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Conserved domains on  [gi|17136286|ref|NP_476614|]
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lace, isoform A [Drosophila melanogaster]

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) ...
 117-587 0e+00

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 PLN02483:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 489  Bit Score: 576.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  117 EVPLHTACLTYLGFYLLMILGYINQLlFVPKVATEKGRD--GYVALYDAFESFYSRYVYRRIKDCWNRPICSVPGDELTL 194
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDF-FRAILDWWKTSNlqGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  195 KDRVTDDYGWSFKFTGTETRCLNLGSYNYLGFAAATGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGV 274
Cdd:PLN02483  82 VERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  275 EDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKGgQPWD 354
Cdd:PLN02483 162 PAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH-RPWK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  355 KVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYL 434
Cdd:PLN02483 241 KIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  435 AGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDGTDIGRKKIHQLARNTRYFRRRLAQLGVITYGHEDSPV 514
Cdd:PLN02483 321 AGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPV 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136286  515 VPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGLKYSR 587
Cdd:PLN02483 401 MPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFP 473
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 117-587 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 576.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  117 EVPLHTACLTYLGFYLLMILGYINQLlFVPKVATEKGRD--GYVALYDAFESFYSRYVYRRIKDCWNRPICSVPGDELTL 194
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDF-FRAILDWWKTSNlqGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  195 KDRVTDDYGWSFKFTGTETRCLNLGSYNYLGFAAATGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGV 274
Cdd:PLN02483  82 VERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  275 EDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKGgQPWD 354
Cdd:PLN02483 162 PAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH-RPWK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  355 KVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYL 434
Cdd:PLN02483 241 KIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  435 AGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDGTDIGRKKIHQLARNTRYFRRRLAQLGVITYGHEDSPV 514
Cdd:PLN02483 321 AGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPV 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136286  515 VPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGLKYSR 587
Cdd:PLN02483 401 MPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFP 473
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 214-577 2.22e-140

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: 411.18  E-value: 2.22e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 214 RCLNLGSYNYLGFAAAtGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPS 293
Cdd:cd06454   2 KVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 294 LLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVcygnpkkggQPWDKVMILVEGIFSMEGSIVRL 373
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR---------RPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 374 PEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVtDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCY 453
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 454 AASISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRYFRRRLAQLGVITYGHEDSPVVPMLVYLFSKIGAVVRTLT 533
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 17136286 534 TRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEI 577
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 173-580 5.32e-113

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: 342.42  E-value: 5.32e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 173 YRRIkdcwnRPICSVPGDELTLKDRvtddygwsfkftgtetRCLNLGSYNYLGFA-------AATgqcaddseESARSSG 245
Cdd:COG0156  18 YRYL-----RVLESPQGPRVTIDGR----------------EVLNFSSNDYLGLAnhprvieAAA--------EALDRYG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 246 LAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATN-ALnLPSLLGPNSLVISDEKNHASIILGLRLSGATTKV 324
Cdd:COG0156  69 TGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANlGV-ISALAGRGDLIFSDELNHASIIDGARLSGAKVVR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 325 FKHNNMRDLERVLRQGVCYGnpkkggqpwdKVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRG 404
Cdd:COG0156 148 FRHNDMDDLERLLKKARAAR----------RKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRG 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 405 VTDYFNVDPkEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDgtdigrKK 484
Cdd:COG0156 218 LVEHFGLED-RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------EL 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 485 IHQLARNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTK 564
Cdd:COG0156 291 RERLWENIAYFREGLKELG-FDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTE 369

                       410
                ....*....|....*.
gi 17136286 565 EQLDFALEAIDEIADD 580
Cdd:COG0156 370 EDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 216-575 3.75e-84

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: 267.21  E-value: 3.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   216 LNLGSYNYLGFAAATgQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLL 295
Cdd:TIGR00858  19 LNFSSNDYLGLASHP-EVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   296 GPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNpkkggqpwdkVMILVEGIFSMEGSIVRLPE 375
Cdd:TIGR00858  98 GKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERR----------KLIVTDGVFSMDGDIAPLPQ 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   376 VIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAA 455
Cdd:TIGR00858 168 LVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFST 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   456 SISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAVVRTLTTR 535
Cdd:TIGR00858 248 ALPPAVAAAALAALELIQEEP------WRREKLLALIARLRAGLEALG-FTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 17136286   536 HIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAID 575
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
215-574 6.42e-41

