|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-408 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.
Pssm-ID: 143482 [Multi-domain] Cd Length: 362 Bit Score: 630.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 197 HVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSED-VKLKFEEITGVINPALDKYFPSDsGVRIIAEP 275
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgVVPSFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 276 GRYYVASAFTLAVNIIAKKIVLKEQtgsddedesseQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSI 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDD-----------RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 563580287 356 WGPTCDGLDRIVERCDLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 408
Cdd:cd00622 309 WGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-387 |
2.35e-154 |
|
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.
Pssm-ID: 459745 [Multi-domain] Cd Length: 340 Bit Score: 441.54 E-value: 2.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLGDILKKHLRWLKAL-PRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVS 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 119 QIKYAANNGVQMMTFDSEVELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLRTSRLLLERAKELNIDV 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 192 VGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGS--EDVKLKFEEITGVINPALDKYFPSDsgV 269
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 270 RIIAEPGRYYVASAFTLAVNIIAKKIvlkeqtgsddedesSEQTFMYYVNDGVYGSFNCILYDHAHVKPLlqKRPKPDEK 349
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 563580287 350 YYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMG 387
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-424 |
2.82e-72 |
|
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439790 [Multi-domain] Cd Length: 417 Bit Score: 233.89 E-value: 2.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLgDILKKHLRWLK-ALPR--VTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:COG0019 28 LYVYDE-AALRRNLRALReAFPGsgAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLRTSRLLLERAKE 186
Cdd:COG0019 107 EEELEEALELGVGHINVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 187 L-NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALDKY 262
Cdd:COG0019 187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 263 FpsDSGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFmYYVNdgvyGSFNC----ILYD--HaHV 336
Cdd:COG0019 267 C--GLGPELILEPGRALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGayH-PI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 337 KPLlqkRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPaWQL 416
Cdd:COG0019 326 VPV---GRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE-ARL 401
|
....*...
gi 563580287 417 MQQFQNPD 424
Cdd:COG0019 402 IRRRETYE 409
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
40-424 |
1.00e-42 |
|
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273415 [Multi-domain] Cd Length: 414 Bit Score: 155.91 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLgDILKKHLRWLK-ALPRVT-PFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQV 117
Cdd:TIGR01048 27 LYVYDE-DTIRRRFRAYKeAFGGRSlVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 118 SQIKYAANNGVqMMTFDSEVELM---KVARAH-PKAKLVLRIATD-DSKAVCRLSV-----KFGATLRTSRLLLERAKEL 187
Cdd:TIGR01048 106 AELERALELGI-CINVDSFSELErlnEIAPELgKKARISLRVNPGvDAKTHPYISTglkdsKFGIDVEEALEAYLYALQL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 -NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEvGFSMYLLDIGGGFPGS---EDVKLKFEEITGVINPALDKYF 263
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-GIDLEFLDLGGGLGIPytpEEEPPDLSEYAQAILNALEGYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 264 PSDSGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFMyyvndGVYGSFN----CILYD--HaHVK 337
Cdd:TIGR01048 264 DLGLDPKLILEPGRSIVANAGVLLTRVGFVK-------------ETGSRNFV-----IVDAGMNdlirPALYGayH-HII 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 338 PLLQKRPKPDEKYyssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVmSGPAWQLM 417
Cdd:TIGR01048 325 VLNRTNDAPTEVA---DVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV-DGGQARLI 400
|
....*..
gi 563580287 418 QQFQNPD 424
Cdd:TIGR01048 401 RRRETYE 407
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
34-403 |
2.11e-27 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 115.95 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 34 SDDKDAFYVADLGdILKKHLRWLKALPRVTP-FYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSL--GVPPERIIY 110
Cdd:PRK08961 499 SDAGSPCYVYHLP-TVRARARALAALAAVDQrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 111 ANPCKQVSQIKYAANNGVqMMTFDSEVELmkvaRAHPKA----KLVLRI--------------ATDDSKavcrlsvkFGA 172
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGV-TVTLDNVEPL----RNWPELfrgrEVWLRIdpghgdghhekvrtGGKESK--------FGL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 173 TLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAisdARCVFDMGAEVGfSMYLLDIGGGFP---GSEDVKLKFE 249
Cdd:PRK08961 645 SQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEPFDLD 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 250 eitgVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqtfMYYVndGVYGSFNCI 329
Cdd:PRK08961 721 ----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETGMNSL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 563580287 330 ----LYDHAHVKPLLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgfQRP 403
Cdd:PRK08961 779 irpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-408 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.
