|
Name |
Accession |
Description |
Interval |
E-value |
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
7-431 |
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: 612.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 7 SRQNQHGHLEIGGVDALYLAEKYGTPLYVYDVALIRERAKSFKQAFISAGlkaQVAYASKAFSSVAMIQLAEEEGLSLDV 86
Cdd:TIGR01048 1 TVENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRS---LVCYAVKANSNLAVLRLLAELGSGFDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 87 VSGGELYTAVAAGFPAERIHFHGNNKSREELRMALEHRIgCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHD 166
Cdd:TIGR01048 78 VSGGELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 167 YITTGQEDSKFGFDLHngQTERAIEQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRDSYSFvsKVLNLG 246
Cdd:TIGR01048 157 YISTGLKDSKFGIDVE--EALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGIDL--EFLDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 247 GGFGIRYTEDDEPLHATEYVEKIIEAVKENASrYGFDiPEIWIEPGRSLVGDAGTTLYTVGSQKEVPgVRQYVAVDGGMN 326
Cdd:TIGR01048 233 GGLGIPYTPEEEPPDLSEYAQAILNALEGYAD-LGLD-PKLILEPGRSIVANAGVLLTRVGFVKETG-SRNFVIVDAGMN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 327 DNIRPALYQAKYEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAV 406
Cdd:TIGR01048 310 DLIRPALYGAYHHIIVLNRTNDAPTEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAE 389
|
410 420
....*....|....*....|....*
gi 1036011971 407 VFVENGEAHLVVKRETYEDIVKLDL 431
Cdd:TIGR01048 390 VLVDGGQARLIRRRETYEDLWALEV 414
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
10-431 |
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: 585.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 10 NQHGHLEIGGVDALYLAEKYGTPLYVYDVALIRERAKSFKQAFisAGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSG 89
Cdd:COG0019 5 ARDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAF--PGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 90 GELYTAVAAGFPAERIHFHGNNKSREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHDYIT 169
Cdd:COG0019 83 GELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHEYIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 170 TGQEDSKFGFDLHngQTERAIEQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRdSYSFVSKVLNLGGGF 249
Cdd:COG0019 163 TGGKDSKFGIPLE--DALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELR-ELGIDLEWLDLGGGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 250 GIRYTEDDEPLHATEYVEKIIEAVKEnasRYGFDiPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNI 329
Cdd:COG0019 240 GIPYTEGDEPPDLEELAAAIKEALEE---LCGLG-PELILEPGRALVGNAGVLLTRVLDVKENGG-RRFVIVDAGMNDLM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 330 RPALYQAKYEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:COG0019 315 RPALYGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLV 394
|
410 420
....*....|....*....|..
gi 1036011971 410 ENGEAHLVVKRETYEDIVKLDL 431
Cdd:COG0019 395 DDGEARLIRRRETYEDLLASEV 416
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
29-409 |
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: 542.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 29 YGTPLYVYDVALIRERAKSFKQAFisAGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFH 108
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAF--SGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 109 GNNKSREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHDYITTGQEDSKFGFDLhnGQTER 188
Cdd:cd06828 79 GNGKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPL--EQALE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 189 AIEQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRdSYSFVSKVLNLGGGFGIRYTEDDEPLHATEYVEK 268
Cdd:cd06828 157 AYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELR-ELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 269 IIEAVKENASryGFDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNIRPALYQAKYEAAAANRIGE 348
Cdd:cd06828 236 IAEALKELCE--GGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGG-KTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036011971 349 AHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:cd06828 313 GETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
33-388 |
2.72e-112 |
|
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: 333.30 E-value: 2.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 33 LYVYDVALIRERAKSFKQAFISaglKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGNNK 112
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALPP---RVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 113 SREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSidVLLRITPGVEAHTHdYITTGQEDSKFGFDLHngQTERAIEQ 192
Cdd:pfam00278 78 TDSEIRYALEAGVLCFNVDSEDELEKIAKLAPELVAR--VALRINPDVDAGTH-KISTGGLSSKFGIDLE--DAPELLAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 193 VlQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRDsYSFVSKVLNLGGGFGIRYtEDDEPLHATEYVEKIIEA 272