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 151.69  E-value: 6.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   215 CLNLGSYNYLGFaaaTGQCADDSEESARSSGlaycsSRCELGDNEQLQELEALTARYFG--------VEDAIVFGMGFAT 286
Cdd:pfam00155   3 KINLGSNEYLGD---TLPAVAKAEKDALAGG-----TRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   287 NALNLPSLLG-PNSLVISDEKNHASIILGLRLSGATTKVFK-------HNNMRDLERVLRQGVcygnpkkggqpwdkVMI 358
Cdd:pfam00155  75 NIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP--------------KVV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   359 LVEGIFSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSVGAMGSRGRgVTDYFNVDPKEVDILMGTFTKSFGSAG---G 432
Cdd:pfam00155 141 LHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrvG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   433 YLAGSKKLIDFLRTNShAHCYAASISPPIAQQILtsmktimgeDGTDIGRKKIHQ----LARNTRYFRRRLAQLGVITYG 508
Cdd:pfam00155 220 YILGNAAVISQLRKLA-RPFYSSTHLQAAAAAAL---------SDPLLVASELEEmrqrIKERRDYLRDGLQAAGLSVLP 289

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136286   509 hEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPatPIMEGRIRFCLsAAHTKEQLDFALEAI 574
Cdd:pfam00155 290 -SQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSS--PGVPGWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 117-587 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 576.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  117 EVPLHTACLTYLGFYLLMILGYINQLlFVPKVATEKGRD--GYVALYDAFESFYSRYVYRRIKDCWNRPICSVPGDELTL 194
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDF-FRAILDWWKTSNlqGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWFDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  195 KDRVTDDYGWSFKFTGTETRCLNLGSYNYLGFAAATGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGV 274
Cdd:PLN02483  82 VERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  275 EDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKGgQPWD 354
Cdd:PLN02483 162 PAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH-RPWK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  355 KVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYL 434
Cdd:PLN02483 241 KIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGGYI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  435 AGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDGTDIGRKKIHQLARNTRYFRRRLAQLGVITYGHEDSPV 514
Cdd:PLN02483 321 AGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPV 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136286  515 VPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGLKYSR 587
Cdd:PLN02483 401 MPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFP 473
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 214-577 2.22e-140

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: 411.18  E-value: 2.22e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 214 RCLNLGSYNYLGFAAAtGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPS 293
Cdd:cd06454   2 KVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 294 LLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVcygnpkkggQPWDKVMILVEGIFSMEGSIVRL 373
Cdd:cd06454  81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR---------RPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 374 PEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVtDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCY 453
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 454 AASISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRYFRRRLAQLGVITYGHEDSPVVPMLVYLFSKIGAVVRTLT 533
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 17136286 534 TRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEI 577
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEV 348
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 173-580 5.32e-113

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: 342.42  E-value: 5.32e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 173 YRRIkdcwnRPICSVPGDELTLKDRvtddygwsfkftgtetRCLNLGSYNYLGFA-------AATgqcaddseESARSSG 245
Cdd:COG0156  18 YRYL-----RVLESPQGPRVTIDGR----------------EVLNFSSNDYLGLAnhprvieAAA--------EALDRYG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 246 LAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATN-ALnLPSLLGPNSLVISDEKNHASIILGLRLSGATTKV 324
Cdd:COG0156  69 TGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANlGV-ISALAGRGDLIFSDELNHASIIDGARLSGAKVVR 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 325 FKHNNMRDLERVLRQGVCYGnpkkggqpwdKVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRG 404
Cdd:COG0156 148 FRHNDMDDLERLLKKARAAR----------RKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRG 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 405 VTDYFNVDPkEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDgtdigrKK 484
Cdd:COG0156 218 LVEHFGLED-RVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------EL 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 485 IHQLARNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTK 564
Cdd:COG0156 291 RERLWENIAYFREGLKELG-FDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTE 369

                       410
                ....*....|....*.
gi 17136286 565 EQLDFALEAIDEIADD 580
Cdd:COG0156 370 EDIDRLLEALAEVGKE 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 216-583 2.75e-87

