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Conserved domains on  [gi|119220554|ref|NP_060797|]
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serine palmitoyltransferase 3 [Homo sapiens]

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) ...
 57-549 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: 638.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  57 EAPLHVMVFTYMGYGIGTLFGYLRDFLRNwgIEKCnaaVERKEQKDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGP 136
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 137 LFDLMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483  78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483 157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAS 376
Cdd:PLN02483 237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483 317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 457 NASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483 397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                        490
                 ....*....|...
gi 119220554 537 SARPELYDETSFE 549
Cdd:PLN02483 477 KKQEQVKKFIKLE 489
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 57-549 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 638.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  57 EAPLHVMVFTYMGYGIGTLFGYLRDFLRNwgIEKCnaaVERKEQKDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGP 136
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 137 LFDLMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483  78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483 157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAS 376
Cdd:PLN02483 237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483 317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 457 NASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483 397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                        490
                 ....*....|...
gi 119220554 537 SARPELYDETSFE 549
Cdd:PLN02483 477 KKQEQVKKFIKLE 489
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 160-524 2.19e-167

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: 478.21  E-value: 2.19e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:cd06454    1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHL 319
Cdd:cd06454   80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 400 ASSMSPPIAEQIIRSLKLIMGldgttqGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHML 479
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 119220554 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMG 524
Cdd:cd06454  305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 160-525 3.50e-131

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: 387.48  E-value: 3.50e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAKyDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:COG0156   37 REVLNFSSNDYLGLANH-PRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHL 319
Cdd:COG0156  116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:COG0156  187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 400 ASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHML 479
Cdd:COG0156  266 STALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDLGPSESP-IVPVIVGDAERALALADALL 338

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 119220554 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGD 525
Cdd:COG0156  339 ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 138-529 1.60e-65

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: 218.44  E-value: 1.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  138 FDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAK 217
Cdd:TIGR01821  23 FADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMG-QHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  218 FLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdAVIYGQPRt 295
Cdd:TIGR01821 102 LHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ-SVDPNRPK- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  296 rrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLdPHEVDVLMGTFTKSFGA 375
Cdd:TIGR01821 180 -------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  376 SGGYIAGRKDLVDYLRVHSHSAVYASSMSPPI---AEQIIRSLKlimgldgTTQGLQRVQQlaKNTRYFRQRLQEMGFII 452
Cdd:TIGR01821 252 VGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIaagATASIRHLK-------ESQDLRRAHQ--ENVKRLKNLLEALGIPV 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119220554  453 YGNEnASVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:TIGR01821 323 IPNP-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 2.22e-50

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 176.73  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  160 KDVINMGSYNFLGLAAKydESMRTIKDVLEvygtgvASTRHEMGTLDKHKELEDLVAKF--------LNVEAAMVFGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP--AVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  232 ATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK-------HNNTQSLEKLLRDAVIygqprtrrawkkiL 303
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  304 ILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGASG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  378 GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIRSLKLIMGldgttQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNEN 457
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS-----ELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA 292

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119220554  458 AsVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARARFCVsAAHTREMLDTVLEAL 520
Cdd:pfam00155 293 G-FFLLTGLDPETAKELAQVLLEEV-GVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 57-549 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 638.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  57 EAPLHVMVFTYMGYGIGTLFGYLRDFLRNwgIEKCnaaVERKEQKDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGP 136
Cdd:PLN02483   3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 137 LFDLMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483  78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483 157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAS 376
Cdd:PLN02483 237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483 317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 457 NASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483 397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                        490
                 ....*....|...
gi 119220554 537 SARPELYDETSFE 549
Cdd:PLN02483 477 KKQEQVKKFIKLE 489
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 160-524 2.19e-167

