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Conserved domains on  [gi|19112640|ref|NP_595848|]
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serine palmitoyl transferase A subunit [Schizosaccharomyces pombe]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 51-493 1.67e-144

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).


The actual alignment was detected with superfamily member PLN02822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 481  Bit Score: 423.38  E-value: 1.67e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   51 FIEFLLLVFAAYYVLRKPRTSPDNnyvEFTEKEINELVDDWKPEPLVAELTDVEKLElksIPVLESVHLHTKLIDGRPIT 130
Cdd:PLN02822  39 VVEGLLIVVIVFLLSQKSYKPPKR---PLTEKEIDELCDEWTPEPLIPPITEEMRPE---PPVLESAAGPHTIINGKDVV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  131 NFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKR 210
Cdd:PLN02822 113 NFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  211 GDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEDDFvKHNRPLtRRFIITEGISENYGDMVDLTKIVAL 290
Cdd:PLN02822 193 GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKKL-RRYIVVEAIYQNSGQIAPLDEIVRL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  291 KKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPA 370
Cdd:PLN02822 271 KEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPP 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  371 SLAVAAYEAISILsRDGGSMLNDLRSKSALFHAKLSRNKFFETSSDIESPIIHLRFKDKDISHDKQVFLLEEIVELCIAE 450
Cdd:PLN02822 351 YLASAAITAIDVL-EDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRMLKE 429

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 19112640  451 -GFLIARAKRvESLERVKVQPSLRICISTGHSAEEIEKLALLIK 493
Cdd:PLN02822 430 dSVLVVVSKR-STLDKCRLPVGIRLFVSAGHTESDILKASESLK 472
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 51-493 1.67e-144

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 423.38  E-value: 1.67e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   51 FIEFLLLVFAAYYVLRKPRTSPDNnyvEFTEKEINELVDDWKPEPLVAELTDVEKLElksIPVLESVHLHTKLIDGRPIT 130
Cdd:PLN02822  39 VVEGLLIVVIVFLLSQKSYKPPKR---PLTEKEIDELCDEWTPEPLIPPITEEMRPE---PPVLESAAGPHTIINGKDVV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  131 NFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKR 210
Cdd:PLN02822 113 NFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  211 GDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEDDFvKHNRPLtRRFIITEGISENYGDMVDLTKIVAL 290
Cdd:PLN02822 193 GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKKL-RRYIVVEAIYQNSGQIAPLDEIVRL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  291 KKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPA 370
Cdd:PLN02822 271 KEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPP 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  371 SLAVAAYEAISILsRDGGSMLNDLRSKSALFHAKLSRNKFFETSSDIESPIIHLRFKDKDISHDKQVFLLEEIVELCIAE 450
Cdd:PLN02822 351 YLASAAITAIDVL-EDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRMLKE 429

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 19112640  451 -GFLIARAKRvESLERVKVQPSLRICISTGHSAEEIEKLALLIK 493
Cdd:PLN02822 430 dSVLVVVSKR-STLDKCRLPVGIRLFVSAGHTESDILKASESLK 472
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 93-494 6.57e-75

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: 241.11  E-value: 6.57e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  93 PEPLVAELTDVEKLEL-KSIPVLESVHLHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQ 171
Cdd:COG0156   2 LDRLEAELAALKAAGLyRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 172 DKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQ 251
Cdd:COG0156  82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 252 ELEDDfvkhnrplTRRFIITEGIsenY---GDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPtDVE 328
Cdd:COG0156 162 KARAA--------RRKLIVTDGV---FsmdGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLED-RVD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 329 IIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPASLAVAAYEAISILsRDGGSMLNDLRSKSALFHAKLSRN 408
Cdd:COG0156 230 IIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEIL-REEPELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 409 KFFETSSdiESPIIHLRFKDkdishDKQVFlleEIVELCIAEGFLI------------ARakrveslervkvqpsLRICI 476
Cdd:COG0156 309 GFDLGPS--ESPIVPVIVGD-----AERAL---ALADALLERGIYVsairpptvpkgtAR---------------LRITL 363

