|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
30-391 |
9.22e-168 |
|
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: 473.52 E-value: 9.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFPYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKR 109
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 110 VDVRSFYEQGVRMFASDSEADLRMIAEEAPGSKIYVRILTEGTHtADWPLSRKFGCQNEMAYDLLVLARELGLVPHGISF 189
Cdd:cd00622 82 SDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSG-ALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 190 HVGSQQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYIDKTNELATYAEQITHFLKEDFGDDLPEVILEP 269
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAA-ELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 270 GRSLLSNAGVLVSEVVLISRKSNTALERWVFTDVGKFSGLIETTDEAIKFPIYT----DRTGELDKCVIAGPTCDSADIM 345
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVlkdgGRDGELYPSSLWGPTCDSLDVI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499816765 346 YEHYSygLPKDLAIGDRMFWLTAGAYTTTYSAVcFNGFPPLKDYYL 391
Cdd:cd00622 320 YEDVL--LPEDLAVGDWLLFENMGAYTTAYAST-FNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
32-369 |
9.59e-106 |
|
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: 314.81 E-value: 9.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 32 FVVIDTKIIAKQYDDMVKNF-PYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRV 110
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 111 DVRSFYEQGVRMFASDSEADLRMIAEEAPG--SKIYVRILTE---GTH-TADWPLSRKFGCQNEMAYDLLVLARELGLVP 184
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHkISTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 185 HGISFHVGSQQRDIGAWDSAIGKVKGIYDRLkEEHGIQLKMINLGGGFPANYID-KTNELATYAEQITHFLKEDFGDDLp 263
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRL-RELGIDLKLLDIGGGFGIPYRDePPPDFEEYAAAIREALDEYFPPDL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 264 EVILEPGRSLLSNAGVLVSEVvlISRKSNTAlERWVFTDVGKFSGLIETTDEAiKFPI---YTDRTGELDKCVIAGPTCD 340
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRV--IAVKTGGG-KTFVIVDAGMNDLFRPALYDA-YHPIpvvKEPGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*....
gi 499816765 341 SADIMYEHYSygLPkDLAIGDRMFWLTAG 369
Cdd:pfam00278 315 SGDVLAKDRE--LP-ELEVGDLLAFEDAG 340
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
20-384 |
3.69e-77 |
|
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: 244.29 E-value: 3.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 20 QIKEFAKDKPTPFVVIDTKIIAKQYDDMVKNFPYAN--VYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSA 97
Cdd:COG0019 16 DLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGakVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 98 DRISYGNTIKKRVDVRSFYEQGVRMFASDSEADLRMIAEEAPGS----KIYVRI---LTEGTH--TADWPLSRKFGCQNE 168
Cdd:COG0019 96 ERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELgkraPVGLRVnpgVDAGTHeyISTGGKDSKFGIPLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 169 MAYDLLVLAREL-GLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYI--DKTNELAT 245
Cdd:COG0019 176 DALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-ELGIDLEWLDLGGGLGIPYTegDEPPDLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 246 YAEQITHFLKEDFGDDlPEVILEPGRSLLSNAGVLVSEVvlISRKSNTAlERWVFTDVGkFSGLIETTDEAIKFPIYT-- 323
Cdd:COG0019 255 LAAAIKEALEELCGLG-PELILEPGRALVGNAGVLLTRV--LDVKENGG-RRFVIVDAG-MNDLMRPALYGAYHPIVPvg 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499816765 324 -DRTGELDKCVIAGPTCDSADIMYEHYSygLPkDLAIGDRMFWLTAGAYTTTYSAVcFNGFP 384
Cdd:COG0019 330 rPSGAEAETYDVVGPLCESGDVLGKDRS--LP-PLEPGDLLAFLDAGAYGFSMASN-YNGRP 387
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
30-371 |
4.29e-45 |
|
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: 160.53 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFP-YANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKK 108
Cdd:TIGR01048 25 TPLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 109 RVDVRSFYEQGVrMFASDSEADLRMIAEEAPGSKIYVRIL-------TEGTH--TADWPLSRKFGCQNEMAYDLLVLARE 179
