|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
1-412 |
0e+00 |
|
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: 581.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 1 MDAFNyRDGELFAEGVALSAIAQRFGTPTYVYSRAHIEAQYRSFTDPLDGVPHLVCYAVKANSNLGVLNVLARLGAGFDI 80
Cdd:COG0019 1 MTHFA-RDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 81 VSRGELERVLAAGGQADKIVFSGVGKSREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHP 160
Cdd:COG0019 80 VSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 161 YISTGLKENKFGIAIADAEDVYIRAAQLPNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGV 240
Cdd:COG0019 160 YISTGGKDSKFGIPLEDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 241 GVRYRDEE-PPAIADYIQAVRERIE---GRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALY 316
Cdd:COG0019 240 GIPYTEGDePPDLEELAAAIKEALEelcGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPALY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 317 QAWMNVTAVTPRNSEA-RAYDIVGPICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLVDGDQA 394
Cdd:COG0019 320 GAYHPIVPVGRPSGAEaETYDVVGPLCESGDVLGKDRSLpPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEA 399
|
410
....*....|....*...
gi 1051689676 395 LEVRRRETVAELYAGESL 412
Cdd:COG0019 400 RLIRRRETYEDLLASEVL 417
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
25-389 |
0e+00 |
|
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: 545.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 25 FGTPTYVYSRAHIEAQYRSFTDPLDGVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGV 104
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 105 GKSREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYIR 184
Cdd:cd06828 81 GKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 185 AAQLPNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEE-PPAIADYIQAVRERI 263
Cdd:cd06828 161 AKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDePLDIEEYAEAIAEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 264 E-----GRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNVTAVTPRNSEARA-YDI 337
Cdd:cd06828 241 KelcegGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGETEkVDV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1051689676 338 VGPICETGDFLAKDRQLA-LEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLV 389
Cdd:cd06828 321 VGPICESGDVFAKDRELPeVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
6-411 |
0e+00 |
|
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: 543.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 6 YRDGELFAEGVALSAIAQRFGTPTYVYSRAHIEAQYRSFtDPLDGVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGE 85
Cdd:TIGR01048 4 NEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAY-KEAFGGRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 86 LERVLAAGGQADKIVFSGVGKSREDMRRALEVGVhCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHPYISTG 165
Cdd:TIGR01048 83 LYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHPYISTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 166 LKENKFGIAIADAEDVYIRAAQLPNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGEcGIYLHHIDLGGGVGVRYR 245
Cdd:TIGR01048 162 LKDSKFGIDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-GIDLEFLDLGGGLGIPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 246 DEE-PPAIADYIQAVRERIE-----GRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAW 319
Cdd:TIGR01048 241 PEEePPDLSEYAQAILNALEgyadlGLDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPALYGAY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 320 MNVTAVTPRNSEARA-YDIVGPICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLVDGDQALEV 397
Cdd:TIGR01048 321 HHIIVLNRTNDAPTEvADVVGPVCESGDVLAKDRELpEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARLI 400
|
410
....*....|....
gi 1051689676 398 RRRETVAELYAGES 411
Cdd:TIGR01048 401 RRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
30-368 |
8.07e-156 |
|
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: 443.08 E-value: 8.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 30 YVYSRAHIEAQYRSFTDPLDGVpHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGKSRE 109
Cdd:pfam00278 2 YVYDLATLRRNYRRWKAALPPR-VKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 110 DMRRALEVGVHCFNVESTDELERLQVVAAEMgvRAPISLRVNPDVDAGTHpYISTGLKENKFGIAIADAEDVYIRAAQLp 189
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPEL--VARVALRINPDVDAGTH-KISTGGLSSKFGIDLEDAPELLALAKEL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 190 NLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEEPPAIADYIQAVRERIE---GR 266
Cdd:pfam00278 157 GLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPDFEEYAAAIREALDeyfPP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 267 DLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNVTAVT-PRNSEARAYDIVGPICETG 345
Cdd:pfam00278 237 DLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKePGEGPLETYDVVGPTCESG 316
|
330 340
....*....|....*....|....
