|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
31-439 |
0e+00 |
|
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: 517.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 31 LLEWVHRYGSPLNLIWPGTLQENLAALEGALVDNRVAHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGAD 110
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 111 GARLVATGPAKTRAFHQELLDCEALISVDSPEELEDLVALLPADAAPQ-PILLRLQPQDQKK-SRFGMPADAVVHCLARL 188
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALARGYTTGPaRVLLRLSPFPASLpSRFGMPAAEVRTALERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 189 SGEN-RLRFDGLHFHLSGYRWETRLAALNQAADLIAGARRMGFSPAMIDIGGGLPVQYVDEAK-YQAHLAAQRPEDYRTG 266
Cdd:cd06842 161 AQLReRVRLVGFHFHLDGYSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAeWEAFLAALTEALYGYG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 267 ------------TIPDSFYPYGGALSAADWLRQLLQAEMSDGRSVATYFAQEALTLAMEPGRALADQAAISVFRILRVKA 334
Cdd:cd06842 241 rpltwrneggtlRGPDDFYPYGQPLVAADWLRAILSAPLPQGRTIAERLRDNGITLALEPGRALLDQCGLTVARVAFVKQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 335 LGPDAHVIFLEGGSFSACEtwFASEFLIDPILVPATRAAAQSAPIRAYLAGHSCLDEDVISNRWLTFPTAPGAGDLLVYA 414
Cdd:cd06842 321 LGDGNHLIGLEGNSFSACE--FSSEFLVDPLLIPAPEPTTDGAPIEAYLAGASCLESDLITRRKIPFPRLPKPGDLLVFP 398
|
410 420
....*....|....*....|....*
gi 1549904856 415 NTGGYQMDLLENEFHRHPMPARFCV 439
Cdd:cd06842 399 NTAGYQMDFLESRFHRHPLPRRVVV 423
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
40-439 |
2.36e-86 |
|
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: 268.79 E-value: 2.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 40 SPLNLIWPGTLQENLAALEGALVDNrvaHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATGP 119
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPSG---VKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 120 AKTRAFHQELLDCE-ALISVDSPEELEDLVALLPADAAPQPILLRLQPQD----------QKKSRFGMPADAVVHCLARL 188
Cdd:cd06810 78 AKSVSEIEAALASGvDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVsagthkistgGLKSKFGLSLSEARAALERA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 189 SGENrLRFDGLHFHLSGYR--WETRLAALNQAADLIAGARRMGFSPAMIDIGGGLPVQYV-DEAKYQAHLAAQRPEDYRT 265
Cdd:cd06810 158 KELD-LRLVGLHFHVGSQIldLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDeQPLDFEEYAALINPLLKKY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 266 GTipdsfypyggalsaadwlrqllqaemsdgrsvatyfAQEALTLAMEPGRALADQAAISVFRILRVKALGpDAHVIFLE 345
Cdd:cd06810 237 FP------------------------------------NDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNG-GRFFAVVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 346 GGSFSACETWFA--SEFLIDPILVPATraaaQSAPIRAYLAGHSCLDEDVISNRWLTFPtaPGAGDLLVYANTGGYQMDL 423
Cdd:cd06810 280 GGMNHSFRPALAydAYHPITPLKAPGP----DEPLVPATLAGPLCDSGDVIGRDRLLPE--LEVGDLLVFEDMGAYGFSE 353
|
410
....*....|....*.
