|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02439 |
PLN02439 |
arginine decarboxylase |
67-448 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 709.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 67 LVVRFPDVLKNRLESLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSSLCKG 146
Cdd:PLN02439 1 LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSCLCKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 147 SSEGLLVCNGFKDAEYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKGKF 226
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 227 GLTTTQILRVVRKLKESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSS 306
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 307 DSDVSVGYGLQDYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSmSLHSFVEKLNDD 386
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKRGVPAADD-DDQYLLLGLTEE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317455896 387 ARADYRNLSAAAIRGEYDTCMLYADQLKQRCVEQFKDGNLDIEQLAAVDAVCDFVSKAIGAS 448
Cdd:PLN02439 320 LRADYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGAS 381
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
1-438 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 557.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 1 WSPELSSDLYRIDGWGAPYFTVNSSGDISVRPHGTdtlPHQEIDLLKVVKKASDpinsggLGLQLPLVVRFPDVLKNRLE 80
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD---PGPSIDLYELVEELRE------RGLSLPVLLRFPDILRDRVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 81 SLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSSLckGSSEGLLVCNGFKDA 160
Cdd:COG1166 76 RLNEAFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALL--DDPGSLIICNGYKDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 161 EYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQILRVVRKL 240
Cdd:COG1166 154 EYIRLALLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 241 KESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSdSDVSVGYGLQDYA 320
Cdd:COG1166 234 KEAGMLDCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSN-SDSSMNYSLQEYA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 321 STVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSM---SLHSFVEKLnddaRADYRNLSAA 397
Cdd:COG1166 313 NDVVYAIKEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPPAppeDAHELLRNL----WETYESLTPR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 317455896 398 AIRGEY-DtcmlyADQLKQRCVEQFKDGNLDIEQLAAVD----AVC 438
Cdd:COG1166 389 NLQECYhD-----ALQYKEEARSLFNLGYLSLEERALAEqlywAIC 429
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
62-376 |
8.84e-166 |
|
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: 472.44 E-value: 8.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 62 GLQLPLVVRFPDVLKNRLESLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMS 141
Cdd:cd06830 2 GYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 142 SLCkgSSEGLLVCNGFKDAEYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSG 221
Cdd:cd06830 82 LLK--TPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 222 EKGKFGLTTTQILRVVRKLKESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYD 301
Cdd:cd06830 160 DRSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317455896 302 GTKSSdSDVSVGYGLQDYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSMSL 376
Cdd:cd06830 240 GSRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKRLADWYFCNFSL 313
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
102-351 |
1.98e-32 |
|
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: 123.16 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 102 VYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSlcKGSSEGLLVCNGFKDAEYISLALVARKlqlnTVIVLE 181
Cdd:pfam02784 21 FYAVKCNSDPAVLRLLAELGTGF----DCASKGELERVLAA--GVPPERIIFANPCKQRSFLRYALEVGV----GCVTVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 182 QEEELDLvidISRKMAVQPVIgLRAKLRTKHSGHFGSTsgekgKFGLTTTQILRVvrkLKESGMLDCLQL--LHFHIGSQ 259
Cdd:pfam02784 91 NVDELEK---LARLAPEARVL-LRIKPDDSAATCPLSS-----KFGADLDEDVEA---LLEAAKLLNLQVvgVSFHVGSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 260 IPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSDSdvsvgygLQDYASTVVQAVRFVCdrKNVKHP 339
Cdd:pfam02784 159 CTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD-------FEEYANVINEALEEYF--PGDPGV 229
|
250
....*....|..