gi 1051689676 346 DFLAKDRQL-ALEEGDLLAVHSAG 368
Cdd:pfam00278 317 DVLAKDRELpELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
27-389 |
4.96e-114 |
|
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: 338.12 E-value: 4.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 27 TPTYVYS----RAHIEAQYRSFTdpldgVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFS 102
Cdd:cd06810 1 TPFYVYDldiiRAHYAALKEALP-----SGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 103 GVGKSREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHpYISTGLKENKFGIAIADAEDVY 182
Cdd:cd06810 76 GPAKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLSLSEARAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 183 IRAAQLpNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYrDEEPPAIADYIQAV--- 259
Cdd:cd06810 155 ERAKEL-DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPY-DEQPLDFEEYAALInpl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 260 --RERIEGRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAW---MNVTAVTPRNSEARA 334
Cdd:cd06810 233 lkKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALAYDAyhpITPLKAPGPDEPLVP 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1051689676 335 YDIVGPICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLV 389
Cdd:cd06810 313 ATLAGPLCDSGDVIGRDRLLpELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
27-402 |
1.09e-93 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 287.46 E-value: 1.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 27 TPTYVYSRAHIEAQYRSFTDPLDGVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGK 106
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALEGLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 107 SREDMRRALEVGVHcFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYIRAA 186
Cdd:PLN02537 98 LLEDLVLAAQEGVF-VNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 187 QLPN-LEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRY--RDEEPPAIADYIQAVRERI 263
Cdd:PLN02537 177 AHPNeLKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYyhAGAVLPTPRDLIDTVRELV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 264 EGRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNVTAVTPR--NSEARAYDIVGPI 341
Cdd:PLN02537 257 LSRDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPPppDAEVSTFDVVGPV 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051689676 342 CETGDFLAKDRQLAL-EEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLVDGDQALE-VRRRET 402
Cdd:PLN02537 337 CESADFLGKDRELPTpPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITkIRHAET 399
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
34-280 |
7.56e-85 |
|
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: 258.75 E-value: 7.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 34 RAHIEAQYRSFTDPLDgvPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGKSREDMRR 113
Cdd:pfam02784 1 LGSIERRHRRWKKALP--RIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 114 ALEVGVHCFNVESTDELERLQVVAAEmgvrAPISLRVNPDVDAGTHPYistglkENKFGIAIADAEDVYIRAAQLPNLEV 193
Cdd:pfam02784 79 ALEVGVGCVTVDNVDELEKLARLAPE----ARVLLRIKPDDSAATCPL------SSKFGADLDEDVEALLEAAKLLNLQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 194 LGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEEPP-AIADYIQAVRERIE-----GRD 267
Cdd:pfam02784 149 VGVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPlDFEEYANVINEALEeyfpgDPG 228
|
250
....*....|...
gi 1051689676 268 LTLMFEPGRYIVA 280
Cdd:pfam02784 229 VTIIAEPGRYFVA 241
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
21-389 |
1.34e-74 |
|
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: 237.49 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 21 IAQRFGTPTYVYSRAHIEAQYR----SFTDPLDgvphlVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQA 96
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAalraALPPAIE-----IYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 97 DKIVFSGVGKSREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGtHPYISTGLKENKFGIAIA 176
Cdd:cd06839 76 EKILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFELK-GSGMKMGGGPSQFGIDVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 177 DAEDVYIRAAQLPNLEVLGVDCHIGSQL----TTLPPFLDALDRLLALIDRLgecGIYLHHIDLGGGVGVRYRDEEPP-- 250
Cdd:cd06839 155 ELPAVLARIAALPNLRFVGLHIYPGTQIldadALIEAFRQTLALALRLAEEL---GLPLEFLDLGGGFGIPYFPGETPld 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 251 ------AIADYIQAVRERIegRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIrpalyQAWMNVTA 324
Cdd:cd06839 232 lealgaALAALLAELGDRL--PGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMHHHL-----AASGNFGQ 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051689676 325 VTPRN-----------SEARAYDIVGPICETGDFLAKDRQLA-LEEGDLLAVHSAGAYGFVMS-SNYNTRGRTAEVLV 389
Cdd:cd06839 305 VLRRNyplailnrmggEERETVTVVGPLCTPLDLLGRNVELPpLEPGDLVAVLQSGAYGLSASpLAFLSHPAPAEVLV 382
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
28-389 |
5.74e-69 |
|
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: 222.31 E-value: 5.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 28 PTYVYSRAHIEAQYRSFTDpLDGVPHLVcYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAA--GGQADKIVFSGVG 105
