907994  325 AAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGII 397
Cdd:TIGR01822 321 HPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 6-393 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: 563.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   6 FLSHLQNTLQEIENDGLYKRERIITSSQSAEIEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGT 85
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  86 QDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQL 165
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 166 IAANEKGHrfKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKA 245
Cdd:COG0156  161 KKARAARR--KLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 246 LgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGDA 325
Cdd:COG0156  239 L-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311907994 326 AIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKE 393
Cdd:COG0156  318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 42-391 4.21e-152

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: 433.53  E-value: 4.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  42 KKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEP 121
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 122 LFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEaQLIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAE 201
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLE-KLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 202 KYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGI 281
Cdd:cd06454  160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 282 VGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDG-DAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVV 360
Cdd:cd06454  239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318

                        330       340       350
                 ....*....|....*....|....*....|.
gi 311907994 361 PKGKARIRVQLSAAHTRAHLDTAIAAFEKIG 391
Cdd:cd06454  319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-387 9.61e-61

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 199.84  E-value: 9.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   42 KKLLNFCANNYLGLSNhPDVIKASQEVmnthgyGISSVRFICGTQDIHKTLEERISKFLGM--------EDTILYAAAFD 113
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  114 ANGGIFEPLFTES-DAIISDELNHASIIDGVRLCKAARYRYK-------NNDMQDLEAQLiaanEKGHrfKIIVTDGVFS 185
Cdd:pfam00155  74 ANIEALIFLLANPgDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAAL----KEKP--KVVLHTSPHN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  186 MDGIVANLKGVCDLAE---KYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKALG--GAMGGFTSGKKEI 260
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGlaGWRVGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  261 IDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGDAAIVPVMLYDAKVSQV 340
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKE 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 311907994  341 MAEKLMDE-GIYVIGFFYPVVPkgkARIRVQLsAAHTRAHLDTAIAAF 387
Cdd:pfam00155 308 LAQVLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 3-397 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 759.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   3 NTSFLSHLQNTLQEIENDGLYKRERIITSSQSAEIE-ANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRF 81
Cdd:PRK06939   2 SGAFYAQLREELEEIKAEGLYKEERVITSPQGADITvADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  82 ICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDL 161
Cdd:PRK06939  82 ICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 162 EAQLIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITST 241
Cdd:PRK06939 162 EAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 242 LGKALGGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIP 321
Cdd:PRK06939 242 LGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLG 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311907994 322 DGDAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGII 397
Cdd:PRK06939 322 PGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 6-397 0e+00

glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130881 [Multi-domain]  Cd Length: 393  Bit Score: 637.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994    6 FLSHLQNTLQEIENDGLYKRERIITSSQSAEIE-ANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICG 84
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRvADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   85 TQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQ 164
Cdd:TIGR01822  81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  165 LIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGK 244
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  245 ALGGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGD 324
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKPAD 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311907994  325 AAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGII 397
Cdd:TIGR01822 321 HPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 6-393 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: 563.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   6 FLSHLQNTLQEIENDGLYKRERIITSSQSAEIEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGT 85
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  86 QDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQL 165
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 166 IAANEKGHrfKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKA 245
Cdd:COG0156  161 KKARAARR--KLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 246 LgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGDA 325
Cdd:COG0156  239 L-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311907994 326 AIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKE 393
Cdd:COG0156  318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 42-391 4.21e-152

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: 433.53  E-value: 4.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  42 KKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEP 121
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 122 LFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEaQLIAANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAE 201
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLE-KLLREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 202 KYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGI 281
Cdd:cd06454  160 KYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 282 VGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDG-DAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVV 360
Cdd:cd06454  239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318

                        330       340       350
                 ....*....|....*....|....*....|.
gi 311907994 361 PKGKARIRVQLSAAHTRAHLDTAIAAFEKIG 391
Cdd:cd06454  319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-388 7.09e-130