Cdd:TIGR01048 105 RAELERALELGI-CINVDSFSELERLNEIAPELGKKARISlrvnpgvDAKTHpyISTGLKDSKFGIDVEEALEAYLYALQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 180 L-GLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKEehGIQLKMINLGGGFPANYIDKTNELAT--YAEQITHFLKE 256
Cdd:TIGR01048 184 LpHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE--GIDLEFLDLGGGLGIPYTPEEEPPDLseYAQAILNALEG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 257 DFGDDL-PEVILEPGRSLLSNAGVLVSEVVLISRKSNTaleRWVFTDVGkFSGLIETTDEAIKFPIY-TDRTGELDK--C 332
Cdd:TIGR01048 262 YADLGLdPKLILEPGRSIVANAGVLLTRVGFVKETGSR---NFVIVDAG-MNDLIRPALYGAYHHIIvLNRTNDAPTevA 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499816765 333 VIAGPTCDSADImyehysygLPKDLAI-----GDRMFWLTAGAY 371
Cdd:TIGR01048 338 DVVGPVCESGDV--------LAKDRELpevepGDLLAVFDAGAY 373
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
57-371 |
2.77e-15 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 77.81 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 57 YYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSI--GVSADRISYGNTIKKRVDVRSFYEQGVrMFASDSEADLRMI 134
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 135 AEEAPGSKIYVRI---LTEGTH----TADwPLSrKFGCQNEMAYDLLVLARELGLVPHGISFHVGSQQRDIGAWdsaigk 207
Cdd:PRK08961 609 PELFRGREVWLRIdpgHGDGHHekvrTGG-KES-KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHW------ 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 208 vKGIYDRLKE--EHGIQLKMINLGGGFPANYIDKTNELATYA-EQITHFLKEDFGDDlpEVILEPGRSLLSNAGVLVSEV 284
Cdd:PRK08961 681 -RRMADELASfaRRFPDVRTIDLGGGLGIPESAGDEPFDLDAlDAGLAEVKAQHPGY--QLWIEPGRYLVAEAGVLLARV 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 285 VLISRKSNTalerwvftdvgKFSGLIETTDEAIKFPIYTDR-----TGELDK-----CVIAGPTCDSADIMyeHYSYGLP 354
Cdd:PRK08961 758 TQVKEKDGV-----------RRVGLETGMNSLIRPALYGAYheivnLSRLDEpaagtADVVGPICESSDVL--GKRRRLP 824
|
330
....*....|....*..
gi 499816765 355 kDLAIGDRMFWLTAGAY 371
Cdd:PRK08961 825 -ATAEGDVILIANAGAY 840
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
30-391 |
9.22e-168 |
|
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: 473.52 E-value: 9.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFPYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKR 109
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 110 VDVRSFYEQGVRMFASDSEADLRMIAEEAPGSKIYVRILTEGTHtADWPLSRKFGCQNEMAYDLLVLARELGLVPHGISF 189
Cdd:cd00622 82 SDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSG-ALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 190 HVGSQQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYIDKTNELATYAEQITHFLKEDFGDDLPEVILEP 269
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAA-ELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 270 GRSLLSNAGVLVSEVVLISRKSNTALERWVFTDVGKFSGLIETTDEAIKFPIYT----DRTGELDKCVIAGPTCDSADIM 345
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVlkdgGRDGELYPSSLWGPTCDSLDVI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499816765 346 YEHYSygLPKDLAIGDRMFWLTAGAYTTTYSAVcFNGFPPLKDYYL 391
Cdd:cd00622 320 YEDVL--LPEDLAVGDWLLFENMGAYTTAYAST-FNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
32-369 |
9.59e-106 |
|
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: 314.81 E-value: 9.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 32 FVVIDTKIIAKQYDDMVKNF-PYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRV 110
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 111 DVRSFYEQGVRMFASDSEADLRMIAEEAPG--SKIYVRILTE---GTH-TADWPLSRKFGCQNEMAYDLLVLARELGLVP 184
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHkISTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 185 HGISFHVGSQQRDIGAWDSAIGKVKGIYDRLkEEHGIQLKMINLGGGFPANYID-KTNELATYAEQITHFLKEDFGDDLp 263
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRL-RELGIDLKLLDIGGGFGIPYRDePPPDFEEYAAAIREALDEYFPPDL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 264 EVILEPGRSLLSNAGVLVSEVvlISRKSNTAlERWVFTDVGKFSGLIETTDEAiKFPI---YTDRTGELDKCVIAGPTCD 340
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRV--IAVKTGGG-KTFVIVDAGMNDLFRPALYDA-YHPIpvvKEPGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*....