Cdd:cd06840 13 PCYVYDLETVRARARQVSA-LKAVDSLF-YAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 106 KSREDMRRALEVGVHCfnveSTDELERLQVvAAEMGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYIRA 185
Cdd:cd06840 91 AARSEYEQALELGVNV----TVDNLHPLRE-WPELFRGREVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELDEARDLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 186 AQLpNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIylhhIDLGGGVGVRYRDEEPPAIADYIQAVRERIEG 265
Cdd:cd06840 166 KKA-GIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHFPAVRI----LNVGGGLGIPEAPGGRPIDLDALDAALAAAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 266 R--DLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNVTAVTpRNSEARAY--DIVGPI 341
Cdd:cd06840 241 AhpQYQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLS-RLDEPPAGnaDVVGPI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1051689676 342 CETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLV 389
Cdd:cd06840 320 CESGDVLGRDRLLpETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
26-390 |
2.10e-68 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 232.28 E-value: 2.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 26 GTPTYVYSRAHIEAQYRSFTDpLDGVPHLVcYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAA--GGQADKIVFSG 103
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAA-LAAVDQRF-YAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTP 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 104 VGKSREDMRRALEVGVHCfnveSTDELERLQVVAAEMGVRApISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVyI 183
Cdd:PRK08961 580 NFAPRAEYEAAFALGVTV----TLDNVEPLRNWPELFRGRE-VWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRIDEF-V 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 184 RAAQLPNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGEcgiyLHHIDLGGGVGVRYRDEEPPAIADYIQAVRERI 263
Cdd:PRK08961 654 DLAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPD----VRTIDLGGGLGIPESAGDEPFDLDALDAGLAEV 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 264 EGR--DLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNVTAVTpRNSEARAY--DIVG 339
Cdd:PRK08961 730 KAQhpGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEIVNLS-RLDEPAAGtaDVVG 808
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1051689676 340 PICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTAEVLVD 390
Cdd:PRK08961 809 PICESSDVLGKRRRLpATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
31-385 |
1.31e-62 |
|
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: 206.48 E-value: 1.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 31 VYSRAHIEAQYRSFTDPLDGvPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGKSRED 110
Cdd:cd06836 7 LYDLDGFRALVARLTAAFPA-PVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 111 MRRALEVGVHcFNVESTDELERLQVVAAEMG-VRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYIRAAQLP 189
Cdd:cd06836 86 LREALELGVA-INIDNFQELERIDALVAEFKeASSRIGLRVNPQVGAGKIGALSTATATSKFGVALEDGARDEIIDAFAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 190 NLEVLGVDCHIGSQ---LTTLPPFLDALDRLLALIDRL-GECGIylHHIDLGGGVGVRYRDEE-PPAIADYIQAVRERI- 263
Cdd:cd06836 165 RPWLNGLHVHVGSQgceLSLLAEGIRRVVDLAEEINRRvGRRQI--TRIDIGGGLPVNFESEDiTPTFADYAAALKAAVp 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 264 ---EGRdLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPA-LYQAW-MNVTAVT----PRNSEARA 334
Cdd:cd06836 243 elfDGR-YQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGAQVATRTAyAPDDWpLRVTVFDangePKTGPEVV 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1051689676 335 YDIVGPICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYNTRGRTA 385
Cdd:cd06836 322 TDVAGPCCFAGDVLAKERALpPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
26-379 |
1.72e-61 |
|
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: 202.72 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 26 GTPTYVYSRAHIEAQYRSFTDPLDGVphLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVG 105
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRV--RPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 106 KSREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVrapiSLRVNPDVDAGTHPyISTglkenKFGIAIADAEDVYIRA 185
Cdd:cd00622 79 KSISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKL----LLRIATDDSGALCP-LSR-----KFGADPEEARELLRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 186 AQLpNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEEPP--AIADYIQAVRERI 263
Cdd:cd00622 149 KEL-GLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSfeEIAAVINRALDEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 264 EG-RDLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAI---VDA----AMNDlirpALYQAWmNVTAVTPRN----SE 331
Cdd:cd00622 228 FPdEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERwyyLNDgvygSFNE----ILFDHI-RYPPRVLKDggrdGE 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1051689676 332 ARAYDIVGPICETGDFLAKDRQL--ALEEGDLLAVHSAGAYGFVMSSNYN 379
