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Conserved domains on  [gi|1112949909|gb|OJT04238|]
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Serine palmitoyltransferase 2 [Trametes pubescens]

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) ...
 133-652 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: 558.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 133 PYYILLTTYISYILVICLGHLRDFvgkrfraaqYRHLLPW------KGYAALNSDFDSFYTRRLKLRIDDCFSHPTTGVP 206
Cdd:PLN02483    5 PYLTALTTYFSYGLLFAFGQLRDF---------FRAILDWwktsnlQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 207 GRTIVLLDRYSSDYNKTMVPTGTRTRALNVSSYNYLGFAQSSGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALI 286
Cdd:PLN02483   76 DAWFDVVERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 287 ARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQPKT 366
Cdd:PLN02483  156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 367 HRPWKKILLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGA 446
Cdd:PLN02483  236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 447 AGGYIAGNKAVVDRLRIQGHSGAYAEAMTPPVLTQIIASMASIMGitlpaekpsspslallrssdfppviseselipgta 526
Cdd:PLN02483  316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILG----------------------------------- 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 527 patalpswmplapsmVDGSD-GLMRLRRIAFNARYLNRGLRKLGFITYGTDDSPVVPLLIFHPGKMAVFSRLMrtYSTPI 605
Cdd:PLN02483  361 ---------------EDGTNrGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSREC--LKQNV 423

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1112949909 606 VVVVVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRACDEIGDVLDLK 652
Cdd:PLN02483  424 AVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIK 470
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 133-652 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 558.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 133 PYYILLTTYISYILVICLGHLRDFvgkrfraaqYRHLLPW------KGYAALNSDFDSFYTRRLKLRIDDCFSHPTTGVP 206
Cdd:PLN02483    5 PYLTALTTYFSYGLLFAFGQLRDF---------FRAILDWwktsnlQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 207 GRTIVLLDRYSSDYNKTMVPTGTRTRALNVSSYNYLGFAQSSGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALI 286
Cdd:PLN02483   76 DAWFDVVERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 287 ARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQPKT 366
Cdd:PLN02483  156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 367 HRPWKKILLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGA 446
Cdd:PLN02483  236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 447 AGGYIAGNKAVVDRLRIQGHSGAYAEAMTPPVLTQIIASMASIMGitlpaekpsspslallrssdfppviseselipgta 526
Cdd:PLN02483  316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILG----------------------------------- 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 527 patalpswmplapsmVDGSD-GLMRLRRIAFNARYLNRGLRKLGFITYGTDDSPVVPLLIFHPGKMAVFSRLMrtYSTPI 605
Cdd:PLN02483  361 ---------------EDGTNrGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSREC--LKQNV 423

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1112949909 606 VVVVVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRACDEIGDVLDLK 652
Cdd:PLN02483  424 AVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIK 470
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 232-646 9.92e-152

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 443.16  E-value: 9.92e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSsGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPA 311
Cdd:cd06454     2 KVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 312 LVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVIsqgqpkthRPWKKILLIVEGLYSMEGTMANLP 391
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIAPLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 392 VIMELKKKYKFYLFVDEAHSVGAIGPHGRGVtDYFGIDPRSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYA 471
Cdd:cd06454   153 ELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFS 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 472 EAMTPPVLTQIIASMASIMGitlpaekpsspslallrssdfppviseselipgtapatalpswmplapsmvdgsdGLMRL 551
Cdd:cd06454   232 TSLPPAVAAAALAALEVLQG-------------------------------------------------------GPERR 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 552 RRIAFNARYLNRGLRKLGFITYGTDDSPVVPLLIFHPGKMAVFSRLMRTYStpIVVVVVGYPATPLVTSRVRFCLSSAHT 631
Cdd:cd06454   257 ERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALLERG--IYVQAIRYPTVPRGTARLRISLSAAHT 334

                         410
                  ....*....|....*
gi 1112949909 632 KEDIDTVLRACDEIG 646
Cdd:cd06454   335 KEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 232-647 4.93e-119