gi 1549904856 424 LENeFHRHPMPARFCV 439
Cdd:cd06810 354 SSN-FNSHPRPAEYLV 368
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
24-450 |
1.84e-45 |
|
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: 163.01 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 24 LTHPGAFLLEWVHRYGSPLNLIWPGTLQENLAALEGALvdNRVAHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRD 103
Cdd:COG0019 10 LTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAF--PGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 104 ARRLGADGARLVATGPAKTRAFHQELLDCEAL-ISVDSPEELEDLVALLPADAAPQPILLRLQPQD-----------QKK 171
Cdd:COG0019 88 ALAAGFPPERIVFSGNGKSEEELEEALELGVGhINVDSLSELERLAELAAELGKRAPVGLRVNPGVdagtheyistgGKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 172 SRFGMPADAVVHCLARLSGENRLRFDGLHFH-------LSGYRwetrlAALNQAADLIAGARRMGFSPAMIDIGGGLPVQ 244
Cdd:COG0019 168 SKFGIPLEDALEAYRRAAALPGLRLVGLHFHigsqildLEPFE-----EALERLLELAEELRELGIDLEWLDLGGGLGIP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 245 YVDEAKYQAhlaaqrPEDYrtgtipdsfypyggalsaADWLRQLLQAemsdgrsvatyFAQEALTLAMEPGRALADQAAI 324
Cdd:COG0019 243 YTEGDEPPD------LEEL------------------AAAIKEALEE-----------LCGLGPELILEPGRALVGNAGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 325 SVFRILRVKAlGPDAHVIFLEGGsFSAcetwfasefLIDPILVPATR------AAAQSAPIRAYLAGHSCLDEDVIsNRW 398
Cdd:COG0019 288 LLTRVLDVKE-NGGRRFVIVDAG-MND---------LMRPALYGAYHpivpvgRPSGAEAETYDVVGPLCESGDVL-GKD 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1549904856 399 LTFPtAPGAGDLLVYANTGGYQMDLLeNEFHRHPMPARFCVTNdaeGRSHLV 450
Cdd:COG0019 356 RSLP-PLEPGDLLAFLDAGAYGFSMA-SNYNGRPRPAEVLVDD---GEARLI 402
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
48-417 |
1.36e-36 |
|
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: 137.23 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 48 GTLQENLAALEGALVDNrvaHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATGPAKTRAFHQ 127
Cdd:pfam00278 7 ATLRRNYRRWKAALPPR---VKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDSEIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 128 ELLDCE-ALISVDSPEELEDLVALLPADAApqPILLRLQPQD----------QKKSRFGMPADAVVHCLARLSgENRLRF 196
Cdd:pfam00278 84 YALEAGvLCFNVDSEDELEKIAKLAPELVA--RVALRINPDVdagthkistgGLSSKFGIDLEDAPELLALAK-ELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 197 DGLHFH-------LSGYRwetrlAALNQAADLIAGARRMGFSPAMIDIGGGLPVqyvdeakyqahlaaqrpeDYRTGTIP 269
Cdd:pfam00278 161 VGVHFHigsqitdLEPFV-----EALQRARELFDRLRELGIDLKLLDIGGGFGI------------------PYRDEPPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 270 DsFYPYGGALSAAdwlrqllqaemsdgrsVATYFAQEaLTLAMEPGRALADQAAISVFRILRVKAlGPDAHVIFLEGGSF 349
Cdd:pfam00278 218 D-FEEYAAAIREA----------------LDEYFPPD-LEIIAEPGRYLVANAGVLVTRVIAVKT-GGGKTFVIVDAGMN 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1549904856 350 SacetwfasefLIDPIL------VPATRAAAQSAPIRAYLAGHSCLDEDVISNRWlTFPtAPGAGDLLVYANTG 417
Cdd:pfam00278 279 D----------LFRPALydayhpIPVVKEPGEGPLETYDVVGPTCESGDVLAKDR-ELP-ELEVGDLLAFEDAG 340
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
38-419 |
9.91e-33 |
|
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: 127.60 E-value: 9.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 38 YGSPLNLIWPGTLQENLAALEGALvdNRVAHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVAT 117
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAF--SGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 118 GPAKTRAFHQELLDC-EALISVDSPEELEDLVALLPADAAPQPILLRLQPQ-----------DQKKSRFGMPADAVVHCL 185
Cdd:cd06828 79 GNGKSDEELELALELgILRINVDSLSELERLGEIAPELGKGAPVALRVNPGvdagthpyistGGKDSKFGIPLEQALEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 186 ARLSGENRLRFDGLHFHL-SGYrweTRLAALNQAA----DLIAGARRMGFSPAMIDIGGGLPVQYVDEAKyqahlaAQRP 260
Cdd:cd06828 159 RRAKELPGLKLVGLHCHIgSQI---LDLEPFVEAAekllDLAAELRELGIDLEFLDLGGGLGIPYRDEDE------PLDI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 261 EDYrtgtipdsfypyggalsaADWLRQLLQAEMSDGRSvatyfaqeaLTLAMEPGRALADQAAISVFRILRVKaLGPDAH 340
Cdd:cd06828 230 EEY------------------AEAIAEALKELCEGGPD---------LKLIIEPGRYIVANAGVLLTRVGYVK-ETGGKT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 341 VIFLEGGsFSAcetwfasefLIDPIL-------VPATRAAAqSAPIRAYLAGHSCLDEDV-ISNRWLtfpTAPGAGDLLV 412
Cdd:cd06828 282 FVGVDAG-MND---------LIRPALygayheiVPVNKPGE-GETEKVDVVGPICESGDVfAKDREL---PEVEEGDLLA 347
|
....*..
gi 1549904856 413 YANTGGY 419
Cdd:cd06828 348 IHDAGAY 354
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
37-421 |
7.61e-32 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.