                       410
                ....*....|....*...
gi 19112640 477 STGHSAEEIEKLALLIKE 494
Cdd:COG0156 364 SAAHTEEDIDRLLEALAE 381
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 127-494 4.07e-65

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: 214.73  E-value: 4.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 127 RPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPA 206
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 207 FSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEddfvkhnRPLTRRFIITEGISENYGDMVDLTK 286
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR-------RPYGKKLIVTEGVYSMDGDIAPLPE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 287 IVALKKKYKYRLILDETWSFGTCGRTGKGLtEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSA 366
Cdd:cd06454 154 LVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFST 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 367 ALPASLAVAAYEAISILSRdGGSMLNDLRSKSALFHAKLSRnKFFETSSDIESPIIHLRFKDKDishdkqvfLLEEIVEL 446
Cdd:cd06454 233 SLPPAVAAAALAALEVLQG-GPERRERLQENVRYLRRGLKE-LGFPVGGSPSHIIPPLIGDDPA--------KAVAFSDA 302

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 19112640 447 CIAEGFLI--ARAKRVEslervKVQPSLRICISTGHSAEEIEKLALLIKE 494
Cdd:cd06454 303 LLERGIYVqaIRYPTVP-----RGTARLRISLSAAHTKEDIDRLLEALKE 347
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
127-489 2.56e-19

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 89.29  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   127 RPITNFASFNFLDLaenkhITECAVATLREcgLGACGPPGFYGTQDKHLRLEKDIASFIG--------VERAIVYAQSFQ 198
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   199 TISSVIPAFSK-RGDILVVDEAcNFA-IQKGIQISRTTIRYFK-------HNNMKDLERILQELeddfvkhnrpltRRFI 269
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAP-TYAsYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK------------PKVV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   270 ITEGISENYGDMV---DLTKIVALKKKYKYRLILDETWSfGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGG---G 343
Cdd:pfam00155 141 LHTSPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYA-GFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   344 FCAGSELMVEHQRLSGMAYIYSAALPAsLAVAAYEAISILSRDGGSMLNDLRSKSALFHAKLSRNKFFETSSdiESPIIH 423
Cdd:pfam00155 220 YILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPS--QAGFFL 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112640   424 LRFKDKDISHDKQVFLLEeivelciaEGFLIARAKRVESlervkVQPSLRICIsTGHSAEEIEKLA 489
Cdd:pfam00155 297 LTGLDPETAKELAQVLLE--------EVGVYVTPGSSPG-----VPGWLRITV-AGGTEEELEELL 348
 
Name Accession Description Interval E-value
PLN02822 PLN02822
serine palmitoyltransferase
 51-493 1.67e-144

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 423.38  E-value: 1.67e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   51 FIEFLLLVFAAYYVLRKPRTSPDNnyvEFTEKEINELVDDWKPEPLVAELTDVEKLElksIPVLESVHLHTKLIDGRPIT 130
Cdd:PLN02822  39 VVEGLLIVVIVFLLSQKSYKPPKR---PLTEKEIDELCDEWTPEPLIPPITEEMRPE---PPVLESAAGPHTIINGKDVV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  131 NFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKR 210
Cdd:PLN02822 113 NFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFCKK 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  211 GDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEDDFvKHNRPLtRRFIITEGISENYGDMVDLTKIVAL 290
Cdd:PLN02822 193 GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEN-KRKKKL-RRYIVVEAIYQNSGQIAPLDEIVRL 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  291 KKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPA 370
Cdd:PLN02822 271 KEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSASLPP 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  371 SLAVAAYEAISILsRDGGSMLNDLRSKSALFHAKLSRNKFFETSSDIESPIIHLRFKDKDISHDKQVFLLEEIVELCIAE 450
Cdd:PLN02822 351 YLASAAITAIDVL-EDNPSVLAKLKENIALLHKGLSDIPGLSIGSNTLSPIVFLHLEKSTGSAKEDLSLLEHIADRMLKE 429