Pssm-ID: 143482 [Multi-domain] Cd Length: 362 Bit Score: 630.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 197 HVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSED-VKLKFEEITGVINPALDKYFPSDsGVRIIAEP 275
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgVVPSFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 276 GRYYVASAFTLAVNIIAKKIVLKEQtgsddedesseQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSI 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDD-----------RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 563580287 356 WGPTCDGLDRIVERCDLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 408
Cdd:cd00622 309 WGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
37-419 |
2.77e-168 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor; Antizyme inhibitor (AZI) is homologous to the fold type III PLP-dependent enzyme ODC but does not retain any decarboxylase activity. Like ODC, AZI is presumed to exist as a homodimer. Antizyme is a regulatory protein that binds directly to the ODC monomer to block its active site, leading to its degradation by the 26S proteasome. AZI binds to Antizyme with a higher affinity than ODC, preventing the formation of the Antizyme-ODC complex. Thus, AZI blocks the ability of Antizyme to promote ODC degradation, which leads to increased ODC enzymatic activity and polyamine levels. AZI also prevents the degradation of other proteins regulated by Antizyme, such as cyclin D1.
Pssm-ID: 143504 Cd Length: 394 Bit Score: 478.96 E-value: 2.77e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:cd06831 12 KNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSF 196
Cdd:cd06831 92 ASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 197 HVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEdvkLKFEEITGVINPALDKYFPSDSGVRIIAEPG 276
Cdd:cd06831 172 HVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 277 RYYVASAFTLAVNIIAKKIVLKEQ-TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSI 355
Cdd:cd06831 249 SYYVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 563580287 356 WGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQ 419
Cdd:cd06831 329 WGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQD 392
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-387 |
2.35e-154 |
|
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.
Pssm-ID: 459745 [Multi-domain] Cd Length: 340 Bit Score: 441.54 E-value: 2.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLGDILKKHLRWLKAL-PRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVS 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 119 QIKYAANNGVQMMTFDSEVELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLRTSRLLLERAKELNIDV 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 192 VGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGS--EDVKLKFEEITGVINPALDKYFPSDsgV 269
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 270 RIIAEPGRYYVASAFTLAVNIIAKKIvlkeqtgsddedesSEQTFMYYVNDGVYGSFNCILYDHAHVKPLlqKRPKPDEK 349
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 563580287 350 YYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMG 387
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
38-408 |
1.41e-151 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.
Pssm-ID: 143485 [Multi-domain] Cd Length: 368 Bit Score: 435.58 E-value: 1.41e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 38 DAFYVADLGDILKKHLRWLKALP-RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAH----PKAKLVLRIATDDSK-----AVCRLSVKFGATLRTSRLLLERAKEL 187
Cdd:cd06810 81 VSEIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSAgthkiSTGGLKSKFGLSLSEARAALERAKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVK-LKFEEITGVINPALDKYFPSD 266
Cdd:cd06810 161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQpLDFEEYAALINPLLKKYFPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 267 SGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKeqtgsddedesseqTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKP 346
Cdd:cd06810 241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGG--------------RFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 563580287 347 DEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 408
Cdd:cd06810 307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
45-281 |
2.31e-129 |
|
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.