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: 360.52  E-value: 4.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSsgP-CTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIP 310
Cdd:COG0156    38 EVLNFSSNDYLGLANH--PrVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 311 ALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvisqgqpktHRPWKKILLIVEGLYSMEGTMANL 390
Cdd:COG0156   116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK---------ARAARRKLIVTDGVFSMDGDIAPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 391 PVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAY 470
Cdd:COG0156   187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDR-VDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 471 AEAMTPPVltqIIASMAsimgitlpaekpsspSLALLRSSdfppviseselipgtapatalpswmplaPSMVDgsdglmR 550
Cdd:COG0156   266 STALPPAV---AAAALA---------------ALEILREE----------------------------PELRE------R 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 551 LRRiafNARYLNRGLRKLGFITyGTDDSPVVPLLIFHPGKMAVFSRLMRT---YSTPIVvvvvgYPATPLVTSRVRFCLS 627
Cdd:COG0156   294 LWE---NIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALLErgiYVSAIR-----PPTVPKGTARLRITLS 364

                         410       420
                  ....*....|....*....|
gi 1112949909 628 SAHTKEDIDTVLRACDEIGD 647
Cdd:COG0156   365 AAHTEEDIDRLLEALAEVGK 384
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 232-641 2.09e-83

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: 2.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSSgPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPA 311
Cdd:TIGR00858  17 RLLNFSSNDYLGLASHP-EVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 312 LVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvisqgqpktHRPWKKILLIVEGLYSMEGTMANLP 391
Cdd:TIGR00858  96 LVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEK---------NRGERRKLIVTDGVFSMDGDIAPLP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 392 VIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYA 471
Cdd:TIGR00858 167 QLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFS 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 472 EAMTPPVLTQIIAsmasimgitlpaekpsspSLALLRSSdfppviseselipgtapatalpSWMPlapsmvdgsdglmrl 551
Cdd:TIGR00858 247 TALPPAVAAAALA------------------ALELIQEE----------------------PWRR--------------- 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 552 RRIAFNARYLNRGLRKLGFiTYGTDDSPVVPLLIFHPGKMAVFSRLMRtySTPIVVVVVGYPATPLVTSRVRFCLSSAHT 631
Cdd:TIGR00858 272 EKLLALIARLRAGLEALGF-TLMPSCTPIVPVIIGDNASALALAEELQ--QQGIFVGAIRPPTVPAGTSRLRLTLSAAHT 348

                         410
                  ....*....|
gi 1112949909 632 KEDIDTVLRA 641
Cdd:TIGR00858 349 PGDIDRLAEA 358
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
234-641 8.93e-42

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 155.16  E-value: 8.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 234 LNVSSYNYLGfaqssGPCTDAVETSIEkygVGAGGTRLEGGTLDLHVQTEALIARFLGM--------EDALVSSMGFATN 305
Cdd:pfam00155   4 INLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 306 -STIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFK-------HNDMKALEDLLREvisqgqpkthrpwKKILLIV 377
Cdd:pfam00155  76 iEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE-------------KPKVVLH 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 378 EGLYSMEGTMANLP---VIMELKKKYKFYLFVDEAHSVGAIGPHGRgVTDYFGIDPRSVDILMGTFTKSFGAAG---GYI 451
Cdd:pfam00155 143 TSPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrvGYI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 452 AGNKAVVDRLRIQghsgayAEAMTPPVLTQIIAsmasimgitlpaekpsspsLALLRSSDFppVISESElipgtapatal 531
Cdd:pfam00155 222 LGNAAVISQLRKL------ARPFYSSTHLQAAA-------------------AAALSDPLL--VASELE----------- 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 532 pswmplapsmvdgsdglMRLRRIAFNARYLNRGLRKLGFITYGtDDSPVVPLLIFHPGKMAVFSRLMRTYstpiVVVVVG 611
Cdd:pfam00155 264 -----------------EMRQRIKERRDYLRDGLQAAGLSVLP-SQAGFFLLTGLDPETAKELAQVLLEE----VGVYVT 321