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 276.31  E-value: 2.75e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  216 LNLGSYNYLGFAA-----ATGQCADDSeesaRSSGLAycSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALN 290
Cdd:PRK06939  45 INFCANNYLGLANhpeliAAAKAALDS----HGFGMA--SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  291 LPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKggqpwdkvMILVEGIFSMEGSI 370
Cdd:PRK06939 119 FETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGARHK--------LIATDGVFSMDGDI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  371 VRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKeVDILMGTFTKSFGSA-GGYLAGSKKLIDFLRTNSH 449
Cdd:PRK06939 191 APLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDR-VDIITGTLGKALGGAsGGYTAGRKEVIDWLRQRSR 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  450 AHCYAASISPPIAQqilTSMKTI-MGEDGTDIgRKKihqLARNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAV 528
Cdd:PRK06939 270 PYLFSNSLAPAIVA---ASIKVLeLLEESDEL-RDR---LWENARYFREGMTAAG-FTLGPGEHPIIPVMLGDAKLAQEF 341

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17136286  529 VRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGL 583
Cdd:PRK06939 342 ADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 216-575 3.75e-84

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: 267.21  E-value: 3.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   216 LNLGSYNYLGFAAATgQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLL 295
Cdd:TIGR00858  19 LNFSSNDYLGLASHP-EVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   296 GPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNpkkggqpwdkVMILVEGIFSMEGSIVRLPE 375
Cdd:TIGR00858  98 GKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERR----------KLIVTDGVFSMDGDIAPLPQ 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   376 VIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAA 455
Cdd:TIGR00858 168 LVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFST 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   456 SISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAVVRTLTTR 535
Cdd:TIGR00858 248 ALPPAVAAAALAALELIQEEP------WRREKLLALIARLRAGLEALG-FTLMPSCTPIVPVIIGDNASALALAEELQQQ 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 17136286   536 HIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAID 575
Cdd:TIGR00858 321 GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 214-578 8.68e-75

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 243.53  E-value: 8.68e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  214 RCLNLGSYNYLGFA------AATGQCAddSEESARSSGlaycsSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATN 287
Cdd:PRK05958  40 RMLNFASNDYLGLArhprliAAAQQAA--RRYGAGSGG-----SRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAAN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  288 ALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQgvcygnpkkggQPWDKVMILVEGIFSME 367
Cdd:PRK05958 113 LAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK-----------WRAGRALIVTESVFSMD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  368 GSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTN 447
Cdd:PRK05958 182 GDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINR 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  448 SHAHCYAASISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRYFRRRLAQLGvITYGHEDSPVVPMLvylfskIGA 527
Cdd:PRK05958 262 ARPFIFTTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALG-FQLMDSQSAIQPLI------VGD 328

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  528 VVRTLTtrhIAAV--GAGF-------PATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIA 578
Cdd:PRK05958 329 NERALA---LAAAlqEQGFwvgairpPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 220-583 2.82e-52

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: 184.16  E-value: 2.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   220 SYNYLGFaaatGQCA---DDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSL-- 294
Cdd:TIGR01821  52 SNDYLGM----GQHPevlQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLak 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   295 LGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLrQGVCYGNPKkggqpwdkvMILVEGIFSMEGSIVRLP 374
Cdd:TIGR01821 128 IIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLL-QSVDPNRPK---------IIAFESVYSMDGDIAPIE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   375 EVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKeVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYA 454
Cdd:TIGR01821 198 EICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHR-IDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFT 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   455 ASISPPIAQQILTSMKTIMGEdgtdIGRKKIHQlaRNTRYFRRRLAQLGvITYGHEDSPVVPMLVYLFSKIGAVVRTLTT 534
Cdd:TIGR01821 277 TSLPPAIAAGATASIRHLKES----QDLRRAHQ--ENVKRLKNLLEALG-IPVIPNPSHIVPVIIGDAALCKKVSDLLLN 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 17136286   535 RHIAAVGA-GFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGL 583
Cdd:TIGR01821 350 KHGIYVQPiNYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 256-583 7.79e-49