gi 317455896 340 VICSESGRAIVS 351
Cdd:pfam02784 230 TIIAEPGRYFVA 241
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
66-362 |
3.82e-25 |
|
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: 106.61 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFdyavqsegyEAHYQGVYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSLcK 145
Cdd:TIGR01048 26 PLYVYDEDTIRRRFRAYKEAF---------GGRSLVCYAVKANSNLAVLRLLAELGSGF----DVVSGGELYRALAAG-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 146 GSSEGLLVCNGFKDAEYislalvARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGH-FGSTSGEKG 224
Cdd:TIGR01048 92 PPEKIVFSGNGKSRAEL------ERALELGICINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHpYISTGLKDS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 225 KFGLTTTQILRVVRKLKESGMLDCLQLlHFHIGSQIPSTELLADGVGEAAQVYSELvRLGAGMKFIDIGGGLGIDYDGTK 304
Cdd:TIGR01048 166 KFGIDVEEALEAYLYALQLPHLELVGI-HCHIGSQITDLSPFVEAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYTPEE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 317455896 305 SSdsdvsvgYGLQDYASTVVQAVRFVCDRknVKHPVICSESGRAIVSHHSVLIFEAVS 362
Cdd:TIGR01048 244 EP-------PDLSEYAQAILNALEGYADL--GLDPKLILEPGRSIVANAGVLLTRVGF 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02439 |
PLN02439 |
arginine decarboxylase |
67-448 |
0e+00 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 709.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 67 LVVRFPDVLKNRLESLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSSLCKG 146
Cdd:PLN02439 1 LIVRFPDVLKNRLESLQSAFDYAIQSQGYNSHYQGVFPVKCNQDRFLVEDIVKFGSPFRFGLEAGSKPELLLAMSCLCKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 147 SSEGLLVCNGFKDAEYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKGKF 226
Cdd:PLN02439 81 SPDAFLICNGYKDAEYVSLALLARKLGLNTVIVLEQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGHFGSTSGEKGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 227 GLTTTQILRVVRKLKESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSS 306
Cdd:PLN02439 161 GLTATEIVRVVRKLRKEGMLDCLQLLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYDGSKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 307 DSDVSVGYGLQDYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSmSLHSFVEKLNDD 386
Cdd:PLN02439 241 SSDMSVAYSLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSVLIFEAVSASKRGVPAADD-DDQYLLLGLTEE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 317455896 387 ARADYRNLSAAAIRGEYDTCMLYADQLKQRCVEQFKDGNLDIEQLAAVDAVCDFVSKAIGAS 448
Cdd:PLN02439 320 LRADYENLYAAADRGDYEECLLYADQLKQECVRLFKEGLLSLEQRAAVDGLCELVSKRVGAS 381
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
1-438 |
0e+00 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 557.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 1 WSPELSSDLYRIDGWGAPYFTVNSSGDISVRPHGTdtlPHQEIDLLKVVKKASDpinsggLGLQLPLVVRFPDVLKNRLE 80
Cdd:COG1166 5 WTIEDARELYNIDRWGEGYFDINEKGHVTVRPDGD---PGPSIDLYELVEELRE------RGLSLPVLLRFPDILRDRVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 81 SLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSSLckGSSEGLLVCNGFKDA 160
Cdd:COG1166 76 RLNEAFAKAIAEYGYQGRYRGVYPIKVNQQRHVVEEIVRAGKPYNFGLEAGSKPELMAVLALL--DDPGSLIICNGYKDR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 161 EYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQILRVVRKL 240
Cdd:COG1166 154 EYIRLALLGRKLGHKVIIVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERSKFGLSASEILEVVERL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 241 KESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSdSDVSVGYGLQDYA 320
Cdd:COG1166 234 KEAGMLDCLQLLHFHLGSQIPNIRDIKRAVREAARFYAELRKLGAPIEYLDVGGGLGVDYDGSRSN-SDSSMNYSLQEYA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 321 STVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSM---SLHSFVEKLnddaRADYRNLSAA 397
Cdd:COG1166 313 NDVVYAIKEVCDEAGVPHPTIISESGRALTAHHSVLIFNVLDVERAPPEPPPPAppeDAHELLRNL----WETYESLTPR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 317455896 398 AIRGEY-DtcmlyADQLKQRCVEQFKDGNLDIEQLAAVD----AVC 438
Cdd:COG1166 389 NLQECYhD-----ALQYKEEARSLFNLGYLSLEERALAEqlywAIC 429
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
1-438 |
0e+00 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 542.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 1 WSPELSSDLYRIDGWGAPYFTVNSSGDISVRPHGTdtlPHQEIDLLKVVKKASDPinsgglGLQLPLVVRFPDVLKNRLE 80
