|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-408 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.
Pssm-ID: 143482 [Multi-domain] Cd Length: 362 Bit Score: 627.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 197 HVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDT-KLKFEEITSVINPALDKYFPSDsGVRIIAEP 275
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvVPSFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 276 GRYYVASAFTLAVNIIAKKTVWKEQPgsddedesneqTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSI 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDDR-----------ERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 131888589 356 WGPTCDGLDRIVERCNLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYV 408
Cdd:cd00622 309 WGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-387 |
4.15e-154 |
|
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.
Pssm-ID: 459745 [Multi-domain] Cd Length: 340 Bit Score: 440.77 E-value: 4.15e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLGDILKKHLRWLKAL-PRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVS 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 119 QIKYAASNGVQMMTFDSEIELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLKTSRLLLERAKELNIDV 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 192 IGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGS--EDTKLKFEEITSVINPALDKYFPSDsgV 269
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 270 RIIAEPGRYYVASAFTLAVNIIAKKTvwkeqpgsddedesNEQTFMYYVNDGVYGSFNCILYDHAHVKALlqKRPKPDEK 349
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 131888589 350 YYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMG 387
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-408 |
1.35e-71 |
|
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: 232.35 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLgDILKKHLRWLK-ALPR--VTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:COG0019 28 LYVYDE-AALRRNLRALReAFPGsgAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLKTSRLLLERAKE 186
Cdd:COG0019 107 EEELEEALELGVGHINVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 187 L-NIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFP---GSEDTKLKFEEITSVINPALDKY 262
Cdd:COG0019 187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 263 FpsDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFmYYVNdgvyGSFNC----ILYDHAHVKA 338
Cdd:COG0019 267 C--GLGPELILEPGRALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGAYHPIV 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 339 LLQKRPKPDEKYYssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYV 408
Cdd:COG0019 327 PVGRPSGAEAETY--DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV 394
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
40-403 |
1.12e-40 |
|
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: 150.13 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLgDILKKHLRWLK-ALPRVT-PFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQV 117
Cdd:TIGR01048 27 LYVYDE-DTIRRRFRAYKeAFGGRSlVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 118 SQIKYAASNGVqMMTFDSEIELM---KVARAH-PKAKLVLRIATD-DSKAVCRLSV-----KFGATLKTSRLLLERAKEL 187
Cdd:TIGR01048 106 AELERALELGI-CINVDSFSELErlnEIAPELgKKARISLRVNPGvDAKTHPYISTglkdsKFGIDVEEALEAYLYALQL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 188 -NIDVIGVSFHVGSGCTDPETFVQAvsdARCVFDMATEVGFSMHL--LDIGGGFPGS---EDTKLKFEEITSVINPALDK 261
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEA---AEKVVKLAESLAEGIDLefLDLGGGLGIPytpEEEPPDLSEYAQAILNALEG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 262 YFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFMyyvndGVYGSFN----CILYD--HaH 335
Cdd:TIGR01048 262 YADLGLDPKLILEPGRSIVANAGVLLTRVGFVK-------------ETGSRNFV-----IVDAGMNdlirPALYGayH-H 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 131888589 336 VKALLQKRPKPDEKYyssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRP 403
Cdd:TIGR01048 323 IIVLNRTNDAPTEVA---DVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRP 387
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
34-403 |
2.74e-27 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 115.56 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 34 SDDKDAFYVADLGdILKKHLRWLKALPRVTP-FYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGL--GVPAERVIY 110
Cdd:PRK08961 499 SDAGSPCYVYHLP-TVRARARALAALAAVDQrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 111 ANPCKQVSQIKYAASNGVqMMTFDSEIELmkvaRAHPKA----KLVLRI--------------ATDDSKavcrlsvkFGA 172
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGV-TVTLDNVEPL----RNWPELfrgrEVWLRIdpghgdghhekvrtGGKESK--------FGL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 173 TLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAvsdARCVFDMATEVGfSMHLLDIGGGFP---GSEDTKLKFE 249
Cdd:PRK08961 645 SQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEPFDLD 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 250 eitsVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKTVWKEQPGsddedesneqtfMYYVndGVYGSFNCI 329
Cdd:PRK08961 721 ----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETGMNSL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 131888589 330 ----LYDHAHVKALLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNgfQRP 403
Cdd:PRK08961 779 irpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-408 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.
