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Conserved domains on  [gi|1622839632|ref|XP_028684014|]
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serine palmitoyltransferase 3 isoform X1 [Macaca mulatta]

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: 641.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632  57 EAPLHVMVFTYMGYGIGTLFGYLRDFMRNwgIEKCnaaVERKEQRDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGA 136
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 137 LFDVMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAA 376
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLMGMDGTTQGLQRVRQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 457 NSPVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                         490
                  ....*....|...
gi 1622839632 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: 641.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632  57 EAPLHVMVFTYMGYGIGTLFGYLRDFMRNwgIEKCnaaVERKEQRDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGA 136
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 137 LFDVMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAA 376
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLMGMDGTTQGLQRVRQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 457 NSPVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                         490
                  ....*....|...
gi 1622839632 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 2.23e-169

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: 483.60  E-value: 2.23e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:cd06454     1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHL 319
Cdd:cd06454    80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:cd06454   152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 400 ASSMSPPIAEQIIRSLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIYGNENSPVVPLLLYMPGKVAAFARHML 479
Cdd:cd06454   231 STSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1622839632 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMG 524
Cdd:cd06454   305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 160-525 1.06e-132

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: 391.34  E-value: 1.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAKyDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:COG0156    37 REVLNFSSNDYLGLANH-PRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHL 319
Cdd:COG0156   116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:COG0156   187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 400 ASSMSPPIAEQIIRSLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIyGNENSPVVPLLLYMPGKVAAFARHML 479
Cdd:COG0156   266 STALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALL 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622839632 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 1.20e-66

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: 221.53  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 138 FDVMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAK 217
Cdd:TIGR01821  23 FADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMG-QHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 218 FLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdAVIYGQPRt 295
Cdd:TIGR01821 102 LHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ-SVDPNRPK- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 296 rrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLdPHEVDVLMGTFTKSFGA 375
Cdd:TIGR01821 180 -------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 376 AGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLMgmdgTTQGLQRVRQlaKNTRYFRQRLQEMGFIIYGN 455
Cdd:TIGR01821 252 VGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIPN 325

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839632 456 EnSPVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:TIGR01821 326 P-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 1.58e-49

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 174.42  E-value: 1.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAKydESMRTIKDVLEvygtgvASTRHEMGTLDKHKELEDLVAKF--------LNVEAAMVFGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP--AVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 232 ATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK-------HNNTQSLEKLLRDAVIygqprtrrawkkiL 303
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 304 ILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGAAG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 378 GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIR-SLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIYGNe 456
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSdPLLVASELE------EMRQRIKERRDYLRDGLQAAGLSVLPS- 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839632 457 NSPVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARARFCVsAAHTREMLDTVLEAL 520
Cdd:pfam00155 291 QAGFFLLTGLDPETAKELAQVLLEEV-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: 641.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632  57 EAPLHVMVFTYMGYGIGTLFGYLRDFMRNwgIEKCnaaVERKEQRDFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGA 136
Cdd:PLN02483    3 TIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 137 LFDVMERVSDDYNWTFRFTGRVIKdVINMGSYNFLGLAAKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVA 216
Cdd:PLN02483   78 WFDVVERVSNDNNKTLKRTTKTRR-CLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 217 KFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTR 296
Cdd:PLN02483  157 RFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRTH 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 297 RAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAA 376
Cdd:PLN02483  237 RPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGSC 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 377 GGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLMGMDGTTQGLQRVRQLAKNTRYFRQRLQEMGFIIYGNE 456
Cdd:PLN02483  317 GGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGDN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 457 NSPVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKK 536
Cdd:PLN02483  397 DSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEP 476

                         490
                  ....*....|...
gi 1622839632 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 2.23e-169

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: 483.60  E-value: 2.23e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:cd06454     1 KKVLNFCSNDYLGLA-NHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtRRAWKKILILVEGVYSMEGSIVHL 319
Cdd:cd06454    80 TLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--------RRPYGKKLIVTEGVYSMDGDIAPL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGlDPHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:cd06454   152 PELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEEFGG-LTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 400 ASSMSPPIAEQIIRSLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIYGNENSPVVPLLLYMPGKVAAFARHML 479
Cdd:cd06454   231 STSLPPAVAAAALAALEVLQGGP------ERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDALL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1622839632 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMG 524
Cdd:cd06454   305 ERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 160-525 1.06e-132