Cdd:PRK05354 9 WSIEDSRELYNIDHWGAGYFDINDKGHVSVRPDGD---PGASIDLAELVKELRER------GLRLPLLLRFPDILQDRVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 81 SLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSSLCKGSSegLLVCNGFKDA 160
Cdd:PRK05354 80 SLNAAFKKAIEEYGYQGDYRGVYPIKVNQQRRVVEEIVASGKPYNLGLEAGSKPELMAVLALAGDPGA--LIVCNGYKDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 161 EYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQILRVVRKL 240
Cdd:PRK05354 158 EYIRLALIGRKLGHKVFIVIEKLSELELILEEAKELGVKPRLGVRARLASQGSGKWQSSGGEKSKFGLSATEVLEAVERL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 241 KESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSdSDVSVGYGLQDYA 320
Cdd:PRK05354 238 REAGLLDCLQLLHFHLGSQIANIRDIKTAVREAARFYVELRKLGAPIQYLDVGGGLGVDYDGTRSQ-SDSSVNYSLQEYA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 321 STVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFE--AVSSTSTRSQELSSMSLHSFVEKLnddaRADYRNLSAAA 398
Cdd:PRK05354 317 NDVVYTLKEICEEHGVPHPTIISESGRALTAHHAVLVFNvlGVESQEYEEPPAPAEDAPPLLQNL----WETYQEISERN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 317455896 399 IRgEYdtcmlYAD--QLKQRCVEQFKDGNLDIEQLAAVD----AVC 438
Cdd:PRK05354 393 LQ-EI-----YHDaqQDLEEALTLFALGYLSLQERAWAEqlywAIC 432
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
62-376 |
8.84e-166 |
|
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: 472.44 E-value: 8.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 62 GLQLPLVVRFPDVLKNRLESLQSAFDYAVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMS 141
Cdd:cd06830 2 GYGLPLLLRFPDILRHRIERLNAAFAKAIEEYGYKGKYQGVYPIKVNQQREVVEEIVKAGKRYNIGLEAGSKPELLAALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 142 SLCkgSSEGLLVCNGFKDAEYISLALVARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSG 221
Cdd:cd06830 82 LLK--TPDALIICNGYKDDEYIELALLARKLGHNVIIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 222 EKGKFGLTTTQILRVVRKLKESGMLDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYD 301
Cdd:cd06830 160 DRSKFGLTASEILEVVEKLKEAGMLDRLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 317455896 302 GTKSSdSDVSVGYGLQDYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTSTRSQELSSMSL 376
Cdd:cd06830 240 GSRSS-SDSSFNYSLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKRLADWYFCNFSL 313
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
66-362 |
2.61e-47 |
|
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: 166.71 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFdyavqsegyEAHYQGVYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSlck 145
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEAL---------PSGVKLFYAVKANPNPHVLRTLAEAGTGF----DVASKGELALALAA--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 146 GSSEGLLVCNG-FKDAEYISLALvarKLQLNTvIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFGSTSGEKG 224
Cdd:cd06810 66 GVPPERIIFTGpAKSVSEIEAAL---ASGVDH-IVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTHKISTGGLKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 225 KFGLTTTQILRVVRKLKESGMLdcLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGtk 304
Cdd:cd06810 142 KFGLSLSEARAALERAKELDLR--LVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDE-- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 317455896 305 ssdsdvsVGYGLQDYASTVVQAVRFVCDRKNVKHpvICSESGRAIVSHHSVLIFEAVS 362
Cdd:cd06810 218 -------QPLDFEEYAALINPLLKKYFPNDPGVT--LILEPGRYIVAQAGVLVTRVVA 266
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
102-351 |
1.98e-32 |
|
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: 123.16 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 102 VYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSlcKGSSEGLLVCNGFKDAEYISLALVARKlqlnTVIVLE 181
Cdd:pfam02784 21 FYAVKCNSDPAVLRLLAELGTGF----DCASKGELERVLAA--GVPPERIIFANPCKQRSFLRYALEVGV----GCVTVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 182 QEEELDLvidISRKMAVQPVIgLRAKLRTKHSGHFGSTsgekgKFGLTTTQILRVvrkLKESGMLDCLQL--LHFHIGSQ 259
Cdd:pfam02784 91 NVDELEK---LARLAPEARVL-LRIKPDDSAATCPLSS-----KFGADLDEDVEA---LLEAAKLLNLQVvgVSFHVGSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 260 IPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSDSdvsvgygLQDYASTVVQAVRFVCdrKNVKHP 339
Cdd:pfam02784 159 CTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLD-------FEEYANVINEALEEYF--PGDPGV 229
|
250
....*....|..
