|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
39-407 |
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: 548.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 39 DSSFMLVDLDKIIERFQLWKRELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKT 118
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 119 RSFIAHAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAVSDPTATCPLNLKFGADPiIAAPQLLKTASEEGINVVGIS 198
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADP-EEARELLRRAKELGLNVVGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 199 FHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEH--HNPFEKIAETIRDALDEFFPDTNKRLIAEP 276
Cdd:cd00622 160 FHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgvVPSFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 277 GRFFAAGPFSLVANIIHATEVPASkitkdpkdcaDHGYMYYINDGVYGSFNCILFDHAHPIGSPLFDTDRN-EKFMSTIW 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDD----------DRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDgELYPSSLW 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17562780 356 GPTCDSLDLVEDKKLMPK-MNVGEWLYYPDMGAYTLAAATTFNGFSKPVPMYV 407
Cdd:cd00622 310 GPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
42-386 |
1.55e-127 |
|
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: 371.82 E-value: 1.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 42 FMLVDLDKIIERFQLWKREL-PMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRS 120
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 121 FIAHAMDRDVKMMTFDNPEELLKIAKLHPN--AEMILRIAV-SDP----TATCPLNLKFGADpIIAAPQLLKTASEEGIN 193
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPdVDAgthkISTGGLSSKFGID-LEDAPELLALAKELGLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 194 VVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEHHNP---FEKIAETIRDALDEFFPDtNK 270
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPppdFEEYAAAIREALDEYFPP-DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 271 RLIAEPGRFFAAGPFSLVANIIhatevpaSKITKDPKdcadhgYMYYINDGVYGSFNCILFDHAHPIgSPLFDTDRNEKF 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVI-------AVKTGGGK------TFVIVDAGMNDLFRPALYDAYHPI-PVVKEPGEGPLE 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 17562780 351 MSTIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMG 386
Cdd:pfam00278 305 TYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
44-417 |
1.87e-68 |
|
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: 222.72 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 44 LVDLDKIIERFQLWKR--ELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSF 121
Cdd:COG0019 30 VYDEAALRRNLRALREafPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 122 IAHAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAV----------SDPTATCPLNLKFGADPIIAAPQLLKTASEEG 191
Cdd:COG0019 110 LEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLrvnpgvdagtHEYISTGGKDSKFGIPLEDALEAYRRAAALPG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 192 INVVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFP----GAEHHNPFEKIAETIRDALDEFFpD 267
Cdd:COG0019 190 LRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipytEGDEPPDLEELAAAIKEALEELC-G 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 268 TNKRLIAEPGRFFA--AGpfSLVANIIHATEVPASKitkdpkdcadhgymYYINDgvyGSFNC----ILFDHAHPIgSPL 341
Cdd:COG0019 269 LGPELILEPGRALVgnAG--VLLTRVLDVKENGGRR--------------FVIVD---AGMNDlmrpALYGAYHPI-VPV 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562780 342 FDTDRNEKFMSTIWGPTCDSLD-LVEDKKLmPKMNVGEWLYYPDMGAYTLAAATTFNGFSKPvPMYVMSEEMWESIR 417
Cdd:COG0019 329 GRPSGAEAETYDVVGPLCESGDvLGKDRSL-PPLEPGDLLAFLDAGAYGFSMASNYNGRPRP-AEVLVDDGEARLIR 403
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
36-411 |
3.80e-38 |
|
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: 142.43 E-value: 3.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 36 QENDSSFMLVDLDKIIERFQLWKRELP-MIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYAN 114
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 115 PCKTRSFIAHAMDRDVkMMTFDNPEELLKIAKLHPNAEMILRIAV----------SDPTATCPLNLKFGADPIIAAPQLL 184
Cdd:TIGR01048 101 NGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLrvnpgvdaktHPYISTGLKDSKFGIDVEEALEAYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 185 KTASEEGINVVGISFHVGSGCNDASAYRNALQH-AKNLCEIGEGLGFKmdIIDMGGGF----------PGAEHHnpFEKI 253
Cdd:TIGR01048 180 YALQLPHLELVGIHCHIGSQITDLSPFVEAAEKvVKLAESLAEGIDLE--FLDLGGGLgipytpeeepPDLSEY--AQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 254 AETIRDALDEFFPdtnKRLIAEPGRffaagpfSLVANI-IHATEVPASKITKDPKDCA-DHGYMYYINDGVYGSFncilf 331
Cdd:TIGR01048 256 LNALEGYADLGLD---PKLILEPGR-------SIVANAgVLLTRVGFVKETGSRNFVIvDAGMNDLIRPALYGAY----- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 332 dhaHPIgSPLFDTDRNEKFMSTIWGPTCDSLD-LVEDKKLmPKMNVGEWLYYPDMGAYTLAAATTFNgfSKPVPMYVMSE 410
Cdd:TIGR01048 321 ---HHI-IVLNRTNDAPTEVADVVGPVCESGDvLAKDREL-PEVEPGDLLAVFDAGAYGFSMSSNYN--SRPRPAEVLVD 393
|
.