Cdd:cd00622 303 LYPSSLWGPTCDSLDVIYEDVLLpeDLAVGDWLLFENMGAYTTAYASTFN 352
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
28-375 |
5.54e-57 |
|
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: 191.34 E-value: 5.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 28 PTYVYSRAHIEAQYRSFTDPL-DGVPHLvcYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQAdKIVFSGVGK 106
Cdd:cd06843 3 CAYVYDLAALRAHARALRASLpPGCELF--YAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDA-PLIFGGPGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 107 SREDMRRALEVGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVDAGTHPYISTGLKENKFGIAIADAEDVYIRAA 186
Cdd:cd06843 80 TDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDALELLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 187 QLPNLEVLGVDCHIGS-QLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRD-EEPPAIADYIQAVRERIE 264
Cdd:cd06843 160 DLPNIRLRGFHFHLMShNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADpEEQFDWAGFCEGLDQLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 265 GR--DLTLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPAlyqAWMNVT--AVTPRNS---------- 330
Cdd:cd06843 240 EYepGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPA---AWGHNHpfSVLPVEEwpypwprpsv 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1051689676 331 EARAYDIVGPICETGDFLAKDRQLA-LEEGDLLAVHSAGAYGFVMS 375
Cdd:cd06843 317 RDTPVTLVGQLCTPKDVLARDVPVDrLRAGDLVVFPLAGAYGWNIS 362
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
21-393 |
6.29e-57 |
|
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: 191.32 E-value: 6.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 21 IAQRFGTPTYVYSRAHIEAQYRSFTDPLDG--VPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADK 98
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKryPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 99 IVFSGVGKSREDMRRALEVGVHcFNVESTDELERLQVVAAEMGVRAPISLRVNPDVdaGTHPYistglkeNKFGI---AI 175
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGAL-INIDSFDELERILEIAKELGRVAKVGIRLNMNY--GNNVW-------SRFGFdieEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 176 ADAEDVYIRAAQLPNLEVLGVDCHIGSQLTTLPPFLDALDRLLALIDRLGecGIYLHHIDLGGGVGVRYRD-------EE 248
Cdd:cd06841 151 GEALAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLF--GLELEYLDLGGGFPAKTPLslaypqeDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 249 PPAIADYIQAVRERIEGRDL------TLMFEPGRYIVANAGVLLTQVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMNV 322
Cdd:cd06841 229 VPDPEDYAEAIASTLKEYYAnkenkpKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPTIFWYHHPILV 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051689676 323 TAVTPRNSEARAYDIVGPICETGDFLAKDRQL-ALEEGDLLAVHSAGAYGFVMSSNYnTRGRTAEVLVDGDQ 393
Cdd:cd06841 309 LRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLpPLNVGDILAIRNVGAYNMTQSNQF-IRPRPAVYLIDNNG 379
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
37-276 |
2.32e-39 |
|
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: 140.15 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 37 IEAQYRSFTDpLDGVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGKSREDMRRALE 116
Cdd:cd06808 1 IRHNYRRLRE-AAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 117 VGVHCFNVESTDELERLQVVAAEMGVRAPISLRVNPDVdagthpyistglKENKFGIAIADAEDVYIRAAQLPNLEVLGV 196
Cdd:cd06808 80 QGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGD------------ENGKFGVRPEELKALLERAKELPHLRLVGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 197 DCHIGSQLTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEEPPaiadyiqavreriegrDLTLMFEPGR 276
Cdd:cd06808 148 HTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPL----------------GTFIIVEPGR 211
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
18-370 |
1.04e-27 |
|
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: 113.51 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 18 LSAIAQRFGTPTYVYSRAHIEAQYRSFTDPLD--GVPHLVCYAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQ 95
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDrhGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 96 ADKIVFSGVGKSREDMRRALEVGVhCFNVESTDELERLQ-VVAAEMGVRAPISLRVNPDVdagthpyistGLKENKFGIA 174
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLaLARGYTTGPARVLLRLSPFP----------ASLPSRFGMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 175 IADAEDVYIRAAQL-PNLEVLGVDCHIGSqlTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRYRDEE----- 248
Cdd:cd06842 150 AAEVRTALERLAQLrERVRLVGFHFHLDG--YSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAaewea 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 249 ------------------------------------PPAIADYI-----------QAVRERIEGRDLTLMFEPGRYIVAN 281
Cdd:cd06842 228 flaaltealygygrpltwrneggtlrgpddfypygqPLVAADWLrailsaplpqgRTIAERLRDNGITLALEPGRALLDQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 282 AGVLLTQVEYLKHTEHkDFAIVDAAMND----------LIRPALYQAwmnvTAVTPRNSEARAYdIVGPICETGDFLAKd 351
Cdd:cd06842 308 CGLTVARVAFVKQLGD-GNHLIGLEGNSfsacefssefLVDPLLIPA----PEPTTDGAPIEAY-LAGASCLESDLITR- 380
|
410 420
....*....|....*....|...