Cdd:pfam00278 153 A-KELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRE-LGIDLKLLDIGGGFGIPY-RDEPPPDFEEYAAAIREA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 273 VKEnasRYGFDIpEIWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNIRPALYQAKYEAAAANRIGEAHDK 352
Cdd:pfam00278 230 LDE---YFPPDL-EIIAEPGRYLVANAGVLVTRVIAVKTGGG-KTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPLE 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 1036011971 353 TVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTG 388
Cdd:pfam00278 305 TYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
31-409 |
1.03e-110 |
|
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: 330.42 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 31 TPLYVYDVALIRERAKSFKQAFisaGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGN 110
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAL---PSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 111 NKSREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHdYITTGQEDSKFGFDLhngQTERAI 190
Cdd:cd06810 78 AKSVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLSL---SEARAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 191 EQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRDsYSFVSKVLNLGGGFGIRYTEDDEPLHatEYVEKII 270
Cdd:cd06810 154 LERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVE-MGFPLEMLDLGGGLGIPYDEQPLDFE--EYAALIN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 271 EAVKEnaSRYGFDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGVRQYVaVDGGMNDNIRPALYQAKYEAAAANRIGEAH 350
Cdd:cd06810 231 PLLKK--YFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAV-VDGGMNHSFRPALAYDAYHPITPLKAPGPD 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036011971 351 DKTV--SIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:cd06810 308 EPLVpaTLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
38-297 |
4.36e-96 |
|
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: 288.41 E-value: 4.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 38 VALIRERAKSFKQAFIsaglKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGNNKSREEL 117
Cdd:pfam02784 1 LGSIERRHRRWKKALP----RIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 118 RMALEHRIGCIVVDNFYEIALLEDLCKEtghsIDVLLRITPGVEAHTHDYittgqeDSKFGFDLHngQTERAIEQVLQSE 197
Cdd:pfam02784 77 RYALEVGVGCVTVDNVDELEKLARLAPE----ARVLLRIKPDDSAATCPL------SSKFGADLD--EDVEALLEAAKLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 198 HIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRdSYSFVSKVLNLGGGFGIRYTEDDEPLHATEYVEKIIEAVKENA 277
Cdd:pfam02784 145 NLQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGA-ELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALEEYF 223
|
250 260
....*....|....*....|
gi 1036011971 278 SryGFDIPEIWIEPGRSLVG 297
Cdd:pfam02784 224 P--GDPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
25-393 |
1.26e-73 |
|
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: 235.57 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 25 LAEKYGTPLYVYDVALIRERAKSFKQAFISAglkAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAER 104
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAALPPA---IEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 105 IHFHGNNKSREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAhTHDYITTGQEDSKFGFDLHng 184
Cdd:cd06839 78 ILFAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFEL-KGSGMKMGGGPSQFGIDVE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 185 QTERAIEQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRDSYSFVSKVLNLGGGFGIRYTEDDEPLHate 264
Cdd:cd06839 155 ELPAVLARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEELGLPLEFLDLGGGFGIPYFPGETPLD--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 265 yVEKIIEAVKENASRYGFDIPE--IWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDN----------IRpa 332
Cdd:cd06839 232 -LEALGAALAALLAELGDRLPGtrVVLELGRYLVGEAGVYVTRVLDRKVSRG-ETFLVTDGGMHHHlaasgnfgqvLR-- 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036011971 333 lyqAKYEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYS 393
Cdd:cd06839 308 ---RNYPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLS 365
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
25-412 |
6.83e-72 |
|
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: 231.00 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 25 LAEKYGTPLYVYDVALIRERAKSFKQAFISAGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAER 104
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 105 IHFHGNNKSREELRMALEHRiGCIVVDNFYEIALLEDLCKETGHSIDVLLRItpgveahTHDYitTGQEDSKFGFDLH-N 183
