|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
46-463 |
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: 535.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 46 LQIGGCDVTTLVEQFGSPLYILDEKTLRSACQQYRDAFKqyyKGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELY 125
Cdd:COG0019 10 LTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFP---GSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 126 TALQAGVNPEKIYLHNNNKSREELIFATEAGC-TIVVDNWHELRTLVEIVESANspsVHPRLLLRLTPGIECHTHEYIRT 204
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAAELG---KRAPVGLRVNPGVDAGTHEYIST 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 205 GQLDSKFGFDPNELEELFTFVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKY 284
Cdd:COG0019 164 GGKDSKFGIPLEDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 285 IESDDPPSIEEWVKPICEVIQEACAvenlPLPKLLCEPGRSLIATACVTAYTIGSSKVIpEIRTYVAIDGGMSDNPRPIT 364
Cdd:COG0019 244 TEGDEPPDLEELAAAIKEALEELCG----LGPELILEPGRALVGNAGVLLTRVLDVKEN-GGRRFVIVDAGMNDLMRPAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 365 YQSVYRAVVANKISSPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVVANGE 444
Cdd:COG0019 319 YGAYHPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE 398
|
410
....*....|....*....
gi 1297078214 445 ANLILQRETYQDLIRQDRL 463
Cdd:COG0019 399 ARLIRRRETYEDLLASEVL 417
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
40-462 |
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: 516.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 40 VYNHD-LLQIGGCDVTTLVEQFGSPLYILDEKTLRSACQQYRDAFKqyykGESQVLYASKAWNCLAVCAIAASEGLGIDV 118
Cdd:TIGR01048 2 VENEDgELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFG----GRSLVCYAVKANSNLAVLRLLAELGSGFDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 119 ASGGELYTALQAGVNPEKIYLHNNNKSREELIFATEAGCTIVVDNWHELRTLVEIVESANSPSvhpRLLLRLTPGIECHT 198
Cdd:TIGR01048 78 VSGGELYRALAAGFPPEKIVFSGNGKSRAELERALELGICINVDSFSELERLNEIAPELGKKA---RISLRVNPGVDAKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 199 HEYIRTGQLDSKFGFDPNELEELFTFVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKyGLKLTELNVGG 278
Cdd:TIGR01048 155 HPYISTGLKDSKFGIDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAE-GIDLEFLDLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 279 GLGIKYIESDDPPSIEEWVKPICEVIQEACAVEnlPLPKLLCEPGRSLIATACVTAYTIGSSKVIPEiRTYVAIDGGMSD 358
Cdd:TIGR01048 234 GLGIPYTPEEEPPDLSEYAQAILNALEGYADLG--LDPKLILEPGRSIVANAGVLLTRVGFVKETGS-RNFVIVDAGMND 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 359 NPRPITYQSVYRAVVANKISSPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAV 438
Cdd:TIGR01048 311 LIRPALYGAYHHIIVLNRTNDAPTEVADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEV 390
|
410 420
....*....|....*....|....