                         410       420       430
                  ....*....|....*....|....*....|
gi 1112949909 612 YPATPLVTSRVRFCLsSAHTKEDIDTVLRA 641
Cdd:pfam00155 322 PGSSPGVPGWLRITV-AGGTEEELEELLEA 350
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 133-652 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 558.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 133 PYYILLTTYISYILVICLGHLRDFvgkrfraaqYRHLLPW------KGYAALNSDFDSFYTRRLKLRIDDCFSHPTTGVP 206
Cdd:PLN02483    5 PYLTALTTYFSYGLLFAFGQLRDF---------FRAILDWwktsnlQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 207 GRTIVLLDRYSSDYNKTMVPTGTRTRALNVSSYNYLGFAQSSGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALI 286
Cdd:PLN02483   76 DAWFDVVERVSNDNNKTLKRTTKTRRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 287 ARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQPKT 366
Cdd:PLN02483  156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 367 HRPWKKILLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGA 446
Cdd:PLN02483  236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 447 AGGYIAGNKAVVDRLRIQGHSGAYAEAMTPPVLTQIIASMASIMGitlpaekpsspslallrssdfppviseselipgta 526
Cdd:PLN02483  316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILG----------------------------------- 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 527 patalpswmplapsmVDGSD-GLMRLRRIAFNARYLNRGLRKLGFITYGTDDSPVVPLLIFHPGKMAVFSRLMrtYSTPI 605
Cdd:PLN02483  361 ---------------EDGTNrGAQKLAQIRENSNFFRSELQKMGFEVLGDNDSPVMPIMLYNPAKIPAFSREC--LKQNV 423

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1112949909 606 VVVVVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRACDEIGDVLDLK 652
Cdd:PLN02483  424 AVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIK 470
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 232-646 9.92e-152

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 443.16  E-value: 9.92e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSsGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPA 311
Cdd:cd06454     2 KVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 312 LVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVIsqgqpkthRPWKKILLIVEGLYSMEGTMANLP 391
Cdd:cd06454    81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIAPLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 392 VIMELKKKYKFYLFVDEAHSVGAIGPHGRGVtDYFGIDPRSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYA 471
Cdd:cd06454   153 ELVDLAKKYGAILFVDEAHSVGVYGPHGRGV-EEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFS 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 472 EAMTPPVLTQIIASMASIMGitlpaekpsspslallrssdfppviseselipgtapatalpswmplapsmvdgsdGLMRL 551
Cdd:cd06454   232 TSLPPAVAAAALAALEVLQG-------------------------------------------------------GPERR 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 552 RRIAFNARYLNRGLRKLGFITYGTDDSPVVPLLIFHPGKMAVFSRLMRTYStpIVVVVVGYPATPLVTSRVRFCLSSAHT 631
Cdd:cd06454   257 ERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALLERG--IYVQAIRYPTVPRGTARLRISLSAAHT 334

                         410
                  ....*....|....*
gi 1112949909 632 KEDIDTVLRACDEIG 646
Cdd:cd06454   335 KEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 232-647 4.93e-119

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: 360.52  E-value: 4.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSsgP-CTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIP 310
Cdd:COG0156    38 EVLNFSSNDYLGLANH--PrVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 311 ALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvisqgqpktHRPWKKILLIVEGLYSMEGTMANL 390
Cdd:COG0156   116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK---------ARAARRKLIVTDGVFSMDGDIAPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 391 PVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAY 470
Cdd:COG0156   187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDR-VDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 471 AEAMTPPVltqIIASMAsimgitlpaekpsspSLALLRSSdfppviseselipgtapatalpswmplaPSMVDgsdglmR 550
Cdd:COG0156   266 STALPPAV---AAAALA---------------ALEILREE----------------------------PELRE------R 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 551 LRRiafNARYLNRGLRKLGFITyGTDDSPVVPLLIFHPGKMAVFSRLMRT---YSTPIVvvvvgYPATPLVTSRVRFCLS 627
Cdd:COG0156   294 LWE---NIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALLErgiYVSAIR-----PPTVPKGTARLRITLS 364