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEG-ALINIDSFDELERILEIAKELGRVAKVGIRL-------NMNY--GNNVWSRFGFDIEeN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 184 GQTERAIEQVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEwrdSYSFVSKVLNLGGGFG------IRYTEDD 257
Cdd:cd06841 151 GEALAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDR---LFGLELEYLDLGGGFPaktplsLAYPQED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 258 EPLHATEYVEKIIEAVKEnASRYGFDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNIRPALYQAK 337
Cdd:cd06841 228 TVPDPEDYAEAIASTLKE-YYANKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYG-RNIAVTDAGINNIPTIFWYHHP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036011971 338 YEAAAANRIGEAHDKTVsIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRiPRPAVVFVENG 412
Cdd:cd06841 306 ILVLRPGKEDPTSKNYD-VYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFIR-PRPAVYLIDNN 378
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
30-410 |
2.29e-70 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 238.44 E-value: 2.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 30 GTPLYVYDVALIRERAKSFkqafisAGLKA--QVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAgFPA---ER 104
Cdd:PRK08961 502 GSPCYVYHLPTVRARARAL------AALAAvdQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFEL-FPElspER 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 105 IHFHGNNKSREELRMALEhrIGCIV-VDNFYEIALLEDLCKETghsiDVLLRITPGVEAHTHDYITTGQEDSKFGfdLHN 183
Cdd:PRK08961 575 VLFTPNFAPRAEYEAAFA--LGVTVtLDNVEPLRNWPELFRGR----EVWLRIDPGHGDGHHEKVRTGGKESKFG--LSQ 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 184 GQTERAIEqVLQSEHIQLLGVHCHIGSQIFDTagfvlaaekifkklDEWRDSYSFVS---------KVLNLGGGFGIRYT 254
Cdd:PRK08961 647 TRIDEFVD-LAKTLGITVVGLHAHLGSGIETG--------------EHWRRMADELAsfarrfpdvRTIDLGGGLGIPES 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 255 EDDEPLHaTEYVEKIIEAVKENASRYgfdipEIWIEPGRSLVGDAGTTLYTVGSQKEVPGVRqYVAVDGGMNDNIRPALY 334
Cdd:PRK08961 712 AGDEPFD-LDALDAGLAEVKAQHPGY-----QLWIEPGRYLVAEAGVLLARVTQVKEKDGVR-RVGLETGMNSLIRPALY 784
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036011971 335 QAKYEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFVE 410
Cdd:PRK08961 785 GAYHEIVNLSRLDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
32-409 |
2.47e-70 |
|
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: 226.93 E-value: 2.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 32 PLYVYDVALIRERAKSFkqafisAGLKA--QVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAA--GFPAERIHF 107
Cdd:cd06840 13 PCYVYDLETVRARARQV------SALKAvdSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 108 HGNNKSREELRMALEhrIGCIV-VDNFYEIALLEDLCKetghSIDVLLRITPGVEAHTHDYITTGQEDSKFGFDLHngQT 186
Cdd:cd06840 87 TPNFAARSEYEQALE--LGVNVtVDNLHPLREWPELFR----GREVILRIDPGQGEGHHKHVRTGGPESKFGLDVD--EL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 187 ERAIeQVLQSEHIQLLGVHCHIGSQIFDTagfvlaaekifkklDEWRDSYSFVSK---------VLNLGGGFGIRYTEDD 257
Cdd:cd06840 159 DEAR-DLAKKAGIIVIGLHAHSGSGVEDT--------------DHWARHGDYLASlarhfpavrILNVGGGLGIPEAPGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 258 EPLHaTEYVEKIIEAVKENASRYgfdipEIWIEPGRSLVGDAGTTLYTVGSQKEVPGVRqYVAVDGGMNDNIRPALYQAK 337
Cdd:cd06840 224 RPID-LDALDAALAAAKAAHPQY-----QLWMEPGRFIVAESGVLLARVTQIKHKDGVR-FVGLETGMNSLIRPALYGAY 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036011971 338 YEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:cd06840 297 HEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
31-428 |
1.11e-60 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 203.10 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 31 TPLYVYDVALIRERAKSFKQAFisAGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGN 110
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEAL--EGLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 111 NKSREELRMALEHRIgCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHDYITTGQEDSKFGfdLHNGQTERAI 190
Cdd:PLN02537 96 GKLLEDLVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFG--IRNEKLQWFL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 191 EQVLQ-SEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRdSYSFVSKVLNLGGGFGIRYTEDDEPLHATEyveKI 269
Cdd:PLN02537 173 DAVKAhPNELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIR-AQGFELSYLNIGGGLGIDYYHAGAVLPTPR---DL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 270 IEAVKENASRYGFDIpeiWIEPGRSLVGDAGTTLYTVGSQKeVPGVRQYVAVDGGMNDNIRPALYQA-KYEAAAANRIGE 348
Cdd:PLN02537 249 IDTVRELVLSRDLTL---IIEPGRSLIANTCCFVNRVTGVK-TNGTKNFIVIDGSMAELIRPSLYDAyQHIELVSPPPPD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 349 AHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFVENGEAHLVVKR-ETYEDIV 427
Cdd:PLN02537 325 AEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHaETFDDHL 404
|
.