Pssm-ID: 397077 [Multi-domain] Cd Length: 241 Bit Score: 373.92 E-value: 2.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 45 LGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAA 124
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 125 NNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTS-RLLLERAKELNIDVVGVSFHVGSGCT 203
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDvEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 204 DPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFpGSEDV----KLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYY 279
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeePLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239
|
..
gi 563580287 280 VA 281
Cdd:pfam02784 240 VA 241
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-424 |
2.82e-72 |
|
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439790 [Multi-domain] Cd Length: 417 Bit Score: 233.89 E-value: 2.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLgDILKKHLRWLK-ALPR--VTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQ 116
Cdd:COG0019 28 LYVYDE-AALRRNLRALReAFPGsgAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 117 VSQIKYAANNGVQMMTFDSEVELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLRTSRLLLERAKE 186
Cdd:COG0019 107 EEELEEALELGVGHINVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 187 L-NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALDKY 262
Cdd:COG0019 187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 263 FpsDSGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFmYYVNdgvyGSFNC----ILYD--HaHV 336
Cdd:COG0019 267 C--GLGPELILEPGRALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGayH-PI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 337 KPLlqkRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPaWQL 416
Cdd:COG0019 326 VPV---GRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE-ARL 401
|
....*...
gi 563580287 417 MQQFQNPD 424
Cdd:COG0019 402 IRRRETYE 409
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
48-277 |
2.52e-64 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 206.40 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 48 ILKKHLRWLKALP-RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANN 126
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 127 GVQMMTFDSEVELMKVARAH----PKAKLVLRIATDDskavcrLSVKFGATLRTSRLLLERAKELN-IDVVGVSFHVGSG 201
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 563580287 202 CTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLkfeeitgvinpaldkyfpsDSGVRIIAEPGR 277
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL-------------------PLGTFIIVEPGR 211
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
40-403 |
1.93e-55 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143501 [Multi-domain] Cd Length: 373 Bit Score: 188.46 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLGDILKKHLRWLKAL--PRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQV 117
Cdd:cd06828 5 LYVYDEATIRENYRRLKEAFsgPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 118 SQIKYAANNGVQMMTFDSEVELMKVARAHP----KAKLVLRIATD-DSKAVCRLSV-----KFGATLRTSRLLLERAKEL 187
Cdd:cd06828 85 EELELALELGILRINVDSLSELERLGEIAPelgkGAPVALRVNPGvDAGTHPYISTggkdsKFGIPLEQALEAYRRAKEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 -NIDVVGVSFHVGSGCTDPETFVQAisdARCVFDMGAEV---GFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALD 260
Cdd:cd06828 165 pGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLGipyRDEDEPLDIEEYAEAIAEALK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 261 KYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFMyyvndGVYGSFNCI----LYD--Ha 334
Cdd:cd06828 242 ELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVK-------------ETGGKTFV-----GVDAGMNDLirpaLYGayH- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 563580287 335 HVKPLLQKRPKPDEKYyssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRP 403
Cdd:cd06828 303 EIVPVNKPGEGETEKV---DVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRP 368
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
40-424 |
1.00e-42 |
|
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273415 [Multi-domain] Cd Length: 414 Bit Score: 155.91 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLgDILKKHLRWLK-ALPRVT-PFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQV 117
Cdd:TIGR01048 27 LYVYDE-DTIRRRFRAYKeAFGGRSlVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 118 SQIKYAANNGVqMMTFDSEVELM---KVARAH-PKAKLVLRIATD-DSKAVCRLSV-----KFGATLRTSRLLLERAKEL 187
Cdd:TIGR01048 106 AELERALELGI-CINVDSFSELErlnEIAPELgKKARISLRVNPGvDAKTHPYISTglkdsKFGIDVEEALEAYLYALQL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 -NIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEvGFSMYLLDIGGGFPGS---EDVKLKFEEITGVINPALDKYF 263
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-GIDLEFLDLGGGLGIPytpEEEPPDLSEYAQAILNALEGYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 264 PSDSGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFMyyvndGVYGSFN----CILYD--HaHVK 337
Cdd:TIGR01048 264 DLGLDPKLILEPGRSIVANAGVLLTRVGFVK-------------ETGSRNFV-----IVDAGMNdlirPALYGayH-HII 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 338 PLLQKRPKPDEKYyssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVmSGPAWQLM 417
Cdd:TIGR01048 325 VLNRTNDAPTEVA---DVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLV-DGGQARLI 400
|
....*..
gi 563580287 418 QQFQNPD 424
Cdd:TIGR01048 401 RRRETYE 407
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
40-393 |
7.74e-35 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.