Pssm-ID: 143482 [Multi-domain] Cd Length: 362 Bit Score: 627.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 197 HVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDT-KLKFEEITSVINPALDKYFPSDsGVRIIAEP 275
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvVPSFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 276 GRYYVASAFTLAVNIIAKKTVWKEQPgsddedesneqTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSI 355
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDDR-----------ERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 131888589 356 WGPTCDGLDRIVERCNLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYV 408
Cdd:cd00622 309 WGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
37-419 |
8.44e-167 |
|
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: 475.11 E-value: 8.44e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 37 KDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:cd06831 12 KNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSF 196
Cdd:cd06831 92 ASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 197 HVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEdtkLKFEEITSVINPALDKYFPSDSGVRIIAEPG 276
Cdd:cd06831 172 HVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 277 RYYVASAFTLAVNIIAKKTVWKEQ-PGSDDEDESNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSI 355
Cdd:cd06831 249 SYYVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131888589 356 WGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYVMSRPMWQLMKQ 419
Cdd:cd06831 329 WGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQD 392
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-387 |
4.15e-154 |
|
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.
Pssm-ID: 459745 [Multi-domain] Cd Length: 340 Bit Score: 440.77 E-value: 4.15e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLGDILKKHLRWLKAL-PRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVS 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 119 QIKYAASNGVQMMTFDSEIELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLKTSRLLLERAKELNIDV 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 192 IGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGS--EDTKLKFEEITSVINPALDKYFPSDsgV 269
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 270 RIIAEPGRYYVASAFTLAVNIIAKKTvwkeqpgsddedesNEQTFMYYVNDGVYGSFNCILYDHAHVKALlqKRPKPDEK 349
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 131888589 350 YYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMG 387
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
38-408 |
2.05e-148 |
|
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: 427.49 E-value: 2.05e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 38 DAFYVADLGDILKKHLRWLKALP-RVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAH----PKAKLVLRIATDDSK-----AVCRLSVKFGATLKTSRLLLERAKEL 187
Cdd:cd06810 81 VSEIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSAgthkiSTGGLKSKFGLSLSEARAALERAKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 188 NIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTK-LKFEEITSVINPALDKYFPSD 266
Cdd:cd06810 161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQpLDFEEYAALINPLLKKYFPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 267 SGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedeSNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKP 346
Cdd:cd06810 241 PGVTLILEPGRYIVAQAGVLVTRVVAVK--------------VNGGRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 131888589 347 DEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYV 408
Cdd:cd06810 307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
45-281 |
2.11e-129 |
|
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.
Pssm-ID: 397077 [Multi-domain] Cd Length: 241 Bit Score: 374.31 E-value: 2.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 45 LGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAA 124
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 125 SNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATL-KTSRLLLERAKELNIDVIGVSFHVGSGCT 203
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 204 DPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFpGSEDT----KLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYY 279
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeePLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239
|
..
gi 131888589 280 VA 281
Cdd:pfam02784 240 VA 241
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-408 |
1.35e-71 |
|
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: 232.35 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLgDILKKHLRWLK-ALPR--VTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQ 116
Cdd:COG0019 28 LYVYDE-AALRRNLRALReAFPGsgAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 117 VSQIKYAASNGVQMMTFDSEIELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLKTSRLLLERAKE 186