gi 17562780 411 E 411
Cdd:TIGR01048 394 G 394
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-397 |
2.20e-20 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 93.61 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 59 RELPMIEP----FYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGT--GVSAERIIYANPCKTRSFIAHAMDRDVkM 132
Cdd:PRK08961 518 RALAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-T 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 133 MTFDNPEELLKIAKLHPNAEMILRIavsDP---------TATCPLNLKFGAdPIIAAPQLLKTASEEGINVVGISFHVGS 203
Cdd:PRK08961 597 VTLDNVEPLRNWPELFRGREVWLRI---DPghgdghhekVRTGGKESKFGL-SQTRIDEFVDLAKTLGITVVGLHAHLGS 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 204 GCNDASAYRnalQHAKNLCEIGEGLGfKMDIIDMGGGF--PGAEHHNPFEkiAETIRDALDEF---FPDTnkRLIAEPGR 278
Cdd:PRK08961 673 GIETGEHWR---RMADELASFARRFP-DVRTIDLGGGLgiPESAGDEPFD--LDALDAGLAEVkaqHPGY--QLWIEPGR 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 279 FFAAGPFSLVAniiHATEVpaskITKDpkdcadhGYMYY-INDGVYGSFNCILFDHAHPIGSpLFDTDRNEKFMSTIWGP 357
Cdd:PRK08961 745 YLVAEAGVLLA---RVTQV----KEKD-------GVRRVgLETGMNSLIRPALYGAYHEIVN-LSRLDEPAAGTADVVGP 809
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17562780 358 TCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFN 397
Cdd:PRK08961 810 ICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
39-407 |
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: 548.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 39 DSSFMLVDLDKIIERFQLWKRELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKT 118
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 119 RSFIAHAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAVSDPTATCPLNLKFGADPiIAAPQLLKTASEEGINVVGIS 198
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADP-EEARELLRRAKELGLNVVGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 199 FHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEH--HNPFEKIAETIRDALDEFFPDTNKRLIAEP 276
Cdd:cd00622 160 FHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgvVPSFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 277 GRFFAAGPFSLVANIIHATEVPASkitkdpkdcaDHGYMYYINDGVYGSFNCILFDHAHPIGSPLFDTDRN-EKFMSTIW 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDD----------DRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDgELYPSSLW 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17562780 356 GPTCDSLDLVEDKKLMPK-MNVGEWLYYPDMGAYTLAAATTFNGFSKPVPMYV 407
Cdd:cd00622 310 GPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
42-386 |
1.55e-127 |
|
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: 371.82 E-value: 1.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 42 FMLVDLDKIIERFQLWKREL-PMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRS 120
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 121 FIAHAMDRDVKMMTFDNPEELLKIAKLHPN--AEMILRIAV-SDP----TATCPLNLKFGADpIIAAPQLLKTASEEGIN 193
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPdVDAgthkISTGGLSSKFGID-LEDAPELLALAKELGLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 194 VVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEHHNP---FEKIAETIRDALDEFFPDtNK 270
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPppdFEEYAAAIREALDEYFPP-DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 271 RLIAEPGRFFAAGPFSLVANIIhatevpaSKITKDPKdcadhgYMYYINDGVYGSFNCILFDHAHPIgSPLFDTDRNEKF 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVI-------AVKTGGGK------TFVIVDAGMNDLFRPALYDAYHPI-PVVKEPGEGPLE 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 17562780 351 MSTIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMG 386
Cdd:pfam00278 305 TYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
47-282 |
4.48e-121 |
|
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: 351.58 E-value: 4.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 47 LDKIIERFQLWKRELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSFIAHAM 126
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 127 DRDVKMMTFDNPEELLKIAKLHPNAEMILRIAVSDPTATCPLNLKFGADPIIAAPQLLKTASEEGINVVGISFHVGSGCN 206
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 207 DASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFpGAEHHN-----PFEKIAETIRDALDEFFP-DTNKRLIAEPGRFF 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTEgeeplDFEEYANVINEALEEYFPgDPGVTIIAEPGRYF 239
|
..