gi 1036011971 428 K 428
Cdd:PLN02537 405 R 405
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
35-406 |
1.43e-47 |
|
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: 167.57 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 35 VYDVALIRERAKSFKQAFISAGLKAqvaYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGNNKSR 114
Cdd:cd06836 7 LYDLDGFRALVARLTAAFPAPVLHT---FAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 115 EELRMALEHRIGcIVVDNFYEIALLEDLCKETGHSIDVL-LRITPGVEAHTHDYITTGQEDSKFGFDLHNGQTERAIEQV 193
Cdd:cd06836 84 AELREALELGVA-INIDNFQELERIDALVAEFKEASSRIgLRVNPQVGAGKIGALSTATATSKFGVALEDGARDEIIDAF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 194 LQSEhiQLLGVHCHIGSQIFdtaGFVLAAEKIFKKLDEWRDSYSFVSK----VLNLGGGFGIRYTEDDEPLHATEYVEKI 269
Cdd:cd06836 163 ARRP--WLNGLHVHVGSQGC---ELSLLAEGIRRVVDLAEEINRRVGRrqitRIDIGGGLPVNFESEDITPTFADYAAAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 270 IEAVKENasrygFDIPEIWI-EPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNIR----PALYQAK---YEAA 341
Cdd:cd06836 238 KAAVPEL-----FDGRYQLVtEFGRSLLAKCGTIVSRVEYTKSSGG-RRIAITHAGAQVATRtayaPDDWPLRvtvFDAN 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036011971 342 AANRIGEAhdKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMANNYNRIPRPAV 406
Cdd:cd06836 312 GEPKTGPE--VVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAV 374
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
30-409 |
5.21e-45 |
|
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: 159.97 E-value: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 30 GTPLYVYDVALIRERAKSFKQAFIsaglKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHG 109
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALP----RVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 110 NNKSREELRMALEHRIGCIVVDNFYEIALLEDLCKEtghsIDVLLRI-TPGVEAHThdyittgQEDSKFGFDLHNgqTER 188
Cdd:cd00622 77 PCKSISDIRYAAELGVRLFTFDSEDELEKIAKHAPG----AKLLLRIaTDDSGALC-------PLSRKFGADPEE--ARE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 189 AIEQVlQSEHIQLLGVHCHIGSQ-----IFDTAgfVLAAEKIFKKLDEwrdsYSFVSKVLNLGGGFGIRYTEDDEPLhat 263
Cdd:cd00622 144 LLRRA-KELGLNVVGVSFHVGSQctdpsAYVDA--IADAREVFDEAAE----LGFKLKLLDIGGGFPGSYDGVVPSF--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 264 eyvEKIIEAVKENASRY-GFDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGVRQYVAV---DG---GMNDnirpALYQ- 335
Cdd:cd00622 214 ---EEIAAVINRALDEYfPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERWYylnDGvygSFNE----ILFDh 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036011971 336 AKYEA---AAANRIGEAHdkTVSIAGKCCESGDMLIWDIDLPE-VKEGDLLAVFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:cd00622 287 IRYPPrvlKDGGRDGELY--PSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
41-264 |
1.16e-43 |
|
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: 152.09 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 41 IRERAKSFKQAFisaGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAERIHFHGNNKSREELRMA 120
Cdd:cd06808 1 IRHNYRRLREAA---PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 121 LEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVeahthdyittgqEDSKFGFDLhnGQTERAIEQVLQSEHIQ 200