                         410       420
                  ....*....|....*....|
gi 1112949909 628 SAHTKEDIDTVLRACDEIGD 647
Cdd:COG0156   365 AAHTEEDIDRLLEALAEVGK 384
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 232-641 2.09e-83

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: 2.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 232 RALNVSSYNYLGFAQSSgPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPA 311
Cdd:TIGR00858  17 RLLNFSSNDYLGLASHP-EVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 312 LVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvisqgqpktHRPWKKILLIVEGLYSMEGTMANLP 391
Cdd:TIGR00858  96 LVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEK---------NRGERRKLIVTDGVFSMDGDIAPLP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 392 VIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYA 471
Cdd:TIGR00858 167 QLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFS 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 472 EAMTPPVLTQIIAsmasimgitlpaekpsspSLALLRSSdfppviseselipgtapatalpSWMPlapsmvdgsdglmrl 551
Cdd:TIGR00858 247 TALPPAVAAAALA------------------ALELIQEE----------------------PWRR--------------- 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 552 RRIAFNARYLNRGLRKLGFiTYGTDDSPVVPLLIFHPGKMAVFSRLMRtySTPIVVVVVGYPATPLVTSRVRFCLSSAHT 631
Cdd:TIGR00858 272 EKLLALIARLRAGLEALGF-TLMPSCTPIVPVIIGDNASALALAEELQ--QQGIFVGAIRPPTVPAGTSRLRLTLSAAHT 348

                         410
                  ....*....|
gi 1112949909 632 KEDIDTVLRA 641
Cdd:TIGR00858 349 PGDIDRLAEA 358
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 234-651 1.52e-79

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 258.59  E-value: 1.52e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 234 LNVSSYNYLGFAqSSGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPALV 313
Cdd:PRK06939   45 INFCANNYLGLA-NHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 314 SKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQpkthrpwKKILLIVEGLYSMEGTMANLPVI 393
Cdd:PRK06939  124 GKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEI 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 394 MELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTFTKSF-GAAGGYIAGNKAVVDRLRIQghsgayae 472
Cdd:PRK06939  197 CDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDR-VDIITGTLGKALgGASGGYTAGRKEVIDWLRQR-------- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 473 amtppvltqiiasmasimgitlpaekpSSPslaLLRSSDFPPVISeselipgTAPATALpswmplapSMVDGSDGLM-RL 551
Cdd:PRK06939  268 ---------------------------SRP---YLFSNSLAPAIV-------AASIKVL--------ELLEESDELRdRL 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 552 RRiafNARYLNRGLRKLGFiTYGTDDSPVVPLLIFHPGKMAVFSRLMRT---YSTPIVvvvvgYPATPLVTSRVRFCLSS 628
Cdd:PRK06939  303 WE---NARYFREGMTAAGF-TLGPGEHPIIPVMLGDAKLAQEFADRLLEegvYVIGFS-----FPVVPKGQARIRTQMSA 373

                         410       420
                  ....*....|....*....|...
gi 1112949909 629 AHTKEDIDTVLRACDEIGDVLDL 651
Cdd:PRK06939  374 AHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 200-646 1.91e-76

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 250.08  E-value: 1.91e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 200 HPTTGVPGRTIVLLDRyssdynktmvptgtrtRALNVSSYNYLGFAQSSGpCTDAVETSIEKYGVGAGGTRLEGGTLDLH 279
Cdd:PRK05958   24 RPREGGAGRWLVVDGR----------------RMLNFASNDYLGLARHPR-LIAAAQQAARRYGAGSGGSRLVTGNSPAH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 280 VQTEALIARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvi 359
Cdd:PRK05958   87 EALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 360 sqgqpkthRPWKKILLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGT 439
Cdd:PRK05958  165 --------WRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 440 FTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYAEAMtPPVLTQiiASMAsimgitlpaekpsspSLALLRssdfppviSES 519
Cdd:PRK05958  237 LGKALGSSGAAVLGSETLIDYLINRARPFIFTTAL-PPAQAA--AARA---------------ALRILR--------REP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 520 ELIpgtapatalpswmplapsmvdgsdglMRLRRiafNARYLNRGLRKLGFiTYGTDDSPVVPLLIFHPGK-MAVFSRLM 598
Cdd:PRK05958  291 ERR--------------------------ERLAA---LIARLRAGLRALGF-QLMDSQSAIQPLIVGDNERaLALAAALQ 340