gi 1297078214 439 VVANGEANLILQRETYQDLIRQDR 462
Cdd:TIGR01048 391 LVDGGQARLIRRRETYEDLWALEV 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
60-440 |
2.64e-168 |
|
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: 478.52 E-value: 2.64e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 60 FGSPLYILDEKTLRSACQQYRDAFKqyyKGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYL 139
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFS---GPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 140 HNNNKSREELIFATEAG-CTIVVDNWHELRTLVEIvesANSPSVHPRLLLRLTPGIECHTHEYIRTGQLDSKFGFDPNEL 218
Cdd:cd06828 78 TGNGKSDEELELALELGiLRINVDSLSELERLGEI---APELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 219 EELFTFVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYIESDDPPSIEEWVK 298
Cdd:cd06828 155 LEAYRRAKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 299 PICEVIQEACavENLPLPKLLCEPGRSLIATACVTAYTIGSSKVIPeIRTYVAIDGGMSDNPRPITYQSVYRAVVANKIS 378
Cdd:cd06828 235 AIAEALKELC--EGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETG-GKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPG 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1297078214 379 SPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVV 440
Cdd:cd06828 312 EGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
62-440 |
7.51e-100 |
|
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: 303.84 E-value: 7.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 62 SPLYILDEKTLRSACQQYRDAFKqyykGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHN 141
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALP----SGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 142 NNKSREELIFATEAG-CTIVVDNWHELRTLVEIVESANSPsvhPRLLLRLTPGIECHTHeYIRTGQLDSKFGFDPNELEE 220
Cdd:cd06810 77 PAKSVSEIEAALASGvDHIVVDSLDELERLNELAKKLGPK---ARILLRVNPDVSAGTH-KISTGGLKSKFGLSLSEARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 221 LFTfVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYieSDDPPSIEEWVKPI 300
Cdd:cd06810 153 ALE-RAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPY--DEQPLDFEEYAALI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 301 CEVIQEACavENLPLPKLLCEPGRSLIATACVTAYTIGSSKVIPEIRTYVaIDGGMSDNPRP-ITYQSVYRA-VVANKIS 378
Cdd:cd06810 230 NPLLKKYF--PNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAV-VDGGMNHSFRPaLAYDAYHPItPLKAPGP 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1297078214 379 SPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVV 440
Cdd:cd06810 307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
64-419 |
1.26e-99 |
|
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: 302.10 E-value: 1.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 64 LYILDEKTLRSACQQYRDAFKqyykGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHNNN 143
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALP----PRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 144 KSREELIFATEAGC-TIVVDNWHELRTLVEIvesanSPSVHPRLLLRLTPGIECHTHeYIRTGQLDSKFGFDPNELEELF 222
Cdd:pfam00278 77 KTDSEIRYALEAGVlCFNVDSEDELEKIAKL-----APELVARVALRINPDVDAGTH-KISTGGLSSKFGIDLEDAPELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 223 TFVsKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYiESDDPPSIEEwvkpICE 302
Cdd:pfam00278 151 ALA-KELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPY-RDEPPPDFEE----YAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 303 VIQEACAVENLPLPKLLCEPGRSLIATACVTAYTIGSSKVIPEiRTYVAIDGGMSDNPRPITYQSVYRAVVANKISSPLT 382
Cdd:pfam00278 225 AIREALDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGG-KTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGPL 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 1297078214 383 QTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTG 419
Cdd:pfam00278 304 ETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
56-443 |
2.02e-67 |
|
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: 220.60 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 56 LVEQFGSPLYILDEKTLRSACQQYRDAFKQYYKGeSQVLYASKAwNCL-AVCAIAASEGLGIDVASGGELYTALQAGVNP 134
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYPN-VVIAYSYKT-NYLpAICKILHEEGGYAEVVSAMEYELALKLGVPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 135 EKIYLHNNNKSREELIFATEAGCTIVVDNWHELRTLVEIVESANSPsvhPRLLLRLTpgiechtheYIRTGQLDSKFGFD 214
Cdd:cd06841 79 KRIIFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGRV---AKVGIRLN---------MNYGNNVWSRFGFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 215 PNELEELFTFVSKQSF---LNCVGLHAHIGSQIfeRQPHRDLAALMvQWLREAAK-YGLKLTELNVGGGLG------IKY 284
Cdd:cd06841 147 IEENGEALAALKKIQEsknLSLVGLHCHVGSNI--LNPEAYSAAAK-KLIELLDRlFGLELEYLDLGGGFPaktplsLAY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 285 IESDDPPSIEEWVKPICEVIQEACAVENlPLPKLLCEPGRSLIATAcvtAYTIGSSKVIPEIR-TYVAI-DGGMSDNPRP 362
Cdd:cd06841 224 PQEDTVPDPEDYAEAIASTLKEYYANKE-NKPKLILEPGRALVDDA---GYLLGRVVAVKNRYgRNIAVtDAGINNIPTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 363 ITY-QSVYraVVANKISSPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRlPRPAAVVVA 441
Cdd:cd06841 300 FWYhHPIL--VLRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFIR-PRPAVYLID 376
|
..