gi 499816765 341 SADIMYEHYSygLPkDLAIGDRMFWLTAG 369
Cdd:pfam00278 315 SGDVLAKDRE--LP-ELEVGDLLAFEDAG 340
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
20-384 |
3.69e-77 |
|
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: 244.29 E-value: 3.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 20 QIKEFAKDKPTPFVVIDTKIIAKQYDDMVKNFPYAN--VYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSA 97
Cdd:COG0019 16 DLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGakVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 98 DRISYGNTIKKRVDVRSFYEQGVRMFASDSEADLRMIAEEAPGS----KIYVRI---LTEGTH--TADWPLSRKFGCQNE 168
Cdd:COG0019 96 ERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELgkraPVGLRVnpgVDAGTHeyISTGGKDSKFGIPLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 169 MAYDLLVLAREL-GLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYI--DKTNELAT 245
Cdd:COG0019 176 DALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-ELGIDLEWLDLGGGLGIPYTegDEPPDLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 246 YAEQITHFLKEDFGDDlPEVILEPGRSLLSNAGVLVSEVvlISRKSNTAlERWVFTDVGkFSGLIETTDEAIKFPIYT-- 323
Cdd:COG0019 255 LAAAIKEALEELCGLG-PELILEPGRALVGNAGVLLTRV--LDVKENGG-RRFVIVDAG-MNDLMRPALYGAYHPIVPvg 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499816765 324 -DRTGELDKCVIAGPTCDSADIMYEHYSygLPkDLAIGDRMFWLTAGAYTTTYSAVcFNGFP 384
Cdd:COG0019 330 rPSGAEAETYDVVGPLCESGDVLGKDRS--LP-PLEPGDLLAFLDAGAYGFSMASN-YNGRP 387
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
30-391 |
1.04e-68 |
|
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: 221.02 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFPY-ANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKK 108
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPSgVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 109 RVDVRSFYEQGVRMFASDSEADLRMIAEEAPGSKIYVRIL----------TEGTHTADWPlsRKFGCQNEMAYDLLVLAR 178
Cdd:cd06810 81 VSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILlrvnpdvsagTHKISTGGLK--SKFGLSLSEARAALERAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 179 ELGLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKEEhGIQLKMINLGGGFPANYIDKTNELATYAEQITHFLKEDF 258
Cdd:cd06810 159 ELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEM-GFPLEMLDLGGGLGIPYDEQPLDFEEYAALINPLLKKYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 259 G-DDLPEVILEPGRSLLSNAGVLVSEVVLISRKSNTaleRWVFTDVGkFSGLIETT-DEAIKFPIYT----DRTGELDKC 332
Cdd:cd06810 238 PnDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGR---FFAVVDGG-MNHSFRPAlAYDAYHPITPlkapGPDEPLVPA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499816765 333 VIAGPTCDSADIMYEHYsygLPKDLAIGDRMFWLTAGAYTTTYSaVCFNGFPPLKDYYL 391
Cdd:cd06810 314 TLAGPLCDSGDVIGRDR---LLPELEVGDLLVFEDMGAYGFSES-SNFNSHPRPAEYLV 368
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
29-371 |
8.36e-62 |
|
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: 203.10 E-value: 8.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 29 PTPFVVIDTKIIAKQYDDMVKNFPYAN--VYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISY-GNt 105
Cdd:cd06828 2 GTPLYVYDEATIRENYRRLKEAFSGPGfkICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFtGN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 106 IKKRVDVRSFYEQGVRMFASDSEADLRMIAEEAP----GSKIYVRI---LTEGTH--TADWPLSRKFGCQNEMAYDLLVL 176
Cdd:cd06828 81 GKSDEELELALELGILRINVDSLSELERLGEIAPelgkGAPVALRVnpgVDAGTHpyISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 177 AREL-GLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYI--DKTNELATYAEQIT-H 252