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 175.04  E-value: 7.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  256 GDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSL--LGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDL 333
Cdd:PRK13392  88 GTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADL 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  334 ERVLrQGVCYGNPKkggqpwdkvMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDP 413
Cdd:PRK13392 168 EEQL-ASVDPDRPK---------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMD 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  414 KeVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTiMGEDGTDigrkkIHQLARNTR 493
Cdd:PRK13392 238 R-IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRH-LKTSQTE-----RDAHQDRVA 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  494 YFRRRLAQLGVItygHEDSP--VVPMLVYLFSKIGAVVRTLTTRH-IAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFA 570
Cdd:PRK13392 311 ALKAKLNANGIP---VMPSPshIVPVMVGDPTLCKAISDRLMSEHgIYIQPINYPTVPRGTERLRITPTPLHDDEDIDAL 387

                        330
                 ....*....|...
gi 17136286  571 LEAIDEIADDLGL 583
Cdd:PRK13392 388 VAALVAIWDRLEL 400
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 216-581 6.34e-44

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 161.23  E-value: 6.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  216 LNLGSYNYLGFAAAT---GQCAddseESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLP 292
Cdd:PLN03227   1 LNFATHDFLSTSSSPtlrQTAL----ESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  293 SLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKGGQPWDKVMILVEGIFSMEGSIVR 372
Cdd:PLN03227  77 AFAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  373 LPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPK-EVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAH 451
Cdd:PLN03227 157 LKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPMvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGY 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  452 CYAASISPPIAQqilTSMKTIMGEDGTDIGRKKIHQLARNTRY--------FRRRLAQLGVITyGHEDSPVVPMLVYLFS 523
Cdd:PLN03227 237 CFSASAPPFLAK---ADATATAGELAGPQLLNRLHDSIANLYStltnsshpYALKLRNRLVIT-SDPISPIIYLRLSDQE 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136286  524 KIGAVVRTLTTRHIAA----VGAGFPAT----PIM-----EGRIRFCLSAAHTKEQLDFALEAIDEIADDL 581
Cdd:PLN03227 313 ATRRTDETLILDQIAHhslsEGVAVVSTgghvKKFlqlvpPPCLRVVANASHTREDIDKLLTVLGEAVEAI 383
PLN02822 PLN02822
serine palmitoyltransferase
 216-581 6.35e-44

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 163.37  E-value: 6.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  216 LNLGSYNYLGFAAATgQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLL 295
Cdd:PLN02822 112 VNFASANYLGLIGNE-KIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  296 GPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQgVCYGNpKKGGQPwdKVMILVEGIFSMEGSIVRLPE 375
Cdd:PLN02822 191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAEN-KRKKKL--RRYIVVEAIYQNSGQIAPLDE 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  376 VIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAA 455
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  456 SISPPIAQQILTSMKTImgEDGTDIgrkkIHQLARNTRYFRRRLAQL-GVITYGHEDSPVV------------------- 515
Cdd:PLN02822 347 SLPPYLASAAITAIDVL--EDNPSV----LAKLKENIALLHKGLSDIpGLSIGSNTLSPIVflhlekstgsakedlslle 420

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  516 ----PMLVYLFSKIGAVVRTLTTRHIAAVGagfpatpimegrIRFCLSAAHTKEQLDFALEAIDEIADDL 581
Cdd:PLN02822 421 hiadRMLKEDSVLVVVSKRSTLDKCRLPVG------------IRLFVSAGHTESDILKASESLKRVAASV 478
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
215-574 6.42e-41

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 151.69  E-value: 6.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   215 CLNLGSYNYLGFaaaTGQCADDSEESARSSGlaycsSRCELGDNEQLQELEALTARYFG--------VEDAIVFGMGFAT 286
Cdd:pfam00155   3 KINLGSNEYLGD---TLPAVAKAEKDALAGG-----TRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   287 NALNLPSLLG-PNSLVISDEKNHASIILGLRLSGATTKVFK-------HNNMRDLERVLRQGVcygnpkkggqpwdkVMI 358
Cdd:pfam00155  75 NIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP--------------KVV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   359 LVEGIFSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSVGAMGSRGRgVTDYFNVDPKEVDILMGTFTKSFGSAG---G 432
Cdd:pfam00155 141 LHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrvG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   433 YLAGSKKLIDFLRTNShAHCYAASISPPIAQQILtsmktimgeDGTDIGRKKIHQ----LARNTRYFRRRLAQLGVITYG 508
Cdd:pfam00155 220 YILGNAAVISQLRKLA-RPFYSSTHLQAAAAAAL---------SDPLLVASELEEmrqrIKERRDYLRDGLQAAGLSVLP 289