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 19112640  451 -GFLIARAKRvESLERVKVQPSLRICISTGHSAEEIEKLALLIK 493
Cdd:PLN02822 430 dSVLVVVSKR-STLDKCRLPVGIRLFVSAGHTESDILKASESLK 472
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 131-502 7.45e-99

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 303.36  E-value: 7.45e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  131 NFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKR 210
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  211 GDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQEL--EDDFVKHNRPLTRRFIITEGISENYGDMVDLTKIV 288
Cdd:PLN03227  82 GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVraQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKELV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  289 ALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPT-DVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAA 367
Cdd:PLN03227 162 ALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPMvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFSAS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  368 LPASLAVAAYEAISILSRDgGSMLNDLRSKSALFHAKLS----------RNKFFeTSSDIESPIIHLRFKDKDIS-HDKQ 436
Cdd:PLN03227 242 APPFLAKADATATAGELAG-PQLLNRLHDSIANLYSTLTnsshpyalklRNRLV-ITSDPISPIIYLRLSDQEATrRTDE 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112640  437 VFLLEEIVELCIAEGF-LIARAKRVESLERVKVQPSLRICISTGHSAEEIEKLALLIKEKTEIVFDK 502
Cdd:PLN03227 320 TLILDQIAHHSLSEGVaVVSTGGHVKKFLQLVPPPCLRVVANASHTREDIDKLLTVLGEAVEAILCK 386
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 93-494 6.57e-75

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: 241.11  E-value: 6.57e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  93 PEPLVAELTDVEKLEL-KSIPVLESVHLHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQ 171
Cdd:COG0156   2 LDRLEAELAALKAAGLyRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 172 DKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQ 251
Cdd:COG0156  82 PLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 252 ELEDDfvkhnrplTRRFIITEGIsenY---GDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPtDVE 328
Cdd:COG0156 162 KARAA--------RRKLIVTDGV---FsmdGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLED-RVD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 329 IIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAALPASLAVAAYEAISILsRDGGSMLNDLRSKSALFHAKLSRN 408
Cdd:COG0156 230 IIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEIL-REEPELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 409 KFFETSSdiESPIIHLRFKDkdishDKQVFlleEIVELCIAEGFLI------------ARakrveslervkvqpsLRICI 476
Cdd:COG0156 309 GFDLGPS--ESPIVPVIVGD-----AERAL---ALADALLERGIYVsairpptvpkgtAR---------------LRITL 363

                       410
                ....*....|....*...
gi 19112640 477 STGHSAEEIEKLALLIKE 494
Cdd:COG0156 364 SAAHTEEDIDRLLEALAE 381
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 127-494 4.07e-65

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: 214.73  E-value: 4.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 127 RPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPA 206
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 207 FSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQELEddfvkhnRPLTRRFIITEGISENYGDMVDLTK 286
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR-------RPYGKKLIVTEGVYSMDGDIAPLPE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 287 IVALKKKYKYRLILDETWSFGTCGRTGKGLtEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSA 366
Cdd:cd06454 154 LVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFST 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 367 ALPASLAVAAYEAISILSRdGGSMLNDLRSKSALFHAKLSRnKFFETSSDIESPIIHLRFKDKDishdkqvfLLEEIVEL 446
Cdd:cd06454 233 SLPPAVAAAALAALEVLQG-GPERRERLQENVRYLRRGLKE-LGFPVGGSPSHIIPPLIGDDPA--------KAVAFSDA 302

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 19112640 447 CIAEGFLI--ARAKRVEslervKVQPSLRICISTGHSAEEIEKLALLIKE 494
Cdd:cd06454 303 LLERGIYVqaIRYPTVP-----RGTARLRISLSAAHTKEDIDRLLEALKE 347
PLN02483 PLN02483
serine palmitoyltransferase
 131-499 3.62e-55