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: 391.34  E-value: 1.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAKyDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:COG0156    37 REVLNFSSNDYLGLANH-PRVIEAAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAviygqprtrRAWKKILILVEGVYSMEGSIVHL 319
Cdd:COG0156   116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:COG0156   187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 400 ASSMSPPIAEQIIRSLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIyGNENSPVVPLLLYMPGKVAAFARHML 479
Cdd:COG0156   266 STALPPAVAAAALAALEILREEP------ELRERLWENIAYFREGLKELGFDL-GPSESPIVPVIVGDAERALALADALL 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622839632 480 EKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGD 525
Cdd:COG0156   339 ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 160-529 1.17e-96

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 299.42  E-value: 1.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAkYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PRK06939   42 KEVINFCANNYLGLAN-HPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQprtrrawKKILILVEGVYSMEGSIVHL 319
Cdd:PRK06939  121 TLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIAPL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFTKSF-GAAGGYIAGRKDLVDYLRVHSHSAV 398
Cdd:PRK06939  194 PEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYL 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 399 YASSMSPPIAEQIIRSLKHLMgmdgttQGLQRVRQLAKNTRYFRQRLQEMGFIIyGNENSPVVPLLLYMPGKVAAFARHM 478
Cdd:PRK06939  273 FSNSLAPAIVAASIKVLELLE------ESDELRDRLWENARYFREGMTAAGFTL-GPGEHPIIPVMLGDAKLAQEFADRL 345

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622839632 479 LEKkiGVVVVGF--PATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:PRK06939  346 LEE--GVYVIGFsfPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 160-524 6.30e-93

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 289.37  E-value: 6.30e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAkyDESMRT-IKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNI 238
Cdd:PRK05958   39 RRMLNFASNDYLGLAR--HPRLIAaAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 239 PALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdaviygQPRTRRAWkkilILVEGVYSMEGSIVH 318
Cdd:PRK05958  117 TALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 319 LPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAV 398
Cdd:PRK05958  187 LAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFI 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 399 YASSMSPPIAEQIIRSLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIyGNENSPVVPLLLYMPGKVAAFARHM 478
Cdd:PRK05958  267 FTTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALALAAAL 339

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1622839632 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 1.20e-66

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: 221.53  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 138 FDVMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAK 217
Cdd:TIGR01821  23 FADLERQAGEFPFAQWHRPDGAKDVTVWCSNDYLGMG-QHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 218 FLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRdAVIYGQPRt 295
Cdd:TIGR01821 102 LHGKESALVFTSGYVANDATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQ-SVDPNRPK- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 296 rrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLdPHEVDVLMGTFTKSFGA 375
Cdd:TIGR01821 180 -------IIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGL-MHRIDIIEGTLAKAFGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 376 AGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLMgmdgTTQGLQRVRQlaKNTRYFRQRLQEMGFIIYGN 455
Cdd:TIGR01821 252 VGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK----ESQDLRRAHQ--ENVKRLKNLLEALGIPVIPN 325

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622839632 456 EnSPVVPLLLYMPGKvAAFARHMLEKKIGVVV--VGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQL 529
Cdd:TIGR01821 326 P-SHIVPVIIGDAAL-CKKVSDLLLNKHGIYVqpINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 109-529 2.90e-62

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 210.10  E-value: 2.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 109 DFENFYTRNLYMRIRDNWNRpicsapgaLFDVMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAaKYDESMRTIKDVL 188
Cdd:PRK13392    3 NYDSYFDAALAQLHQEGRYR--------VFADLEREAGRFPRARDHGPDGPRRVTIWCSNDYLGMG-QHPDVIGAMVDAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 189 EVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGK--GCLILSDELNHTSLVLGARLSG 266
Cdd:PRK13392   74 DRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 267 ATIRIFKHNNTQSLEKLLRdAVIYGQPRtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGP 346
Cdd:PRK13392  154 AEKQVFRHNDLADLEEQLA-SVDPDRPK--------LIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 347 TGRGVTEFFGLdPHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKHLmgmdgTTQ 426
Cdd:PRK13392  225 RGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHL-----KTS 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 427 GLQRvRQLAKNTRYFRQRLQEMGFIIYGNEnSPVVPLLLYMPGKVAAFA-RHMLEKKIGVVVVGFPATPLAEARARFCVS 505
Cdd:PRK13392  299 QTER-DAHQDRVAALKAKLNANGIPVMPSP-SHIVPVMVGDPTLCKAISdRLMSEHGIYIQPINYPTVPRGTERLRITPT 376