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136286   509 hEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPatPIMEGRIRFCLsAAHTKEQLDFALEAI 574
Cdd:pfam00155 290 -SQAGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSS--PGVPGWLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
255-583 8.73e-29

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 118.57  E-value: 8.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  255 LGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLE 334
Cdd:PRK07179  95 LHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  335 RVLRQgvcYGnpkKGgqpwdkvMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDpK 414
Cdd:PRK07179 175 RQIER---HG---PG-------IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-S 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  415 EVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDgtdigrKKIHQLARNTRY 494
Cdd:PRK07179 241 RVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVIESAD------DRRARLHANARF 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  495 FRRRLAQLGV-ItygHEDSPVVPMLVYLFSKIGAVVRTLTTRHIaaVGAGF--PATPIMEGRIRFCLSAAHTKEQLDFAL 571
Cdd:PRK07179 315 LREGLSELGYnI---RSESQIIALETGSERNTEVLRDALEERNV--FGAVFcaPATPKNRNLIRLSLNADLTASDLDRVL 389

                        330
                 ....*....|..
gi 17136286  572 EAIDEIADDLGL 583
Cdd:PRK07179 390 EVCREARDEVDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 189-567 1.95e-25

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 109.76  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  189 GDELTLKDRVTDDYGWSFK----FTGTETrcLNLGSYNYLGFAAAtgqcaddseESARSSGLAYCSSRCELGDNEQLQEL 264
Cdd:PLN02955  84 GEEIFSGDALAEERKGRFKklllFSGNDY--LGLSSHPTISNAAA---------NAAKEYGMGPKGSALICGYTTYHRLL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  265 EALTARYFGVEDAIVFGMGFATN-----AL-NLPSLLGPNSLVISDEK--------NHASIILGLRLS----GATTKVFK 326
Cdd:PLN02955 153 ESSLADLKKKEDCLVCPTGFAANmaamvAIgSVASLLAASGKPLKNEKvaifsdalNHASIIDGVRLAerqgNVEVFVYR 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  327 HNNMRDLERVLRQgvCygnpkkggqPWDKVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVT 406
Cdd:PLN02955 233 HCDMYHLNSLLSS--C---------KMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVA 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  407 DYFNVDpKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEdgtdIGRKKih 486
Cdd:PLN02955 302 EEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKE----KWRRK-- 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  487 QLARNTRYFRrrlaQLGVITYGhedSPVVPMLVylfskiGAVVRTL-TTRHIaaVGAGF-------PATPIMEGRIRFCL 558
Cdd:PLN02955 375 AIWERVKEFK----ALSGVDIS---SPIISLVV------GNQEKALkASRYL--LKSGFhvmairpPTVPPNSCRLRVTL 439


                 ....*....
gi 17136286  559 SAAHTKEQL 567
Cdd:PLN02955 440 SAAHTTEDV 448
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 222-488 3.83e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 104.48  E-value: 3.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  222 NYLGFAAATG-----------QCADDSEESarssgLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALN 290
Cdd:PRK05937  13 DFLGFSRSDTlvhevekryrlYCRQFPHAQ-----LGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  291 LPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLrqgVCYGNPKKGgqpwdKVMILVEGIFSMEGSI 370
Cdd:PRK05937  88 CAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL---ESCRQRSFG-----RIFIFVCSVYSFKGTL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  371 VRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTD---YFNVDPKEVdilmgTFTKSFGSAGGYLAGSKKLIDFLRTN 447
Cdd:PRK05937 160 APLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHslgYENFYAVLV-----TYSKALGSMGAALLSSSEVKQDLMLN 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 17136286  448 SHAHCYAASISPPIAQQILTSMKTIMGEDgtDIGRKKIHQL 488
Cdd:PRK05937 235 SPPLRYSTGLPPHLLISIQVAYDFLSQEG--ELARKQLFRL 273
PRK07505 PRK07505
hypothetical protein; Provisional
 196-582 3.35e-17

