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Conserved domains on  [gi|6755656|ref|NP_035609|]
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serine palmitoyltransferase 2 [Mus musculus]

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) ...
 65-540 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: 683.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    65 PMLVAVLTYVGYGVLTLFGYLRDFLRhwRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGAKV 144
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   145 DIMERKSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARF 224
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   225 LGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 304
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   305 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGG 384
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   385 YIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEDS 464
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755656   465 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 540
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 65-540 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 683.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    65 PMLVAVLTYVGYGVLTLFGYLRDFLRhwRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGAKV 144
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   145 DIMERKSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARF 224
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   225 LGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 304
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   305 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGG 384
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   385 YIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEDS 464
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755656   465 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 540
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 166-530 0e+00

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: 512.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  166 KGVINMGSYNYLGFARNtGSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIP 245
Cdd:cd06454   1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  246 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 325
Cdd:cd06454  80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  326 PEVIALKKKYKAYLYLDEAHSIGALGPSGRGvVDYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 405
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  406 ATSMSPPVMEQIITSMKCIMGqdgtslGKECIQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREML 485
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6755656  486 KRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVG 530
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 134-531 8.91e-136

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: 399.43  E-value: 8.91e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  134 RPICSVPGAKVDIMERKshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDK 213
Cdd:COG0156  22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  214 HEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 293
Cdd:COG0156  84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  294 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDpEDVDVMMG 373
Cdd:COG0156 164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  374 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDgtslgkECIQQLAENTRYFRRRLKE 453
Cdd:COG0156 234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKE 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755656  454 MGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGD 531
Cdd:COG0156 308 LGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 173-535 4.75e-56

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: 193.79  E-value: 4.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    173 SYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGK-- 250
Cdd:TIGR01821  52 SNDYLGMGQHP-EVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIip 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    251 GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRPwkKIlILVEGIYSMEGSIVRLPEVIA 330
Cdd:TIGR01821 131 GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP--KI-IAFESVYSMDGDIAPIEEICD 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    331 LKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLdPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSMS 410
Cdd:TIGR01821 202 LADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLP 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    411 PPVMEQIITSMKCIMGQDgtslgKECIQQlAENTRYFRRRLKEMGFIIYGNeDSPVVPLMLYMPAKIGAFGrEMLKRNIG 490
Cdd:TIGR01821 281 PAIAAGATASIRHLKESQ-----DLRRAH-QENVKRLKNLLEALGIPVIPN-PSHIVPVIIGDAALCKKVS-DLLLNKHG 352

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 6755656    491 VVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 535
Cdd:TIGR01821 353 IYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
166-526 3.00e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    166 KGVINMGSYNYLGFarntgsCQEAAAEVLKEYGAGvcSTRQEIGNLDKHEELEKLVARFLG--------VEAAMTYGMGF 237
Cdd:pfam00155   1 TDKINLGSNEYLGD------TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    238 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 309
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    310 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPSGRgVVDYFGLDPEDVDVMMGTFTKSFGASG--- 383
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    384 GYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSmkcimgQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEd 463
Cdd:pfam00155 219 GYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDP------LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755656    464 SPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIIESRARFCLsAAHTKEILDTALKEI 526
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 65-540 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 683.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    65 PMLVAVLTYVGYGVLTLFGYLRDFLRhwRIEKCHHATEreeQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGAKV 144
Cdd:PLN02483   5 PYLTALTTYFSYGLLFAFGQLRDFFR--AILDWWKTSN---LQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDAWF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   145 DIMERKSHDYNWSFKYTGNIIKgVINMGSYNYLGFARNTGSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARF 224
Cdd:PLN02483  80 DVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   225 LGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRP 304
Cdd:PLN02483 159 VGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTHRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   305 WKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGG 384
Cdd:PLN02483 239 WKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSCGG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   385 YIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEDS 464
Cdd:PLN02483 319 YIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDNDS 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755656   465 PVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRH 540
Cdd:PLN02483 399 PVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 166-530 0e+00

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: 512.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  166 KGVINMGSYNYLGFARNtGSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIP 245
Cdd:cd06454   1 KKVLNFCSNDYLGLANH-PEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  246 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqprtRRPWKKILILVEGIYSMEGSIVRL 325
Cdd:cd06454  80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  326 PEVIALKKKYKAYLYLDEAHSIGALGPSGRGvVDYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 405
Cdd:cd06454 152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRG-VEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  406 ATSMSPPVMEQIITSMKCIMGqdgtslGKECIQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREML 485
Cdd:cd06454 231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 6755656  486 KRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVG 530
Cdd:cd06454 305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 134-531 8.91e-136