Cdd:cd06828 161 AKELpGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIPYRdeDEPLDIEEYAEAIAeA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 253 FLKEDFGDDLPEVILEPGRSLLSNAGVLVSEVVLISRKSNTaleRWVFTDVGkFSGLIETT-----DEAIkfPIYTDRTG 327
Cdd:cd06828 240 LKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGK---TFVGVDAG-MNDLIRPAlygayHEIV--PVNKPGEG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499816765 328 ELDKCVIAGPTCDSADIMYEHysYGLPKdLAIGDRMFWLTAGAY 371
Cdd:cd06828 314 ETEKVDVVGPICESGDVFAKD--RELPE-VEEGDLLAIHDAGAY 354
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
40-273 |
2.09e-56 |
|
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: 185.18 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 40 IAKQYDDMVKNFPYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRVDVRSFYEQG 119
Cdd:pfam02784 4 IERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 120 VRMFASDSEADLRMIAEEAPGSKIYVRILTE---GTHtadwPLSRKFGCQ-NEMAYDLLVLARELGLVPHGISFHVGSQQ 195
Cdd:pfam02784 84 VGCVTVDNVDELEKLARLAPEARVLLRIKPDdsaATC----PLSSKFGADlDEDVEALLEAAKLLNLQVVGVSFHVGSGC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 196 RDIGAWDSAIGKVKGIYDRLkEEHGIQLKMINLGGGFPANYIDKTNELAT--YAEQITHFLKEDF-GDDLPEVILEPGRS 272
Cdd:pfam02784 160 TDAEAFVLALEDARGVFDQG-AELGFNLKILDLGGGFGVDYTEGEEPLDFeeYANVINEALEEYFpGDPGVTIIAEPGRY 238
|
.
gi 499816765 273 L 273
Cdd:pfam02784 239 F 239
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
30-371 |
4.29e-45 |
|
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: 160.53 E-value: 4.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFP-YANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKK 108
Cdd:TIGR01048 25 TPLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 109 RVDVRSFYEQGVrMFASDSEADLRMIAEEAPGSKIYVRIL-------TEGTH--TADWPLSRKFGCQNEMAYDLLVLARE 179
Cdd:TIGR01048 105 RAELERALELGI-CINVDSFSELERLNEIAPELGKKARISlrvnpgvDAKTHpyISTGLKDSKFGIDVEEALEAYLYALQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 180 L-GLVPHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKEehGIQLKMINLGGGFPANYIDKTNELAT--YAEQITHFLKE 256
Cdd:TIGR01048 184 LpHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE--GIDLEFLDLGGGLGIPYTPEEEPPDLseYAQAILNALEG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 257 DFGDDL-PEVILEPGRSLLSNAGVLVSEVVLISRKSNTaleRWVFTDVGkFSGLIETTDEAIKFPIY-TDRTGELDK--C 332
Cdd:TIGR01048 262 YADLGLdPKLILEPGRSIVANAGVLLTRVGFVKETGSR---NFVIVDAG-MNDLIRPALYGAYHHIIvLNRTNDAPTevA 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499816765 333 VIAGPTCDSADImyehysygLPKDLAI-----GDRMFWLTAGAY 371
Cdd:TIGR01048 338 DVVGPVCESGDV--------LAKDRELpevepGDLLAVFDAGAY 373
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
30-385 |
2.60e-38 |
|
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: 141.58 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMVKNFPYA-NVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKK 108
Cdd:cd06839 7 TPFYVYDRDRVRERYAALRAALPPAiEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 109 RVDVRSFYEQGVRMFASDSEADLRMIAE--EAPG--SKIYVRIltegthTADWPL----------SRKFGCQNEMAYDLL 174
Cdd:cd06839 87 DAELRRAIEAGIGTINVESLEELERIDAlaEEHGvvARVALRI------NPDFELkgsgmkmgggPSQFGIDVEELPAVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 175 -VLARELGLVPHGISFHVGSQQRD----IGAWDSAIGKVKgiydRLKEEHGIQLKMINLGGGFPANYI--DKTNELATYA 247
Cdd:cd06839 161 aRIAALPNLRFVGLHIYPGTQILDadalIEAFRQTLALAL----RLAEELGLPLEFLDLGGGFGIPYFpgETPLDLEALG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 248 EQItHFLKEDFGDDLPE--VILEPGRSLLSNAGVLVSEVVliSRKSNTAlERWVFTDVG-----KFSGLIETTdeaIK-- 318