gi 17562780 281 AA 282
Cdd:pfam02784 240 VA 241
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
41-419 |
1.82e-94 |
|
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: 289.44 E-value: 1.82e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 41 SFMLVDLDKIIERFQLWKRELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRS 120
Cdd:cd06831 14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 121 FIAHAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAVSDPTATCPLNLKFGADpIIAAPQLLKTASEEGINVVGISFH 200
Cdd:cd06831 94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTT-LKNCRHLLECAKELDVQIVGVKFH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 201 VGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEHHnpFEKIAETIRDALDEFFPD-TNKRLIAEPGRF 279
Cdd:cd06831 173 VSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQ--LEEVNHVIRPLLDVYFPEgSGIQIIAEPGSY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 280 FAAGPFSLVANIIHATEVPASKITKDPKDCADH--GYMYYINDGVYGSFNCILFDHAHPIGSPLFDTDRNEK-FMSTIWG 356
Cdd:cd06831 251 YVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDepAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPlFTSSLWG 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17562780 357 PTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFNGFSKPVPMYVMSEEMWESIRDS 419
Cdd:cd06831 331 PSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDA 393
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
42-402 |
7.45e-89 |
|
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: 273.80 E-value: 7.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 42 FMLVDLDKIIERFQLWKRELPM-IEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRS 120
Cdd:cd06810 3 FYVYDLDIIRAHYAALKEALPSgVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKSVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 121 FIAHAMDRDVKMMTFDNPEELLKIAKLH----PNAEMILRIAVSDP-----TATCPLNLKFGADPiIAAPQLLKTASEEG 191
Cdd:cd06810 83 EIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSagthkISTGGLKSKFGLSL-SEARAALERAKELD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 192 INVVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEH--HNPFEKIAETIRDALDEFFP-DT 268
Cdd:cd06810 162 LRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDeqPLDFEEYAALINPLLKKYFPnDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 269 NKRLIAEPGRFFAAGPFSLVANIIHATEVPASKItkdpkdcadhgymYYINDGVYGSFNCILFDHAHPIGSPLFDTDRNE 348
Cdd:cd06810 242 GVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFF-------------AVVDGGMNHSFRPALAYDAYHPITPLKAPGPDE 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17562780 349 K-FMSTIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFNGFSKP 402
Cdd:cd06810 309 PlVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRP 363
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
44-417 |
1.87e-68 |
|
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: 222.72 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 44 LVDLDKIIERFQLWKR--ELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSF 121
Cdd:COG0019 30 VYDEAALRRNLRALREafPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 122 IAHAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAV----------SDPTATCPLNLKFGADPIIAAPQLLKTASEEG 191
Cdd:COG0019 110 LEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLrvnpgvdagtHEYISTGGKDSKFGIPLEDALEAYRRAAALPG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 192 INVVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFP----GAEHHNPFEKIAETIRDALDEFFpD 267
Cdd:COG0019 190 LRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipytEGDEPPDLEELAAAIKEALEELC-G 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 268 TNKRLIAEPGRFFA--AGpfSLVANIIHATEVPASKitkdpkdcadhgymYYINDgvyGSFNC----ILFDHAHPIgSPL 341