Pssm-ID: 143506 [Multi-domain] Cd Length: 382 Bit Score: 133.49 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 40 FYVADLgDILKKHLRWL-KALPRVTP-FYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQV 117
Cdd:cd06839 9 FYVYDR-DRVRERYAALrAALPPAIEiYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 118 SQIKYAANNGVQMMTFDSEVELMKVARAHPK----AKLVLRIATDDSKAVCRLSV-----KFGATLRT-SRLLLERAKEL 187
Cdd:cd06839 88 AELRRAIEAGIGTINVESLEELERIDALAEEhgvvARVALRINPDFELKGSGMKMgggpsQFGIDVEElPAVLARIAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 NIDVVGVSFHVGSGCTDPETFVQAISDARCVF-DMGAEVGFSMYLLDIGGGF-----PGSEDvkLKFEEITGVINPALDK 261
Cdd:cd06839 168 NLRFVGLHIYPGTQILDADALIEAFRQTLALAlRLAEELGLPLEFLDLGGGFgipyfPGETP--LDLEALGAALAALLAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 262 YFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIvlkeqtgSDDEDesseqtfmYYVNDG-------VYGSFNCILYDHA 334
Cdd:cd06839 246 LGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-------SRGET--------FLVTDGgmhhhlaASGNFGQVLRRNY 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 563580287 335 HVKPLLQKRPKPDEKYyssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAA 393
Cdd:cd06839 311 PLAILNRMGGEERETV---TVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLSA 366
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
34-406 |
5.86e-32 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.
Pssm-ID: 143508 [Multi-domain] Cd Length: 379 Bit Score: 125.45 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 34 SDDKDAFYVADLGDILKKHLRWLKALPRVTP----FYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERII 109
Cdd:cd06841 3 ESYGSPFFVFDEDALRENYRELLGAFKKRYPnvviAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 110 YANPCKQVSQIKYAANNGVqMMTFDSEVEL---MKVARAHP-KAKLVLRIATDDSKAVcrLSvKFGATLRTSRLLLERAK 185
Cdd:cd06841 83 FNGPYKSKEELEKALEEGA-LINIDSFDELeriLEIAKELGrVAKVGIRLNMNYGNNV--WS-RFGFDIEENGEALAALK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 186 EL----NIDVVGVSFHVGSGCTDPETFVQAISDarCVFDMGAEVGFSMYLLDIGGGFPGseDVKLKFEEITGVINPALDK 261
Cdd:cd06841 159 KIqeskNLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPA--KTPLSLAYPQEDTVPDPED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 262 YFPSDSGV------------RIIAEPGRYYVASAFTLAVNIIAKKIVlkeqtgsddEDESSEQTfmyyvnDGVYGSFNCI 329
Cdd:cd06841 235 YAEAIASTlkeyyankenkpKLILEPGRALVDDAGYLLGRVVAVKNR---------YGRNIAVT------DAGINNIPTI 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 563580287 330 LYDHAHVKPLlqkRPKPDEKYYSSS-IWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgFQRPTIY 406
Cdd:cd06841 300 FWYHHPILVL---RPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFI-RPRPAVY 373
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
34-403 |
2.11e-27 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 115.95 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 34 SDDKDAFYVADLGdILKKHLRWLKALPRVTP-FYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSL--GVPPERIIY 110
Cdd:PRK08961 499 SDAGSPCYVYHLP-TVRARARALAALAAVDQrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 111 ANPCKQVSQIKYAANNGVqMMTFDSEVELmkvaRAHPKA----KLVLRI--------------ATDDSKavcrlsvkFGA 172
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGV-TVTLDNVEPL----RNWPELfrgrEVWLRIdpghgdghhekvrtGGKESK--------FGL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 173 TLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAisdARCVFDMGAEVGfSMYLLDIGGGFP---GSEDVKLKFE 249
Cdd:PRK08961 645 SQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEPFDLD 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 250 eitgVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqtfMYYVndGVYGSFNCI 329
Cdd:PRK08961 721 ----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETGMNSL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 563580287 330 ----LYDHAHVKPLLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgfQRP 403
Cdd:PRK08961 779 irpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
63-239 |
3.22e-24 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.