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: 399.43  E-value: 8.91e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  134 RPICSVPGAKVDIMERKshdynwsfkytgniikgVINMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDK 213
Cdd:COG0156  22 RVLESPQGPRVTIDGRE-----------------VLNFSSNDYLGLANHP-RVIEAAAEALDRYGTGSGGSRLVSGTTPL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  214 HEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDA 293
Cdd:COG0156  84 HEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  294 ivygqprtrRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDpEDVDVMMG 373
Cdd:COG0156 164 ---------RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  374 TFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDgtslgkECIQQLAENTRYFRRRLKE 453
Cdd:COG0156 234 TLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKE 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755656  454 MGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGD 531
Cdd:COG0156 308 LGFDL-GPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 113-535 1.77e-98

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 304.43  E-value: 1.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   113 YQDFENFYTRNLyMRIRDN--WN--RPICSVPGAKVDIMERKShdynwsfkytgniikgVINMGSYNYLGFArNTGSCQE 188
Cdd:PRK06939   2 SGAFYAQLREEL-EEIKAEglYKeeRVITSPQGADITVADGKE----------------VINFCANNYLGLA-NHPELIA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   189 AAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGA 268
Cdd:PRK06939  64 AAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   269 RLSGATIRIFKHNNMQSLEKLLKDAIVYGQprtrrpwKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIG 348
Cdd:PRK06939 144 RLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   349 ALGPSGRGVVDYFGLDpEDVDVMMGTFTKSF-GASGGYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKciMGQ 427
Cdd:PRK06939 217 FVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLE--LLE 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   428 DGTSLgkecIQQLAENTRYFRRRLKEMGFIIyGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRAR 507
Cdd:PRK06939 294 ESDEL----RDRLWENARYFREGMTAAGFTL-GPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIR 368

                        410       420
                 ....*....|....*....|....*...
gi 6755656   508 FCLSAAHTKEILDTALKEIDEVGDLLQL 535
Cdd:PRK06939 369 TQMSAAHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 166-530 7.53e-94

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 292.06  E-value: 7.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   166 KGVINMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIP 245
Cdd:PRK05958  39 RRMLNFASNDYLGLARHP-RLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   246 ALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdaivygQPRTRRPWkkilILVEGIYSMEGSIVRL 325
Cdd:PRK05958 118 ALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAPL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   326 PEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVY 405
Cdd:PRK05958 188 AELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIF 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   406 ATSMSPPVMEQIITSMKCIMGQDgtslgkECIQQLAENTRYFRRRLKEMGFIIyGNEDSPVVPLMLYMPAKIGAFGREML 485
Cdd:PRK05958 268 TTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALALAAALQ 340

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 6755656   486 KRniGVVVVGF--PATPIIESRARFCLSAAHTKEILDTALKEIDEVG 530
Cdd:PRK05958 341 EQ--GFWVGAIrpPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
PLN02822 PLN02822
serine palmitoyltransferase
 164-519 1.23e-59

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 205.36  E-value: 1.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   164 IIKG--VINMGSYNYLGFA---RNTGSCQEAaaevLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFA 238
Cdd:PLN02822 105 IINGkdVVNFASANYLGLIgneKIKESCTSA----LEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   239 TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaIVYGQPRTRRPWKkiLILVEGIYSM 318
Cdd:PLN02822 181 TIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEK-LTAENKRKKKLRR--YIVVEAIYQN 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   319 EGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRT 398
Cdd:PLN02822 258 SGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRL 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   399 HSHSAVYATSMSPPVMEQIITSMKcIMGQDGTSLGKeciqqLAENTRYFRRRLKEM-GFIIYGNEDSPVVPLMLYMP--- 474
Cdd:PLN02822 338 SSSGYVFSASLPPYLASAAITAID-VLEDNPSVLAK-----LKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKStgs 411

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6755656   475 -----AKIGAFGREMLKRNiGVVVVGFPATPIIESRA----RFCLSAAHT-KEIL 519
Cdd:PLN02822 412 akedlSLLEHIADRMLKED-SVLVVVSKRSTLDKCRLpvgiRLFVSAGHTeSDIL 465
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 173-535 4.75e-56