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: 377.38  E-value: 7.09e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   27 RIITSSQSAEIEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTI 106
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  107 LYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQLIAAneKGHRFKIIVTDGVFSM 186
Cdd:TIGR00858  81 LFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKN--RGERRKLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  187 DGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHE-ANEVMGRVDIITSTLGKALGGaMGGFTSGKKEIIDLLR 265
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEhFGLKPEPVDIQVGTLSKALGS-YGAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  266 QRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGDAAIVPVMLYDAKVSQVMAEKL 345
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 311907994  346 MDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFE 388
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 5-391 3.51e-128

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 374.11  E-value: 3.51e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   5 SFLSHLQNTLQEIENDGLYKRERIITSSQSAEIEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICG 84
Cdd:PRK05958   2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  85 TQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQ 164
Cdd:PRK05958  82 NSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 165 LIAAnekGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRG-THEANEVMGRVDIITSTLG 243
Cdd:PRK05958 162 LAKW---RAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGlAAEAGLAGEPDVILVGTLG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 244 KALgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDG 323
Cdd:PRK05958 239 KAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDS 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311907994 324 DAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIG 391
Cdd:PRK05958 318 QSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 5-396 1.84e-82

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: 257.73  E-value: 1.84e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994    5 SFLSHLQNTLQEIENDGLYKR----ERIITSSQSAE--IEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISS 78
Cdd:TIGR01821   2 DYDQFFNKEIDKLHLEGRYRVfadlERQAGEFPFAQwhRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   79 VRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDAN-------GGIFEPLftesdAIISDELNHASIIDGVRLCKAARY 151
Cdd:TIGR01821  82 TRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdatlatlAKIIPGC-----VIFSDELNHASMIEGIRHSGAEKF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  152 RYKNNDMQDLEAQLIAANEKghRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEV 231
Cdd:TIGR01821 157 IFRHNDVAHLEKLLQSVDPN--RPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  232 MGRVDIITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRT 311
Cdd:TIGR01821 235 MHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKN 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  312 EMKKRGFDIPDGDAAIVPVMLYDAKVSQVMAEKLMDE-GIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKI 390
Cdd:TIGR01821 314 LLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLV 393


                  ....*.
gi 311907994  391 GKELGI 396
Cdd:TIGR01821 394 WDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 6-396 1.93e-77

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 245.15  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   6 FLSHLQNTLQEIENDGLYK------RER---IITSSQSAEIEangKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGI 76
Cdd:PRK13392   4 YDSYFDAALAQLHQEGRYRvfadleREAgrfPRARDHGPDGP---RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  77 SSVRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPL--FTESDAIISDELNHASIIDGVRLCKAARYRYK 154
Cdd:PRK13392  81 GGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 155 NNDMQDLEAQLIAANEkgHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGR 234
Cdd:PRK13392 161 HNDLADLEEQLASVDP--DRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 235 VDIITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMK 314
Cdd:PRK13392 239 IDMIQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 315 KRGFDIPDGDAAIVPVMLYDAKVSQVMAEKLMDE-GIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKE 393
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397


                 ...
gi 311907994 394 LGI 396
Cdd:PRK13392 398 LEL 400
PLN02483 PLN02483
serine palmitoyltransferase
 40-396 3.96e-69

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 225.80  E-value: 3.96e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  40 NGKKLLNFCANNYLGLSNH-----PDVIKASQEvmnthgYGIS--SVRFICGTQDIHKTLEERISKFLGMEDTILYAAAF 112
Cdd:PLN02483  98 KTRRCLNLGSYNYLGFAAAdeyctPRVIESLKK------YSAStcSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGY 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 113 DANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEA----QLIAANEKGHR--FKIIV-TDGVFS 185
Cdd:PLN02483 172 ATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEvlreQIAEGQPRTHRpwKKIIViVEGIYS 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 186 MDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGR-VDIITSTLGKALgGAMGGFTSGKKEIIDLL 264
Cdd:PLN02483 252 MEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSF-GSCGGYIAGSKELIQYL 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 265 RQRSRPYLFSNSLAPGIVG---AALKVLdMIETDTSR----RDTVMENAAYFRTEMKKRGFD-IPDGDAAIVPVMLYD-A 335
Cdd:PLN02483 331 KRTCPAHLYATSMSPPAVQqviSAIKVI-LGEDGTNRgaqkLAQIRENSNFFRSELQKMGFEvLGDNDSPVMPIMLYNpA 409