                         410       420
                  ....*....|....*....|....
gi 1622839632 506 AAHTREMLDTVLEALDEMGDLLQL 529
Cdd:PRK13392  377 PLHDDEDIDALVAALVAIWDRLEL 400
PLN02822 PLN02822
serine palmitoyltransferase
 160-520 5.59e-58

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 200.74  E-value: 5.59e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAkYDESMRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PLN02822  109 KDVVNFASANYLGLIG-NEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLrDAVIYGQPRTRRAWKkiLILVEGVYSMEGSIVHL 319
Cdd:PLN02822  188 AFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTL-EKLTAENKRKKKLRR--YIVVEAIYQNSGQIAPL 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 320 PQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVY 399
Cdd:PLN02822  265 DEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVF 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 400 ASSMSPPIAEQIIRSLKHLmgmDGTTQGLQRVRQlakNTRYFRQRLQEM-GFIIYGNENSPVVPLLLYMPGKVA------ 472
Cdd:PLN02822  345 SASLPPYLASAAITAIDVL---EDNPSVLAKLKE---NIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKSTGSAkedlsl 418

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622839632 473 --AFARHMLeKKIGVVVVGFPATPLAEARA----RFCVSAAHTREMLDTVLEAL 520
Cdd:PLN02822  419 leHIADRML-KEDSVLVVVSKRSTLDKCRLpvgiRLFVSAGHTESDILKASESL 471
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 163-536 9.96e-55

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 189.73  E-value: 9.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 163 INMGSYNFLGLAAkyDESMR-TIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPAL 241
Cdd:PLN03227    1 LNFATHDFLSTSS--SPTLRqTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 242 VGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLL-----RDAVIYGQPRTRRAWkkilILVEGVYSMEGSI 316
Cdd:PLN03227   79 AKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGTL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 317 VHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDP-HEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSH 395
Cdd:PLN03227  155 APLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 396 SAVYASSMSPPIAEQiirSLKHLMGMDGTTQGLQRVRQLAKNTRY--------FRQRLqEMGFIIYGNENSPVVPLLLY- 466
Cdd:PLN03227  235 GYCFSASAPPFLAKA---DATATAGELAGPQLLNRLHDSIANLYStltnsshpYALKL-RNRLVITSDPISPIIYLRLSd 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 467 MPGK--------VAAFARHMLEKKIGVVVVGFPATPLAEARA----RFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRH 534
Cdd:PLN03227  311 QEATrrtdetliLDQIAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGEAVEAILCKIIDE 390


                  ..
gi 1622839632 535 KK 536
Cdd:PLN03227  391 NK 392
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 1.58e-49

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 174.42  E-value: 1.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAKydESMRTIKDVLEvygtgvASTRHEMGTLDKHKELEDLVAKF--------LNVEAAMVFGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP--AVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFlgrspvlkLDREAAVVFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 232 ATNSMNIPALVG-KGCLILSDELNHTSLVLGARLSGATIRIFK-------HNNTQSLEKLLRDAVIygqprtrrawkkiL 303
Cdd:pfam00155  73 GANIEALIFLLAnPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 304 ILVEGVYSMEGSIVHLPQ---IIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgLDPHEVDVLMGTFTKSFGAAG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 378 GYIAGRKDLVDYLRVHShSAVYASSMSPPIAEQIIR-SLKHLMGMDgttqglQRVRQLAKNTRYFRQRLQEMGFIIYGNe 456
Cdd:pfam00155 219 GYILGNAAVISQLRKLA-RPFYSSTHLQAAAAAALSdPLLVASELE------EMRQRIKERRDYLRDGLQAAGLSVLPS- 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622839632 457 NSPVVPLLLYMPGKVAAFARHMLEKKiGVVVVGFpATPLAEARARFCVsAAHTREMLDTVLEAL 520
Cdd:pfam00155 291 QAGFFLLTGLDPETAKELAQVLLEEV-GVYVTPG-SSPGVPGWLRITV-AGGTEEELEELLEAI 351
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
211-529 1.62e-35

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 137.45  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 211 LEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDaviY 290
Cdd:PRK07179  104 FEKKLAAFTGFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---H 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 291 GQPrtrrawkkiLILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDpHEVDVLMGTFT 370
Cdd:PRK07179  181 GPG---------IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLT-SRVHFITASLA 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 371 KSFGAAGGYIAGRKDLVDYLRVHSHSAVYASSMSPpiaEQIIRSLKHLmgmDGTTQGLQRVRQLAKNTRYFRQRLQEMGF 450
Cdd:PRK07179  251 KAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLP---HEIAGLEATL---EVIESADDRRARLHANARFLREGLSELGY 324