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: 193.79  E-value: 4.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    173 SYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGK-- 250
Cdd:TIGR01821  52 SNDYLGMGQHP-EVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIip 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    251 GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAivygqpRTRRPwkKIlILVEGIYSMEGSIVRLPEVIA 330
Cdd:TIGR01821 131 GCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSV------DPNRP--KI-IAFESVYSMDGDIAPIEEICD 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    331 LKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLdPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSMS 410
Cdd:TIGR01821 202 LADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLP 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    411 PPVMEQIITSMKCIMGQDgtslgKECIQQlAENTRYFRRRLKEMGFIIYGNeDSPVVPLMLYMPAKIGAFGrEMLKRNIG 490
Cdd:TIGR01821 281 PAIAAGATASIRHLKESQ-----DLRRAH-QENVKRLKNLLEALGIPVIPN-PSHIVPVIIGDAALCKKVS-DLLLNKHG 352

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 6755656    491 VVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 535
Cdd:TIGR01821 353 IYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 147-535 4.71e-55

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 191.22  E-value: 4.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   147 MERKSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLG 226
Cdd:PRK13392  27 LEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMGQHP-DVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   227 VEAAMTYGMGFATNSMNIPALVGK--GCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKdAIVYGQPRtrrp 304
Cdd:PRK13392 106 KESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLA-SVDPDRPK---- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   305 wkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLdPEDVDVMMGTFTKSFGASGG 384
Cdd:PRK13392 181 ----LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGG 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   385 YIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSMKCiMGQDGTSLgkeciQQLAENTRYFRRRLKEMGFIIYGNeDS 464
Cdd:PRK13392 256 YIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRH-LKTSQTER-----DAHQDRVAALKAKLNANGIPVMPS-PS 328

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755656   465 PVVPLMLYMPAKIGAFGrEMLKRNIGVVV--VGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQL 535
Cdd:PRK13392 329 HIVPVMVGDPTLCKAIS-DRLMSEHGIYIqpINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLEL 400
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 169-537 8.41e-54

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 187.42  E-value: 8.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   169 INMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALV 248
Cdd:PLN03227   1 LNFATHDFLSTSSSP-TLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   249 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLL-----KDAIVYGQPRTRRPWkkilILVEGIYSMEGSIV 323
Cdd:PLN03227  80 KRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   324 RLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDP-EDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHS 402
Cdd:PLN03227 156 PLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   403 AVYATSmSPPVMEQIitSMKCIMGQDGtslGKECIQQLAENTRYFRRRLK----------EMGFIIYGNEDSPVVPLMLY 472
Cdd:PLN03227 236 YCFSAS-APPFLAKA--DATATAGELA---GPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLRLS 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   473 MPAKIGAF---------GREMLKRNIGVVVVGfpATPIIESRA------RFCLSAAHTKEILDTALKEIDEVGDLLQLKY 537
Cdd:PLN03227 310 DQEATRRTdetlildqiAHHSLSEGVAVVSTG--GHVKKFLQLvpppclRVVANASHTREDIDKLLTVLGEAVEAILCKI 387
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
166-526 3.00e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.24  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    166 KGVINMGSYNYLGFarntgsCQEAAAEVLKEYGAGvcSTRQEIGNLDKHEELEKLVARFLG--------VEAAMTYGMGF 237
Cdd:pfam00155   1 TDKINLGSNEYLGD------TLPAVAKAEKDALAG--GTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    238 ATNSMNIPALVG-KGCLILSDELNHASLVLGARLSGATIRIFK-------HNNMQSLEKLLKDAIVygqprtrrpwkkiL 309
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    310 ILVEGIYSMEGSIVRLPE---VIALKKKYKAYLYLDEAHSIGALGPSGRgVVDYFGLDPEDVDVMMGTFTKSFGASG--- 383
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    384 GYIGGKKELIDYLRTHSHSAVYATSMSPPVMEQIITSmkcimgQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIYGNEd 463
Cdd:pfam00155 219 GYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDP------LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755656    464 SPVVPLMLYMPAKIGAFGREMLKRnIGVVVVGFpATPIIESRARFCLsAAHTKEILDTALKEI 526
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEE-VGVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
169-532 1.73e-36