gi 1051689676 352 RQLAL----EEGDLLAVHSAGAY 370
Cdd:cd06842 381 RKIPFprlpKPGDLLVFPNTAGY 403
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
56-301 |
1.63e-14 |
|
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: 74.53 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 56 CYAVKANSNLGVLNVLARLG----AGFDIVSRGELERVLAAGGQAD-KIVFSGVgKSRE---DMRRALEVGVHCFNV-ES 126
Cdd:cd06830 42 VYPIKVNQQREVVEEIVKAGkrynIGLEAGSKPELLAALALLKTPDaLIICNGY-KDDEyieLALLARKLGHNVIIViEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 127 TDELERLQVVAAEMGVRAPISLRVNPDVDAGTHPYISTGLKEnKFGIAIADAEDVY--IRAAQLPN-LEVLgvDCHIGSQ 203
Cdd:cd06830 121 LSELDLILELAKKLGVKPLLGVRIKLASKGSGKWQESGGDRS-KFGLTASEILEVVekLKEAGMLDrLKLL--HFHIGSQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 204 LTTLPPFLDALDRLLALIDRLGECGIYLHHIDLGGGVGVRY---RDEEPPAI--------ADYIQAVRERIEGRDL---T 269
Cdd:cd06830 198 ITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYdgsRSSSDSSFnysleeyaNDIVKTVKEICDEAGVphpT 277
|
250 260 270
....*....|....*....|....*....|..
gi 1051689676 270 LMFEPGRYIVANAGVLLTQVEYLKHTEHKDFA 301
Cdd:cd06830 278 IVTESGRAIVAHHSVLIFEVLGVKRLADWYFC 309
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
57-300 |
1.91e-09 |
|
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: 59.09 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 57 YAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGQADKIVFSGVGKSREDMRRALEVGVHCFNVESTDELERLqvv 136
Cdd:cd06831 41 YTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKI--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 137 aAEMGVRAPISLRVnpdvdaGTHPYISTGLKENKFGIAIADAEDVYIRAAQLpNLEVLGVDCHIGSQLTTLPPFLDALDR 216
Cdd:cd06831 118 -ARNHPNAKLLLHI------ATEDNIGGEEMNMKFGTTLKNCRHLLECAKEL-DVQIVGVKFHVSSSCKEYQTYVHALSD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 217 LLALIDRLGECGIYLHHIDLGGG-VGVRYRDEEppaiadYIQAVRERI-----EGRDLTLMFEPGRYIVANAGVLLTQVE 290
Cdd:cd06831 190 ARCVFDMAEEFGFKMNMLDIGGGfTGSEIQLEE------VNHVIRPLLdvyfpEGSGIQIIAEPGSYYVSSAFTLAVNVI 263
|
250
....*....|
gi 1051689676 291 YLKHTEHKDF 300
Cdd:cd06831 264 AKKAVENDKH 273
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
222-379 |
5.40e-06 |
|
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: 47.93 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 222 DRLGEcgiYLHHID---LGGGVGVRYRDEEPPAIADYIQAVRERiegRDLTLMFEPGRYIVANAGVLLTQVEYLKHTEhK 298
Cdd:cd06829 180 ERFGE---YLPQLKwlnLGGGHHITRPDYDVDRLIALIKRFKEK---YGVEVYLEPGEAVALNTGYLVATVLDIVENG-M 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 299 DFAIVDAA----MNDLI----RPALYQAWMNvtavtprNSEARAYDIVGPICETGDFL---AKDRQLALeeGDLLAVHSA 367
Cdd:cd06829 253 PIAILDASatahMPDVLempyRPPIRGAGEP-------GEGAHTYRLGGNSCLAGDVIgdySFDEPLQV--GDRLVFEDM 323
|
170
....*....|..