Cdd:COG0019 107 EEELEEALELGVGHINVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 187 L-NIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFP---GSEDTKLKFEEITSVINPALDKY 262
Cdd:COG0019 187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 263 FpsDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFmYYVNdgvyGSFNC----ILYDHAHVKA 338
Cdd:COG0019 267 C--GLGPELILEPGRALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGAYHPIV 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 339 LLQKRPKPDEKYYssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYV 408
Cdd:COG0019 327 PVGRPSGAEAETY--DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV 394
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
48-277 |
4.75e-61 |
|
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: 197.93 E-value: 4.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 48 ILKKHLRWLKALP-RVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASN 126
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 127 GVQMMTFDSEIELMKVARAH----PKAKLVLRIATDDskavcrLSVKFGATLKTSRLLLERAKELN-IDVIGVSFHVGSG 201
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 131888589 202 CTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTKLkfeeitsvinpaldkyfpsDSGVRIIAEPGR 277
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL-------------------PLGTFIIVEPGR 211
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
40-403 |
4.30e-54 |
|
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: 184.99 E-value: 4.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLGDILKKHLRWLKAL--PRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQV 117
Cdd:cd06828 5 LYVYDEATIRENYRRLKEAFsgPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 118 SQIKYAASNGVQMMTFDSEIELMKVARAHP----KAKLVLRIATD-DSKAVCRLSV-----KFGATLKTSRLLLERAKEL 187
Cdd:cd06828 85 EELELALELGILRINVDSLSELERLGEIAPelgkGAPVALRVNPGvDAGTHPYISTggkdsKFGIPLEQALEAYRRAKEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 188 -NIDVIGVSFHVGSGCTDPETFVQAvsdARCVFDMATEV---GFSMHLLDIGGGFP---GSEDTKLKFEEITSVINPALD 260
Cdd:cd06828 165 pGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLGipyRDEDEPLDIEEYAEAIAEALK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 261 KYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFMyyvndGVYGSFNCI----LYDHAHV 336
Cdd:cd06828 242 ELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVK-------------ETGGKTFV-----GVDAGMNDLirpaLYGAYHE 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 131888589 337 KALLQKRPKPDEKYYssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRP 403
Cdd:cd06828 304 IVPVNKPGEGETEKV--DVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRP 368
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
40-403 |
1.12e-40 |
|
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: 150.13 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLgDILKKHLRWLK-ALPRVT-PFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQV 117
Cdd:TIGR01048 27 LYVYDE-DTIRRRFRAYKeAFGGRSlVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 118 SQIKYAASNGVqMMTFDSEIELM---KVARAH-PKAKLVLRIATD-DSKAVCRLSV-----KFGATLKTSRLLLERAKEL 187
Cdd:TIGR01048 106 AELERALELGI-CINVDSFSELErlnEIAPELgKKARISLRVNPGvDAKTHPYISTglkdsKFGIDVEEALEAYLYALQL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 188 -NIDVIGVSFHVGSGCTDPETFVQAvsdARCVFDMATEVGFSMHL--LDIGGGFPGS---EDTKLKFEEITSVINPALDK 261
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEA---AEKVVKLAESLAEGIDLefLDLGGGLGIPytpEEEPPDLSEYAQAILNALEG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 262 YFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFMyyvndGVYGSFN----CILYD--HaH 335
Cdd:TIGR01048 262 YADLGLDPKLILEPGRSIVANAGVLLTRVGFVK-------------ETGSRNFV-----IVDAGMNdlirPALYGayH-H 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 131888589 336 VKALLQKRPKPDEKYyssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRP 403
Cdd:TIGR01048 323 IIVLNRTNDAPTEVA---DVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRP 387
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
40-393 |
1.93e-36 |
|
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: 138.11 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 40 FYVADLgDILKKHLRWL-KALPRVTP-FYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQV 117
Cdd:cd06839 9 FYVYDR-DRVRERYAALrAALPPAIEiYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 118 SQIKYAASNGVQMMTFDSEIELMKVARAHPK----AKLVLRIATDDSKAVCRLSVKFGAT---LKTSRL---LLERAKEL 187
Cdd:cd06839 88 AELRRAIEAGIGTINVESLEELERIDALAEEhgvvARVALRINPDFELKGSGMKMGGGPSqfgIDVEELpavLARIAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 188 NIDVIGVSFHVGSGCTDPETFVQAVSDARCVF-DMATEVGFSMHLLDIGGGF--P-GSEDTKLKFEEITSVINPALDKYF 263
Cdd:cd06839 168 NLRFVGLHIYPGTQILDADALIEAFRQTLALAlRLAEELGLPLEFLDLGGGFgiPyFPGETPLDLEALGAALAALLAELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 264 PSDSGVRIIAEPGRYYVASAFTLAVNIIAKKtvwkeqpgsddedESNEQTFmyYVNDG-------VYGSFNCILYDHAHV 336