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1112949909 599 RtysTPIVVVVVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRACDEIG 646
Cdd:PRK05958  341 E---QGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 238-661 3.10e-54

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 191.22  E-value: 3.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 238 SYNYLGFAQSSGPCTDAVEtSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPALVSK-- 315
Cdd:PRK13392   53 SNDYLGMGQHPDVIGAMVD-ALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlp 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 316 GCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLrevisQGQPkTHRPwkkILLIVEGLYSMEGTMANLPVIME 395
Cdd:PRK13392  132 GCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQL-----ASVD-PDRP---KLIAFESVYSMDGDIAPIEAICD 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 396 LKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYAEAMT 475
Cdd:PRK13392  203 LADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR-IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALP 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 476 PPVLTQIIASMASImgitlpaekpsspslallrssdfppviseselipgtapatalpswmplapsMVDGSDGLMRLRRIA 555
Cdd:PRK13392  282 PAVAAGATAAIRHL---------------------------------------------------KTSQTERDAHQDRVA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 556 -FNARYLNRGLRKLgfitygTDDSPVVPLLIFHPGKM-AVFSRLMRTYStpIVVVVVGYPATPLVTSRVRFCLSSAHTKE 633
Cdd:PRK13392  311 aLKAKLNANGIPVM------PSPSHIVPVMVGDPTLCkAISDRLMSEHG--IYIQPINYPTVPRGTERLRITPTPLHDDE 382

                         410       420
                  ....*....|....*....|....*...
gi 1112949909 634 DIDTVLRACDEIGDVLDLKqasgeRWPV 661
Cdd:PRK13392  383 DIDALVAALVAIWDRLELP-----RWRE 405
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 238-651 6.88e-54

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: 190.32  E-value: 6.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 238 SYNYLGFAQSSgPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPALVSK-- 315
Cdd:TIGR01821  52 SNDYLGMGQHP-EVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIip 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 316 GCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREViSQGQPKthrpwkkiLLIVEGLYSMEGTMANLPVIME 395
Cdd:TIGR01821 131 GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV-DPNRPK--------IIAFESVYSMDGDIAPIEEICD 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 396 LKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTFTKSFGAAGGYIAGNKAVVDRLRiqghsgayaeamt 475
Cdd:TIGR01821 202 LADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHR-IDIIEGTLAKAFGVVGGYIAASRKLIDAIR------------- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 476 ppvltqiiaSMASimgitlpaekpsspslALLRSSDFPPVISeselipgtAPATAlpswmplAPSMVDGSDGLMrlRRIA 555
Cdd:TIGR01821 268 ---------SYAP----------------GFIFTTSLPPAIA--------AGATA-------SIRHLKESQDLR--RAHQ 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 556 FNARYLNRGLRKLGfITYGTDDSPVVPLLIFHPGKMAVFSR-LMRTYStpIVVVVVGYPATPLVTSRVRFCLSSAHTKED 634
Cdd:TIGR01821 306 ENVKRLKNLLEALG-IPVIPNPSHIVPVIIGDAALCKKVSDlLLNKHG--IYVQPINYPTVPRGTERLRITPTPAHTDKM 382

                         410
                  ....*....|....*..
gi 1112949909 635 IDTVLRACDEIGDVLDL 651
Cdd:TIGR01821 383 IDDLVEALLLVWDRLGL 399
PLN02822 PLN02822
serine palmitoyltransferase
 234-500 1.56e-53

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 191.49  E-value: 1.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 234 LNVSSYNYLGFAQSSGPCTDAVETsIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPALV 313
Cdd:PLN02822  112 VNFASANYLGLIGNEKIKESCTSA-LEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPAFC 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 314 SKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLrEVISQGQPKTHRPWKKIllIVEGLYSMEGTMANLPVI 393
Cdd:PLN02822  191 KKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTL-EKLTAENKRKKKLRRYI--VVEAIYQNSGQIAPLDEI 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 394 MELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGhSGAYAEA 473
Cdd:PLN02822  268 VRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSS-SGYVFSA 346