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311907994 336 KVSQVMAEKLmDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGI 396
Cdd:PLN02483 410 KIPAFSRECL-KQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
42-387 9.61e-61

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 199.84  E-value: 9.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994   42 KKLLNFCANNYLGLSNhPDVIKASQEVmnthgyGISSVRFICGTQDIHKTLEERISKFLGM--------EDTILYAAAFD 113
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  114 ANGGIFEPLFTES-DAIISDELNHASIIDGVRLCKAARYRYK-------NNDMQDLEAQLiaanEKGHrfKIIVTDGVFS 185
Cdd:pfam00155  74 ANIEALIFLLANPgDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAAL----KEKP--KVVLHTSPHN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  186 MDGIVANLKGVCDLAE---KYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKALG--GAMGGFTSGKKEI 260
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGlaGWRVGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  261 IDLLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIPDGDAAIVPVMLYDAKVSQV 340
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKE 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 311907994  341 MAEKLMDE-GIYVIGFFYPVVPkgkARIRVQLsAAHTRAHLDTAIAAF 387
Cdd:pfam00155 308 LAQVLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
PLN02822 PLN02822
serine palmitoyltransferase
 28-394 6.98e-57

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 193.42  E-value: 6.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  28 IITSSQSAEIEANGKKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTIL 107
Cdd:PLN02822  95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 108 YAAAFDANGGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQL--IAANEKGHR--FKIIVTDGV 183
Cdd:PLN02822 175 YSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekLTAENKRKKklRRYIVVEAI 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 184 FSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEV-MGRVDIITSTLGKALGGAmGGFTSGKKEIID 262
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSARVVD 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 263 LLRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRTEMKK-RGFDIpdGDAAIVPVMLY-------- 333
Cdd:PLN02822 334 HQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDiPGLSI--GSNTLSPIVFLhlekstgs 411

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311907994 334 ---DAKVSQVMAEK-LMDEGIYVIGFFYPVVPKGK--ARIRVQLSAAHTRAHLDTAIAAFEKIGKEL 394
Cdd:PLN02822 412 akeDLSLLEHIADRmLKEDSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRVAASV 478
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 42-387 3.55e-54

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 186.42  E-value: 3.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  42 KKLLNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIF-- 119
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMva 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 120 ------------EPLFTESDAIISDELNHASIIDGVRLCK----AARYRYKNNDMQDLEAQLiaANEKGHRfKIIVTDGV 183
Cdd:PLN02955 182 igsvasllaasgKPLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLL--SSCKMKR-KVVVTDSL 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 184 FSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKAlGGAMGGFTSGKKEIIDL 263
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQL 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 264 LRQRSRPYLFSNSLAPGIVGAALKVLDMIETDTSRRDTVMENAAYFRtemKKRGFDIpdgDAAIVPVMLYDAKVSQVMAE 343
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDI---SSPIISLVVGNQEKALKASR 411

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 311907994 344 KLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAF 387
Cdd:PLN02955 412 YLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
50-396 4.35e-47