Cdd:cd06839 237 AAL-AALLAELGDRLPGtrVVLELGRYLVGEAGVYVTRVL--DRKVSRG-ETFLVTDGGmhhhlAASGNFGQV---LRrn 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 319 FPIYTDR---TGELDKCVIAGPTCDSADIMYEhySYGLPKdLAIGDRMFWLTAGAYTTTYSAVCFNGFPP 385
Cdd:cd06839 310 YPLAILNrmgGEERETVTVVGPLCTPLDLLGR--NVELPP-LEPGDLVAVLQSGAYGLSASPLAFLSHPA 376
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
30-376 |
2.54e-34 |
|
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: 130.46 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFVVIDTKIIAKQYDDMV----KNFPYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNT 105
Cdd:cd06841 7 SPFFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 106 IKKRVDVRSFYEQGVrMFASDSEADLRMIAEEAPGSKIYVRI-LTEGTHTADWPLSRkFGCQNEMAYDLLVLARELGLVP 184
Cdd:cd06841 87 YKSKEELEKALEEGA-LINIDSFDELERILEIAKELGRVAKVgIRLNMNYGNNVWSR-FGFDIEENGEALAALKKIQESK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 185 H----GISFHVGSQQRDIGAWDSAigkVKGIYDRLKEEHGIQLKMINLGGGFPAN--------YIDKTNELATYAEQITH 252
Cdd:cd06841 165 NlslvGLHCHVGSNILNPEAYSAA---AKKLIELLDRLFGLELEYLDLGGGFPAKtplslaypQEDTVPDPEDYAEAIAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 253 FLKEDFGDDL--PEVILEPGRSLLSNAGVLVSEVVLISRKSNtalERWVFTDVGKFS-GLIETTDEAIKFPIYTDRTGEL 329
Cdd:cd06841 242 TLKEYYANKEnkPKLILEPGRALVDDAGYLLGRVVAVKNRYG---RNIAVTDAGINNiPTIFWYHHPILVLRPGKEDPTS 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499816765 330 DKCVIAGPTCDSADIMYEHYSYglpKDLAIGDRMFWLTAGAYTTTYS 376
Cdd:cd06841 319 KNYDVYGFNCMESDVLFPNVPL---PPLNVGDILAIRNVGAYNMTQS 362
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
40-271 |
4.20e-27 |
|
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: 107.02 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 40 IAKQYDDMVKNFPY-ANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRVDVRSFYEQ 118
Cdd:cd06808 1 IRHNYRRLREAAPAgITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 119 GVRMFASDSEADLRMIAE----EAPGSKIYVRILTEgthtadwPLSRKFGCQNEMAYDLLVLAREL-GLVPHGISFHVGS 193
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEaalkAGPPARVLLRIDTG-------DENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499816765 194 QQRDIGAWDSAIGKVKGIYDRLKeEHGIQLKMINLGGGFPANYIDKtnelatyaeqithflkedfGDDLPEVILEPGR 271
Cdd:cd06808 154 ADEDYSPFVEALSRFVAALDQLG-ELGIDLEQLSIGGSFAILYLQE-------------------LPLGTFIIVEPGR 211
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
32-391 |
4.26e-24 |
|
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: 102.62 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 32 FVVIDTKIIAKQYDDMVKNFPYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRVD 111
Cdd:cd06831 15 FFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 112 VRSFYEQGVRMFASDSEADLRMIAEEAPGSKIYVRILTEGtHTADWPLSRKFGCQNEMAYDLLVLARELGLVPHGISFHV 191
Cdd:cd06831 95 IKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATED-NIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 192 GSQQRDIGAWDSAIGKVKGIYDrLKEEHGIQLKMINLGGGFPANYIDktnelatyAEQITHFLKEDFGDDLPE-----VI 266
Cdd:cd06831 174 SSSCKEYQTYVHALSDARCVFD-MAEEFGFKMNMLDIGGGFTGSEIQ--------LEEVNHVIRPLLDVYFPEgsgiqII 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 267 LEPGRSLLSNAGVLVSEVV---------LISRKSNTALERWVFTD----------VGKFSGLIETTDEAIKF-----PIY 322
Cdd:cd06831 245 AEPGSYYVSSAFTLAVNVIakkavendkHLSSVEKNGSDEPAFVYymndgvygsfASKLSEKLNTTPEVHKKykedePLF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499816765 323 TDRtgeldkcvIAGPTCDSADIMYEHYsygLPKDLAIGDRMFWLTAGAYTTTYSAVcFNGF--PPLkdYYL 391