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: 478.21  E-value: 2.19e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:cd06454    1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHL 319
Cdd:cd06454   80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:cd06454  152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 400 ASSMSPPIAEQIIRSLKLIMGldgttqGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHML 479
Cdd:cd06454  231 STSLPPAVAAAALAALEVLQG------GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 119220554 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMG 524
Cdd:cd06454  305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 160-525 3.50e-131

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: 387.48  E-value: 3.50e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAKyDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:COG0156   37 REVLNFSSNDYLGLANH-PRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHL 319
Cdd:COG0156  116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:COG0156  187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 400 ASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHML 479
Cdd:COG0156  266 STALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDLGPSESP-IVPVIVGDAERALALADALL 338

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 119220554 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGD 525
Cdd:COG0156  339 ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 160-529 1.57e-97

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 301.73  E-value: 1.57e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAkYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PRK06939  42 KEVINFCANNYLGLAN-HPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQprtrrawKKILILVEGVYSMEGSIVHL 319
Cdd:PRK06939 121 TLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPL 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSF-GASGGYIAGRKDLVDYLRVHSHSAV 398
Cdd:PRK06939 194 PEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 399 YASSMSPPIAEQIIRSLKLIMgldgttQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHM 478
Cdd:PRK06939 273 FSNSLAPAIVAASIKVLELLE------ESDELRDRLWENARYFREGMTAAGFTLGPGEHP-IIPVMLGDAKLAQEFADRL 345

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119220554 479 LEKkiGVVVVGF--PATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:PRK06939 346 LEE--GVYVIGFsfPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 160-524 1.98e-93

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 290.52  E-value: 1.98e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAkyDESMRT-IKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNI 238
Cdd:PRK05958  39 RRMLNFASNDYLGLAR--HPRLIAaAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 239 PALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdaviygQPRTRRAWkkilILVEGVYSMEGSIVH 318
Cdd:PRK05958 117 TALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAP 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 319 LPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAV 398
Cdd:PRK05958 187 LAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFI 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 399 YASSMSPPIAEQIIRSLKLIMGLDgttqglQRVQQLAKNTRYFRQRLQEMGFIIYGNENAsVVPLLLYMPGKVAAFARHM 478
Cdd:PRK05958 267 FTTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQLMDSQSA-IQPLIVGDNERALALAAAL 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 119220554 479 LEKkiGVVVVGF--PATPLAEARARFCVSAAHTREMLDTVLEALDEMG 524
Cdd:PRK05958 340 QEQ--GFWVGAIrpPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 138-529 1.60e-65

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: 218.44  E-value: 1.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  138 FDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAK 217
Cdd:TIGR01821  23 FADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMG-QHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  218 FLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdAVIYGQPRt 295
Cdd:TIGR01821 102 LHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ-SVDPNRPK- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  296 rrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLdPHEVDVLMGTFTKSFGA 375
Cdd:TIGR01821 180 -------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  376 SGGYIAGRKDLVDYLRVHSHSAVYASSMSPPI---AEQIIRSLKlimgldgTTQGLQRVQQlaKNTRYFRQRLQEMGFII 452
Cdd:TIGR01821 252 VGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIaagATASIRHLK-------ESQDLRRAHQ--ENVKRLKNLLEALGIPV 322

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119220554  453 YGNEnASVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:TIGR01821 323 IPNP-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 109-529 2.81e-59

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 202.39  E-value: 2.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 109 DFENFYTRNLYMRIRDNWNRpicsapgpLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVL 188
Cdd:PRK13392   3 NYDSYFDAALAQLHQEGRYR--------VFADLEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMG-QHPDVIGAMVDAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 189 EVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSG 266
Cdd:PRK13392  74 DRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 267 ATIRIFKHNNTQSLEKLLRdAVIYGQPRtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGP 346
Cdd:PRK13392 154 AEKQVFRHNDLADLEEQLA-SVDPDRPK--------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 347 TGRGVTEFFGLdPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQI---IRSLKlimgldg 423
Cdd:PRK13392 225 RGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGAtaaIRHLK------- 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 424 tTQGLQRvQQLAKNTRYFRQRLQEMGFIIYGNEnASVVPLLLYMPGKVAAFA-RHMLEKKIGVVVVGFPATPLAEARARF 502
Cdd:PRK13392 297 -TSQTER-DAHQDRVAALKAKLNANGIPVMPSP-SHIVPVMVGDPTLCKAISdRLMSEHGIYIQPINYPTVPRGTERLRI 373

