|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
89-489 |
3.47e-135 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 394.26 E-value: 3.47e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 89 FFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLRKLRALVGW--SSGDGIFCPGGSISNMYAVNLARYQ 166
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLpsEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 167 RYPDCKQRGLRTLPPLALFTSKECHYSIQKGAAFLGlgtDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFLVSATSG 246
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 247 TTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQdtsnllk 326
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 327 rchgsqasylfqqdkfydvaldtgdkvvqcgrrvdCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVME 406
Cdd:cd06450 231 -----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 407 PEFVNVCFWFVPPSlrgkqespdyheRLSKVAPVLKERMVKEGSMMIGYQPHGTRgNFFRVVVANSALTCADMDFLLNEL 486
Cdd:cd06450 276 PNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLEDI 342
|
...
gi 119617073 487 ERL 489
Cdd:cd06450 343 ERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
21-492 |
1.45e-133 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 394.20 E-value: 1.45e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 21 LRAVFGVVVDEAIQKGTSVSQKVCEWkEPEELKQLLDLELRSQGESQKQILER-CRAVIRYSVKTGHPRFFNQLFSGLDP 99
Cdd:COG0076 2 FRALLHQALDLAADYLAGLDRPVFGP-SPEELRAALDEPLPEEGLPPEEALAElEDLVLPGSVDWNHPRFLAFVTGGTTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 100 HALAGRIITESLNTSQYTYEIAPVFVLMEEEVLRKLRALVGWSSG-DGIFCPGGSISNMYAVNLARYQRYP-DCKQRGLR 177
Cdd:COG0076 81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGaGGVFTSGGTEANLLALLAARDRALArRVRAEGLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 178 TLPPLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLE 257
Cdd:COG0076 161 GAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 258 AIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDTSnLLKRCHGSQASYLF 337
Cdd:COG0076 241 EIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPE-LLREAFSFHASYLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 338 QQDkfyDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFV 417
Cdd:COG0076 320 PAD---DGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119617073 418 PPSLRGKQEspDYHErlskvapvLKERMVKEGSMMIGYQPHGTRgNFFRVVVANSALTCADMDFLLNELERLGQD 492
Cdd:COG0076 397 PAGLDEEDA--LNYA--------LRDRLRARGRAFLSPTKLDGR-VVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
49-417 |
1.50e-121 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 360.58 E-value: 1.50e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 49 PEELKQLLDLELRSQGESQKQILERCRAVIRYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLM 127
Cdd:pfam00282 1 PGYLKPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 128 EEEVLRKLRALVGWS------SGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLPP-----LALFTSKECHYSIQK 196
Cdd:pfam00282 81 ENVVMNWLGEMLGLPaeflgqEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSSgilakLVAYTSDQAHSSIEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 197 GAAFLGLGtdsVRVVKADERGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAW 276
Cdd:pfam00282 161 AALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 277 GGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDtSNLLKRCHGSQASYLFQQDKFYdvalDTGDKVVQC 356
Cdd:pfam00282 238 GGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKD-KEALQQAFQFNPLYLGHTDSAY----DTGHKQIPL 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617073 357 GRRVDCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFV 417
Cdd:pfam00282 313 SRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVCFRLK 373
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
48-433 |