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 140.53  E-value: 1.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   169 INMGSYNYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALV 248
Cdd:PRK07179  57 IILQSNDYLNLSGHP-DIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   249 GKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDaivYGQPrtrrpwkkiLILVEGIYSMEGSIVRLPEV 328
Cdd:PRK07179 136 DPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPG---------IIVVDSVYSTTGTIAPLADI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   329 IALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATS 408
Cdd:PRK07179 204 VDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSST 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   409 MSPPVMEQIITSMKCIMGQDgtslgkECIQQLAENTRYFRRRLKEMGFIIYGNedSPVVPLMLYMPAKIGAFGREMLKRN 488
Cdd:PRK07179 283 LLPHEIAGLEATLEVIESAD------DRRARLHANARFLREGLSELGYNIRSE--SQIIALETGSERNTEVLRDALEERN 354

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 6755656   489 IGVVVVGFPATPIIESRARFCLSAAHTKEILD---TALKEIDEVGDL 532
Cdd:PRK07179 355 VFGAVFCAPATPKNRNLIRLSLNADLTASDLDrvlEVCREARDEVDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 175-517 2.24e-30

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 124.02  E-value: 2.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   175 NYLGFARNTgSCQEAAAEVLKEYGAGVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGKGCL- 253
Cdd:PLN02955 111 DYLGLSSHP-TISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIGSVASLl 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   254 -------------ILSDELNHASLVLGARLS----GATIRIFKHNNMQSLEKLLKDAIVygqprtrrpwKKILILVEGIY 316
Cdd:PLN02955 190 aasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KRKVVVTDSLF 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   317 SMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLDpEDVDVMMGTFTKSFGASGGYIGGKKELIDYL 396
Cdd:PLN02955 260 SMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   397 RTHSHSAVYATSMSPPVMEQIITSMkcIMGQdgtslgKECIQQLAENTRYfrRRLKEMGFIIYGnedSPVVPLMLYMPAK 476
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMAAAAYAAV--VVAR------KEKWRRKAIWERV--KEFKALSGVDIS---SPIISLVVGNQEK 405

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 6755656   477 IGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKE 517
Cdd:PLN02955 406 ALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 168-411 6.04e-25

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 106.40  E-value: 6.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   168 VINMGSYNYLGFARNTGscqeAAAEVLKEYGA----------GVCSTRQEIGNLDKHEELEKLVARFLGVEAAMTYGMGF 237
Cdd:PRK05937   6 SIDFVTNDFLGFSRSDT----LVHEVEKRYRLycrqfphaqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   238 ATNsMNIPALVGKGC-LILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLkdaivygQPRTRRPWKKILILVEGIY 316
Cdd:PRK05937  82 MAN-LGLCAHLSSVTdYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL-------ESCRQRSFGRIFIFVCSVY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   317 SMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVVDYFGLdpEDVDVMMGTFTKSFGASGGYIGGKKELIDYL 396
Cdd:PRK05937 154 SFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY--ENFYAVLVTYSKALGSMGAALLSSSEVKQDL 231

                        250
                 ....*....|....*
gi 6755656   397 RTHSHSAVYATSMSP 411
Cdd:PRK05937 232 MLNSPPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 168-526 4.72e-21

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 95.43  E-value: 4.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   168 VINMGSYNYLGFaRNTGSCQEAAAEVLKEYGA-GVCSTRQEIgNLDKHEELEKLVARFLGVEAAmTYGMGFATNSMNIPa 246
Cdd:PRK07505  48 FVNFVSCSYLGL-DTHPAIIEGAVDALKRTGSlHLSSSRTRV-RSQILKDLEEALSELFGASVL-TFTSCSAAHLGILP- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   247 LVGKGCL-------ILSDELNHASL-VLGARLS--GATIRIfKHNNMQSLEKLLKdaivygqpRTRRPwkkiLILVEGIY 316
Cdd:PRK07505 124 LLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDALEDICK--------TNKTV----AYVADGVY 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   317 SMeGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPSGRGVV--DYFGLDPEDVdVMMGTFTKSFGASGGYIG-GKKELI 393
Cdd:PRK07505 191 SM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERT-IIAASLGKAFGASGGVIMlGDAEQI 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656   394 DYLRTHSHSAVYATSMSPPVMEQIITSMKCIMGQDGTSLGkeciQQLAENTRYF--------RRRLKEMGFIIYGNEDSP 465
Cdd:PRK07505 269 ELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQ----QKLQNNIALFdslipteqSGSFLPIRLIYIGDEDTA 344