                        410       420
                 ....*....|....*....|....*..
gi 119220554 503 CVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:PRK13392 374 TPTPLHDDEDIDALVAALVAIWDRLEL 400
PLN02822 PLN02822
serine palmitoyltransferase
 160-520 1.87e-55

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 193.80  E-value: 1.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAkYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PLN02822 109 KDVVNFASANYLGLIG-NEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLrDAVIYGQPRTRRAWKkiLILVEGVYSMEGSIVHL 319
Cdd:PLN02822 188 AFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTL-EKLTAENKRKKKLRR--YIVVEAIYQNSGQIAPL 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:PLN02822 265 DEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVF 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 400 ASSMSPPIAEQIIRSLKLimgLDGTTQGLQRvqqLAKNTRYFRQRLQEM-GFIIYGNENASVVPLLLYMPGKVA------ 472
Cdd:PLN02822 345 SASLPPYLASAAITAIDV---LEDNPSVLAK---LKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKSTGSAkedlsl 418

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119220554 473 --AFARHMLeKKIGVVVVGFPATPLAEARA----RFCVSAAHTREMLDTVLEAL 520
Cdd:PLN02822 419 leHIADRML-KEDSVLVVVSKRSTLDKCRLpvgiRLFVSAGHTESDILKASESL 471
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 163-536 3.46e-52

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 182.80  E-value: 3.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 163 INMGSYNFLGLAAkyDESMR-TIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPAL 241
Cdd:PLN03227   1 LNFATHDFLSTSS--SPTLRqTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 242 VGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLL-----RDAVIYGQPRTRRAWkkilILVEGVYSMEGSI 316
Cdd:PLN03227  79 AKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 317 VHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDP-HEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSH 395
Cdd:PLN03227 155 APLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 396 SAVYASSMSPPIAEQIIRSlklimgLDGTTQGLQRVQQLAKNTRYFRQRLQ----------EMGFIIYGNENASVVPLLL 465
Cdd:PLN03227 235 GYCFSASAPPFLAKADATA------TAGELAGPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLRL 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 466 Y-MPGK--------VAAFARHMLEKKIGVVVVGFPATPLAEARA----RFCVSAAHTREMLDTVLEALDEMGDLLQLKYS 532
Cdd:PLN03227 309 SdQEATrrtdetliLDQIAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGEAVEAILCKII 388


                 ....
gi 119220554 533 RHKK 536
Cdd:PLN03227 389 DENK 392
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 2.22e-50

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 176.73  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  160 KDVINMGSYNFLGLAAKydESMRTIKDVLEvygtgvASTRHEMGTLDKHKELEDLVAKF--------LNVEAAMVFGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP--AVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  232 ATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK-------HNNTQSLEKLLRDAVIygqprtrrawkkiL 303
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  304 ILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGASG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  378 GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIRSLKLIMGldgttQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNEN 457
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSDPLLVAS-----ELEEMRQRIKERRDYLRDGLQAAGLSVLPSQA 292

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119220554  458 AsVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARARFCVsAAHTREMLDTVLEAL 520
Cdd:pfam00155 293 G-FFLLTGLDPETAKELAQVLLEEV-GVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
211-529 2.48e-36