3.11e-41 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 154.87 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 48 EPEELKQLLDLELRSQGESQKQILERCRAVIRYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:PLN02590 91 QPGYLRDMLPDSAPERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 127 MEEEVLRKLRALVGW-----SSGDGifcpGGSISN-----MYAVNLARYQRYpdCKQRGLRTLPPLALFTSKECHYSIQK 196
Cdd:PLN02590 171 LEIIVLDWLAKLLQLpdhflSTGNG----GGVIQGtgceaVLVVVLAARDRI--LKKVGKTLLPQLVVYGSDQTHSSFRK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 197 GAAFLGLGTDSVRVVKADERGK--MVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDA 274
Cdd:PLN02590 245 ACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 275 AWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKfYDVALDTGDKVV 354
Cdd:PLN02590 325 AYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSK-KDTVVNYKDWQI 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617073 355 QCGRRVDCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPpsLRGKQESPDYHER 433
Cdd:PLN02590 404 SLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAP--VDGDEDQCNERNR 480
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
48-420 |
3.97e-40 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 151.21 E-value: 3.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 48 EPEELKQLLDLELRSQGESQKQILERCRAVIRYSVKTGH-PRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVL 126
Cdd:PLN02880 43 QPGYLRELLPDSAPNQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 127 MEEEVLRKLRALVG-----WSSGDGIFCPGGSISNMYAVNLARyQRYPDCKQRGLRTLPPLALFTSKECHYSIQKGAAFL 201
Cdd:PLN02880 123 LEMIVLDWLAKLLNlpeqfLSTGNGGGVIQGTASEAVLVVLLA-ARDRVLRKVGKNALEKLVVYASDQTHSALQKACQIA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 202 GLGTDSVRVVKADERGK--MVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGS 279
Cdd:PLN02880 202 GIHPENCRLLKTDSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 280 VLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDTSNLLKRChGSQASYLFQQDKFYDVALDTGDKVVQCGRR 359
Cdd:PLN02880 282 ACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSL-STNPEFLKNKASQANSVVDYKDWQIPLGRR 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119617073 360 VDCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS 420
Cdd:PLN02880 361 FRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRIFSLVCFRLVPPK 421
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
151-399 |
2.97e-16 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 80.47 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 151 GGSISNMYAVNLARyQRYPDCkqrglrtlpplALFTSKECHYSIQKGAAFLGLGTdsvRVVKADERGKMVPEDLERQIgm 230
Cdd:PRK02769 92 GGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRIKS---RVITSLPNGEIDYDDLISKI-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 231 aEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGL---WLHVDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLL 307
Cdd:PRK02769 155 -KENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 308 AAGLQCSALllqdtsnLLKRCHGSQASylfqqdkfYDVA-LDTGDKVVQCGRR-VDCLKLWLMWKAQGDQGLERRIDQAF 385
Cdd:PRK02769 234 GSPMPCGIV-------LAKKKYVERIS--------VDVDyIGSRDQTISGSRNgHTALLLWAAIRSLGSKGLRQRVQHCL 298
|
250
....*....|....
gi 119617073 386 VLARYLVEEMKKRE 399
Cdd:PRK02769 299 DMAQYAVDRLQANG 312
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
128-309 |
2.37e-08 |
|
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: 53.54 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 128 EEEVLRKLRALVGWSSGDGIFCPGGSISN-MYAVNLARYQRYpdckqrglrtlpplALFTSKECHYSIQKGAAFLGLGTD 206
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANeAALLALLGPGDE--------------VIVDANGHGSRYWVAAELAGAKPV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 207 SVRVVKADERGKMVPEDLERQIGmaeaegAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGsvlLSQTH 286
Cdd:cd01494 68 PVPVDDAGYGGLDVAILEELKAK------PNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG---GASPA 138
|
170 180
....*....|....*....|...