Pssm-ID: 143509 [Multi-domain] Cd Length: 423 Bit Score: 104.27 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 63 TPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVqMMTFDSEVELMKV 142
Cdd:cd06842 39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 143 -----ARAHPKAKLVLRIATDDSKAVCRlsvkFGATLRTSRLLLERAKELN--IDVVGVSFHVGSgcTDPETFVQAISDA 215
Cdd:cd06842 118 lalarGYTTGPARVLLRLSPFPASLPSR----FGMPAAEVRTALERLAQLRerVRLVGFHFHLDG--YSAAQRVAALQEC 191
|
170 180
....*....|....*....|....
gi 563580287 216 RCVFDMGAEVGFSMYLLDIGGGFP 239
Cdd:cd06842 192 LPLIDRARALGLAPRFIDIGGGFP 215
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
34-398 |
2.82e-22 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.
Pssm-ID: 143507 [Multi-domain] Cd Length: 368 Bit Score: 97.89 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 34 SDDKDAFYVADLgDILKKHLRWLKALPRV-TPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSL--GVPPERIIY 110
Cdd:cd06840 8 APDVGPCYVYDL-ETVRARARQVSALKAVdSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 111 ANPCKQVSQIKYAANNGVQmMTFDSevelMKVARAHPK----AKLVLRI------------ATDDSKAvcrlsvKFGATL 174
Cdd:cd06840 87 TPNFAARSEYEQALELGVN-VTVDN----LHPLREWPElfrgREVILRIdpgqgeghhkhvRTGGPES------KFGLDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 175 RTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISD-ARCVFDMGAevgfsMYLLDIGGGFP---GSEDVKLKFEE 250
Cdd:cd06840 156 DELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYlASLARHFPA-----VRILNVGGGLGipeAPGGRPIDLDA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 251 ITGVINpALDKYFPsdsGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqTFMYYVNDGVYGSFNCIL 330
Cdd:cd06840 231 LDAALA-AAKAAHP---QYQLWMEPGRFIVAESGVL----LARVTQIKHKDG----------VRFVGLETGMNSLIRPAL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 563580287 331 YDHAH-VKPLLQKRPkpdEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFN 398
Cdd:cd06840 293 YGAYHeIVNLSRLDE---PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
25-408 |
1.32e-21 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 96.40 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 25 DQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP--RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLG 102
Cdd:PLN02537 5 GLRVQDIMESVEKRPFYLYSKPQITRNYEAYKEALEglRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 103 VPPERIIYANPCKQVSQIKYAANNGVqMMTFDSEVELMKVARAH----PKAKLVLRIATD-DSK-----AVCRLSVKFGa 172
Cdd:PLN02537 85 FDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAAriagKKVNVLLRINPDvDPQvhpyvATGNKNSKFG- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 173 tLRTSRL--LLE--RAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGfpgsedVKLKF 248
Cdd:PLN02537 163 -IRNEKLqwFLDavKAHPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGG------LGIDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 249 EEiTGVINPAldkyfPSD-----------SGVRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedesSEQTFMYY 317
Cdd:PLN02537 236 YH-AGAVLPT-----PRDlidtvrelvlsRDLTLIIEPGRSLIANTCCFVNRVTGVK---------------TNGTKNFI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 318 VNDGVYGSF-NCILYD-HAHVKplLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAAS 395
Cdd:PLN02537 295 VIDGSMAELiRPSLYDaYQHIE--LVSPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMAS 372
|
410
....*....|...
gi 563580287 396 TFNGFQRPTIYYV 408
Cdd:PLN02537 373 TYNLKMRPPEYWV 385
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
67-406 |
1.64e-19 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with similarity to Ornithine and Diaminopimelate Decarboxylases; This subfamily contains uncharacterized proteins with similarity to ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.