Cdd:cd06808 78 AEQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGD------------ENGKFGVRP--EELKALLERAKELPHLR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036011971 201 LLGVHCHIGSQIFDTAGFVLAAEKiFKKLDEWRDSYSFVSKVLNLGGGFGIRYTEDDEPLHATE 264
Cdd:cd06808 144 LVGLHTHFGSADEDYSPFVEALSR-FVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFII 206
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
34-409 |
7.90e-35 |
|
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: 133.17 E-value: 7.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 34 YVYDVALIRERAKSfkqafISAGLKAQVA--YASKAFSSVAMIQLAEEEGLSLDVVSGGELyTAVAAGFPAERIHFHGNN 111
Cdd:cd06843 5 YVYDLAALRAHARA-----LRASLPPGCElfYAIKANSDPPILRALAPHVDGFEVASGGEI-AHVRAAVPDAPLIFGGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 112 KSREELRMALEHRIGCIVVDNFYEIALLEDLCKETGHSIDVLLRITPGVEAHTHDYITTGQEDSKFGFDlhNGQTERAIE 191
Cdd:cd06843 79 KTDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGID--EADLPDALE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 192 QVLQSEHIQLLGVHCHIGSQIFDTAGFVLAAEKIFKKLDEWRDSYSFVSKVLNLGGGFGIRYTEDDEPLHATEYVEKIIE 271
Cdd:cd06843 157 LLRDLPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEHGLDLDVVNVGGGIGVNYADPEEQFDWAGFCEGLDQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 272 AVKENAsrygfDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPGvRQYVAVDGGMNDNIRPALYQ------------AKYE 339
Cdd:cd06843 237 LLAEYE-----PGLTLRFECGRYISAYCGYYVTEVLDLKRSHG-EWFAVLRGGTHHFRLPAAWGhnhpfsvlpveeWPYP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036011971 340 AAAAnrigEAHDKTVSIAGKCCESGDMLIWDIDLPEVKEGDLLAVFCTGAYGYSMAN-NYNRIPRPAVVFV 409
Cdd:cd06843 311 WPRP----SVRDTPVTLVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGWNISHhDFLMHPHPERIYL 377
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
25-409 |
6.26e-34 |
|
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: 131.61 E-value: 6.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 25 LAEKYGTPLYVYDVALIRERAKSFKQAFISAGLKAQVAYASKAFSSVAMIQLAEEEGLSLDVVSGGELYTAVAAGFPAER 104
Cdd:cd06842 4 LVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 105 IHFHGNNKSREELRMALEHRIgCIVVDNFYEIALLEDLCK-ETGHSIDVLLRITPgvEAHTHdyittgqeDSKFGFDLHn 183
Cdd:cd06842 84 IVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLALARgYTTGPARVLLRLSP--FPASL--------PSRFGMPAA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 184 gQTERAIEQVLQS-EHIQLLGVHCHIGSqiFDTAGFVLAAEKIFKKLDEWRdSYSFVSKVLNLGGGFGIRYTEDDE---- 258
Cdd:cd06842 152 -EVRTALERLAQLrERVRLVGFHFHLDG--YSAAQRVAALQECLPLIDRAR-ALGLAPRFIDIGGGFPVSYLADAAewea 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 259 ------------------------------------PLHATEYVEKIIEAVKENASRYGFDIPE----IWIEPGRSLVGD 298
Cdd:cd06842 228 flaaltealygygrpltwrneggtlrgpddfypygqPLVAADWLRAILSAPLPQGRTIAERLRDngitLALEPGRALLDQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 299 AGTTLYTVGSQKEVPGVRQYVAVDGGMndnirpalYQAKYEAA----------AANRIGEAHDKTVSIAGKCCESGDMLI 368