Pssm-ID: 143508 [Multi-domain] Cd Length: 379 Bit Score: 125.07 E-value: 7.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 37 RYGSPLNLIWPGTLQENLAALEGALVDNRVAHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVA 116
Cdd:cd06841 4 SYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 117 TGPAKTRAFHQELLDCEALISVDSPEELEDLVALLPADAAPQPILLRL--QPQDQKKSRFGMPADAVVHCLARLS---GE 191
Cdd:cd06841 84 NGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGRVAKVGIRLnmNYGNNVWSRFGFDIEENGEALAALKkiqES 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 192 NRLRFDGLHFH-------LSGYRWetrlaALNQAADLIagARRMGFSPAMIDIGGGLPVQYVDEAKYQAHLAAQRPEDYr 264
Cdd:cd06841 164 KNLSLVGLHCHvgsnilnPEAYSA-----AAKKLIELL--DRLFGLELEYLDLGGGFPAKTPLSLAYPQEDTVPDPEDY- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 265 TGTIPDSFYPYGGALSaadwlrqllqaemsdgrsvatyfaqEALTLAMEPGRALADQAAISVFRILRVKALgPDAHVIFL 344
Cdd:cd06841 236 AEAIASTLKEYYANKE-------------------------NKPKLILEPGRALVDDAGYLLGRVVAVKNR-YGRNIAVT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 345 EGGSFsacetWFASEFLIDPILVPATRAAAQSAPIRAYLAGHSCLDEDVIsnrwltFPTAPGA----GDLLVYANTGGYQ 420
Cdd:cd06841 290 DAGIN-----NIPTIFWYHHPILVLRPGKEDPTSKNYDVYGFNCMESDVL------FPNVPLPplnvGDILAIRNVGAYN 358
|
.
gi 1549904856 421 M 421
Cdd:cd06841 359 M 359
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
35-435 |
6.02e-28 |
|
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: 114.23 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 35 VHRYGSPLNLIWPGTLQENLAALEGALVDnrvAHAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARL 114
Cdd:cd06839 2 ADAYGTPFYVYDRDRVRERYAALRAALPP---AIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 115 VATGPAKTRAFHQELLDC-EALISVDSPEELEDLVALLPADAAPQPILLRLQPQDQKK----------SRFGMPADAVVH 183
Cdd:cd06839 79 LFAGPGKSDAELRRAIEAgIGTINVESLEELERIDALAEEHGVVARVALRINPDFELKgsgmkmgggpSQFGIDVEELPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 184 CLARLSGENRLRFDGLHFHL--SGYRWETRLAALNQAADLIAG-ARRMGFSPAMIDIGGGLPVQYvdeakyqahlaaqrp 260
Cdd:cd06839 159 VLARIAALPNLRFVGLHIYPgtQILDADALIEAFRQTLALALRlAEELGLPLEFLDLGGGFGIPY--------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 261 edYRTGTIPDsFYPYGGALSAAdwlrqllqaemsdgrsVATYFAQEALT-LAMEPGRALADQAAISVFRILRVKALGpDA 339
Cdd:cd06839 224 --FPGETPLD-LEALGAALAAL----------------LAELGDRLPGTrVVLELGRYLVGEAGVYVTRVLDRKVSR-GE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 340 HVIFLEGGS--FSACETWFASEFLIDPILVPATRAAAqSAPIRAYLAGHSCLDEDVISNRwLTFPTAPgAGDLLVYANTG 417
Cdd:cd06839 284 TFLVTDGGMhhHLAASGNFGQVLRRNYPLAILNRMGG-EERETVTVVGPLCTPLDLLGRN-VELPPLE-PGDLVAVLQSG 360
|
410
....*....|....*...