gi 317455896 340 VICSESGRAIVS 351
Cdd:pfam02784 230 TIIAEPGRYFVA 241
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
73-359 |
7.25e-30 |
|
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: 118.74 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 73 DVLKNRLESLQSAFDYAVQSegyeahyqgVYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSlckGSSEGLL 152
Cdd:pfam00278 7 ATLRRNYRRWKAALPPRVKI---------FYAVKANPNPAVLRLLAELGAGF----DVASGGELERALAA---GVDPERI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 153 VCNG-FKDAEYISLALVARKLQLNtvivLEQEEELDLVIDISRKMAVQpvIGLRAKLRTKHSGHFGSTSGEKGKFGLTTT 231
Cdd:pfam00278 71 VFAGpGKTDSEIRYALEAGVLCFN----VDSEDELEKIAKLAPELVAR--VALRINPDVDAGTHKISTGGLSSKFGIDLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 232 QILRVVRKLKESGmldcLQL--LHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSDsd 309
Cdd:pfam00278 145 DAPELLALAKELG----LNVvgVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPD-- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 317455896 310 vsvgygLQDYASTVVQAVrfvcDRKNVKHPVICSESGRAIVSHHSVLIFE 359
Cdd:pfam00278 219 ------FEEYAAAIREAL----DEYFPPDLEIIAEPGRYLVANAGVLVTR 258
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
66-357 |
7.47e-29 |
|
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: 117.17 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFDYAvqseGYEAHYqgvyPVKCNQDRFVVEDIVKFGSGF--------RFGLEAGSKPELL 137
Cdd:COG0019 27 PLYVYDEAALRRNLRALREAFPGS----GAKVLY----AVKANSNLAVLRLLAEEGLGAdvvsggelRLALAAGFPPERI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 138 LAMSslckgssegllvcNGFKDAEyISLALVARKLQlntvIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGH-F 216
Cdd:COG0019 99 VFSG-------------NGKSEEE-LEEALELGVGH----INVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHeY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 217 GSTSGEKGKFGLTTTQILRVVRKLKESGMLDCLQLlHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGL 296
Cdd:COG0019 161 ISTGGKDSKFGIPLEDALEAYRRAAALPGLRLVGL-HFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 317455896 297 GIDYdgtKSSDSDVSvgygLQDYASTVVQAVRFVCDRknvkHPVICSESGRAIVSHHSVLI 357
Cdd:COG0019 240 GIPY---TEGDEPPD----LEELAAAIKEALEELCGL----GPELILEPGRALVGNAGVLL 289
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
66-357 |
6.19e-28 |
|
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: 114.12 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFdyavQSEGYEAHYQgvypVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSLCK 145
Cdd:cd06828 4 PLYVYDEATIRENYRRLKEAF----SGPGFKICYA----VKANSNLAILKLLAEEGLGA----DVVSGGELYRALKAGFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 146 GSsEGLLVCNGFKDAEyISLALVARKLQLNtvivLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGHFG-STSGEKG 224