Cdd:cd06842 308 CGLTVARVAFVKQLGDGNHLIGLEGNS--------FSACEFSSeflvdpllipAPEPTTDGAPIEAYLAGASCLESDLIT 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1036011971 369 WD-IDLPE-VKEGDLLAVFCTGayGYSM---ANNYNRIPRPAVVFV 409
Cdd:cd06842 380 RRkIPFPRlPKPGDLLVFPNTA--GYQMdflESRFHRHPLPRRVVV 423
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
27-409 |
1.27e-20 |
|
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: 93.40 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 27 EKYGTPLYVYDVALIRERAKS----FKQAFISAGLKA--QVAYASKA--FSSV--AMIQLAEEEGLSLDVVSGGELYTAV 96
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERlnaaFAKAIEEYGYKGkyQGVYPIKVnqQREVveEIVKAGKRYNIGLEAGSKPELLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 97 AAGFPAERIHFHGNNKSREELRMALEHRIGC----IVVDNFYEIALLEDLCKETGHSIDVLLRITPgVEAHTHDYITTGQ 172
Cdd:cd06830 81 ALLKTPDALIICNGYKDDEYIELALLARKLGhnviIVIEKLSELDLILELAKKLGVKPLLGVRIKL-ASKGSGKWQESGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 173 EDSKFGfdLHNGQTERAIEQVLQS---EHIQLLgvHCHIGSQIFDTAgfvlaaeKIFKKLDEWRDSYSFVSKV------L 243
Cdd:cd06830 160 DRSKFG--LTASEILEVVEKLKEAgmlDRLKLL--HFHIGSQITDIR-------RIKSALREAARIYAELRKLganlryL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 244 NLGGGFGIRYTEDDEPLHAT------EYVEKIIEAVKENASRYGFDIPEIWIEPGRSLVGDAGTTLYTVGSQKEVPgvRQ 317
Cdd:cd06830 229 DIGGGLGVDYDGSRSSSDSSfnysleEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKRLA--DW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 318 YVA---VDGGMNDNIrpALYQaKYEAAAANRIGEAHDKTVSIAGKCCESGDMLIWDIDLPEVK-----------EGDLLA 383
Cdd:cd06830 307 YFCnfsLFQSLPDSW--AIDQ-LFPIMPLHRLNEKPTRRAVLGDITCDSDGKIDSFIDPPDILptlplhplrkdEPYYLG 383
|
410 420
....*....|....*....|....*.
gi 1036011971 384 VFCTGAYGYSMANNYNRIPRPAVVFV 409
Cdd:cd06830 384 FFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
31-407 |
2.43e-11 |
|
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: 64.88 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 31 TPLYVYDVALIRERAKSFKQAFISAGlkAQVAYASKAF------------------SSVAMIQLAEEEGlsldvvsGGEL 92
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSG--AKILLALKAFsmwsvfplireyldgttaSSLFEARLGREEF-------GGEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 93 YTAvAAGFPAERIhfhgnnksREELRMAlEHrigcIVVDNFYEIALLEDLCKETGHSidVLLRITPGV-EAHTHDYITTG 171
Cdd:cd06829 72 HTY-SPAYRDDEI--------DEILRLA-DH----IIFNSLSQLERFKDRAKAAGIS--VGLRINPEYsEVETDLYDPCA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 172 QeDSKFGFDLhngqtERAIEQVLqsEHIQllGVHCH-IGSQIFDTagFVLAAEKIFKKLDEWRDSYsfvsKVLNLGGGfg 250
Cdd:cd06829 136 P-GSRLGVTL-----DELEEEDL--DGIE--GLHFHtLCEQDFDA--LERTLEAVEERFGEYLPQL----KWLNLGGG-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 251 IRYTEDDEPlhateyVEKIIEAVKENASRYGFdipEIWIEPGRSLVGDAG----TTLYTVGSQKEVPGVRqyVAVDGGMN 326
Cdd:cd06829 198 HHITRPDYD------VDRLIALIKRFKEKYGV---EVYLEPGEAVALNTGylvaTVLDIVENGMPIAILD--ASATAHMP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 327 DNI----RPALYQAkyeaaaanRIGEAHDKTVSIAGKCCESGDMlIWDIDLPE-VKEGDLLaVFCTGAyGYSM--ANNYN 399
Cdd:cd06829 267 DVLempyRPPIRGA--------GEPGEGAHTYRLGGNSCLAGDV-IGDYSFDEpLQVGDRL-VFEDMA-HYTMvkTNTFN 335
|
....*...