Cdd:COG0019 269 LGPELILEPGRALVgnAG--VLLTRVLDVKENGGRR--------------FVIVD---AGMNDlmrpALYGAYHPI-VPV 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562780 342 FDTDRNEKFMSTIWGPTCDSLD-LVEDKKLmPKMNVGEWLYYPDMGAYTLAAATTFNGFSKPvPMYVMSEEMWESIR 417
Cdd:COG0019 329 GRPSGAEAETYDVVGPLCESGDvLGKDRSL-PPLEPGDLLAFLDAGAYGFSMASNYNGRPRP-AEVLVDDGEARLIR 403
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
46-402 |
1.84e-49 |
|
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: 171.90 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 46 DLDKIIERFQLWKRELPMIEP--FYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSFIA 123
Cdd:cd06828 9 DEATIRENYRRLKEAFSGPGFkiCYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 124 HAMDRDVKMMTFDNPEELLKIAKLHPNAEMILRIAV----------SDPTATCPLNLKFGAdPIIAAPQLLKTASE-EGI 192
Cdd:cd06828 89 LALELGILRINVDSLSELERLGEIAPELGKGAPVALrvnpgvdagtHPYISTGGKDSKFGI-PLEQALEAYRRAKElPGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 193 NVVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFP----GAEHHNPFEKIAETIRDALDEFFPD- 267
Cdd:cd06828 168 KLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGipyrDEDEPLDIEEYAEAIAEALKELCEGg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 268 TNKRLIAEPGRFfaagpfsLVANI-IHATEVPASKITkdpkdcadHGYMYYINDG---------VYGSFncilfdhaHPI 337
Cdd:cd06828 248 PDLKLIIEPGRY-------IVANAgVLLTRVGYVKET--------GGKTFVGVDAgmndlirpaLYGAY--------HEI 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17562780 338 gSPLFDTDRNEKFMSTIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFNGFSKP 402
Cdd:cd06828 305 -VPVNKPGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRP 368
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
50-278 |
6.31e-42 |
|
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: 147.08 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 50 IIERFQLWKRELPM-IEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSFIAHAMDR 128
Cdd:cd06808 1 IRHNYRRLREAAPAgITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 129 DVKMMTFDNPEELLKIA----KLHPNAEMILRIAVSDptatcpLNLKFGADPIIAAPQLLKTASEEGINVVGISFHVGSG 204
Cdd:cd06808 81 GVIVVTVDSLEELEKLEeaalKAGPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17562780 205 CNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEHHNPFEKIaetirdaldeffpdtnkRLIAEPGR 278
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGT-----------------FIIVEPGR 211
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
36-411 |
3.80e-38 |
|
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: 142.43 E-value: 3.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 36 QENDSSFMLVDLDKIIERFQLWKRELP-MIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYAN 114
Cdd:TIGR01048 21 QEFGTPLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 115 PCKTRSFIAHAMDRDVkMMTFDNPEELLKIAKLHPNAEMILRIAV----------SDPTATCPLNLKFGADPIIAAPQLL 184
Cdd:TIGR01048 101 NGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLrvnpgvdaktHPYISTGLKDSKFGIDVEEALEAYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 185 KTASEEGINVVGISFHVGSGCNDASAYRNALQH-AKNLCEIGEGLGFKmdIIDMGGGF----------PGAEHHnpFEKI 253
Cdd:TIGR01048 180 YALQLPHLELVGIHCHIGSQITDLSPFVEAAEKvVKLAESLAEGIDLE--FLDLGGGLgipytpeeepPDLSEY--AQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 254 AETIRDALDEFFPdtnKRLIAEPGRffaagpfSLVANI-IHATEVPASKITKDPKDCA-DHGYMYYINDGVYGSFncilf 331
Cdd:TIGR01048 256 LNALEGYADLGLD---PKLILEPGR-------SIVANAgVLLTRVGFVKETGSRNFVIvDAGMNDLIRPALYGAY----- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 332 dhaHPIgSPLFDTDRNEKFMSTIWGPTCDSLD-LVEDKKLmPKMNVGEWLYYPDMGAYTLAAATTFNgfSKPVPMYVMSE 410
Cdd:TIGR01048 321 ---HHI-IVLNRTNDAPTEVADVVGPVCESGDvLAKDREL-PEVEPGDLLAVFDAGAYGFSMSSNYN--SRPRPAEVLVD 393
|
.