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 451 IIYGneNSPVVPLllyMPGKVAA--FARHMLEKK--IGVVVVGfPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDL 526
Cdd:PRK07179  325 NIRS--ESQIIAL---ETGSERNteVLRDALEERnvFGAVFCA-PATPKNRNLIRLSLNADLTASDLDRVLEVCREARDE 398


                  ...
gi 1622839632 527 LQL 529
Cdd:PRK07179  399 VDL 401
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 160-530 1.59e-27

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 115.54  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 160 KDVINMGSYNFLGLAAKYDESMRTIKDVLEvYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIP 239
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKE-YGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMV 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 240 ALVGKGCL--------------ILSDELNHTSLVLGARLS----GATIRIFKHNNTQSLEKLLRDAVIygqprtrrawKK 301
Cdd:PLN02955  181 AIGSVASLlaasgkplknekvaIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KR 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 302 ILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPhEVDVLMGTFTKSFGAAGGYIA 381
Cdd:PLN02955  251 KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEA-DVDLCVGTLSKAAGCHGGFIA 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 382 GRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKhlmgmdgttqglqrvrqLAKNTRYFR----QRLQEMGFIIYGNEN 457
Cdd:PLN02955  330 CSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVV-----------------VARKEKWRRkaiwERVKEFKALSGVDIS 392

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622839632 458 SPVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLK 530
Cdd:PLN02955  393 SPIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTA 465
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 194-405 4.23e-22

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 97.93  E-value: 4.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 194 GVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLGARLSGATIRIFK 273
Cdd:PRK05937   44 GYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 274 HNNTQSLEKLLrdaviygQPRTRRAWKKILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTE 353
Cdd:PRK05937  124 HNDLDHLESLL-------ESCRQRSFGRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCH 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622839632 354 FFGLDphEVDVLMGTFTKSFGAAGGYIAGRKDLVDYLRVHSHSAVYASSMSP 405
Cdd:PRK05937  197 SLGYE--NFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
PRK07505 PRK07505
hypothetical protein; Provisional
 143-525 1.62e-19

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 90.81  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 143 RVSDDYNWTFR-FTGRVikdVINMGSYNFLGLaakyDESMRTIK---DVLEVYGT---GVASTRHEMGTL-DKHKELEDL 214
Cdd:PRK07505   31 TVGEREGILITlADGHT---FVNFVSCSYLGL----DTHPAIIEgavDALKRTGSlhlSSSRTRVRSQILkDLEEALSEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 215 ----VAKFLNVEAAmvfgmgfatnSMNIPALVGKGCL-------ILSDELNHTSL-VLGARLS--GATIRIfKHNNTQSL 280
Cdd:PRK07505  104 fgasVLTFTSCSAA----------HLGILPLLASGHLtggvpphMVFDKNAHASLnILKGICAdeTEVETI-DHNDLDAL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 281 EKLLRdaviygqprtrrAWKKILILVEGVYSMeGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRG-VTEFFGLDP 359
Cdd:PRK07505  173 EDICK------------TNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 360 HEVDVLMGTFTKSFGAAGGYIA-GRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLK-HLmgmDGTTQGLQrvRQLAKN 437
Cdd:PRK07505  240 NERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEiHL---SEELDQLQ--QKLQNN 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 438 TRYFRQRLQemgfiiygNENSPV-VPLLLYMPGK---VAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTREML 513
Cdd:PRK07505  315 IALFDSLIP--------TEQSGSfLPIRLIYIGDedtAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEI 386

                         410
                  ....*....|..
gi 1622839632 514 DTVLEALDEMGD 525
Cdd:PRK07505  387 KRLCSLLKEILD 398
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 262-522 1.24e-13

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: 72.37  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 262 ARLSGATIRIF--KHNNTQSLEKLLRDAVIygQPRTrrawkKILILV-----EG-VYSMEgsivHLPQIIALKKKYKAYL 333
Cdd:cd00609   100 ARLAGAEVVPVplDEEGGFLLDLELLEAAK--TPKT-----KLLYLNnpnnpTGaVLSEE----ELEELAELAKKHGILI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 334 YIDEAHSigAVGPTGRGVTEFFGLDPHEVDVLMGTFTKSFGAAG---GYIAGRKDLVDYLRVHSHSavYASSMSPPIAEQ 410
Cdd:cd00609   169 ISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLP--YTTSGPSTLSQA 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 411 IIRSLkhlmgMDGTTQGLQRVRQ-LAKNTRYFRQRLQEMGFIIygnENSPVVPLLLYM---PGKVAAFARHMLEKKIGVV 486
Cdd:cd00609   245 AAAAA-----LDDGEEHLEELRErYRRRRDALLEALKELGPLV---VVKPSGGFFLWLdlpEGDDEEFLERLLLEAGVVV 316