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 83.88  E-value: 3.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  196 DRVTDDYGWSFkftgtetrcLNLGSYNYLGF-------AAAtgqcaddSEESARSSGLAYCSSRCELgdNEQ-LQELEAL 267
Cdd:PRK07505  38 ILITLADGHTF---------VNFVSCSYLGLdthpaiiEGA-------VDALKRTGSLHLSSSRTRV--RSQiLKDLEEA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  268 TARYFGVEdAIVFGMGFATNALNLPsLLGPNSL-------VISDEKNHASIILGLRLSGATTKV--FKHNnmrDLERvLR 338
Cdd:PRK07505 100 LSELFGAS-VLTFTSCSAAHLGILP-LLASGHLtggvpphMVFDKNAHASLNILKGICADETEVetIDHN---DLDA-LE 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  339 QgVCYGNPKkggqpwdkVMILVEGIFSMeGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRG-VTDYFNVDPKEVD 417
Cdd:PRK07505 174 D-ICKTNKT--------VAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRLNERT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  418 ILMGTFTKSFGSAGGYLA-GSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKtIMGEDGTDIGRKKIHQlarNTRYFR 496
Cdd:PRK07505 244 IIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAE-IHLSEELDQLQQKLQN---NIALFD 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286  497 RRLA--QLGVitygheDSPVvpMLVYlfskIGAVVRTLTT-RHIAAvgAGFPATPIM-----EGR--IRFCLSAAHTKEQ 566
Cdd:PRK07505 320 SLIPteQSGS------FLPI--RLIY----IGDEDTAIKAaKQLLD--RGFYTSPVFfpvvaKGRagLRIMFRASHTNDE 385

                        410
                 ....*....|....*.
gi 17136286  567 LDFALEAIDEIADDLG 582
Cdd:PRK07505 386 IKRLCSLLKEILDEGL 401
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 256-576 2.42e-12

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: 68.52  E-value: 2.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 256 GDNEQLQELEALTARYFGV-------EDAIVFGMGfATNALNL--PSLLGPNSLVISDEKNHASIILGLRLSGAT----- 321
Cdd:cd00609  33 YPDPGLPELREAIAEWLGRrggvdvpPEEIVVTNG-AQEALSLllRALLNPGDEVLVPDPTYPGYEAAARLAGAEvvpvp 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 322 -TKVFKHNNMRDLERVLRQG------VCY-GNPkkGGQPWDKVmilvegifsmegsivRLPEVIALKKKYKAYLYLDEAH 393
Cdd:cd00609 112 lDEEGGFLLDLELLEAAKTPktkllyLNNpNNP--TGAVLSEE---------------ELEELAELAKKHGILIISDEAY 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 394 SvgAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAG---GYLAGSKK-LIDFLRTnshAHCYAASISPPIAQQILTSM 469
Cdd:cd00609 175 A--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEeLLERLKK---LLPYTTSGPSTLSQAAAAAA 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 470 KtimgEDGTDIGRKKIHQLARNTRYFRRRLAQLGvityghEDSPVVP---MLVYL----FSKIGAVVRTLTTRHIAAV-G 541
Cdd:cd00609 250 L----DDGEEHLEELRERYRRRRDALLEALKELG------PLVVVKPsggFFLWLdlpeGDDEEFLERLLLEAGVVVRpG 319

                       330       340       350
                ....*....|....*....|....*....|....*
gi 17136286 542 AGFPATPimEGRIRFCLsaAHTKEQLDFALEAIDE 576
Cdd:cd00609 320 SAFGEGG--EGFVRLSF--ATPEEELEEALERLAE 350
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
269-579 9.63e-10

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 60.92  E-value: 9.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 269 ARYFGVEDA--IVFGMGfATNALNLP----SLLGPNSLVISDEKNHASIILGLRLS----GATTKVFKHN-----NMRDL 333
Cdd:COG0520  69 ARFIGAASPdeIIFTRG-TTEAINLVayglGRLKPGDEILITEMEHHSNIVPWQELaertGAEVRVIPLDedgelDLEAL 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 334 ERVLRqgvcyGNPKkggqpwdkvMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGsrgrgvtdyFNVDP 413
Cdd:COG0520 148 EALLT-----PRTK---------LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLP---------VDVQA 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 414 KEVDILMGTFTKSFGSAG-GYLAGSKKLIDFLR-----------TNSHAHCYAASI------SPPIAQQI--LTSMKTIM 473
Cdd:COG0520 205 LGCDFYAFSGHKLYGPTGiGVLYGKRELLEALPpflggggmiewVSFDGTTYADLPrrfeagTPNIAGAIglGAAIDYLE 284