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 165.57  E-value: 4.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  50 NNYLGLSNHPDVIKASQEVMNTHGYGI--SSVrFICGTQDIHkTLEERISKFLGMEDTILYAAAFDANGGIFEPLFTESD 127
Cdd:PRK07179  62 NDYLNLSGHPDIIKAQIAALQEEGDSLvmSAV-FLHDDSPKP-QFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNT 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 128 AIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEaQLIAANEKGhrfkIIVTDGVFSMDGIVANLKGVCDLAEKYDALV 207
Cdd:PRK07179 140 PVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR-RQIERHGPG----IIVVDSVYSTTGTIAPLADIVDIAEEFGCVL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 208 MVDDSHATGFIGQTGRGTHEANEVMGRVDIITSTLGKALGGaMGGFTSGKKEIIDLLRQRSRPYLFSNSLAP-GIVGAAl 286
Cdd:PRK07179 215 VVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLLPhEIAGLE- 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 287 KVLDMIETDTSRRDTVMENAAYFRTEMKKRGFDIpDGDAAIVPVMLYDAKVSQVMAEKLMDEGIYVIGFFYPVVPKGKAR 366
Cdd:PRK07179 293 ATLEVIESADDRRARLHANARFLREGLSELGYNI-RSESQIIALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNL 371

                        330       340       350
                 ....*....|....*....|....*....|
gi 311907994 367 IRVQLSAAHTRAHLDTAIAAFEKIGKELGI 396
Cdd:PRK07179 372 IRLSLNADLTASDLDRVLEVCREARDEVDL 401
PRK07505 PRK07505
hypothetical protein; Provisional
 39-396 2.39e-42

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 152.83  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  39 ANGKKLLNFCANNYLGLSNHPDVIK-ASQEVMNTHGYGISSVRFICGTQdIHKTLEERISKFLGMEdTILYAAAFDANGG 117
Cdd:PRK07505  43 ADGHTFVNFVSCSYLGLDTHPAIIEgAVDALKRTGSLHLSSSRTRVRSQ-ILKDLEEALSELFGAS-VLTFTSCSAAHLG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 118 IFePL-----FTESDAI--ISDELNHASIIDGVRLCK--AARYRYKNNDMQDLEAQLiaaneKGHRFKIIVTDGVFSMDG 188
Cdd:PRK07505 121 IL-PLlasghLTGGVPPhmVFDKNAHASLNILKGICAdeTEVETIDHNDLDALEDIC-----KTNKTVAYVADGVYSMGG 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 189 iVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRG--THEANEVMGRVDIITSTLGKALGGAMGGFTSGKKEIIDLLRQ 266
Cdd:PRK07505 195 -IAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILR 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 267 RSRPYLFSNSLAPGIVGAALKVLDMIETD--TSRRDTVMENAAYFRTEM--KKRGFDIPdgdaaIVPVMLYDAKVSQVMA 342
Cdd:PRK07505 274 YAGPLAFSQSLNVAALGAILASAEIHLSEelDQLQQKLQNNIALFDSLIptEQSGSFLP-----IRLIYIGDEDTAIKAA 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 311907994 343 EKLMDEGIYVIGFFYPVVPKGKARIRVQLSAAHTRAHLDTAIAAFEKIGKELGI 396
Cdd:PRK07505 349 KQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 45-389 3.32e-42

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 152.37  E-value: 3.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  45 LNFCANNYLGLSNHPDVIKASQEVMNTHGYGISSVRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDANGGIFEPLFT 124
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 125 ESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDL-------EAQLIAANEKGH-RFKIIVTDGVFSMDGIVANLKGV 196
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvRAQDVALKRKPTdQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 197 CDLAEKYDALVMVDDSHATGFIGQTGRGT--HEANEVMGRVDIITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLFS 274
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSleHAGLKPMVHAEIVTFSLENAF-GSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 275 NSLAPGIVGAALKVLDMIETDTSRRDTVMENAAY-----------FRTEMKKRGFDIPDGDAAIVPVMLYDAKVS----Q 339
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANlystltnsshpYALKLRNRLVITSDPISPIIYLRLSDQEATrrtdE 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 311907994 340 VM-----AEKLMDEGIYVIGFFYPVVPKGKAR----IRVQLSAAHTRAHLDTAIAAFEK 389
Cdd:PLN03227 320 TLildqiAHHSLSEGVAVVSTGGHVKKFLQLVpppcLRVVANASHTREDIDKLLTVLGE 378
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 92-257 2.42e-24