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 192.28  E-value: 3.62e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  131 NFASFNFLDLAE-NKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSK 209
Cdd:PLN02483 104 NLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALIG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  210 RGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQE-LEDDFVKHNRPLTRRFIITEGISENYGDMVDLTKIV 288
Cdd:PLN02483 184 KGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREqIAEGQPRTHRPWKKIIVIVEGIYSMEGELCKLPEIV 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  289 ALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGMAYIYSAAL 368
Cdd:PLN02483 264 AVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSM 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  369 PaslAVAAYEAIS----ILSRDGGSM----LNDLRSKSALFHAKLsRNKFFETSSDIESPIIHLRF----KDKDISHDkq 436
Cdd:PLN02483 344 S---PPAVQQVISaikvILGEDGTNRgaqkLAQIRENSNFFRSEL-QKMGFEVLGDNDSPVMPIMLynpaKIPAFSRE-- 417

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112640  437 vfLLEEIVELCI----AEGFLIARAkrveslervkvqpslRICISTGHSAEEIEKLALLIKEKTEIV 499
Cdd:PLN02483 418 --CLKQNVAVVVvgfpATPLLLARA---------------RICISASHSREDLIKALEVISEVGDLV 467
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 108-488 2.39e-42

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 154.93  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  108 LKSIPVLESVHLHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGV 187
Cdd:PRK05958  20 YRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  188 ERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQEleddfvkhnRPLTRR 267
Cdd:PRK05958 100 ERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK---------WRAGRA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  268 FIITEGISENYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGGGFCAG 347
Cdd:PRK05958 171 LIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  348 SELMVEHqrLSGMA--YIYSAALPASLAVAAYEAISILSRDggsmlNDLRSK----SALFHAKLSRNKFfeTSSDIESPI 421
Cdd:PRK05958 251 SETLIDY--LINRArpFIFTTALPPAQAAAARAALRILRRE-----PERRERlaalIARLRAGLRALGF--QLMDSQSAI 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112640  422 IHLRFKDKDISHDKQVFLLEeivelciaEGFLiARAKRveslervkvQPS-------LRICISTGHSAEEIEKL 488
Cdd:PRK05958 322 QPLIVGDNERALALAAALQE--------QGFW-VGAIR---------PPTvpagtsrLRITLTAAHTEADIDRL 377
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 96-487 1.98e-39

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 147.26  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   96 LVAELTDVEKLEL-KSIPVLESVH-LHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGLGA------CGppgf 167
Cdd:PRK06939   9 LREELEEIKAEGLyKEERVITSPQgADITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMasvrfiCG---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  168 ygTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLE 247
Cdd:PRK06939  85 --TQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  248 RILQELEDDFVKHnrpltrRFIITEGISENYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVppTD- 326
Cdd:PRK06939 163 AQLKEAKEAGARH------KLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGV--MDr 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  327 VEIIIGSLTTSLAGG-GGFCAGSELMVEHQRLSGMAYIYSAALPASLAVAAYEAISILSRDGgsmlnDLRSK----SALF 401
Cdd:PRK06939 235 VDIITGTLGKALGGAsGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESD-----ELRDRlwenARYF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  402 HAKLSRNKFfeTSSDIESPIIHLRFKDKDISHDKQVFLLEEIVelcIAEGF---LIARAKrveslERVKVQPslriciST 478
Cdd:PRK06939 310 REGMTAAGF--TLGPGEHPIIPVMLGDAKLAQEFADRLLEEGV---YVIGFsfpVVPKGQ-----ARIRTQM------SA 373


                 ....*....
gi 19112640  479 GHSAEEIEK 487
Cdd:PRK06939 374 AHTKEQLDR 382
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 127-408 1.56e-24

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 105.71  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  127 RPITNFASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSF-------QT 199
Cdd:PRK13392  46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYvsndaalST 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  200 ISSVIPafskrGDILVVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQEleddfVKHNRPltrRFIITEGISENYG 279
Cdd:PRK13392 126 LGKLLP-----GCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLAS-----VDPDRP---KLIAFESVYSMDG 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  280 DMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVPpTDVEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSG 359
Cdd:PRK13392 193 DIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLM-DRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFA 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 19112640  360 MAYIYSAALPASLAVAAYEAISILSRDGGSMlNDLRSKSALFHAKLSRN 408
Cdd:PRK13392 272 PGFIFTTALPPAVAAGATAAIRHLKTSQTER-DAHQDRVAALKAKLNAN 319
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 132-488 2.69e-21