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 474 gedgtDIGRKKIHQ-LARNTRYFRRRLAQL-GVITYGHED----SPVVPmlvylFSKIG----AVVRTLTTRHIAAVGAG 543
Cdd:COG0520 285 -----AIGMEAIEArERELTAYALEGLAAIpGVRILGPADpedrSGIVS-----FNVDGvhphDVAALLDDEGIAVRAGH 354

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 17136286 544 FPATPIME-----GRIRFCLSAAHTKEQLDFALEAIDEIAD 579
Cdd:COG0520 355 HCAQPLMRrlgvpGTVRASFHLYNTEEEIDRLVEALKKLAE 395
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 261-432 1.39e-09

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


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 57.39  E-value: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 261 LQELEALTARYF--GVEDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIIL-GLRLSGATTKVFKHNnmrDLERVL 337
Cdd:cd01494   2 LEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWvAAELAGAKPVPVPVD---DAGYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 338 RQGVCYGNPKKGGQPwdkVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFnvdpkeVD 417
Cdd:cd01494  79 LDVAILEELKAKPNV---ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG------AD 149

                       170
                ....*....|....*
gi 17136286 418 ILMGTFTKSFGSAGG 432
Cdd:cd01494 150 VVTFSLHKNLGGEGG 164
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 256-574 1.16e-06

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


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 50.79  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 256 GDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLLGPNSLVISDEKNH--------ASIILGLRLSGATTKVFKH 327
Cdd:cd06502  29 GEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHiytdeagaPEFLSGVKLLPVPGENGKL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 328 nNMRDLERVLRQGVCYGNPKKGgqpwdkvMILVEGifSMEGSIVRLPEVI----ALKKKYKAYLYLDEAHSVGAMGSRGR 403
Cdd:cd06502 109 -TPEDLEAAIRPRDDIHFPPPS-------LVSLEN--TTEGGTVYPLDELkaisALAKENGLPLHLDGARLANAAAALGV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 404 GVTDYfnvdPKEVDILMGTFTKSFGSAGG-YLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKtimgedgTDIGR 482
Cdd:cd06502 179 ALKTY----KSGVDSVSFCLSKGGGAPVGaVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAGLAALE-------NDLWL 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286 483 KKIHQLARNTRYFRRRLAQLGvityGHEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAH 562
Cdd:cd06502 248 RRLRHDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDT 323

                       330
                ....*....|..
gi 17136286 563 TKEQLDFALEAI 574
Cdd:cd06502 324 TEEDVDELLSAL 335
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 259-568 1.26e-03

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


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 41.46  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   259 EQLQELEALTARYFGVEDA--IVF----GMGFATNALNLPSLLGP-NSLVISDEKNHASIILGLRLS---GATTKVFKHN 328
Cdd:pfam00266  43 QAYEEAREKVAEFINAPSNdeIIFtsgtTEAINLVALSLGRSLKPgDEIVITEMEHHANLVPWQELAkrtGARVRVLPLD 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   329 -----NMRDLERVLRQGVCYgnpkkggqpwdkVMI-LVEGIFsmeGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMgsrg 402
Cdd:pfam00266 123 edgllDLDELEKLITPKTKL------------VAItHVSNVT---GTIQPVPEIGKLAHQYGALVLVDAAQAIGHR---- 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   403 rgvtdyfNVDPKEVDILMGTFT--KSFGSAG-GYLAGSKKLIDFLR------------TNSHAHCYAA-----SISPPIA 462
Cdd:pfam00266 184 -------PIDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDLLEKMPpllggggmietvSLQESTFADApwkfeAGTPNIA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136286   463 QQI-LTSMKTIMGEDGTDIGRKKIHQLArntRYFRRRLAQLGVIT-YG-HEDSPVVPmlvylFSKIG----AVVRTLTTR 535
Cdd:pfam00266 257 GIIgLGAALEYLSEIGLEAIEKHEHELA---QYLYERLLSLPGIRlYGpERRASIIS-----FNFKGvhphDVATLLDES 328

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 17136286   536 HIaAVGAGFP-ATPIM-----EGRIRFCLSAAHTKEQLD 568
Cdd:pfam00266 329 GI-AVRSGHHcAQPLMvrlglGGTVRASFYIYNTQEDVD 366
 
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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