                         250       260
                  ....*....|....*....|....*..
gi 1112949909 474 MTPPVLtqiiASmASIMGITLPAEKPS 500
Cdd:PLN02822  347 SLPPYL----AS-AAITAIDVLEDNPS 368
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 234-492 1.54e-47

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 172.40  E-value: 1.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 234 LNVSSYNYLGfAQSSGPCTDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPALV 313
Cdd:PLN03227    1 LNFATHDFLS-TSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 314 SKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQP-KTHRPWKKILLIVEGLYSMEGTMANLPV 392
Cdd:PLN03227   80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVAlKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 393 IMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDP-RSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGhSGAYA 471
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSG-SGYCF 238

                         250       260
                  ....*....|....*....|.
gi 1112949909 472 EAMTPPVLTQiiASMASIMGI 492
Cdd:PLN03227  239 SASAPPFLAK--ADATATAGE 257
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
234-641 8.93e-42

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 155.16  E-value: 8.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 234 LNVSSYNYLGfaqssGPCTDAVETSIEkygVGAGGTRLEGGTLDLHVQTEALIARFLGM--------EDALVSSMGFATN 305
Cdd:pfam00155   4 INLGSNEYLG-----DTLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 306 -STIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFK-------HNDMKALEDLLREvisqgqpkthrpwKKILLIV 377
Cdd:pfam00155  76 iEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE-------------KPKVVLH 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 378 EGLYSMEGTMANLP---VIMELKKKYKFYLFVDEAHSVGAIGPHGRgVTDYFGIDPRSVDILMGTFTKSFGAAG---GYI 451
Cdd:pfam00155 143 TSPHNPTGTVATLEeleKLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrvGYI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 452 AGNKAVVDRLRIQghsgayAEAMTPPVLTQIIAsmasimgitlpaekpsspsLALLRSSDFppVISESElipgtapatal 531
Cdd:pfam00155 222 LGNAAVISQLRKL------ARPFYSSTHLQAAA-------------------AAALSDPLL--VASELE----------- 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 532 pswmplapsmvdgsdglMRLRRIAFNARYLNRGLRKLGFITYGtDDSPVVPLLIFHPGKMAVFSRLMRTYstpiVVVVVG 611
Cdd:pfam00155 264 -----------------EMRQRIKERRDYLRDGLQAAGLSVLP-SQAGFFLLTGLDPETAKELAQVLLEE----VGVYVT 321

                         410       420       430
                  ....*....|....*....|....*....|
gi 1112949909 612 YPATPLVTSRVRFCLsSAHTKEDIDTVLRA 641
Cdd:pfam00155 322 PGSSPGVPGWLRITV-AGGTEEELEELLEA 350
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 228-653 1.93e-32

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 131.34  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 228 GTRTRALNVSSYNYLGFaqSSGPC-TDAVETSIEKYGVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNS 306
Cdd:PLN02955   99 GRFKKLLLFSGNDYLGL--SSHPTiSNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANM 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 307 TIIPALVSKGCL--------------VISDELNHASIRFGVRLS----GANVRMFKHNDMKALEDLLREVisqgqpkthr 368
Cdd:PLN02955  177 AAMVAIGSVASLlaasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSC---------- 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 369 PWKKILLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPrSVDILMGTFTKSFGAAG 448
Cdd:PLN02955  247 KMKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEA-DVDLCVGTLSKAAGCHG 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 449 GYIAGNKAVVDRLRIQGHSGAYAEAMTPPVltqIIASMASImgitlpaekpsspslallrssdfppVISESELipgtapa 528
Cdd:PLN02955  326 GFIACSKKWKQLIQSRGRSFIFSTAIPVPM---AAAAYAAV-------------------------VVARKEK------- 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 529 talpsWmplapsmvdgsdglmrlRRIAFNARYlnRGLRKLGFITYGtddSPVVPLLIFHPGKMAVFSRLMrtYSTPIVVV 608
Cdd:PLN02955  371 -----W-----------------RRKAIWERV--KEFKALSGVDIS---SPIISLVVGNQEKALKASRYL--LKSGFHVM 421