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 96.67  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  132 FASFNFLDLAENKHITECAVATLRECGLGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQ----------TIS 201
Cdd:PLN02955 107 FSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAanmaamvaigSVA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  202 SVIPAFSK---RGDILVVDEACNFA-IQKGIQISR----TTIRYFKHNNMKDLERILQeleddfvkhNRPLTRRFIITEG 273
Cdd:PLN02955 187 SLLAASGKplkNEKVAIFSDALNHAsIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLS---------SCKMKRKVVVTDS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  274 ISENYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVpPTDVEIIIGSLTTSLAGGGGFCAGSELMVE 353
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNC-EADVDLCVGTLSKAAGCHGGFIACSKKWKQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  354 HQRLSGMAYIYSAALPASLAVAAYEAISILSRDggsmlnDLRSKsalfhAKLSRNKFFE--TSSDIESPIIHLRFKDKDI 431
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKE------KWRRK-----AIWERVKEFKalSGVDISSPIISLVVGNQEK 405

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  432 SHDKQVFLLEeivelciaEGFliarakRVESLERVKVQPS---LRICISTGHSAEEIEKL 488
Cdd:PLN02955 406 ALKASRYLLK--------SGF------HVMAIRPPTVPPNscrLRVTLSAAHTTEDVKKL 451
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
127-489 2.56e-19

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 89.29  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   127 RPITNFASFNFLDLaenkhITECAVATLREcgLGACGPPGFYGTQDKHLRLEKDIASFIG--------VERAIVYAQSFQ 198
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   199 TISSVIPAFSK-RGDILVVDEAcNFA-IQKGIQISRTTIRYFK-------HNNMKDLERILQELeddfvkhnrpltRRFI 269
Cdd:pfam00155  74 ANIEALIFLLAnPGDAILVPAP-TYAsYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK------------PKVV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   270 ITEGISENYGDMV---DLTKIVALKKKYKYRLILDETWSfGTCGRTGKGLTEHFGVPPTDVEIIIGSLTTSLAGGG---G 343
Cdd:pfam00155 141 LHTSPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYA-GFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640   344 FCAGSELMVEHQRLSGMAYIYSAALPAsLAVAAYEAISILSRDGGSMLNDLRSKSALFHAKLSRNKFFETSSdiESPIIH 423
Cdd:pfam00155 220 YILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPS--QAGFFL 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112640   424 LRFKDKDISHDKQVFLLEeivelciaEGFLIARAKRVESlervkVQPSLRICIsTGHSAEEIEKLA 489
Cdd:pfam00155 297 LTGLDPETAKELAQVLLE--------EVGVYVTPGSSPG-----VPGWLRITV-AGGTEEELEELL 348
PRK07505 PRK07505
hypothetical protein; Provisional
 108-494 6.00e-16