Cdd:cd06828 72 PE-RIVFTGNGKSDEE-LELALELGILRIN----VDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYiSTGGKDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 225 KFGLTTTQILRVVRKLKESGMLDCLQLlHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDY-DGT 303
Cdd:cd06828 146 KFGIPLEQALEAYRRAKELPGLKLVGL-HCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYrDED 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 317455896 304 KSSDsdvsvgygLQDYASTVVQAVRFVCDRKNVKHpvICSESGRAIVSHHSVLI 357
Cdd:cd06828 225 EPLD--------IEEYAEAIAEALKELCEGGPDLK--LIIEPGRYIVANAGVLL 268
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
66-362 |
3.82e-25 |
|
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: 106.61 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFdyavqsegyEAHYQGVYPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSLcK 145
Cdd:TIGR01048 26 PLYVYDEDTIRRRFRAYKEAF---------GGRSLVCYAVKANSNLAVLRLLAELGSGF----DVVSGGELYRALAAG-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 146 GSSEGLLVCNGFKDAEYislalvARKLQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGH-FGSTSGEKG 224
Cdd:TIGR01048 92 PPEKIVFSGNGKSRAEL------ERALELGICINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHpYISTGLKDS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 225 KFGLTTTQILRVVRKLKESGMLDCLQLlHFHIGSQIPSTELLADGVGEAAQVYSELvRLGAGMKFIDIGGGLGIDYDGTK 304
Cdd:TIGR01048 166 KFGIDVEEALEAYLYALQLPHLELVGI-HCHIGSQITDLSPFVEAAEKVVKLAESL-AEGIDLEFLDLGGGLGIPYTPEE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 317455896 305 SSdsdvsvgYGLQDYASTVVQAVRFVCDRknVKHPVICSESGRAIVSHHSVLIFEAVS 362
Cdd:TIGR01048 244 EP-------PDLSEYAQAILNALEGYADL--GLDPKLILEPGRSIVANAGVLLTRVGF 292
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
103-417 |
6.49e-14 |
|
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: 72.91 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 103 YPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSsLCkGSSEGLLVCNGFKDAEYISLALvarklQLN-TVIVLE 181
Cdd:cd00622 30 YAVKCNPDPAVLRTLAALGAGF----DCASKGEIELVLG-LG-VSPERIIFANPCKSISDIRYAA-----ELGvRLFTFD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 182 QEEELDlvidisrKMAvQPVIGLRAKLRTKHSGhfgSTSGEK--GKFGLTTTQILRVVRKLKESGmldcLQL--LHFHIG 257
Cdd:cd00622 99 SEDELE-------KIA-KHAPGAKLLLRIATDD---SGALCPlsRKFGADPEEARELLRRAKELG----LNVvgVSFHVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 258 SQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYDGTKSSdsdvsvgygLQDYASTVVQAV-RFVCDRkNV 336
Cdd:cd00622 164 SQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPS---------FEEIAAVINRALdEYFPDE-GV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 337 KhpVICsESGRAIVSHHSVLIFEaVSSTSTRSQELSSMSL-------HSFVEKLNDDARADYRNLSAAAIRGEYDTCMLY 409
Cdd:cd00622 234 R--IIA-EPGRYLVASAFTLAVN-VIAKRKRGDDDRERWYylndgvyGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLW 309
|
330
....*....|....