gi 17562780 411 E 411
Cdd:TIGR01048 394 G 394
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
35-411 |
1.51e-37 |
|
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: 140.09 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 35 LQENDSSFMLVDLDKIIERFQL----WKRELPMIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERI 110
Cdd:cd06841 2 LESYGSPFFVFDEDALRENYREllgaFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 111 IYANPCKTRSFIAHAMDRDVkMMTFDNPEELLKIAKLHPNAEMILRIA--VSDPTATCPLNlKFGADP--IIAAPQLLKT 186
Cdd:cd06841 82 IFNGPYKSKEELEKALEEGA-LINIDSFDELERILEIAKELGRVAKVGirLNMNYGNNVWS-RFGFDIeeNGEALAALKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 187 ASE-EGINVVGISFHVGSGCNDASAYRNAlqhAKNLCE-IGEGLGFKMDIIDMGGGFPGA---------EHHNP-FEKIA 254
Cdd:cd06841 160 IQEsKNLSLVGLHCHVGSNILNPEAYSAA---AKKLIElLDRLFGLELEYLDLGGGFPAKtplslaypqEDTVPdPEDYA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 255 ETIRDALDEFFPDTNK--RLIAEPGRFFAAGPFSLVANIIHATEVPASKItkdpkdcadhgymyYINDGVYGSFNCILFD 332
Cdd:cd06841 237 EAIASTLKEYYANKENkpKLILEPGRALVDDAGYLLGRVVAVKNRYGRNI--------------AVTDAGINNIPTIFWY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 333 HaHPIgsPLFDTDRNEKFMS--TIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLaaaTTFNGFSKP-VPMYVMS 409
Cdd:cd06841 303 H-HPI--LVLRPGKEDPTSKnyDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNM---TQSNQFIRPrPAVYLID 376
|
..
gi 17562780 410 EE 411
Cdd:cd06841 377 NN 378
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
42-408 |
3.06e-37 |
|
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: 139.27 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 42 FMLVDLDKIIERFQLWKRELP-MIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRS 120
Cdd:cd06839 9 FYVYDRDRVRERYAALRAALPpAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 121 FIAHAMDRDVKMMTFDNPEELLKIAKL------HPNAemILRIAVSDPTATCPLNL-----KFGADpIIAAPQLLKT-AS 188
Cdd:cd06839 89 ELRRAIEAGIGTINVESLEELERIDALaeehgvVARV--ALRINPDFELKGSGMKMgggpsQFGID-VEELPAVLARiAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 189 EEGINVVGISFHVGSGCNDA----SAYRNALQHAKNLCeigEGLGFKMDIIDMGGGF--PGAEHHNP--FEKIAETIRDA 260
Cdd:cd06839 166 LPNLRFVGLHIYPGTQILDAdaliEAFRQTLALALRLA---EELGLPLEFLDLGGGFgiPYFPGETPldLEALGAALAAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 261 LDEF---FPDTnkRLIAEPGRFFAAGPFSLVaniihaTEVPASKITkdpkdcadHGYMYYINDG-----VYGSFNCILFD 332
Cdd:cd06839 243 LAELgdrLPGT--RVVLELGRYLVGEAGVYV------TRVLDRKVS--------RGETFLVTDGgmhhhLAASGNFGQVL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17562780 333 HAHPIGSPLFDTDRNEKFMSTIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTfnGF-SKPVPMYVM 408
Cdd:cd06839 307 RRNYPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLSASPL--AFlSHPAPAEVL 381
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
43-404 |
2.41e-23 |
|
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: 100.55 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 43 MLVDLDKIIERFQLWKRELPmiEPF---YAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTR 119
Cdd:cd06836 6 GLYDLDGFRALVARLTAAFP--APVlhtFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 120 SFIAHAMDRDVKmMTFDNPEELLKI----AKLHPNAEMI-LRI----------AVSDPTATCplnlKFG-------ADPI 177
Cdd:cd06836 84 AELREALELGVA-INIDNFQELERIdalvAEFKEASSRIgLRVnpqvgagkigALSTATATS----KFGvaledgaRDEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 178 IAApqllkTASEEGINvvGISFHVGS-GC---NDASAYRNALQHAKnlcEIGEGLG-FKMDIIDMGGGFP---GAEHHNP 249
Cdd:cd06836 159 IDA-----FARRPWLN--GLHVHVGSqGCelsLLAEGIRRVVDLAE---EINRRVGrRQITRIDIGGGLPvnfESEDITP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 250 -FEKIAETIRDALDEFFPDTnKRLIAEPGRFFAAGPFSLVAN-------------IIHATEVPASKITKDPKDcadhgym 315
Cdd:cd06836 229 tFADYAAALKAAVPELFDGR-YQLVTEFGRSLLAKCGTIVSRveytkssggrriaITHAGAQVATRTAYAPDD------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 316 YYINDGVYGSfncilfdHAHPIGSPLFDTDrnekfmstIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATT 395
Cdd:cd06836 301 WPLRVTVFDA-------NGEPKTGPEVVTD--------VAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSS 365
|
....*....