gi 119617073 287 RHLLDGIQRADSVAWNPHKLLAA 309
Cdd:cd01494 139 PGVLIPEGGADVVTFSLHKNLGG 161
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
129-308 |
2.65e-08 |
|
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: 55.72 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 129 EEVLRKLRALVGWSSGDGI-FCPGGSIS-NMYAVNLARYQRYPDCkqrglrtlpplALFTSKEcHYSI----QKGAAFLG 202
Cdd:pfam00266 46 EEAREKVAEFINAPSNDEIiFTSGTTEAiNLVALSLGRSLKPGDE-----------IVITEME-HHANlvpwQELAKRTG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 203 LgtdSVRVVKADERGKMVPEDLERQIgmaeAEGAVpfLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAwggsvll 282
Cdd:pfam00266 114 A---RVRVLPLDEDGLLDLDELEKLI----TPKTK--LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAA------- 177
|
170 180 190
....*....|....*....|....*....|
gi 119617073 283 sQT--HRHlLDgIQR--ADSVAWNPHKLLA 308
Cdd:pfam00266 178 -QAigHRP-ID-VQKlgVDFLAFSGHKLYG 204
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
129-276 |
1.60e-07 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 53.15 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 129 EEVLRKLRALVGwsSGDGIFCPGGSISNMYAVN--LARYQrypdckqrglrtlpplALFTSKECHysIQK----GAAFL- 201
Cdd:COG2008 38 NRLEERVAELFG--KEAALFVPSGTMANQLALRahTRPGD----------------EVICHETAH--IYVdeggAPEALs 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617073 202 GLgtdSVRVVkADERGKMVPEDLERQIGMAEAEGAVPFLVS---ATSGTTVLgAFDPLEAIADVCQRHGLWLHVDAAW 276
Cdd:COG2008 98 GV---KLLPV-PGEDGKLTPEDLEAAIRPGDVHFPQPGLVSlenTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
256-411 |
1.22e-06 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 50.88 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 256 LEAIADVCQRHGLWLHVDAAWGGsvllsqtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLQDT---SNLLK 326
Cdd:COG1982 179 LKAIAELAHEHGIPVLVDEAHGA-------HFGFHPDLPRsameagADLVVQSTHKTLGALTQSSMLHVKGGrvdHERVN 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 327 RC---HGS-QASYLFqqdkfydVA-LDTgdkvvqcGRRvdclklwlMWKAQGdqglERRIDQAFVLARYLVEEMKKREGF 401
Cdd:COG1982 252 EAlmlLQStSPSYLL-------MAsLDV-------ARR--------QMAGEG----EELLDEALELAIEARKEINKIPGL 305
|
170
....*....|
gi 119617073 402 ElVMEPEFVN 411
Cdd:COG1982 306 Y-VFGPEDLG 314
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
208-308 |
1.16e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 47.44 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 208 VRVVKADERGKMVPEDLERQIGmaeaEGAVpfLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAwggsvllsQT-- 285
Cdd:COG0520 131 VRVIPLDEDGELDLEALEALLT----PRTK--LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--------QSvp 196
|
90 100
....*....|....*....|....*..
gi 119617073 286 HRHL----LDgiqrADSVAWNPHKLLA 308
Cdd:COG0520 197 HLPVdvqaLG----CDFYAFSGHKLYG 219
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
128-275 |
2.13e-05 |
|
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: 46.56 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 128 EEEVLRKLRALVGWSSGD--GIFCPGGSISNmyavnlaryqrypdckQRGLRTL--PPLALFTSKECHYSI--QKGAAFL 201
Cdd:cd06502 30 EDPTTAKLEARAAELFGKeaALFVPSGTAAN----------------QLALAAHtqPGGSVICHETAHIYTdeAGAPEFL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617073 202 GlgtdSVRVVKAD-ERGKMVPEDLERQI-GMAEAEGAVPFLVSATSgTTVLGAFDPLE---AIADVCQRHGLWLHVDAA 275
Cdd:cd06502 94 S----GVKLLPVPgENGKLTPEDLEAAIrPRDDIHFPPPSLVSLEN-TTEGGTVYPLDelkAISALAKENGLPLHLDGA 167
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
175-317 |
5.35e-05 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 45.59 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 175 GLRTLPPLALFTSKECHYSIQKGAAFLGLGTDSVRVVkadERGKMVPEDLERQIgmAEAEGAvPFLVSATSGTTVLGAFD 254
Cdd:PLN03032 105 GREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLERAL--AKNRDK-PAILNVNIGTTVKGAVD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119617073 255 PLEAIADVCQRHG-----LWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALL 317