gi 1549904856 418 GYQMDLLENEFHRHPMPA 435
Cdd:cd06839 361 AYGLSASPLAFLSHPAPA 378
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
39-419 |
1.74e-26 |
|
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: 109.89 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 39 GSPLNLIWPGTLQENLAALEGALvdNRVAhaIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATG 118
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKAL--PRVR--PFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 119 PAKTRAFHQELLDCE-ALISVDSPEELEDLvallpADAAPQP-ILLRLQPQDQKK----SR-FGMPADAVVHcLARLSGE 191
Cdd:cd00622 77 PCKSISDIRYAAELGvRLFTFDSEDELEKI-----AKHAPGAkLLLRIATDDSGAlcplSRkFGADPEEARE-LLRRAKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 192 NRLRFDGLHFHL-SG----YRWETrlaALNQAADLIAGARRMGFSPAMIDIGGGLPVQYVDEakyqahlaaqrpedyrtg 266
Cdd:cd00622 151 LGLNVVGVSFHVgSQctdpSAYVD---AIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGV------------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 267 tiPDSFYPYGGALSAAdwlrqllqaemsdgrsVATYFAQEALTLAMEPGRALADQAAISVFRIL--RVKALGPDAHVIFL 344
Cdd:cd00622 210 --VPSFEEIAAVINRA----------------LDEYFPDEGVRIIAEPGRYLVASAFTLAVNVIakRKRGDDDRERWYYL 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1549904856 345 -EG--GSFSacETWFasEFLIDPILVPAtRAAAQSAPIRAYLAGHSCLDEDVIS-NRWLtfPTAPGAGDLLVYANTGGY 419
Cdd:cd00622 272 nDGvyGSFN--EILF--DHIRYPPRVLK-DGGRDGELYPSSLWGPTCDSLDVIYeDVLL--PEDLAVGDWLLFENMGAY 343
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
50-436 |
9.67e-19 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 87.34 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 50 LQENLAALEGALVDNRvahAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADgARLVATGPAKTRAFHQEL 129
Cdd:cd06843 12 LRAHARALRASLPPGC---ELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPD-APLIFGGPGKTDSELAQA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 130 LDCE-ALISVDSPEELEDLVALLPADAAPQPILLRLQPQDQ-----------KKSRFGMPADAVVHCLARLSGENRLRFD 197
Cdd:cd06843 88 LAQGvERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPdlpsstltmggQPTPFGIDEADLPDALELLRDLPNIRLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 198 GLHFHL-SGYRWETRLAALnqAADLIAGARRM----GFSPAMIDIGGGLPVQYVDeakyqahlaaqrpedyrtgtiPDSF 272
Cdd:cd06843 168 GFHFHLmSHNLDAAAHLAL--VKAYLETARQWaaehGLDLDVVNVGGGIGVNYAD---------------------PEEQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 273 YPYGGalsAADWLRQLLQAemsdgrsvatyfAQEALTLAMEPGRALADQAAISVFRILRVKALGpDAHVIFLEGGS--FS 350
Cdd:cd06843 225 FDWAG---FCEGLDQLLAE------------YEPGLTLRFECGRYISAYCGYYVTEVLDLKRSH-GEWFAVLRGGThhFR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 351 ACETWFASE-FLIDPI---LVPATRAAAQSAPIRayLAGHSCLDEDVISnRWLTFPTApGAGDLLVYANTGGYQMDLLEN 426
Cdd:cd06843 289 LPAAWGHNHpFSVLPVeewPYPWPRPSVRDTPVT--LVGQLCTPKDVLA-RDVPVDRL-RAGDLVVFPLAGAYGWNISHH 364
|
410
....*....|
gi 1549904856 427 EFHRHPMPAR 436
Cdd:cd06843 365 DFLMHPHPER 374
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
69-248 |
7.88e-18 |
|
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: 81.98 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 69 AIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATGPAKTRAfhqELLDCEAL----ISVDSPEEL 144
Cdd:cd06808 17 TLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVS---ELEDAAEQgvivVTVDSLEEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 145 EDLVALLPADAAPQPILLRLQPqDQKKSRFGMPADAVVHCLARLSGENRLRFDGLHFHLS----GYRWETRlaALNQAAD 220
Cdd:cd06808 94 EKLEEAALKAGPPARVLLRIDT-GDENGKFGVRPEELKALLERAKELPHLRLVGLHTHFGsadeDYSPFVE--ALSRFVA 170
|
170 180
....*....|....*....|....*...