Cdd:cd06839 248 DRLPGTRVVLELGRYLVGEAGVYVTRVLDRK-------------VSRGETF--LVTDGgmhhhlaASGNFGQVLRRNYPL 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 131888589 337 KALLQKRPKPDEKYyssSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAA 393
Cdd:cd06839 313 AILNRMGGEERETV---TVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLSA 366
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
34-406 |
1.18e-31 |
|
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: 124.68 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 34 SDDKDAFYVADLGDILKKHLRWLKALPRVTP----FYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVI 109
Cdd:cd06841 3 ESYGSPFFVFDEDALRENYRELLGAFKKRYPnvviAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 110 YANPCKQVSQIKYAASNG--VQMMTFDSEIELMKVARAHP-KAKLVLRIATDDSKAVcrLSvKFGATLKTSRLLLERAKE 186
Cdd:cd06841 83 FNGPYKSKEELEKALEEGalINIDSFDELERILEIAKELGrVAKVGIRLNMNYGNNV--WS-RFGFDIEENGEALAALKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 187 L----NIDVIGVSFHVGSGCTDPETFVQAVSDarCVFDMATEVGFSMHLLDIGGGFPGSEDTKLK---------FEEITS 253
Cdd:cd06841 160 IqeskNLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAKTPLSLAypqedtvpdPEDYAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 254 VINPALDKYFPSDSG-VRIIAEPGRYYVASAFTLAVNIIAKKtvwkEQPGSDdedesneqtfmYYVNDGVYGSFNCILYD 332
Cdd:cd06841 238 AIASTLKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVK----NRYGRN-----------IAVTDAGINNIPTIFWY 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 131888589 333 HAHVKALlqkRPKPDEKYYSSS-IWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNgFQRPNIY 406
Cdd:cd06841 303 HHPILVL---RPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFI-RPRPAVY 373
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
34-403 |
2.74e-27 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 115.56 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 34 SDDKDAFYVADLGdILKKHLRWLKALPRVTP-FYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGL--GVPAERVIY 110
Cdd:PRK08961 499 SDAGSPCYVYHLP-TVRARARALAALAAVDQrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 111 ANPCKQVSQIKYAASNGVqMMTFDSEIELmkvaRAHPKA----KLVLRI--------------ATDDSKavcrlsvkFGA 172
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGV-TVTLDNVEPL----RNWPELfrgrEVWLRIdpghgdghhekvrtGGKESK--------FGL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 173 TLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAvsdARCVFDMATEVGfSMHLLDIGGGFP---GSEDTKLKFE 249
Cdd:PRK08961 645 SQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEPFDLD 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 250 eitsVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKTVWKEQPGsddedesneqtfMYYVndGVYGSFNCI 329
Cdd:PRK08961 721 ----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETGMNSL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 131888589 330 ----LYDHAHVKALLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNgfQRP 403
Cdd:PRK08961 779 irpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
34-398 |
4.50e-22 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.
Pssm-ID: 143507 [Multi-domain] Cd Length: 368 Bit Score: 97.12 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 34 SDDKDAFYVADLgDILKKHLRWLKALPRV-TPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGL--GVPAERVIY 110
Cdd:cd06840 8 APDVGPCYVYDL-ETVRARARQVSALKAVdSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 111 ANPCKQVSQIKYAASNGVQmMTFDSeielMKVARAHPK----AKLVLRI------------ATDDSKAvcrlsvKFGATL 174
Cdd:cd06840 87 TPNFAARSEYEQALELGVN-VTVDN----LHPLREWPElfrgREVILRIdpgqgeghhkhvRTGGPES------KFGLDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 175 KTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDarcVFDMATEVGfSMHLLDIGGGFP---GSEDTKLKFEEI 251
Cdd:cd06840 156 DELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDY---LASLARHFP-AVRILNVGGGLGipeAPGGRPIDLDAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 252 TSVINpALDKYFPsdsGVRIIAEPGRYYVASAFTLavniIAKKTVWKEQPGsddedesneqTFMYYVNDGVYGSFNCILY 331
Cdd:cd06840 232 DAALA-AAKAAHP---QYQLWMEPGRFIVAESGVL----LARVTQIKHKDG----------VRFVGLETGMNSLIRPALY 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 131888589 332 DHAHVKALLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFN 398
Cdd:cd06840 294 GAYHEIVNLSRLDEP--PAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
63-239 |
1.20e-21 |
|
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: 96.56 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 63 TPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASNGVqMMTFDSEIELMKV 142
Cdd:cd06842 39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 143 -----ARAHPKAKLVLRIATDDSKAVCRlsvkFGATLKTSRLLLERAKELN--IDVIGVSFHVGSgcTDPETFVQAVSDA 215
Cdd:cd06842 118 lalarGYTTGPARVLLRLSPFPASLPSR----FGMPAAEVRTALERLAQLRerVRLVGFHFHLDG--YSAAQRVAALQEC 191
|
170 180
....*....|....*....|....