Pssm-ID: 143505 [Multi-domain] Cd Length: 379 Bit Score: 89.76 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 67 AVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMM--TFDsEVELMKVAR 144
Cdd:cd06836 33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAINidNFQ-ELERIDALV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 145 AH---PKAKLVLRI-------ATDDSKAVCRLSvKFGATLRtsrlllERAKELNID-------VVGVSFHVGS-GCTDPe 206
Cdd:cd06836 112 AEfkeASSRIGLRVnpqvgagKIGALSTATATS-KFGVALE------DGARDEIIDafarrpwLNGLHVHVGSqGCELS- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 207 tfvQAISDARCVFDMGAEVGFSMYL-----LDIGGGFP---GSEDVKLKFEEITGVINPALDKYFpsDSGVRIIAEPGRY 278
Cdd:cd06836 184 ---LLAEGIRRVVDLAEEINRRVGRrqitrIDIGGGLPvnfESEDITPTFADYAAALKAAVPELF--DGRYQLVTEFGRS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 279 YVASA-FTLAVNIIAKKIVLKE----QTGSDDEDESSEQTFMYYVNDGVYGSfncilydHAHVKpllQKRPKPdekyysS 353
Cdd:cd06836 259 LLAKCgTIVSRVEYTKSSGGRRiaitHAGAQVATRTAYAPDDWPLRVTVFDA-------NGEPK---TGPEVV------T 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 563580287 354 SIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIY 406
Cdd:cd06836 323 DVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
41-281 |
1.64e-17 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 83.87 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 41 YVADLgDILKKHLRWLKA-LP-RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLgVPPERIIYANPCKQVS 118
Cdd:cd06843 5 YVYDL-AALRAHARALRAsLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 119 QIKYAANNGVQMMTFDSEVELMK---VARAHPK-AKLVLR--IATDDSKAvCRLSV-----KFGATLRTSRLLLERAKEL 187
Cdd:cd06843 83 ELAQALAQGVERIHVESELELRRlnaVARRAGRtAPVLLRvnLALPDLPS-STLTMggqptPFGIDEADLPDALELLRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 188 -NIDVVGVSFHVGSGCTDPETFVQAISD-ARCVFDMGAEVGFSMYLLDIGGGFpG--SEDVKLKFEEITGV--INPALDK 261
Cdd:cd06843 162 pNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI-GvnYADPEEQFDWAGFCegLDQLLAE 240
|
250 260
....*....|....*....|
gi 563580287 262 YFPsdsGVRIIAEPGRYYVA 281
Cdd:cd06843 241 YEP---GLTLRFECGRYISA 257
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
344-406 |
1.85e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.
Pssm-ID: 143502 [Multi-domain] Cd Length: 346 Bit Score: 46.77 E-value: 1.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 563580287 344 PKPDEKYYSSSIWGPTCDGLDRIVE-RCDLPeMHVGDWMLFENMGAYTVAAASTFNGFQRPTIY 406
Cdd:cd06829 281 GEPGEGAHTYRLGGNSCLAGDVIGDySFDEP-LQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIA 343
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
180-275 |
3.04e-04 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 42.31 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580287 180 LLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPAL 259
Cdd:COG1082 45 LRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELA 124
|
90
....*....|....*.
gi 563580287 260 DKYfpSDSGVRIIAEP 275
Cdd:COG1082 125 ELA--EEAGVTLALEN 138
|
|
| |