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622839632 487 VVGFPATPLAEARARFCVsaAHTREMLDTVLEALDE 522
Cdd:cd00609   317 RPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 207-383 2.92e-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: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 207 KHKELEDLVAKFLN--VEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTS-LVLGARLSGATIRIFKHNNTQslekl 283
Cdd:cd01494     1 KLEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAG----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 284 lrDAVIYGQPRTRRAWKKI--LILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFgldphe 361
Cdd:cd01494    76 --YGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG------ 147

                         170       180
                  ....*....|....*....|...
gi 1622839632 362 VDVLMGTFTKSFGAAG-GYIAGR 383
Cdd:cd01494   148 ADVVTFSLHKNLGGEGgGVVIVK 170
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 210-520 2.13e-08

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: 56.19  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 210 ELEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLV-LGA--RLSGATIRIFKHNN-TQSLEKLLR 285
Cdd:cd06502    36 KLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDeAGApeFLSGVKLLPVPGENgKLTPEDLEA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 286 DAVIYGQ---PRTRrawkkiLILVE------GVYSMEgsivHLPQIIALKKKYKAYLYIDEAHSIGAVgpTGRGVTEFFG 356
Cdd:cd06502   116 AIRPRDDihfPPPS------LVSLEntteggTVYPLD----ELKAISALAKENGLPLHLDGARLANAA--AALGVALKTY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 357 LDPheVDVLMGTFTKSFGAAGGYI-AGRKDLV---DYLRVHSHSAVYASSMsppIAEQIIRSLKH-LMgmdgttqgLQRV 431
Cdd:cd06502   184 KSG--VDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQAGGGMRQSGF---LAAAGLAALENdLW--------LRRL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 432 RQLAKNTRYFRQRLQEMGfiiyGNENSPVVPLLLYMPGKVAAFARHMLEKKIGVVVVGFPATPLAEARARFCVSAAHTRE 511
Cdd:cd06502   251 RHDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHWDTTEE 326


                  ....*....
gi 1622839632 512 MLDTVLEAL 520
Cdd:cd06502   327 DVDELLSAL 335
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 364-522 8.81e-08

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


Pssm-ID: 439849 [Multi-domain]  Cd Length: 341  Bit Score: 54.37  E-value: 8.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 364 VLMGTFTKSFGAAG---GYIAGRKDLVDYL-RVHSHSAVyaSSMSPPIAEQIIRSLKHLmgmdgttqgLQRVRQLAKNTR 439
Cdd:COG0079   198 VVLRTFSKAYGLAGlrlGYAIASPELIAALrRVRGPWNV--NSLAQAAALAALEDRAYL---------EETRARLRAERE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 440 YFRQRLQEMGFiiygnensPVVP-----LLLYMPGKVAAFARHMLEKkiGVVVVGFPATPLAEArARFCVSaahTREMLD 514
Cdd:COG0079   267 RLAAALRALGL--------TVYPsqanfVLVRVPEDAAELFEALLER--GILVRDFSSFGLPDY-LRITVG---TPEEND 332


                  ....*...
gi 1622839632 515 TVLEALDE 522
Cdd:COG0079   333 RLLAALKE 340
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
189-457 1.19e-07