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1112949909 609 VVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRAcdeIGDVLDLKQ 653
Cdd:PLN02955  422 AIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITA---LSSCLDFDN 463
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
281-660 3.17e-29

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 120.50  E-value: 3.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 281 QTEALIARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREvis 360
Cdd:PRK07179  103 QFEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER--- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 361 qgqpktHRPWkkiLLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDPRsVDILMGTF 440
Cdd:PRK07179  180 ------HGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSR-VHFITASL 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 441 TKSFGAAGGYIAGNKAVVDRLRIQghsgAYAEAMTPPVLTQIIASMASimgitlpaekpsspSLALLRSSDfppvisese 520
Cdd:PRK07179  250 AKAFAGRAGIITCPRELAEYVPFV----SYPAIFSSTLLPHEIAGLEA--------------TLEVIESAD--------- 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 521 lipgtapatalpswmplapsmvdgsdglMRLRRIAFNARYLNRGLRKLGFITYGTddSPVVPLlifHPGKMAVFSRLmRT 600
Cdd:PRK07179  303 ----------------------------DRRARLHANARFLREGLSELGYNIRSE--SQIIAL---ETGSERNTEVL-RD 348

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1112949909 601 Y--STPIVVVVVGYPATPLVTSRVRFCLSSAHTKEDIDTVLRACDEIGDVLDLkqasgERWP 660
Cdd:PRK07179  349 AleERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDL-----WFWK 405
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 240-485 1.19e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 106.40  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 240 NYLGFAQSSGpCTDAVETSIEKY-------GVGAGGTRLEGGTLDLHVQTEALIARFLGMEDALVSSMGFATNSTIIPAL 312
Cdd:PRK05937   13 DFLGFSRSDT-LVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 313 VSKGCLVISDELNHASIRFGVRLSGANVRMFKHNDMKALEDLLREVISQGQpkthrpwKKILLIVEGLYSMEGTMANLPV 392
Cdd:PRK05937   92 SSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSF-------GRIFIFVCSVYSFKGTLAPLEQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 393 IMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYFGIDprSVDILMGTFTKSFGAAGGYIAGNKAVVDRLRIQGHSGAYAE 472
Cdd:PRK05937  165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYE--NFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYST 242

                         250
                  ....*....|...
gi 1112949909 473 AMTPPVLTQIIAS 485
Cdd:PRK05937  243 GLPPHLLISIQVA 255
PRK07505 PRK07505
hypothetical protein; Provisional
 214-485 1.58e-17

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 85.42  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 214 DRYSSDYNKTMVptgtrtralNVSSYNYLGFaQSSGPCTDAVETSIEKYGV---GAGGTRLEggtLDLHVQTEALIARFL 290
Cdd:PRK07505   38 ILITLADGHTFV---------NFVSCSYLGL-DTHPAIIEGAVDALKRTGSlhlSSSRTRVR---SQILKDLEEALSELF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 291 GMEDALVSSMGfATNSTIIPALVS------KGCLVISDELNHASIRF--GVRLSGANVRMFKHNDMKALEDLlrevisqg 362
Cdd:PRK07505  105 GASVLTFTSCS-AAHLGILPLLASghltggVPPHMVFDKNAHASLNIlkGICADETEVETIDHNDLDALEDI-------- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 363 qpktHRPWKKILLIVEGLYSMeGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGPHGRG-VTDYFG--IDPRSvdILMGT 439
Cdd:PRK07505  176 ----CKTNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDyrLNERT--IIAAS 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1112949909 440 FTKSFGAAGGYIAGNKAVVDRLrIQGHSGAYA--EAMTPPVLTQIIAS 485
Cdd:PRK07505  249 LGKAFGASGGVIMLGDAEQIEL-ILRYAGPLAfsQSLNVAALGAILAS 295
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 283-449 4.45e-10