gi 17562780 396 FNgfSKPVP 404
Cdd:cd06836 366 YN--SLPRP 372
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
67-397 |
1.25e-21 |
|
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: 95.58 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 67 FYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGT--GVSAERIIYANPCKTRSFIAHAMDRDVKmMTFDNPEELLKI 144
Cdd:cd06840 39 FYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVN-VTVDNLHPLREW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 145 AKLHPNAEMILRIavsDP---------TATCPLNLKFG--ADPIIAAPQLLKTAseeGINVVGISFHVGSGCNDASAYRN 213
Cdd:cd06840 118 PELFRGREVILRI---DPgqgeghhkhVRTGGPESKFGldVDELDEARDLAKKA---GIIVIGLHAHSGSGVEDTDHWAR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 214 alqHAKNLCEIGEGLGfKMDIIDMGGGF--PGAEHHNPFEkiaetiRDALDEFFPDTNKR-----LIAEPGRFFAAGPFS 286
Cdd:cd06840 192 ---HGDYLASLARHFP-AVRILNVGGGLgiPEAPGGRPID------LDALDAALAAAKAAhpqyqLWMEPGRFIVAESGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 287 LVANIIHATEVPASKITKdpkdcadhgymyyINDGVYGSFNCILFDHAHPIGSpLFDTDRNEKFMSTIWGPTCDSLDLVE 366
Cdd:cd06840 262 LLARVTQIKHKDGVRFVG-------------LETGMNSLIRPALYGAYHEIVN-LSRLDEPPAGNADVVGPICESGDVLG 327
|
330 340 350
....*....|....*....|....*....|.
gi 17562780 367 DKKLMPKMNVGEWLYYPDMGAYTLAAATTFN 397
Cdd:cd06840 328 RDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-397 |
2.20e-20 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 93.61 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 59 RELPMIEP----FYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGT--GVSAERIIYANPCKTRSFIAHAMDRDVkM 132
Cdd:PRK08961 518 RALAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-T 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 133 MTFDNPEELLKIAKLHPNAEMILRIavsDP---------TATCPLNLKFGAdPIIAAPQLLKTASEEGINVVGISFHVGS 203
Cdd:PRK08961 597 VTLDNVEPLRNWPELFRGREVWLRI---DPghgdghhekVRTGGKESKFGL-SQTRIDEFVDLAKTLGITVVGLHAHLGS 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 204 GCNDASAYRnalQHAKNLCEIGEGLGfKMDIIDMGGGF--PGAEHHNPFEkiAETIRDALDEF---FPDTnkRLIAEPGR 278
Cdd:PRK08961 673 GIETGEHWR---RMADELASFARRFP-DVRTIDLGGGLgiPESAGDEPFD--LDALDAGLAEVkaqHPGY--QLWIEPGR 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 279 FFAAGPFSLVAniiHATEVpaskITKDpkdcadhGYMYY-INDGVYGSFNCILFDHAHPIGSpLFDTDRNEKFMSTIWGP 357
Cdd:PRK08961 745 YLVAEAGVLLA---RVTQV----KEKD-------GVRRVgLETGMNSLIRPALYGAYHEIVN-LSRLDEPAAGTADVVGP 809
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17562780 358 TCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFN 397
Cdd:PRK08961 810 ICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
66-242 |
6.26e-20 |
|
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: 91.17 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 66 PFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYANPCKTRSFIAHAMDRDVkMMTFDNPEELLKIA 145
Cdd:cd06842 40 VYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 146 KL-----HPNAEMILRiaVSDPTATcpLNLKFG--ADPIIAAPQLLKTASeEGINVVGISFHVGSGcnDASAYRNALQHA 218
Cdd:cd06842 119 ALargytTGPARVLLR--LSPFPAS--LPSRFGmpAAEVRTALERLAQLR-ERVRLVGFHFHLDGY--SAAQRVAALQEC 191
|
170 180
....*....|....*....|....