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 79.64  E-value: 6.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  108 LKSIPVLESVHLHTKLIDGRPITNFASFNFLDLAENKHITECAVATLRECGL-------GACGPPGFygtqdkhLRLEKD 180
Cdd:PRK07505  27 LNGLTVGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlhlsssrTRVRSQIL-------KDLEEA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  181 IASFIGVErAIVYAQSFQTISSVIP-----AFSKRGDIL-VVDEACNFAIQ--KGIQISRTTIRYFKHNnmkDLERilqe 252
Cdd:PRK07505 100 LSELFGAS-VLTFTSCSAAHLGILPllasgHLTGGVPPHmVFDKNAHASLNilKGICADETEVETIDHN---DLDA---- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  253 LEDDFVKHNRPltrrFIITEGISeNYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLT-EHFGVPPTDVEIII 331
Cdd:PRK07505 172 LEDICKTNKTV----AYVADGVY-SMGGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrSELDYRLNERTIIA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  332 GSLTTSLAGGGGFCA-GSELMVEHQRLSGMAYIYSaalpASLAVAAYEAISI-----LSRDGGSMLNDLRSKSALFHAKL 405
Cdd:PRK07505 247 ASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFS----QSLNVAALGAILAsaeihLSEELDQLQQKLQNNIALFDSLI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  406 SrNKFFETSSDIEspIIHLRFKDKDISHDKQVFlleeivelciAEGFL--------IARAKrveslervkvqPSLRICIS 477
Cdd:PRK07505 323 P-TEQSGSFLPIR--LIYIGDEDTAIKAAKQLL----------DRGFYtspvffpvVAKGR-----------AGLRIMFR 378

                        410
                 ....*....|....*..
gi 19112640  478 TGHSAEEIEKLALLIKE 494
Cdd:PRK07505 379 ASHTNDEIKRLCSLLKE 395
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
132-368 1.82e-12

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 68.88  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  132 FASFNFLDLAENKHITECAVATLRECGLGACGPPGF-YGTQDKHlRLEKDIASFIGVERAIVyAQS--------FQTI-S 201
Cdd:PRK07179  59 LQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFlHDDSPKP-QFEKKLAAFTGFESCLL-CQSgwaanvglLQTIaD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  202 SVIPAFskrgdilvVDEACNFAIQKGIQISRTTIRYFKHNNMKDLERILQeleddfvkHNRPltrRFIITEGISENYGDM 281
Cdd:PRK07179 137 PNTPVY--------IDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIE--------RHGP---GIIVVDSVYSTTGTI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  282 VDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTEHFGVppTD-VEIIIGSLTTSLAGGGGFCAGSELMVEHQRLSGM 360
Cdd:PRK07179 198 APLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGL--TSrVHFITASLAKAFAGRAGIITCPRELAEYVPFVSY 275


                 ....*...
gi 19112640  361 AYIYSAAL 368
Cdd:PRK07179 276 PAIFSSTL 283
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 159-406 1.63e-11

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 65.96  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  159 LGACGPPGFYGTQDKHLRLEKDIASFIGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFAIQKGIQISRTTIRYF 238
Cdd:PRK05937  43 LGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  239 KHNNMKDLERILQELEddfvkhNRPLTRRFIITEGISENYGDMVDLTKIVALKKKYKYRLILDETWSFGTCGRTGKGLTE 318
Cdd:PRK05937 123 RHNDLDHLESLLESCR------QRSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCH 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640  319 HFGVPPTDVEIIIGSLTTSLAGGGGFCAG---SELMVEHQRLSgmayiYSAALPASLAVAAYEAISILSRDGGSMLNDLR 395
Cdd:PRK05937 197 SLGYENFYAVLVTYSKALGSMGAALLSSSevkQDLMLNSPPLR-----YSTGLPPHLLISIQVAYDFLSQEGELARKQLF 271

                        250
                 ....*....|.
gi 19112640  396 SKSALFHAKLS 406
Cdd:PRK05937 272 RLKEYFAQKFS 282
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 173-343 6.33e-03

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: 37.75  E-value: 6.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 173 KHLRLEKDIASF--IGVERAIVYAQSFQTISSVIPAFSKRGDILVVDEACNFA-IQKGIQISRTTIRYFKHNNMKDLERI 249
Cdd:cd01494   1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112640 250 LQELEDDFVKHNRpltrRFIITEGISENYGDMVDLTKIVALKKKYKYRLILDETWSFGtcGRTGKGLTEHFGVPptdvEI 329
Cdd:cd01494  81 VAILEELKAKPNV----ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG--ASPAPGVLIPEGGA----DV 150

                       170
                ....*....|....
gi 19112640 330 IIGSLTTSLAGGGG 343
Cdd:cd01494 151 VTFSLHKNLGGEGG 164
 
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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