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755656   466 VvplmlympakigAFGREMLKRNIGVVVVGFPATPiiESRA--RFCLSAAHTKEILDT---ALKEI 526
Cdd:PRK07505 345 I------------KAAKQLLDRGFYTSPVFFPVVA--KGRAglRIMFRASHTNDEIKRlcsLLKEI 396
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 213-389 8.96e-13

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: 66.64  E-value: 8.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  213 KHEELEKLVARFL--GVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHAS-LVLGARLSGATIRIFKHNNmqslekl 289
Cdd:cd01494   1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDD------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  290 LKDAIVYGQPRTRRPWKKI--LILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGAlgpsgRGVVDYFGLDpED 367
Cdd:cd01494  74 AGYGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGA-----SPAPGVLIPE-GG 147

                       170       180
                ....*....|....*....|...
gi 6755656  368 VDVMMGTFTKSFGASG-GYIGGK 389
Cdd:cd01494 148 ADVVTFSLHKNLGGEGgGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 268-528 1.20e-09

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 60.05  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  268 ARLSGATIRIF--KHNNMQSLEKLLKDAIVygQPRTrrpwkKILILV-----EG-IYSMEgsivRLPEVIALKKKYKAYL 339
Cdd:cd00609 100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  340 YLDEAHSigALGPSGRGVVDYFGLDPEDVDVMMGTFTKSFGASG---GY-IGGKKELIDYLRTHSHsavYATSMSPPVME 415
Cdd:cd00609 169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLLP---YTTSGPSTLSQ 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  416 QIITSMKcimgQDGTSLGKECIQQLAENTRYFRRRLKEMGFIIygnedsPVVP-----LMLYMPAKIGA-FGREMLKRNI 489
Cdd:cd00609 244 AAAAAAL----DDGEEHLEELRERYRRRRDALLEALKELGPLV------VVKPsggffLWLDLPEGDDEeFLERLLLEAG 313

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6755656  490 GVVVVGFPATPIIESRARFCLsaAHTKEILDTALKEIDE 528
Cdd:cd00609 314 VVVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 215-529 1.34e-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: 50.41  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  215 EELEKLVARFLGVEAAMTYGMGFATNSMNIPALVGKGCLILSDELNHASLV-LGA--RLSGATIRIFKHNNMQSLEKLLK 291
Cdd:cd06502  35 AKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENGKLTPEDLE 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  292 DAIVYGQ----PRTRrpwkkiLILVEGiySMEGSIVRLPEVI----ALKKKYKAYLYLDEAHSIGALGPSGRGVVDYfgl 363
Cdd:cd06502 115 AAIRPRDdihfPPPS------LVSLEN--TTEGGTVYPLDELkaisALAKENGLPLHLDGARLANAAAALGVALKTY--- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  364 dPEDVDVMMGTFTKSFGASGGYI-GGKKELI---DYLRTHSHsavyatsmsppvmeQIITSMKCIMGQDGTSLGKECIQQ 439
Cdd:cd06502 184 -KSGVDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQAG--------------GGMRQSGFLAAAGLAALENDLWLR 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  440 LAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEIL 519
Cdd:cd06502 249 RLRHDHEMARRLAEALEELGGLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEEDV 328

                       330
                ....*....|
gi 6755656  520 DTALKEIDEV 529
Cdd:cd06502 329 DELLSALKAV 338
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
197-529 1.45e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.52  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  197 YGAGVCSTRQEignlDKHEELEKLVARFLGV----EAAMTYGmgfATNSMNIPA----LVGKGCLILSDELNHASLVLG- 267
Cdd:COG0520  48 RGAHELSAEAT----DAYEAAREKVARFIGAaspdEIIFTRG---TTEAINLVAyglgRLKPGDEILITEMEHHSNIVPw 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  268 ---ARLSGATIRIFKHN-----NMQSLEKLLKdaivygqPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYL 339
Cdd:COG0520 121 qelAERTGAEVRVIPLDedgelDLEALEALLT-------PRTK------LVAVTHVSNVTGTVNPVKEIAALAHAHGALV 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  340 YLDEAHSIGALgpsgrgVVDyfgLDPEDVDVMMGTFTKSFGASGgyIG---GKKELIDYLR-----------THSHSAVY 405
Cdd:COG0520 188 LVDGAQSVPHL------PVD---VQALGCDFYAFSGHKLYGPTG--IGvlyGKRELLEALPpflggggmiewVSFDGTTY 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  406 A---------TsmsPPVMEQI--ITSMKCIMgqdgtSLGKECIQQ-LAENTRYFRRRLKEM-GFIIYGNED----SPVVP 468
Cdd:COG0520 257 AdlprrfeagT---PNIAGAIglGAAIDYLE-----AIGMEAIEArERELTAYALEGLAAIpGVRILGPADpedrSGIVS 328