Cdd:cd06831 325 TSS--------LWGPSCDELDQIVESC---LLPELNVGDWLIFDNMGAGSLHEPST-FNDFqrPAI--YYM 381
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
30-389 |
8.54e-21 |
|
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: 92.84 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 30 TPFV-VIDTKIIAKQYDDMVKNFPyANVYY--AVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTI 106
Cdd:cd06836 2 HPAVgLYDLDGFRALVARLTAAFP-APVLHtfAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 107 KKRVDVRSFYEQGVRMFASDSEA----DLRMIAEEAPGSKIYVRI-----------LTEGTHTADWPLSRKFGCQNEM-- 169
Cdd:cd06836 81 KTRAELREALELGVAINIDNFQEleriDALVAEFKEASSRIGLRVnpqvgagkigaLSTATATSKFGVALEDGARDEIid 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 170 AYdllvlARELGLvpHGISFHVGSQQRDIGAWDSAIGKVKGIYDRLKEEHG-IQLKMINLGGGFPANY--IDKTNELATY 246
Cdd:cd06836 161 AF-----ARRPWL--NGLHVHVGSQGCELSLLAEGIRRVVDLAEEINRRVGrRQITRIDIGGGLPVNFesEDITPTFADY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 247 AEQITHFLKEDFgDDLPEVILEPGRSLLSNAGVLVSEV----------VLISRKSNTALERWVFtdvgkfsgliETTDEA 316
Cdd:cd06836 234 AAALKAAVPELF-DGRYQLVTEFGRSLLAKCGTIVSRVeytkssggrrIAITHAGAQVATRTAY----------APDDWP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499816765 317 IKFPIYT----DRTGELDKCVIAGPTCDSADIMYEHYSygLPKdLAIGDRMFWLTAGAYT-TTYSAVCFNGFPPLKDY 389
Cdd:cd06836 303 LRVTVFDangePKTGPEVVTDVAGPCCFAGDVLAKERA--LPP-LEPGDYVAVHDTGAYYfSSHSSYNSLPRPAVYGV 377
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
52-289 |
3.64e-19 |
|
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: 88.11 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 52 PYANVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSAdRISYGNTIKKRVDVRSFYEQGVRMFASDSEADL 131
Cdd:cd06843 25 PGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDA-PLIFGGPGKTDSELAQALAQGVERIHVESELEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 132 RMIAEEAPGSKIYVRILTEGTHTADWPLSRK---------FGCQNEMAYDLLVLAREL-GLVPHGISFHVGSQQRDIGAW 201
Cdd:cd06843 104 RRLNAVARRAGRTAPVLLRVNLALPDLPSSTltmggqptpFGIDEADLPDALELLRDLpNIRLRGFHFHLMSHNLDAAAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 202 DSAIGKVKGIYDRLKEEHGIQLKMINLGGGFPANYIDKTN--ELATYAEQItHFLKEDFGDDLpEVILEPGRSLLSNAGV 279
Cdd:cd06843 184 LALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADPEEqfDWAGFCEGL-DQLLAEYEPGL-TLRFECGRYISAYCGY 261
|
250
....*....|
gi 499816765 280 LVSEVVLISR 289
Cdd:cd06843 262 YVTEVLDLKR 271
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
57-371 |
8.51e-16 |
|
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: 77.86 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 57 YYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSI--GVSADRISYGNTIKKRVDVRSFYEQGVRMFASDSEAdLRMI 134
Cdd:cd06840 39 FYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNVTVDNLHP-LREW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 135 AEEAPGSKIYVRI---LTEGTH----TADwPLSrKFGC-QNEMAyDLLVLARELGLVPHGISFHVGSQQRDIGAWdsaig 206
Cdd:cd06840 118 PELFRGREVILRIdpgQGEGHHkhvrTGG-PES-KFGLdVDELD-EARDLAKKAGIIVIGLHAHSGSGVEDTDHW----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 207 kvKGIYDRLKE--EHGIQLKMINLGGGFPANYI--DKTNELATYAEQITHfLKEDFGDdlPEVILEPGRSLLSNAGVLVS 282
Cdd:cd06840 190 --ARHGDYLASlaRHFPAVRILNVGGGLGIPEApgGRPIDLDALDAALAA-AKAAHPQ--YQLWMEPGRFIVAESGVLLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 283 EVVLISRKSNTalerwvftdvgKFSGLIETTDEAIKFPIY--------TDRTGELDK--CVIAGPTCDSADIMyeHYSYG 352
Cdd:cd06840 265 RVTQIKHKDGV-----------RFVGLETGMNSLIRPALYgayheivnLSRLDEPPAgnADVVGPICESGDVL--GRDRL 331
|
330
....*....|....*....