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: 98.22  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  92 LEERISKFL--GMEDTILYAAAFDANGGIFEPLFTESDAIISDELNHAS---IIDGVRLCKAARYRYKNNDMQDLEAQLI 166
Cdd:cd01494    5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDVAIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 167 AANEKGHRFKIIVTDGVFSMDGIVANLKGVCDLAEKYDALVMVDDSHATGFIGQTGRGTHEanevmGRVDIITSTLGKAL 246
Cdd:cd01494   85 EELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADVVTFSLHKNL 159

                        170
                 ....*....|.
gi 311907994 247 GGAMGGFTSGK 257
Cdd:cd01494  160 GGEGGGVVIVK 170
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 45-385 4.44e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 93.69  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  45 LNFCANNYLGLSNHPDVIKASQEVMNTH---------GYGISsvRFICGTQDIHKTLEERISKFLGMEDTILYAAAFDAN 115
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaqlGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 116 GGIFEPLFTESDAIISDELNHASIIDGVRLCKAARYRYKNNDMQDLEAQLIAANEKGHRFKIIVTDGVFSMDGIVANLKG 195
Cdd:PRK05937  85 LGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIFIFVCSVYSFKGTLAPLEQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 196 VCDLAEKYDALVMVDDSHATGFIGQTGRGTHEAnevMGRVDI--ITSTLGKALgGAMGGFTSGKKEIIDLLRQRSRPYLF 273
Cdd:PRK05937 165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHS---LGYENFyaVLVTYSKAL-GSMGAALLSSSEVKQDLMLNSPPLRY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 274 SNSLAPGI---VGAALKVLdMIETDTSRRDtVMENAAYFRtemKKRGFDIPdgdAAIVPVMLYDAKvSQVMAEKLMDEGI 350
Cdd:PRK05937 241 STGLPPHLlisIQVAYDFL-SQEGELARKQ-LFRLKEYFA---QKFSSAAP---GCVQPIFLPGIS-EQELYSKLVETGI 311

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 311907994 351 YViGFfypVVPKGKARIRVQLSAAHTRAHLDTAIA 385
Cdd:PRK05937 312 RV-GV---VCFPTGPFLRVNLHAFNTEDEVDILVS 342
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 27-390 2.37e-16

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: 79.92  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994  27 RIITSSQSAEIE-ANGKKLLNFCANNY---LGLsNHPDVIKASQEVMNThgyGISSVRFICGTQDIHKtLEERISKFLGM 102
Cdd:cd00610   20 LVIVRAEGAYLYdVDGNRYLDFLSGIGvlnLGH-NHPEVVEALKEQLAK---LTHFSLGFFYNEPAVE-LAELLLALTPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 103 E-DTILYAaafdaNGGifeplfTES--------------DAIIS-----------------DELNHA---SIIDGVRLCK 147
Cdd:cd00610   95 GlDKVFFV-----NSG------TEAveaalklaraytgrKKIISfegayhgrtlgalsltgSKKYRGgfgPLLPGVLHVP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 148 A-ARYRYKNNDMQDLEAqLIAANEKGHRfKI---IV-----TDGVfsmdgIVAN---LKGVCDLAEKYDALVMVDDShAT 215
Cdd:cd00610  164 YpYRYRPPAELADDLEA-LEEALEEHPE-EVaavIVepiqgEGGV-----IVPPpgyLKALRELCRKHGILLIADEV-QT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 216 GFiGQTGR-GTHEANEVmgRVDIITstLGKALGGAM--GGFTsGKKEIIDLLrqRSRPYLFSNSLAPGIVG--AALKVLD 290
Cdd:cd00610  236 GF-GRTGKmFAFEHFGV--EPDIVT--LGKGLGGGLplGAVL-GREEIMDAF--PAGPGLHGGTFGGNPLAcaAALAVLE 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 291 MIEtdtsrRDTVMENAA----YFRTEMK--KRGFDIPdGD-------AAIVPV-----MLYDAKVSQVMAEKLMDEGIYV 352
Cdd:cd00610  308 VLE-----EEGLLENAAelgeYLRERLRelAEKHPLV-GDvrgrglmIGIELVkdratKPPDKELAAKIIKAALERGLLL 381