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755656  469 LML--YMPAKIGAFgreMLKRNIGVVVVGFPATPI-----IESRARFCLSAAHTKEILDTALKEIDEV 529
Cdd:COG0520 329 FNVdgVHPHDVAAL---LDDEGIAVRAGHHCAQPLmrrlgVPGTVRASFHLYNTEEEIDRLVEALKKL 393
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
199-445 1.79e-05

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 47.11  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    199 AGVCSTRQEIGNLDKHE----ELEKLVARFLGveAAMTYGMGFATNSMN---IPALVGKGCLILSDELNHASLVLGARLS 271
Cdd:pfam01276  49 IDVCIEDVELGDLLDHEgaikEAQKYAARVFG--ADKSYFVVNGTSGSNktvGMAVCTPGDTILIDRNCHKSIHHALMLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    272 GAT------------------IRIFKHnnmQSLEKLLKDAivygqPRTRrpWKKILILVEGIYsmEGSIVRLPEVIALKK 333
Cdd:pfam01276 127 GATpvylepsrnaygiiggipLHEFQE---ETLKEAIAEV-----PDAK--GPRLAVITNPTY--DGVLYNAKEIVDTLH 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    334 KYKAYLYLDEAHS---------IGALGPSGRGVVDYFGLDPEDVDVMMGTFTKS--FGASGGYIGGKKELIDYLRTHShs 402
Cdd:pfam01276 195 HLSDPILFDSAWVgyeqfipiyADASPMGGENENGPGIFVTQSVHKLLAALSQAsyIHKKEGHIVNHDRFNEAFMMHA-- 272

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 6755656    403 avyATSMSPPVMEQIITSMKCIMGQDGTSLGKECIqQLAENTR 445
Cdd:pfam01276 273 ---TTSPSYPIFASLDVAAKMLEGNSGRRLWNECV-ERAIEFR 311
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 212-358 3.90e-05

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: 46.09  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    212 DKHEELEKLVARFLGVEAA----MTYGmgfATNSMNI------PALVGKGCLILSDELNHASLVLGARLS---GATIRIF 278
Cdd:pfam00266  43 QAYEEAREKVAEFINAPSNdeiiFTSG---TTEAINLvalslgRSLKPGDEIVITEMEHHANLVPWQELAkrtGARVRVL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656    279 KHNNMQSLE-KLLKDAIvygQPRTRrpwkkiLILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGA-------- 349
Cdd:pfam00266 120 PLDEDGLLDlDELEKLI---TPKTK------LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHrpidvqkl 190

                         170       180
                  ....*....|....*....|.
gi 6755656    350 ------------LGPSGRGVV 358
Cdd:pfam00266 191 gvdflafsghklYGPTGIGVL 211
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 207-453 9.36e-04

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


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 41.47  E-value: 9.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  207 EIGNLDKHE----ELEKLVARFLGVEAA--MTYGMGFATNSMnIPALVGKGCLILSDELNHASLVLGARLSGAT------ 274
Cdd:cd00615  50 GLDDLLDPTgpikEAQELAARAFGAKHTffLVNGTSSSNKAV-ILAVCGPGDKILIDRNCHKSVINGLVLSGAVpvylkp 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  275 -----IRIFKHNNMQSLEKLLKDAivygqprtrrPWKKILILVEGIYsmEGSIVRLPEVIALKKKYKAYLYLDEAHsiGA 349
Cdd:cd00615 129 ernpyYGIAGGIPPETFKKALIEH----------PDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH--GA 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755656  350 lgpsgrgvvdYFGLDPE----------DVDV-----MMGTFTKsfgasGGYIGGKKELID------YLRTHshsavyaTS 408
Cdd:cd00615 195 ----------HFRFHPIlpssaamagaDIVVqsthkTLPALTQ-----GSMIHVKGDLVNpdrvneALNLH-------QS 252

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6755656  409 MSPPVmeQIITSMKCIMGQDGTSlGKECIQQLAENTRYFRRRLKE 453
Cdd:cd00615 253 TSPSY--LILASLDVARAMMALE-GKELVEELIELALYARQEINK 294
 
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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