Cdd:PLN03032 179 DLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVAL 246
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
146-299 |
1.59e-04 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 43.91 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 146 GIFCPGGSISNMYAVNLaryqrypDCKQRGLRtlpplaLFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLE 225
Cdd:PLN02721 58 ALFVPSGTMGNLISVLV-------HCDVRGSE------VILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 226 RQI-GMAEAEGAVPFLV-----SATSGttvlGAFDPLE---AIADVCQRHGLWLHVDAA--WGGSVLLSQTHRHLLdgiQ 294
Cdd:PLN02721 125 AAIrPKGDDHFPTTRLIclentHANCG----GRCLSVEytdKVGELAKRHGLKLHIDGAriFNASVALGVPVHRLV---K 197
|
....*
gi 119617073 295 RADSV 299
Cdd:PLN02721 198 AADSV 202
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
207-275 |
5.84e-04 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 42.07 E-value: 5.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119617073 207 SVRVVKADERGKMVPEDLERQIGMAEAegavpfLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAA 275
Cdd:cd06453 115 KLKVVPVDDDGQLDLEALEKLLTERTK------LVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGA 177
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
118-275 |
6.79e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 41.43 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 118 YEIAPVFVLMEEEVlrklRALVGWSSGdgIFCPGGSISNmyavnlaryqrypdckQRGLRTL--PPLALFTSKECHYSI- 194
Cdd:pfam01212 28 YGGDPTVNRLEDRV----AELFGKEAA--LFVPSGTAAN----------------QLALMAHcqRGDEVICGEPAHIHFd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 195 -QKGAAFLGLGTdsVRVVKADERGKMVPEDLERQI-GMAEAEGAVPFLVSAT-----SGTTVLgAFDPLEAIADVCQRHG 267
Cdd:pfam01212 86 eTGGHAELGGVQ--PRPLDGDEAGNMDLEDLEAAIrEVGADIFPPTGLISLEnthnsAGGQVV-SLENLREIAALAREHG 162
|
....*...
gi 119617073 268 LWLHVDAA 275
Cdd:pfam01212 163 IPVHLDGA 170
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
256-338 |
1.18e-03 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 40.69 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 256 LEAIADVCQRHGLWLHVDAAWGGsvllsqtHRHLLDGIQR------ADSVAWNPHKLLAAGLQCSALLLQDtsNLLKRCH 329
Cdd:cd00615 172 LRKIVEEAHHRGLPVLVDEAHGA-------HFRFHPILPSsaamagADIVVQSTHKTLPALTQGSMIHVKG--DLVNPDR 242
|
....*....
gi 119617073 330 GSQASYLFQ 338
Cdd:cd00615 243 VNEALNLHQ 251
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
129-275 |
2.38e-03 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 40.03 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 129 EEVLRKLRALVGWSSGDGIFCPGGSISNmyavNLA---RYQRYPDCKQRglrtlpplaLFTSK-EcHYSIQKGAAFL-GL 203
Cdd:COG1104 48 EEAREQVAALLGADPEEIIFTSGGTEAN----NLAikgAARAYRKKGKH---------IITSAiE-HPAVLETARFLeKE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119617073 204 GTDsVRVVKADERGKMVPEDLERQIgmaeAEGAVpfLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAA 275
Cdd:COG1104 114 GFE-VTYLPVDEDGRVDLEALEAAL----RPDTA--LVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAV 178
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
175-278 |
2.80e-03 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 40.18 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119617073 175 GLRTLPPLALFTSKECHYSIQKGAAFLglgtdSVRVVKAD--ERGKMVPEDLERQIgMAEAEGavPFLVSATSGTTVLGA 252
Cdd:PLN02263 172 GREVFPDGILYASRESHYSVFKAARMY-----RMECVKVDtlVSGEIDCADFKAKL-LANKDK--PAIINVNIGTTVKGA 243
|
90 100 110
....*....|....*....|....*....|.
gi 119617073 253 FDPLEAIADVCQRHG-----LWLHVDAAWGG 278
Cdd:PLN02263 244 VDDLDLVIKTLEECGfsqdrFYIHCDGALFG 274
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
221-275 |
3.42e-03 |
|
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: 39.47 E-value: 3.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 119617073 221 PEDLERQIgmAEA-EGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAA 275
Cdd:cd06454 117 MEDLEKLL--REArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEA 170
|
|
| |