gi 1036011971 400 RIPRPAVV 407
Cdd:cd06829 336 GVRLPSIA 343
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
12-108 |
1.44e-05 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 47.06 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 12 HGHLEIGGVDALYLAEKYGTPLYV----YDVALIRERAKSFKQAFiSAGLKAQVAYASKAFSSVAmiqlaeeeglsldvV 87
Cdd:cd05844 86 HAHFGRDGVYALPLARALGVPLVVtfhgFDITTSRAWLAASPGWP-SQFQRHRRALQRPAALFVA--------------V 150
|
90 100
....*....|....*....|.
gi 1036011971 88 SGGELYTAVAAGFPAERIHFH 108
Cdd:cd05844 151 SGFIRDRLLARGLPAERIHVH 171
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
112-296 |
2.67e-05 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 46.62 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 112 KSREELRMALehrIGC-------IVVDNFYEIALLEDLCKETGhsIDVLL--RITPGVEAHTHdYITTGQEDSKFGfdLH 182
Cdd:COG1166 151 KDREYIRLAL---LGRklghkviIVIEKLSELELILEEAKELG--VKPLIgvRVKLASKGSGK-WQNSGGERSKFG--LS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 183 NGQTERAIEQvLQSEH----IQLLgvHCHIGSQIFD-----TAgfVLAAEKIFKKLdewrdsysfVS-----KVLNLGGG 248
Cdd:COG1166 223 ASEILEVVER-LKEAGmldcLQLL--HFHLGSQIPNirdikRA--VREAARFYAEL---------RKlgapiEYLDVGGG 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1036011971 249 FGIRYteddEPLHAT----------EYVEKIIEAVKENASRYGFDIPEIWIEPGRSLV 296
Cdd:COG1166 289 LGVDY----DGSRSNsdssmnyslqEYANDVVYAIKEVCDEAGVPHPTIISESGRALT 342
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
112-296 |
3.17e-05 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 46.27 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 112 KSREELRMALehrIGC-------IVVDNFYEIALLEDLCKETGhsidvllrITP--GVEA--HTH---DYITTGQEDSKF 177
Cdd:PRK05354 155 KDREYIRLAL---IGRklghkvfIVIEKLSELELILEEAKELG--------VKPrlGVRArlASQgsgKWQSSGGEKSKF 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 178 GfdLHNGQTERAIEQvLQSEH----IQLLgvHCHIGSQIFD-----TAgfVLAAEKIFKKLdewrdsysfvSKV------ 242
Cdd:PRK05354 224 G--LSATEVLEAVER-LREAGlldcLQLL--HFHLGSQIANirdikTA--VREAARFYVEL----------RKLgapiqy 286
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 243 LNLGGGFGIRYTEDDEPLHA------TEYVEKIIEAVKENASRYGFDIPEIWIEPGRSLV 296
Cdd:PRK05354 287 LDVGGGLGVDYDGTRSQSDSsvnyslQEYANDVVYTLKEICEEHGVPHPTIISESGRALT 346
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
112-296 |
1.35e-04 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 44.29 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 112 KSREELRMALEHR-IGC---IVVDNFYEIALLEDLCKETGHsidvllRITPGVEA-----HTHDYITTGQEDSKFGfdLH 182
Cdd:PLN02439 92 KDAEYVSLALLARkLGLntvIVLEQEEELDLVIEASQRLGV------RPVIGVRAklrtkHSGHFGSTSGEKGKFG--LT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036011971 183 NGQTERAI---EQVLQSEHIQLLgvHCHIGSQIFDTAGF---VLAAEKIFKKLdewrdsysfVS-----KVLNLGGGFGI 251
Cdd:PLN02439 164 ATEIVRVVrklRKEGMLDCLQLL--HFHIGSQIPSTSLLkdgVSEAAQIYCEL---------VRlgapmRVIDIGGGLGI 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1036011971 252 RY-----TEDDEPLHAT--EYVEKIIEAVKENASRYGFDIPEIWIEPGRSLV 296
Cdd:PLN02439 233 DYdgsksGSSDMSVAYSleEYANAVVAAVRDVCDRKGVKHPVICSESGRALV 284
|
|
| |