gi 1549904856 221 LIAGARRMGFSPAMIDIGGGLPVQYVDE 248
Cdd:cd06808 171 ALDQLGELGIDLEQLSIGGSFAILYLQE 198
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
68-319 |
2.86e-17 |
|
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: 80.79 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 68 HAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATGPAKTRAFHQELLDCEA-LISVDSPEELED 146
Cdd:pfam02784 18 IKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGVgCVTVDNVDELEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 147 LvallpADAAP-QPILLRLQPQD-----QKKSRFGMPADAVVHCLARLSGENRLRFDGLHFHL-SG-YRWETRLAALNQA 218
Cdd:pfam02784 98 L-----ARLAPeARVLLRIKPDDsaatcPLSSKFGADLDEDVEALLEAAKLLNLQVVGVSFHVgSGcTDAEAFVLALEDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 219 ADLIAGARRMGFSPAMIDIGGGLPVQYVDeakyqahlaaqrpedyrtGTIPDSFYPYGGALSAAdwlrqllqaemsdgrs 298
Cdd:pfam02784 173 RGVFDQGAELGFNLKILDLGGGFGVDYTE------------------GEEPLDFEEYANVINEA---------------- 218
|
250 260
....*....|....*....|..
gi 1549904856 299 VATYFAQ-EALTLAMEPGRALA 319
Cdd:pfam02784 219 LEEYFPGdPGVTIIAEPGRYFV 240
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
48-261 |
3.27e-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: 64.72 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 48 GTLQENLAALEGALvDNRVAHAIyyGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVATGPAKTRAFHQ 127
Cdd:cd06836 11 DGFRALVARLTAAF-PAPVLHTF--AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 128 ELLDCEALISVDSPEELEDLVALLPADAAPQ-PILLRLQPQ-----------DQKKSRFGMP-----ADAVVHCLARlsg 190
Cdd:cd06836 88 EALELGVAINIDNFQELERIDALVAEFKEASsRIGLRVNPQvgagkigalstATATSKFGVAledgaRDEIIDAFAR--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 191 enRLRFDGLHFHLSGYRWETRLAA--------LNQAADLIAGARRMGFspamIDIGGGLPVQYVDE------AKYQAHLA 256
Cdd:cd06836 165 --RPWLNGLHVHVGSQGCELSLLAegirrvvdLAEEINRRVGRRQITR----IDIGGGLPVNFESEditptfADYAAALK 238
|
....*
gi 1549904856 257 AQRPE 261
Cdd:cd06836 239 AAVPE 243
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
40-442 |
6.76e-11 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 63.66 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 40 SPLNLIWPGTLQENLAALEGAL--VDNRVAHAIyygaKVNKSPGLMQAALAAGAGLDVSSVYELRDARRLGADGARLVAT 117
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALegLRSIIGYAI----KANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 118 GPAKTraFHQELLDCE--ALISVDSPEELEDLVALLPADAAPQPILLRLQPQ-----------DQKKSRFGMPADAVVHC 184
Cdd:PLN02537 94 GNGKL--LEDLVLAAQegVFVNVDSEFDLENIVEAARIAGKKVNVLLRINPDvdpqvhpyvatGNKNSKFGIRNEKLQWF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 185 LARLSGE-NRLRFDGLHFHLSGYRweTRLAALNQAA----DLIAGARRMGFSPAMIDIGGGLPVQYvdeakYQAHLAAQR 259
Cdd:PLN02537 172 LDAVKAHpNELKLVGAHCHLGSTI--TKVDIFRDAAvlmvNYVDEIRAQGFELSYLNIGGGLGIDY-----YHAGAVLPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 260 PEDYrtgtipdsfypyggalsaADWLRQLLQaemsdgrsvatyfaQEALTLAMEPGRALADQAAISVFRILRVKALGpDA 339
Cdd:PLN02537 245 PRDL------------------IDTVRELVL--------------SRDLTLIIEPGRSLIANTCCFVNRVTGVKTNG-TK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 340 HVIFLEGgsfSACEtwfasefLIDPILVPA------TRAAAQSAPIRAY-LAGHSCLDEDVI-SNRWLtfPTaPGAGDLL 411
Cdd:PLN02537 292 NFIVIDG---SMAE-------LIRPSLYDAyqhielVSPPPPDAEVSTFdVVGPVCESADFLgKDREL--PT-PPKGAGL 358
|
410 420 430
....*....|....*....|....*....|.