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 311907994 353 IgffypvvPKGKARIRVQLSAAHTRAHLDTAIAAFEKI 390
Cdd:cd00610  382 R-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 127-389 3.00e-09

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: 58.12  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 127 DAIISDELNHASIIDGVRL--CKAARYRYKNNDMQDLEAQLIAAnEKGHRFKIIV-------TDGVFSMDgivaNLKGVC 197
Cdd:cd00609   84 DEVLVPDPTYPGYEAAARLagAEVVPVPLDEEGGFLLDLELLEA-AKTPKTKLLYlnnpnnpTGAVLSEE----ELEELA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 198 DLAEKYDALVMVDDSHAtGFIGQTGRGTHEANEVMGRVDIITSTLGKALG--GAMGGFTSGKKEIIDLLRQRSRPYLFSN 275
Cdd:cd00609  159 ELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGlpGLRIGYLIAPPEELLERLKKLLPYTTSG 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 276 SLAPGIVGAAlkvlDMIETDTS----RRDTVMENAAYFRTEMKKRGF--------------DIPDGDAAivpvmlydakv 337
Cdd:cd00609  238 PSTLSQAAAA----AALDDGEEhleeLRERYRRRRDALLEALKELGPlvvvkpsggfflwlDLPEGDDE----------- 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311907994 338 sQVMAEKLMDEGIYVI---GFFYPvvpkGKARIRvqLSAAHTRAHLDTAIAAFEK 389
Cdd:cd00609  303 -EFLERLLLEAGVVVRpgsAFGEG----GEGFVR--LSFATPEEELEEALERLAE 350
ArgD COG4992
Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and ...
 193-394 1.21e-05

Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and metabolism]; Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 444016 [Multi-domain]  Cd Length: 396  Bit Score: 46.96  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 193 LKGVCDLAEKYDALVMVDDSHaTGFiGQTGR--GtHEANEVmgRVDIITstLGKALGG--AMGGFTsGKKEIIDLLRqrs 268
Cdd:COG4992  204 LKGLRELCDEHGALLILDEVQ-TGM-GRTGKlfA-YEHYGV--EPDILT--LAKGLGGgfPIGAVL-AREEVADVFT--- 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 269 rpylfsnslaPGIVG-----------AALKVLDMIEtdtsrRDTVMENA----AYFRTEMKKrgfdIPDGDAAIVPV--- 330
Cdd:COG4992  273 ----------PGDHGstfggnplacaAALAVLDVLE-----EEGLLENVaekgAYLREGLEA----LAAKYPLVKEVrgr 333

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311907994 331 --ML---YDAKVSQVmAEKLMDEGIYVigffypVVPKGKArIRVQLSAAHTRAHLDTAIAAFEKIGKEL 394
Cdd:COG4992  334 glMIgieLDDPAAEV-VKALLEEGLLV------NAAGPNV-IRLLPPLIITEEEIDEALAALEEALAEL 394
BioA COG0161
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; ...
 193-315 2.57e-03

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; Adenosylmethionine-8-amino-7-oxononanoate aminotransferase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439931 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311907994 193 LKGVCDLAEKYDALvMVDDSHATGFigqtGR-GTHEANEVMGRV-DIITstLGKALGGA---MGGfTSGKKEIIDLLRQR 267
Cdd:COG0161  236 LKRLREICDKYGIL-LIADEVITGF----GRtGKMFACEHAGVTpDIIT--LAKGLTGGylpLGA-TLVSDEIYDAFLDG 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 311907994 268 SRP------YLFS-NSLAPGivgAALKVLDMIEtdtsrRDTVMENAA----YFRTEMKK 315
Cdd:COG0161  308 DEAgafmhgHTYSgHPLACA---AALANLDILE-----EEDLLENVAaigaYLRAGLAE 358
 
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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