gi 17562780 219 KNLCEIGEGLGFKMDIIDMGGGFP 242
Cdd:cd06842 192 LPLIDRARALGLAPRFIDIGGGFP 215
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
36-417 |
5.98e-18 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 85.23 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 36 QENDSSFMLVDLDKIIERFQLWKRELPMIE--PFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAERIIYA 113
Cdd:PLN02537 14 SVEKRPFYLYSKPQITRNYEAYKEALEGLRsiIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 114 NPCKTRSFIAHAMDRDVkMMTFDNPEELLKIAKLHPNA----EMILRIAVS-DP-----TATCPLNLKFGA--------- 174
Cdd:PLN02537 94 GNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAgkkvNVLLRINPDvDPqvhpyVATGNKNSKFGIrneklqwfl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 175 DPIIAAPQLLKtaseeginVVGISFHVGSGCNDASAYRNALQHAKNLCEIGEGLGFKMDIIDMGGGFPGAEHHNpfEKIA 254
Cdd:PLN02537 173 DAVKAHPNELK--------LVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYYHA--GAVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 255 ETIRDALD---EFFPDTNKRLIAEPGRffaagpfSLVAN----IIHATEVPaskiTKDPKD--CADHGYMYYINDGVYGS 325
Cdd:PLN02537 243 PTPRDLIDtvrELVLSRDLTLIIEPGR-------SLIANtccfVNRVTGVK----TNGTKNfiVIDGSMAELIRPSLYDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 326 FNCILFDHAHPIGSPL--FDtdrnekfmstIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFNGFSKPV 403
Cdd:PLN02537 312 YQHIELVSPPPPDAEVstFD----------VVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPP 381
|
410
....*....|....
gi 17562780 404 PMYVMSEEMWESIR 417
Cdd:PLN02537 382 EYWVEEDGSITKIR 395
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
44-282 |
2.25e-12 |
|
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: 68.08 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 44 LVDLDKIIERFQLWKRELP-MIEPFYAVKCNTDLVLIRILASLGCGFDCASKDEIDIVMGTGVSAeRIIYANPCKTRSFI 122
Cdd:cd06843 6 VYDLAALRAHARALRASLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDA-PLIFGGPGKTDSEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 123 AHAMDRDVKMMTFDNPEELLKIAKL----HPNAEMILRI---AVSDPTATCPLNLK---FGADP--IIAAPQLLKTASee 190
Cdd:cd06843 85 AQALAQGVERIHVESELELRRLNAVarraGRTAPVLLRVnlaLPDLPSSTLTMGGQptpFGIDEadLPDALELLRDLP-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 191 GINVVGISFHVGSGCNDASAY----RNALQHAKNLCEIGeglGFKMDIIDMGGGFpGAEHHNP---F------EKIAETI 257
Cdd:cd06843 163 NIRLRGFHFHLMSHNLDAAAHlalvKAYLETARQWAAEH---GLDLDVVNVGGGI-GVNYADPeeqFdwagfcEGLDQLL 238
|
250 260
....*....|....*....|....*
gi 17562780 258 RDALDEFfpdtnkRLIAEPGRFFAA 282
Cdd:cd06843 239 AEYEPGL------TLRFECGRYISA 257
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
66-361 |
1.43e-11 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC 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. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.