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 139.76  E-value: 2.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 211 LEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDaviY 290
Cdd:PRK07179 104 FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---H 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 291 GQPrtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFT 370
Cdd:PRK07179 181 GPG---------IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLA 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 371 KSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPpiaeqiirslKLIMGLDGTT----QGLQRVQQLAKNTRYFRQRLQ 446
Cdd:PRK07179 251 KAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLP----------HEIAGLEATLevieSADDRRARLHANARFLREGLS 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 447 EMGFIIYGNENasVVPLllyMPGKVAA--FARHMLEKK--IGVVVVGfPATPLAEARARFCVSAAHTREMLDTVLEALDE 522
Cdd:PRK07179 321 ELGYNIRSESQ--IIAL---ETGSERNteVLRDALEERnvFGAVFCA-PATPKNRNLIRLSLNADLTASDLDRVLEVCRE 394


                 ....*..
gi 119220554 523 MGDLLQL 529
Cdd:PRK07179 395 ARDEVDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 160-530 4.55e-26

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 111.31  E-value: 4.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 160 KDVINMGSYNFLGLAAKYDESMRTIKDVLEvYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKE-YGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMV 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 240 ALVGKGCL--------------ILSDELNHTSLVLGARLS----GATIRIFKHNNTQSLEKLLRDAVIygqprtrrawKK 301
Cdd:PLN02955 181 AIGSVASLlaasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KR 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 302 ILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPhEVDVLMGTFTKSFGASGGYIA 381
Cdd:PLN02955 251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEA-DVDLCVGTLSKAAGCHGGFIA 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 382 GRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLimgldgTTQGLQRVQQLAKNTRYFRqrlqEMGFIIYGnenASVV 461
Cdd:PLN02955 330 CSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVV------ARKEKWRRKAIWERVKEFK----ALSGVDIS---SPII 396

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119220554 462 PLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLK 530
Cdd:PLN02955 397 SLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTA 465
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 194-405 1.03e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 96.77  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 194 GVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFK 273
Cdd:PRK05937  44 GYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFR 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 274 HNNTQSLEKLLrdaviygQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTE 353
Cdd:PRK05937 124 HNDLDHLESLL-------ESCRQRSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCH 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119220554 354 FFGLDphEVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSP 405
Cdd:PRK05937 197 SLGYE--NFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 143-525 8.37e-21

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 94.66  E-value: 8.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 143 RVSDDYNWTFR-FTGRVikdVINMGSYNFLGLaakyDESMRTIK---DVLEVYGT---GVASTRHEMGTL-DKHKELEDL 214
Cdd:PRK07505  31 TVGEREGILITlADGHT---FVNFVSCSYLGL----DTHPAIIEgavDALKRTGSlhlSSSRTRVRSQILkDLEEALSEL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 215 ----VAKFLNVEAAmvfgmgfatnSMNIPALVGKGCL-------ILSDELNHTSL-VLGARLS--GATIRIfKHNNTQSL 280
Cdd:PRK07505 104 fgasVLTFTSCSAA----------HLGILPLLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDAL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 281 EKLLRdaviygqprtrrAWKKILILVEGVYSMeGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRG-VTEFFGLDP 359
Cdd:PRK07505 173 EDICK------------TNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 360 HEVDVLMGTFTKSFGASGGYIA-GRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLimGLDGTTQGLQrvQQLAKNT 438
Cdd:PRK07505 240 NERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEI--HLSEELDQLQ--QKLQNNI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 439 RYFRQRLQemgfiiygNENA-SVVPLLLYMPGK---VAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLD 514
Cdd:PRK07505 316 ALFDSLIP--------TEQSgSFLPIRLIYIGDedtAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIK 387

                        410
                 ....*....|.
gi 119220554 515 TVLEALDEMGD 525
Cdd:PRK07505 388 RLCSLLKEILD 398
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 262-522 1.14e-12