gi 1549904856 412 VYANTGGYQMDLLENeFHRHPMPARFCVTND 442
Cdd:PLN02537 359 VVHDAGAYCMSMAST-YNLKMRPPEYWVEED 388
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
39-419 |
7.31e-11 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 64.33 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 39 GSPLNLIWPGTLQENLAALEG-ALVDnrvahAIYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRL--GADGARLV 115
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAAlAAVD-----QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 116 ATGPAKTRAFHQELLDCEALISVDSPEELEdlvaLLPADAAPQPILLRLQPQDQ-----------KKSRFGMPADAVVHc 184
Cdd:PRK08961 577 FTPNFAPRAEYEAAFALGVTVTLDNVEPLR----NWPELFRGREVWLRIDPGHGdghhekvrtggKESKFGLSQTRIDE- 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 185 LARLSGENRLRFDGLHFH-----LSGYRWEtrlaalnQAADLIAG-ARRMGfSPAMIDIGGGLPVQYVDEakyqahlaaQ 258
Cdd:PRK08961 652 FVDLAKTLGITVVGLHAHlgsgiETGEHWR-------RMADELASfARRFP-DVRTIDLGGGLGIPESAG---------D 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 259 RPEDYrtgtipdsfypyggalsaaDWLRQLLQAemsdgrsVATyfAQEALTLAMEPGRALADQAAISVFRILRVKALGpD 338
Cdd:PRK08961 715 EPFDL-------------------DALDAGLAE-------VKA--QHPGYQLWIEPGRYLVAEAGVLLARVTQVKEKD-G 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 339 AHVIFLEGGSFSacetwfasefLIDPILVPA----------TRAAAQSAPIraylAGHSCLDEDVISNRWLTFPTAPgaG 408
Cdd:PRK08961 766 VRRVGLETGMNS----------LIRPALYGAyheivnlsrlDEPAAGTADV----VGPICESSDVLGKRRRLPATAE--G 829
|
410
....*....|.
gi 1549904856 409 DLLVYANTGGY 419
Cdd:PRK08961 830 DVILIANAGAY 840
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
135-365 |
2.82e-08 |
|
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: 55.65 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 135 LISVDSPEELEDLVALLPA-DAAPQpILLRLQPQDQ----------KKSRFGMPADAVVHCLARLSGENRL-RFDGLHFH 202
Cdd:cd06830 115 IIVIEKLSELDLILELAKKlGVKPL-LGVRIKLASKgsgkwqesggDRSKFGLTASEILEVVEKLKEAGMLdRLKLLHFH 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 203 L-SGYRWETRLA-ALNQAADLIAGARRMGFSPAMIDIGGGLPVQYvdeakyqahlaaqrpedYRTGTIPDSFYPYGGALS 280
Cdd:cd06830 194 IgSQITDIRRIKsALREAARIYAELRKLGANLRYLDIGGGLGVDY-----------------DGSRSSSDSSFNYSLEEY 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 281 AADWLRQLlqAEMSDGRSVATyfaqeaLTLAMEPGRALADQAAISVFRILRVKALgpdAHVIFLEGGSF-SACETWFAS- 358
Cdd:cd06830 257 ANDIVKTV--KEICDEAGVPH------PTIVTESGRAIVAHHSVLIFEVLGVKRL---ADWYFCNFSLFqSLPDSWAIDq 325
|
....*..