gi 131888589 216 RCVFDMATEVGFSMHLLDIGGGFP 239
Cdd:cd06842 192 LPLIDRARALGLAPRFIDIGGGFP 215
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
25-408 |
6.36e-20 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 91.39 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 25 DQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP--RVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLG 102
Cdd:PLN02537 5 GLRVQDIMESVEKRPFYLYSKPQITRNYEAYKEALEglRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 103 VPAERVIYANPCKQVSQIKYAASNGVqMMTFDSEIELMKVARAH----PKAKLVLRIATD-DSK-----AVCRLSVKFGA 172
Cdd:PLN02537 85 FDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAAriagKKVNVLLRINPDvDPQvhpyvATGNKNSKFGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 173 TLKTSRLLLE--RAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGF-----------P 239
Cdd:PLN02537 164 RNEKLQWFLDavKAHPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLgidyyhagavlP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 240 GSEDTklkfeeITSVINPALDKyfpsdsGVRIIAEPGRYYVASAFTLAVNIIAKKTvwkeqpgsddedesnEQTFMYYVN 319
Cdd:PLN02537 244 TPRDL------IDTVRELVLSR------DLTLIIEPGRSLIANTCCFVNRVTGVKT---------------NGTKNFIVI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 320 DGVYGSF-NCILYD-HAHVKalLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTF 397
Cdd:PLN02537 297 DGSMAELiRPSLYDaYQHIE--LVSPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTY 374
|
410
....*....|.
gi 131888589 398 NGFQRPNIYYV 408
Cdd:PLN02537 375 NLKMRPPEYWV 385
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
41-281 |
9.13e-20 |
|
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: 90.42 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 41 YVADLgDILKKHLRWLKA-LP-RVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLgVPAERVIYANPCKQVS 118
Cdd:cd06843 5 YVYDL-AALRAHARALRAsLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 119 QIKYAASNGVQMMTFDSEIELMK---VARAHPK-AKLVLR--IATDDSKAvCRLSV-----KFGatLKTSRL--LLERAK 185
Cdd:cd06843 83 ELAQALAQGVERIHVESELELRRlnaVARRAGRtAPVLLRvnLALPDLPS-STLTMggqptPFG--IDEADLpdALELLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 186 EL-NIDVIGVSFHVGSGCTDPETFVQAVSD-ARCVFDMATEVGFSMHLLDIGGGF------PgseDTKLKFEEITSVINP 257
Cdd:cd06843 160 DLpNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGIgvnyadP---EEQFDWAGFCEGLDQ 236
|
250 260
....*....|....*....|....
gi 131888589 258 ALDKYFPsdsGVRIIAEPGRYYVA 281
Cdd:cd06843 237 LLAEYEP---GLTLRFECGRYISA 257
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
67-406 |
1.32e-17 |
|
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: 84.37 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 67 AVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASNGVQMM--TFDsEIELMKVAR 144
Cdd:cd06836 33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAINidNFQ-ELERIDALV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 145 AH---PKAKLVLRI-------ATDDSKAVCRLSvKFGATLKtsrlllERAKELNIDVI-------GVSFHVGS-GCTDPe 206
Cdd:cd06836 112 AEfkeASSRIGLRVnpqvgagKIGALSTATATS-KFGVALE------DGARDEIIDAFarrpwlnGLHVHVGSqGCELS- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 207 tfvQAVSDARCVFDMATEVGFSMHL-----LDIGGGFP---GSEDTKLKFEEITSVINPALDKYFpsDSGVRIIAEPGRY 278
Cdd:cd06836 184 ---LLAEGIRRVVDLAEEINRRVGRrqitrIDIGGGLPvnfESEDITPTFADYAAALKAAVPELF--DGRYQLVTEFGRS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 279 YVASA-FTLAVNIIAKKTVWKE----QPGSDDEDESNEQTFMYYVNDGVYGSfncilydHAHVKallQKRPKPdekyysS 353
Cdd:cd06836 259 LLAKCgTIVSRVEYTKSSGGRRiaitHAGAQVATRTAYAPDDWPLRVTVFDA-------NGEPK---TGPEVV------T 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 131888589 354 SIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIY 406
Cdd:cd06836 323 DVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
344-406 |
2.46e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.
Pssm-ID: 143502 [Multi-domain] Cd Length: 346 Bit Score: 46.39 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131888589 344 PKPDEKYYSSSIWGPTCDGLDRIVERcNLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPNIY 406
Cdd:cd06829 281 GEPGEGAHTYRLGGNSCLAGDVIGDY-SFDEpLQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIA 343
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
180-275 |
2.86e-04 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 42.31 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888589 180 LLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTKLKFEEITSVINPAL 259
Cdd:COG1082 45 LRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELA 124
|
90
....*....|....*.
gi 131888589 260 DKYfpSDSGVRIIAEP 275
Cdd:COG1082 125 ELA--EEAGVTLALEN 138
|
|
| |