gi 317455896 410 ------ADQLKQRC 417
Cdd:cd00622 310 gptcdsLDVIYEDV 323
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
66-300 |
1.25e-12 |
|
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: 69.21 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 66 PLVVRFPDVLKNRLESLQSAFD-YAVQSEGYEAHyqgvypvKCNQDRFVVEDIVKFGsgfrFGLEAGSKPELLLAMSSLC 144
Cdd:cd06842 11 PLNVLFPQTFRENIAALRAVLDrHGVDGRVYFAR-------KANKSLALVRAAAAAG----IGVDVASLAELRQALAAGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 145 KGSSeglLVCNG-FKDAEYISLALvarklQLNTVIVLEQEEELDLVIDISRKMAVQPV-IGLRAklrtkhsGHFGSTSge 222
Cdd:cd06842 80 RGDR---IVATGpAKTDEFLWLAV-----RHGATIAVDSLDELDRLLALARGYTTGPArVLLRL-------SPFPASL-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 317455896 223 KGKFGLTTTQILRVVRKLKESGMLDCLQLLHFHIGSQIPSTELLAdgVGEAAQVYSELVRLGAGMKFIDIGGGLGIDY 300
Cdd:cd06842 143 PSRFGMPAAEVRTALERLAQLRERVRLVGFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFPVSY 218
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
155-362 |
1.48e-11 |
|
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: 65.75 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 155 NG-FKDAEYISLALvarklQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTkhSGHFGStsgekgKFGLTTTQI 233
Cdd:cd06841 84 NGpYKSKEELEKAL-----EEGALINIDSFDELERILEIAKELGRVAKVGIRLNMNY--GNNVWS------RFGFDIEEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 234 LRVVRKLKESGMLDCLQL--LHFHIGSQIPSTELLADgvgEAAQVYSELVRLGAG-MKFIDIGGGLGIDYDGTKSSDSDV 310
Cdd:cd06841 151 GEALAALKKIQESKNLSLvgLHCHVGSNILNPEAYSA---AAKKLIELLDRLFGLeLEYLDLGGGFPAKTPLSLAYPQED 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 317455896 311 SVgYGLQDYASTVVQAVRfVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVS 362
Cdd:cd06841 228 TV-PDPEDYAEAIASTLK-EYYANKENKPKLILEPGRALVDDAGYLLGRVVA 277
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
93-367 |
2.10e-11 |
|
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: 65.11 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 93 EGYEAHYQGVYPVKCNQDRFVVEDIVKFGsgfrFGLEAGSKPELLLAMSSLCkgSSEGLLVcngfkDAEYISLALVARKL 172
Cdd:cd06836 22 AAFPAPVLHTFAVKANPLVPVLRLLAEAG----AGAEVASPGELELALAAGF--PPERIVF-----DSPAKTRAELREAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 173 QLNTVIVLEQEEELDlVID--ISRKMAVQPVIGLRAKLRTKhSGHFG--STSGEKGKFG--LTTTQILRVVRKLKESGML 246
Cdd:cd06836 91 ELGVAINIDNFQELE-RIDalVAEFKEASSRIGLRVNPQVG-AGKIGalSTATATSKFGvaLEDGARDEIIDAFARRPWL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 247 DCLqllHFHIGSQIPSTELLADGVGEAAQVYSELVRLgAG---MKFIDIGGGLGIDYDGTKSSDSdvsvgygLQDYASTV 323
Cdd:cd06836 169 NGL---HVHVGSQGCELSLLAEGIRRVVDLAEEINRR-VGrrqITRIDIGGGLPVNFESEDITPT-------FADYAAAL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 317455896 324 VQAV-RFVCDRKNVKhpvicSESGRAIVSHHSVLI--FEAVSSTSTR 367
Cdd:cd06836 238 KAAVpELFDGRYQLV-----TEFGRSLLAKCGTIVsrVEYTKSSGGR 279
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
178-300 |
2.21e-09 |
|
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: 58.76 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 178 IVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTkHSGHFGSTSGEKGK-FGLTTTQILRVVRKLKESGMLDcLQLLHFHI 256