gi 1549904856 359 EFLIDPI 365
Cdd:cd06830 326 LFPIMPL 332
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
51-419 |
1.18e-05 |
|
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: 47.43 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 51 QENLAALEGalVDNRvahaiYYGAKVNKSPGLMQAALAAGAGLDVSSVYELRDARRL--GADGARLVATGPAKTRAFHQE 128
Cdd:cd06840 26 ARQVSALKA--VDSL-----FYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 129 LLDCEALISVDSPEELEdlvaLLPADAAPQPILLRLQPQDQ-----------KKSRFGMPADAVVHcLARLSGENRLRFD 197
Cdd:cd06840 99 ALELGVNVTVDNLHPLR----EWPELFRGREVILRIDPGQGeghhkhvrtggPESKFGLDVDELDE-ARDLAKKAGIIVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 198 GLHFHL-SGYRWETRLAalnQAADLIAG-ARRMGfSPAMIDIGGGLPVqyvdeakyqahlaaqrpeDYRTGTIPDSFYPY 275
Cdd:cd06840 174 GLHAHSgSGVEDTDHWA---RHGDYLASlARHFP-AVRILNVGGGLGI------------------PEAPGGRPIDLDAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 276 GGALSAadwlrqllqaemsdgrsVATYFAQeaLTLAMEPGRALADQAAISVFRILRVKAlGPDAHVIFLEGGSFSacetw 355
Cdd:cd06840 232 DAALAA-----------------AKAAHPQ--YQLWMEPGRFIVAESGVLLARVTQIKH-KDGVRFVGLETGMNS----- 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 356 fasefLIDPILVPATRAA---AQSAPIRAYLA---GHSCLDEDVISNRWLTFPTAPgaGDLLVYANTGGY 419
Cdd:cd06840 287 -----LIRPALYGAYHEIvnlSRLDEPPAGNAdvvGPICESGDVLGRDRLLPETEE--GDVILIANAGAY 349
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
95-204 |
1.40e-03 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 39.90 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 95 VSSVYELRDARRLGADGARLVATGPAKTRAfhQELLDCEALISVDSPEELEDLVALLPADAAPQPILLRLqpqDQKKSRF 174
Cdd:pfam01168 53 VATLDEALELREAGITAPILVLGGFPPEEL--ALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKI---DTGMGRL 127
|
90 100 110
....*....|....*....|....*....|
gi 1549904856 175 GMPADAVVHCLARLSGENRLRFDGLHFHLS 204
Cdd:pfam01168 128 GFRPEEALALLARLAALPGLRLEGLMTHFA 157
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
134-245 |
2.17e-03 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 40.44 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 134 ALISVDSPEELeDLVALLPADAAPQPIL-----LRLQ------PQDQKKSRFGMPADAVVHCLARLSGENRLR-FDGLHF 201
Cdd:PLN02439 110 TVIVLEQEEEL-DLVIEASQRLGVRPVIgvrakLRTKhsghfgSTSGEKGKFGLTATEIVRVVRKLRKEGMLDcLQLLHF 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1549904856 202 HLSGYRWETRLA--ALNQAADLIAGARRMGFSPAMIDIGGGLPVQY 245
Cdd:PLN02439 189 HIGSQIPSTSLLkdGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDY 234
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
171-245 |
4.00e-03 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 39.72 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 171 KSRFGMPADAVVHCLARLSGENRL-RFDGLHFHL-------SGYRwetrlAALNQAADLIAGARRMGFSPAMIDIGGGLP 242
Cdd:PRK05354 220 KSKFGLSATEVLEAVERLREAGLLdCLQLLHFHLgsqianiRDIK-----TAVREAARFYVELRKLGAPIQYLDVGGGLG 294
|
...
gi 1549904856 243 VQY 245
Cdd:PRK05354 295 VDY 297
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
95-239 |
6.16e-03 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 38.58 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 95 VSSVYElrdARRLGADGAR--LVA---TGPAKTRAFHQEL-LDCEALISVDSPEELEDLVALLPADAAPQPILLRLqpqD 168
Cdd:COG3616 62 VATLAE---AEVLAAAGVDdiLLAyplVGPAKLARLAALArAGARLTVLVDSVEQAEALAAAAAAAGRPLRVLVEL---D 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 169 qkksrFGM------PADAVVHCLARLSGENRLRFDGLHF---HLSGYR-WETRLAALNQAADLIAGARRM----GFSPAM 234
Cdd:COG3616 136 -----VGGgrtgvrPPEAALALARAIAASPGLRLAGLMTyegHIYGADdAEERRAAAREELARLAAAAEAlraaGLPCPI 210
|
....*
gi 1549904856 235 IDIGG 239
Cdd:COG3616 211 VSGGG 215
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
171-245 |
6.38e-03 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 38.92 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549904856 171 KSRFGMPADAVVHCLARLSGENRLrfDGL---HFHLsG--------YRwetrlAALNQAADLIAGARRMGFSPAMIDIGG 239
Cdd:COG1166 216 RSKFGLSASEILEVVERLKEAGML--DCLqllHFHL-GsqipnirdIK-----RAVREAARFYAELRKLGAPIEYLDVGG 287
|
....*.
gi 1549904856 240 GLPVQY 245
Cdd:COG1166 288 GLGVDY 293
|
|
| |