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 69.29  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 262 ARLSGATIRIF--KHNNTQSLEKLLRDAVIygQPRTrrawkKILILV-----EG-VYSMEgsivHLPQIIALKKKYKAYL 333
Cdd:cd00609  100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 334 YIDEAHSigAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGASG---GYIAGRKDLVDYLRVHSHSavYASSMSPPIAEQ 410
Cdd:cd00609  169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLP--YTTSGPSTLSQA 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 411 IIRSLklimgLDGTTQGLQRV-QQLAKNTRYFRQRLQEMGFIIYGNENASvvpllLYM-----PGKVAAFARHMLEKKIG 484
Cdd:cd00609  245 AAAAA-----LDDGEEHLEELrERYRRRRDALLEALKELGPLVVVKPSGG-----FFLwldlpEGDDEEFLERLLLEAGV 314

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 119220554 485 VVVVGFPATPLAEARARFCVsaAHTREMLDTVLEALDE 522
Cdd:cd00609  315 VVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 207-383 2.98e-12

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: 65.10  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 207 KHKELEDLVAKFLN--VEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTS-LVLGARLSGATIRIFKHNNTQslekl 283
Cdd:cd01494    1 KLEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAG----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 284 lrDAVIYGQPRTRRAWKKI--LILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgldphe 361
Cdd:cd01494   76 --YGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG------ 147

                        170       180
                 ....*....|....*....|...
gi 119220554 362 VDVLMGTFTKSFGASG-GYIAGR 383
Cdd:cd01494  148 ADVVTFSLHKNLGGEGgGVVIVK 170
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 210-520 1.35e-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: 53.49  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 210 ELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLV-LGA--RLSGATIRIFKHNN-TQSLEKLLR 285
Cdd:cd06502   36 KLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENgKLTPEDLEA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 286 DAVIYGQ---PRTRrawkkiLILVE------GVYSMEgsivHLPQIIALKKKYKAYLYIDEAHSIGAVgpTGRGVTEFFG 356
Cdd:cd06502  116 AIRPRDDihfPPPS------LVSLEntteggTVYPLD----ELKAISALAKENGLPLHLDGARLANAA--AALGVALKTY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 357 LDPheVDVLMGTFTKSFGASGGYI-AGRKDLV---DYLRVHSHSAVYASSMsppIAEQIIRSLKlimgldgTTQGLQRVQ 432
Cdd:cd06502  184 KSG--VDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQAGGGMRQSGF---LAAAGLAALE-------NDLWLRRLR 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 433 QLAKNTRYFRQRLQEMGfiiyGNENASVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREM 512
Cdd:cd06502  252 HDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEED 327


                 ....*...
gi 119220554 513 LDTVLEAL 520
Cdd:cd06502  328 VDELLSAL 335
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
189-457 1.35e-07

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 53.37  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  189 EVYGtGVASTRHemgtldkhkeLEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLG---ARLS 265
Cdd:pfam01212  26 EVYG-GDPTVNR----------LEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  266 GATIRIFKHNNT-----QSLEKLLRDAVIYGQPRTRrawkkiLILVE--------GVYSMEgsivHLPQIIALKKKYKAY 332
Cdd:pfam01212  95 GVQPRPLDGDEAgnmdlEDLEAAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  333 LYIDEAHSIGAVGPTGRGVTEFFGLdpheVDVLMGTFTKSFGAS-GGYIAGRKDLVDYlRVHSHSAvYASSMSP---PIA 408
Cdd:pfam01212 165 VHLDGARFANAAVALGVIVKEITSY----ADSVTMCLSKGLGAPvGSVLAGSDDFIAK-AIRQRKY-LGGGLRQagvLAA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119220554  409 eqiirslkliMGLDGTTQGLQRVQQLAKNTRYFRQRLQEMGFII----YGNEN 457
Cdd:pfam01212 239 ----------AGLRALEEGVARLARDHATARRLAEGLELLRLAIprrvYTNTH 281
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 181-461 5.19e-06