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: 58.93  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 283 EALIARFL--GMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHAS-IRFGVRLSGANVRMFKHNDMKALEDllrevi 359
Cdd:cd01494     6 EEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGL------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 360 sqgQPKTHRPWKKI----LLIVEGLYSMEGTMANLPVIMELKKKYKFYLFVDEAHSVGAIGphGRGVTDYFGidprSVDI 435
Cdd:cd01494    80 ---DVAILEELKAKpnvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASP--APGVLIPEG----GADV 150

                         170
                  ....*....|....
gi 1112949909 436 LMGTFTKSFGAAGG 449
Cdd:cd01494   151 VTFSLHKNLGGEGG 164
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 283-462 1.68e-07

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: 53.88  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 283 EALIARFLGMEDALVSSMGFATNSTIIPALVSKGCLVISDELNHASIRFG---VRLSGANVRMFKHNDMKALEDLLREVI 359
Cdd:cd06502    38 EARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDEAgapEFLSGVKLLPVPGENGKLTPEDLEAAI 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 360 SQGqPKTHRPWKKILLI-----VEGLYSMEGTMAnlpvIMELKKKYKFYLFVDEAHSVGAIGPHGRGVTDYfgidPRSVD 434
Cdd:cd06502   118 RPR-DDIHFPPPSLVSLentteGGTVYPLDELKA----ISALAKENGLPLHLDGARLANAAAALGVALKTY----KSGVD 188

                         170       180
                  ....*....|....*....|....*....
gi 1112949909 435 ILMGTFTKSFGAAGGYI-AGNKAVVDRLR 462
Cdd:cd06502   189 SVSFCLSKGGGAPVGAVvVGNRDFIARAR 217
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 393-487 1.13e-06

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: 51.19  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 393 IMELKKKYKFYLFVDEAHSvgAIGPHGRGVTDYFGIDPRSVDILMGTFTKSFGAAG---GYIAGNKAVVDRLRIQGHSGA 469
Cdd:cd00609   157 LAELAKKHGILIISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLPYT 234

                          90
                  ....*....|....*...
gi 1112949909 470 YaeaMTPPVLTQIIASMA 487
Cdd:cd00609   235 T---SGPSTLSQAAAAAA 249
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
279-410 2.61e-05

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 47.11  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 279 HVQTEALIARFLGMEDALVSSMGFAT-NSTIIPALVSKGCLVISDELNHASIRFGVRLSGAnVRMFKHNDMKAL------ 351
Cdd:pfam01276  68 IKEAQKYAARVFGADKSYFVVNGTSGsNKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGA-TPVYLEPSRNAYgiiggi 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1112949909 352 ------EDLLREVISQGQPKThrpWKKILLIVEGLYsmEGTMANLPVIMELKKKYKFYLFVDEAH 410
Cdd:pfam01276 147 plhefqEETLKEAIAEVPDAK---GPRLAVITNPTY--DGVLYNAKEIVDTLHHLSDPILFDSAW 206
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 279-418 1.93e-03

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


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 40.69  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1112949909 279 HVQTEALIARFLGMEDALVSSMGFAT-NSTIIPALVSKGCLVISDELNHASIRFGVRLSGAN---VRMFKHNDMK----- 349
Cdd:cd00615    61 IKEAQELAARAFGAKHTFFLVNGTSSsNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVpvyLKPERNPYYGiaggi 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1112949909 350 ALEDLLREVISqgqpkthRPWKKILLIVEGLYsmEGTMANLPVIMELKKKYKFYLFVDEAHsvgaiGPH 418
Cdd:cd00615   141 PPETFKKALIE-------HPDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH-----GAH 195
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 435-462 9.28e-03

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


Pssm-ID: 439849 [Multi-domain]  Cd Length: 341  Bit Score: 38.96  E-value: 9.28e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1112949909 435 ILMGTFTKSFGAAG---GYIAGNKAVVDRLR 462
Cdd:COG0079   198 VVLRTFSKAYGLAGlrlGYAIASPELIAALR 228
 
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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