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 53.37  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 189 EVYGtGVASTRHemgtldkhkeLEDLVAKFLNVEAAMVFGMGFATNSMNIPALVGKGCLILSDELNHTSLVLG---ARLS 265
Cdd:pfam01212  26 EVYG-GDPTVNR----------LEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETgghAELG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 266 GATIRIFKHNNT-----QSLEKLLRDAVIYGQPRTRrawkkiLILVE--------GVYSMEgsivHLPQIIALKKKYKAY 332
Cdd:pfam01212  95 GVQPRPLDGDEAgnmdlEDLEAAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 333 LYIDEAHSIGAVGPTGRGVTEFFGLdpheVDVLMGTFTKSFGA-AGGYIAGRKDLVDYlRVHSHSAvYASSMSP---PIA 408
Cdd:pfam01212 165 VHLDGARFANAAVALGVIVKEITSY----ADSVTMCLSKGLGApVGSVLAGSDDFIAK-AIRQRKY-LGGGLRQagvLAA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622839632 409 EQiIRSLKHlmgmdgttqGLQRVRQLAKNTRYFRQRLQEMGFII----YGNEN 457
Cdd:pfam01212 239 AG-LRALEE---------GVARLARDHATARRLAEGLELLRLAIprrvYTNTH 281
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 181-459 8.96e-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: 48.01  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 181 MRTIKDVLEVYGTGVASTRHEMGTL--DKHKELEDLVAKFLNVEAA--MVFGMGfATNSMNI------PALVGKGCLILS 250
Cdd:pfam00266  16 LDAIQEYYTDYNGNVHRGVHTLGKEatQAYEEAREKVAEFINAPSNdeIIFTSG-TTEAINLvalslgRSLKPGDEIVIT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 251 DELNHTSLVLGARLS---GATIRIFKHN-----NTQSLEKLLRdaviygqPRTRrawkkiLILVEGVYSMEGSIVHLPQI 322
Cdd:pfam00266  95 EMEHHANLVPWQELAkrtGARVRVLPLDedgllDLDELEKLIT-------PKTK------LVAITHVSNVTGTIQPVPEI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 323 IALKKKYKAYLYIDEAHSIGAvGPtgrgvteffgLDPHEVDVLMGTFT--KSFGAAG-GYIAGRKDLVDYLR-------- 391
Cdd:pfam00266 162 GKLAHQYGALVLVDAAQAIGH-RP----------IDVQKLGVDFLAFSghKLYGPTGiGVLYGRRDLLEKMPpllggggm 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 392 ---VHSHSAVYASSMS------PPIAeQII---RSLKHLMGMdGTTQGLQRVRQLAKntrYFRQRLQEMGFI-IYGNENS 458
Cdd:pfam00266 231 ietVSLQESTFADAPWkfeagtPNIA-GIIglgAALEYLSEI-GLEAIEKHEHELAQ---YLYERLLSLPGIrLYGPERR 305


                  .
gi 1622839632 459 P 459
Cdd:pfam00266 306 A 306
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 356-523 2.94e-05

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: 46.75  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 356 GLDPHEVDVLMGTFTKSFgAAG---GYIAGRKDLVDYLRvhshSAVYASSMSPPIAEQiiRSLKHLMgmdgtTQG----- 427
Cdd:COG1167   299 ALDAPGRVIYIGSFSKTL-APGlrlGYLVAPGRLIERLA----RLKRATDLGTSPLTQ--LALAEFL-----ESGhydrh 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 428 LQRVRQ-LAKNTRYFRQRLQEmgfiIYGNENSPVVP-----LLLYMPGKV--AAFARHMLEKKIGVV-VVGFPATPLAEA 498
Cdd:COG1167   367 LRRLRReYRARRDLLLAALAR----HLPDGLRVTGPpgglhLWLELPEGVdaEALAAAALARGILVApGSAFSADGPPRN 442

                         170       180
                  ....*....|....*....|....*...
gi 1622839632 499 RARFCVSAAHTREM---LDTVLEALDEM 523
Cdd:COG1167   443 GLRLGFGAPSEEELeeaLRRLAELLREL 470
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
 396-522 3.36e-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: 46.56  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 396 SAVYASSMSPpiaeqiirslkhlmgmdgttQGLQRV-RQLAKNTRYFRQRLQEMGFIIYGNE---NSPVVPLllymPGKV 471
Cdd:COG0403   339 ASMYAVYHGP--------------------EGLKEIaERIHQKAHYLAERLAALGVEVPFNGpffDEFVVRL----PKPA 394

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622839632 472 AAFARHMLEKKIgvvVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDE 522
Cdd:COG0403   395 AEINAALLEKGI---LGGLNLRRVDDDTLLVAVTETTTKEDIDALVEALAE 442
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
426-523 1.06e-03

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 41.66  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622839632 426 QGLQRV-RQLAKNTRYFRQRLQEMGFII-----YGNENspVVPLllymPGKVAAFARHMLEKKIgvvVVGFPAT---PLA 496
Cdd:PRK00451  348 EGLRELaEQNHQKAHYLAERLAEIGGVElfdgpFFNEF--VVRL----PKPAEEVNEALLEKGI---LGGYDLGryyPEL 418

                          90       100
                  ....*....|....*....|....*..
gi 1622839632 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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