Cdd:cd06839 101 INVESLEELERIDALAEEHGVVARVALRINPDF-ELKGSGMKMGGGPSqFGIDVEELPAVLARIAALPNLR-FVGLHIYP 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 317455896 257 GSQIPSTELLADGVGEAAQVYSELV-RLGAGMKFIDIGGGLGIDY 300
Cdd:cd06839 179 GTQILDADALIEAFRQTLALALRLAeELGLPLEFLDLGGGFGIPY 223
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
103-301 |
2.29e-09 |
|
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: 57.33 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 103 YPVKCNQDRFVVEDIVKFGSGFrfglEAGSKPELLLAMSSLCkgSSEGLLVCNGFKDAEYISLALvarkLQLNTVIVLEQ 182
Cdd:cd06808 20 AVVKANANPEVARTLAALGTGF----DVASLGEALLLRAAGI--PPEPILFLGPCKQVSELEDAA----EQGVIVVTVDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 183 EEELDLVIDISRKMAvqpvIGLRAKLRTkhsghfgSTSGEKGKFGLTTTQILRVVRKLKEsgmLDCLQL--LHFHIGSQI 260
Cdd:cd06808 90 LEELEKLEEAALKAG----PPARVLLRI-------DTGDENGKFGVRPEELKALLERAKE---LPHLRLvgLHTHFGSAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 317455896 261 PSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDYD 301
Cdd:cd06808 156 EDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYL 196
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
218-300 |
2.18e-07 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 53.55 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 218 STSGEKGKFGLTTTQILRVVRKLKESGMLdcLQLLHFHIGSQIPSTELLAdgvgeaaQVYSELVRLGAGM---KFIDIGG 294
Cdd:PRK08961 634 RTGGKESKFGLSQTRIDEFVDLAKTLGIT--VVGLHAHLGSGIETGEHWR-------RMADELASFARRFpdvRTIDLGG 704
|
....*.
gi 317455896 295 GLGIDY 300
Cdd:PRK08961 705 GLGIPE 710
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
89-300 |
6.05e-07 |
|
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: 51.28 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 89 AVQSEGYEAHYQGVYPVKCNQDRFVVEDIVKFGsgfrFGLEAGSKPELLLAMSSLCKGSSEGLLVCNGFKD-AEYislal 167
Cdd:cd06840 26 ARQVSALKAVDSLFYAIKANPHPDVLRTLEEAG----LGFECVSIGELDLVLKLFPDLDPRRVLFTPNFAArSEY----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 168 vARKLQLNTVIVLEQEEELDLVIDISRKMAVQpvigLRAKLRTK--HSGHFgSTSGEKGKFGLTTTQILRVVRKLKESGM 245
Cdd:cd06840 97 -EQALELGVNVTVDNLHPLREWPELFRGREVI----LRIDPGQGegHHKHV-RTGGPESKFGLDVDELDEARDLAKKAGI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 317455896 246 LdcLQLLHFHIGSQIPSTELLAdgvgeaaQVYSELVRLGAGM---KFIDIGGGLGIDY 300
Cdd:cd06840 171 I--VIGLHAHSGSGVEDTDHWA-------RHGDYLASLARHFpavRILNVGGGLGIPE 219
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
93-300 |
1.32e-05 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 47.09 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 93 EGYEAHYQGV-----YPVKCNQDRFVVEDIVKFGSGFRfgLEAGSkpELLLAMSSlckGSSEGLLVCNGF-KDAEYISLA 166
Cdd:PLN02537 33 EAYKEALEGLrsiigYAIKANNNLKILEHLRELGCGAV--LVSGN--ELRLALRA---GFDPTRCIFNGNgKLLEDLVLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317455896 167 LvarklQLNTVIVLEQEEELDLVIDISRKMAVQPVIGLRAKLRTKHSGH-FGSTSGEKGKFGLTTTQILRVVRKLKESGM 245
Cdd:PLN02537 106 A-----QEGVFVNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHpYVATGNKNSKFGIRNEKLQWFLDAVKAHPN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 317455896 246 LDCLQLLHFHIGSQIPSTELLADGVGEAAQVYSELVRLGAGMKFIDIGGGLGIDY 300
Cdd:PLN02537 181 ELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDY 235
|
|
| |