Pssm-ID: 143503 [Multi-domain] Cd Length: 409 Bit Score: 65.67 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 66 PFYAVKCNTDLVLIRILASLGC----GFDCASKDEIDIVMGTGVSAERIIYANPCKTRSFIAHAMdRDVKM-----MTFD 136
Cdd:cd06830 41 GVYPIKVNQQREVVEEIVKAGKryniGLEAGSKPELLAALALLKTPDALIICNGYKDDEYIELAL-LARKLghnviIVIE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 137 NPEEL---LKIAKLHPNAEMI-LRIAVSD-----PTATCPLNLKFG--ADPIIAAPQLLKTASEEGiNVVGISFHVGSGC 205
Cdd:cd06830 120 KLSELdliLELAKKLGVKPLLgVRIKLASkgsgkWQESGGDRSKFGltASEILEVVEKLKEAGMLD-RLKLLHFHIGSQI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 206 NDASAYRNALQHAKNL-CEIGEgLGFKMDIIDMGGGFP----GAEHHNPF----------EKIAETIRDALDEF---FPD 267
Cdd:cd06830 199 TDIRRIKSALREAARIyAELRK-LGANLRYLDIGGGLGvdydGSRSSSDSsfnysleeyaNDIVKTVKEICDEAgvpHPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 268 tnkrLIAEPGRFFAAGPFSLVANIIHATEVPaskitkdpkdcadhgYMYYINdgvyGSF-----NCILFDHAHPIgSPLF 342
Cdd:cd06830 278 ----IVTESGRAIVAHHSVLIFEVLGVKRLA---------------DWYFCN----FSLfqslpDSWAIDQLFPI-MPLH 333
|
330
....*....|....*....
gi 17562780 343 DTDRNEKFMSTIWGPTCDS 361
Cdd:cd06830 334 RLNEKPTRRAVLGDITCDS 352
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
171-308 |
1.58e-03 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 40.87 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 171 KFG--ADPIIAAPQLLKtasEEGI--NVVGISFHVGSGCNDASAYRNALQHAKNL-CEIGEgLGFKMDIIDMGGG----F 241
Cdd:PRK05354 222 KFGlsATEVLEAVERLR---EAGLldCLQLLHFHLGSQIANIRDIKTAVREAARFyVELRK-LGAPIQYLDVGGGlgvdY 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 242 PGAEHHNPFEK----------IAETIRDALDEF---FPDtnkrLIAEPGRFFAAgPFS-LVANIIHATEVPASKITKDPK 307
Cdd:PRK05354 298 DGTRSQSDSSVnyslqeyandVVYTLKEICEEHgvpHPT----IISESGRALTA-HHAvLVFNVLGVESQEYEEPPAPAE 372
|
.
gi 17562780 308 D 308
Cdd:PRK05354 373 D 373
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
95-398 |
2.47e-03 |
|
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: 39.84 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 95 DEIDIVMGTgvsAERIIYANPCKTRSFIAHAMDRDVKMMTFDNPEellkiaklHPNAEMILriavSDPTATCPlnlKFGA 174
Cdd:cd06829 81 DEIDEILRL---ADHIIFNSLSQLERFKDRAKAAGISVGLRINPE--------YSEVETDL----YDPCAPGS---RLGV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 175 DPIIAAPQLLktaseEGINvvGISFHVGsgC-NDASAYRNALQHAKNLceIGEGLGfKMDIIDMGGGfpgaeHHnpFEKI 253
Cdd:cd06829 143 TLDELEEEDL-----DGIE--GLHFHTL--CeQDFDALERTLEAVEER--FGEYLP-QLKWLNLGGG-----HH--ITRP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562780 254 A---ETIRDALDEFFPDTNKRLIAEPGRFFAAGPFSLVANI--IHATEVP-----ASkITKDPKDCADhgyMYY----IN 319
Cdd:cd06829 204 DydvDRLIALIKRFKEKYGVEVYLEPGEAVALNTGYLVATVldIVENGMPiaildAS-ATAHMPDVLE---MPYrppiRG 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17562780 320 DGVYGsfncilfDHAHpigsplfdTDRnekfmstIWGPTCDSLDLVEDKKLMPKMNVGEWLYYPDMGAYTLAAATTFNG 398
Cdd:cd06829 280 AGEPG-------EGAH--------TYR-------LGGNSCLAGDVIGDYSFDEPLQVGDRLVFEDMAHYTMVKTNTFNG 336
|
|
| |