gi 499816765 353 LPkDLAIGDRMFWLTAGAY 371
Cdd:cd06840 332 LP-ETEEGDVILIANAGAY 349
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
57-371 |
2.77e-15 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 77.81 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 57 YYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSI--GVSADRISYGNTIKKRVDVRSFYEQGVrMFASDSEADLRMI 134
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 135 AEEAPGSKIYVRI---LTEGTH----TADwPLSrKFGCQNEMAYDLLVLARELGLVPHGISFHVGSQQRDIGAWdsaigk 207
Cdd:PRK08961 609 PELFRGREVWLRIdpgHGDGHHekvrTGG-KES-KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHW------ 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 208 vKGIYDRLKE--EHGIQLKMINLGGGFPANYIDKTNELATYA-EQITHFLKEDFGDDlpEVILEPGRSLLSNAGVLVSEV 284
Cdd:PRK08961 681 -RRMADELASfaRRFPDVRTIDLGGGLGIPESAGDEPFDLDAlDAGLAEVKAQHPGY--QLWIEPGRYLVAEAGVLLARV 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 285 VLISRKSNTalerwvftdvgKFSGLIETTDEAIKFPIYTDR-----TGELDK-----CVIAGPTCDSADIMyeHYSYGLP 354
Cdd:PRK08961 758 TQVKEKDGV-----------RRVGLETGMNSLIRPALYGAYheivnLSRLDEpaagtADVVGPICESSDVL--GKRRRLP 824
|
330
....*....|....*..
gi 499816765 355 kDLAIGDRMFWLTAGAY 371
Cdd:PRK08961 825 -ATAEGDVILIANAGAY 840
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
55-292 |
2.47e-14 |
|
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: 73.83 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 55 NVYYAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKrvdvRSFYEQGVR---MFASDSEADL 131
Cdd:cd06842 39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKT----DEFLWLAVRhgaTIAVDSLDEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 132 RMIAEEAPGSKIY-VRILTEGTHTADWPLSRkFGCQNEMAYDLLVLARELGLVPH--GISFHVG---SQQRdigawDSAI 205
Cdd:cd06842 115 DRLLALARGYTTGpARVLLRLSPFPASLPSR-FGMPAAEVRTALERLAQLRERVRlvGFHFHLDgysAAQR-----VAAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 206 GKVKGIYDRLKeEHGIQLKMINLGGGFPANYIDKTNELATYAEQITHFL------------------KEDF--------- 258
Cdd:cd06842 189 QECLPLIDRAR-ALGLAPRFIDIGGGFPVSYLADAAEWEAFLAALTEALygygrpltwrneggtlrgPDDFypygqplva 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499816765 259 GDDLPEVI----------------------LEPGRSLLSNAGVLVSEVVLISRKSN 292
Cdd:cd06842 268 ADWLRAILsaplpqgrtiaerlrdngitlaLEPGRALLDQCGLTVARVAFVKQLGD 323
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
58-371 |
2.09e-12 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 67.90 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 58 YAVKANPAKEVLTLLRDKGSNFDIASIYELEMVTSIGVSADRISYGNTIKKRVDVRSFYEQGVrMFASDSEADLRMIAEE 137
Cdd:PLN02537 48 YAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 138 A--PGSKIYV--RILTE-----GTHTADWPLSRKFGCQNEMAYDLLVLAR----ELGLVphGISFHVGSQQRDIGAWDSA 204
Cdd:PLN02537 127 AriAGKKVNVllRINPDvdpqvHPYVATGNKNSKFGIRNEKLQWFLDAVKahpnELKLV--GAHCHLGSTITKVDIFRDA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 205 IGKVKGIYDRLKEEhGIQLKMINLGGGFPANYIDKTNELATYAEQITHFLKEDFGDDLpEVILEPGRSLLSNAGVLVSEV 284
Cdd:PLN02537 205 AVLMVNYVDEIRAQ-GFELSYLNIGGGLGIDYYHAGAVLPTPRDLIDTVRELVLSRDL-TLIIEPGRSLIANTCCFVNRV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 285 VLIsrKSNtALERWVFTDvGKFSGLIETT----DEAIKFPIYTDRTGELDKCVIAGPTCDSADIMYEHYSYGLPKDlaiG 360
Cdd:PLN02537 283 TGV--KTN-GTKNFIVID-GSMAELIRPSlydaYQHIELVSPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPK---G 355
|
330
....*....|.