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: 48.78  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  181 MRTIKDVLEVYGTGVASTRHEMGTL--DKHKELEDLVAKFLNVEAA--MVFGMGfATNSMNI------PALVGKGCLILS 250
Cdd:pfam00266  16 LDAIQEYYTDYNGNVHRGVHTLGKEatQAYEEAREKVAEFINAPSNdeIIFTSG-TTEAINLvalslgRSLKPGDEIVIT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  251 DELNHTSLVLGARLS---GATIRIFKHN-----NTQSLEKLLRdaviygqPRTRrawkkiLILVEGVYSMEGSIVHLPQI 322
Cdd:pfam00266  95 EMEHHANLVPWQELAkrtGARVRVLPLDedgllDLDELEKLIT-------PKTK------LVAITHVSNVTGTIQPVPEI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  323 IALKKKYKAYLYIDEAHSIGAvGPtgrgvteffgLDPHEVDVLMGTFT--KSFGASG-GYIAGRKDLVDYLR-------- 391
Cdd:pfam00266 162 GKLAHQYGALVLVDAAQAIGH-RP----------IDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDLLEKMPpllggggm 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554  392 ---VHSHSAVYASSMS------PPIAeQII---RSLKLIMGLdGTTQGLQRVQQLAKntrYFRQRLQEMGFI-IYGN-EN 457
Cdd:pfam00266 231 ietVSLQESTFADAPWkfeagtPNIA-GIIglgAALEYLSEI-GLEAIEKHEHELAQ---YLYERLLSLPGIrLYGPeRR 305


                  ....
gi 119220554  458 ASVV 461
Cdd:pfam00266 306 ASII 309
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 396-522 3.93e-05

Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 46.18  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 396 SAVYASSMSPpiaeqiirslklimgldgttQGLQRV-QQLAKNTRYFRQRLQEMGFIIYGNE---NASVVPLllymPGKV 471
Cdd:COG0403  339 ASMYAVYHGP--------------------EGLKEIaERIHQKAHYLAERLAALGVEVPFNGpffDEFVVRL----PKPA 394

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119220554 472 AAFARHMLEKKIgvvVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDE 522
Cdd:COG0403  395 AEINAALLEKGI---LGGLNLRRVDDDTLLVAVTETTTKEDIDALVEALAE 442
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 356-523 6.81e-04

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 42.12  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 356 GLDPHEVDVLMGTFTKSFgASG---GYIAGRKDLVDYLRvhshSAVYASSMSPPIAEQiirslkLIMGL---DGT-TQGL 428
Cdd:COG1167  299 ALDAPGRVIYIGSFSKTL-APGlrlGYLVAPGRLIERLA----RLKRATDLGTSPLTQ------LALAEfleSGHyDRHL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 429 QRV-QQLAKNTRYFRQRLQEmgfiiYGNENASVVP------LLLYMPGKV--AAFARHMLEKKIGVV-VVGFPATPLAEA 498
Cdd:COG1167  368 RRLrREYRARRDLLLAALAR-----HLPDGLRVTGppgglhLWLELPEGVdaEALAAAALARGILVApGSAFSADGPPRN 442

                        170       180
                 ....*....|....*....|....*...
gi 119220554 499 RARFCVSAAHTREM---LDTVLEALDEM 523
Cdd:COG1167  443 GLRLGFGAPSEEELeeaLRRLAELLREL 470
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
426-523 1.08e-03

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 41.66  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119220554 426 QGLQRV-QQLAKNTRYFRQRLQEMGFII-----YGNENAsvvpllLYMPGKVAAFARHMLEKKIgvvVVGFPAT---PLA 496
Cdd:PRK00451 348 EGLRELaEQNHQKAHYLAERLAEIGGVElfdgpFFNEFV------VRLPKPAEEVNEALLEKGI---LGGYDLGryyPEL 418

                         90       100
                 ....*....|....*....|....*..
gi 119220554 497 EARARFCVSAAHTREMLDTVLEALDEM 523
Cdd:PRK00451 419 GNHLLVCVTEKRTKEDIDALVAALGEV 445
 
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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