gi 1051689676 368 GAYGFVMSSNYN 379
Cdd:cd06829 324 AHYTMVKTNTFN 335
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
33-196 |
1.77e-05 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 45.68 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 33 SRAHIEAQYRSFTDPLDGVPHLVCyAVKANS-NLGVLNV---LARLGA-GFDIVSRGELERVLAAGGQADKIVFSGVgkS 107
Cdd:pfam01168 2 DLDALRHNLRRLRRRAGPGAKLMA-VVKANAyGHGAVEVaraLLEGGAdGFAVATLDEALELREAGITAPILVLGGF--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 108 REDMRRALEVGVHCFnVESTDELERLQVVAAEMGVRAPISLRVNpdvdagthpyisTGLkeNKFGIAIADAEDVYIRAAQ 187
Cdd:pfam01168 79 PEELALAAEYDLTPT-VDSLEQLEALAAAARRLGKPLRVHLKID------------TGM--GRLGFRPEEALALLARLAA 143
|
....*....
gi 1051689676 188 LPNLEVLGV 196
Cdd:pfam01168 144 LPGLRLEGL 152
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
82-329 |
4.01e-05 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 45.85 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 82 SRGELERVLAAGGQAD-KIVFSGVgKSREDMRRAL---EVGVHCFNV-ESTDELERLQVVAAEMGVRAPISLRVNPDVDA 156
Cdd:COG1166 127 SKPELMAVLALLDDPGsLIICNGY-KDREYIRLALlgrKLGHKVIIViEKLSELELILEEAKELGVKPLIGVRVKLASKG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 157 GTHPYISTGLKeNKFGIAIADAEDV--YIRAA-QLPNLEVLgvDCHIGSQLTtlppfldaldrllaLIDR----LGECG- 228
Cdd:COG1166 206 SGKWQNSGGER-SKFGLSASEILEVveRLKEAgMLDCLQLL--HFHLGSQIP--------------NIRDikraVREAAr 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 229 IY--LH-------HIDLGGGVGVRY---RDEEPPAI--------ADYIQAVRERIEGRDL---TLMFEPGRYIVANAGVL 285
Cdd:COG1166 269 FYaeLRklgapieYLDVGGGLGVDYdgsRSNSDSSMnyslqeyaNDVVYAIKEVCDEAGVphpTIISESGRALTAHHSVL 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1051689676 286 LTQVeyLKHTEHKDFAIVDAAMND---LIRpALYQAWMNvtaVTPRN 329
Cdd:COG1166 349 IFNV--LDVERAPPEPPPPAPPEDaheLLR-NLWETYES---LTPRN 389
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
55-196 |
1.68e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family 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. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 43.25 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051689676 55 VCYAVKANS-NLGVLNV---LARLGA-GFDIVSRGELERVLAAGGQADKIVFSGVgkSREDMRRALEVGVHCFnVESTDE 129
Cdd:cd00430 28 IMAVVKADAyGHGAVEVakaLEEAGAdYFAVATLEEALELREAGITAPILVLGGT--PPEEAEEAIEYDLTPT-VSSLEQ 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051689676 130 LERLQVVAAEMGVRAPISLRVNpdvdagthpyisTGLkeNKFGIAIADAEDVYIRAAQLPNLEVLGV 196
Cdd:cd00430 105 AEALSAAAARLGKTLKVHLKID------------TGM--GRLGFRPEEAEELLEALKALPGLELEGV 157
|
|
| |