gi 499816765 361 DRMFWLTAGAY 371
Cdd:PLN02537 356 AGLVVHDAGAY 366
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
53-345 |
5.93e-12 |
|
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: 66.44 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 53 YANVY---YAVKANPAKEVLTLLRDKGSNFDI----ASIYELEMVTSIGVSADRISYGNTIKKRvdvrSFYE---QGVRM 122
Cdd:cd06830 35 YKGKYqgvYPIKVNQQREVVEEIVKAGKRYNIgleaGSKPELLAALALLKTPDALIICNGYKDD----EYIElalLARKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 123 FAS-----DSEADLRMIAEEA------PgsKIYVRILTEGTHTADW----PLSRKFGCQ-NEM--AYDLLvlaRELGLVP 184
Cdd:cd06830 111 GHNviiviEKLSELDLILELAkklgvkP--LLGVRIKLASKGSGKWqesgGDRSKFGLTaSEIleVVEKL---KEAGMLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 185 -----HgisFHVGSQQRDIGAWDSAIGKVKGIYDRLKEEhGIQLKMINLGGGFPANYI-DKTNE-------LATYAEQIT 251
Cdd:cd06830 186 rlkllH---FHIGSQITDIRRIKSALREAARIYAELRKL-GANLRYLDIGGGLGVDYDgSRSSSdssfnysLEEYANDIV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 252 HFLKE---DFGDDLPEVILEPGRSLLSNAGVLVSEVVLISRksntaLERWVFTDVGKFSGLIETTdeAI--KFPI----- 321
Cdd:cd06830 262 KTVKEicdEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKR-----LADWYFCNFSLFQSLPDSW--AIdqLFPImplhr 334
|
330 340
....*....|....*....|....*..
gi 499816765 322 ---YTDRtgeldKCVIAGPTCDSADIM 345
Cdd:cd06830 335 lneKPTR-----RAVLGDITCDSDGKI 356
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
222-384 |
1.56e-08 |
|
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: 55.63 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 222 QLKMINLGGGF----PANYIDKtnelatYAEQITHFlKEDFGddlPEVILEPGRSLLSNAGVLVSEVV-LISRKSNTALe 296
Cdd:cd06829 188 QLKWLNLGGGHhitrPDYDVDR------LIALIKRF-KEKYG---VEVYLEPGEAVALNTGYLVATVLdIVENGMPIAI- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 297 rwvfTDVGkFSGLIETTDEAIKFPIYTD--RTGELDKCV-IAGPTCDSADIMYEhysYGLPKDLAIGDRMFWLTAGAYT- 372
Cdd:cd06829 257 ----LDAS-ATAHMPDVLEMPYRPPIRGagEPGEGAHTYrLGGNSCLAGDVIGD---YSFDEPLQVGDRLVFEDMAHYTm 328
|
170
....*....|....
gi 499816765 373 --TTYsavcFNGFP 384
Cdd:cd06829 329 vkTNT----FNGVR 338
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
189-285 |
3.84e-03 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 39.28 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499816765 189 FHVGSQQRDIGAWDSAIGKVKGIYDRLKEEhGIQLKMINLGGGFPANYiDKTN----------ELATYAEQITHFLKE-- 256
Cdd:PLN02439 188 FHIGSQIPSTSLLKDGVSEAAQIYCELVRL-GAPMRVIDIGGGLGIDY-DGSKsgssdmsvaySLEEYANAVVAAVRDvc 265
|
90 100 110
....*....|....*....|....*....|
gi 499816765 257 -DFGDDLPEVILEPGRSLLSNAGVLVSEVV 285
Cdd:PLN02439 266 dRKGVKHPVICSESGRALVSHHSVLIFEAV 295
|
|
| |