gi 1297078214 442 NG 443
Cdd:cd06841 377 NN 378
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
56-440 |
2.54e-61 |
|
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: 204.75 E-value: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 56 LVEQFGSPLYILDEKTLRSACQQYRDAFKQyykgESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPE 135
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAALPP----AIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 136 KIYLHNNNKSREELIFATEAGC-TIVVDNWHELRTLVEIVESANspsVHPRLLLRLTPGIEChTHEYIRTGQLDSKFGFD 214
Cdd:cd06839 77 KILFAGPGKSDAELRRAIEAGIgTINVESLEELERIDALAEEHG---VVARVALRINPDFEL-KGSGMKMGGGPSQFGID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 215 PNELEELFTFVSKQSFLNCVGLHAHIGSQIferqphRDLAALMVQW-------LREAAKYGLKLTELNVGGGLGIKYIES 287
Cdd:cd06839 153 VEELPAVLARIAALPNLRFVGLHIYPGTQI------LDADALIEAFrqtlalaLRLAEELGLPLEFLDLGGGFGIPYFPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 288 DDPPSIEEWVKPICEVIQEACAveNLPLPKLLCEPGRSLIATACVTAYTIGSSKViPEIRTYVAIDGGMSDN-----PRP 362
Cdd:cd06839 227 ETPLDLEALGAALAALLAELGD--RLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-SRGETFLVTDGGMHHHlaasgNFG 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1297078214 363 ITYQSVYRAVVANKISSPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSmASNYNRLPRPAAVVV 440
Cdd:cd06839 304 QVLRRNYPLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLS-ASPLAFLSHPAPAEV 380
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
52-459 |
4.23e-61 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 205.03 E-value: 4.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 52 DVTTLVEQfgSPLYILDEKTLRSACQQYRDAFKQYykgESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAG 131
Cdd:PLN02537 10 DIMESVEK--RPFYLYSKPQITRNYEAYKEALEGL---RSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 132 VNPEKIYLHNNNKSREELIFATEAGCTIVVDNWHELRtlvEIVESANSPSVHPRLLLRLTPGIECHTHEYIRTGQLDSKF 211
Cdd:PLN02537 85 FDPTRCIFNGNGKLLEDLVLAAQEGVFVNVDSEFDLE---NIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 212 GFDPNELEELFTFVSKQS-FLNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYIESDDP 290
Cdd:PLN02537 162 GIRNEKLQWFLDAVKAHPnELKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYYHAGAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 291 -PSIEEWVKPICEVIQEacavENLplpKLLCEPGRSLIATACVTAYTIGSSKViPEIRTYVAIDGGMSDNPRPityqSVY 369
Cdd:PLN02537 242 lPTPRDLIDTVRELVLS----RDL---TLIIEPGRSLIANTCCFVNRVTGVKT-NGTKNFIVIDGSMAELIRP----SLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 370 RAVVANKISSPLT-----QTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVVAN-G 443
Cdd:PLN02537 310 DAYQHIELVSPPPpdaevSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEdG 389
|
410
....*....|....*.
gi 1297078214 444 EANLILQRETYQDLIR 459
Cdd:PLN02537 390 SITKIRHAETFDDHLR 405
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
61-441 |
1.08e-53 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 192.99 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 61 GSPLYILDEKTLRSACQQYrdafkQYYKGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQA--GVNPEKIY 138
Cdd:PRK08961 502 GSPCYVYHLPTVRARARAL-----AALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 139 LHNNNKSREELIFATEAGCTIVVDNWHELRTLVEIVESANspsvhprLLLRLTPGIECHTHEYIRTGQLDSKFGFDPNEL 218
Cdd:PRK08961 577 FTPNFAPRAEYEAAFALGVTVTLDNVEPLRNWPELFRGRE-------VWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRI 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 219 EELFTfVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLRE--AAKYglklteLNVGGGLGIKYIESDDPPSIEEW 296
Cdd:PRK08961 650 DEFVD-LAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRfpDVRT------IDLGGGLGIPESAGDEPFDLDAL 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 297 VKPICEVIQEAcavenlPLPKLLCEPGRSLIATACVTAYTIGSSKVIPEIRtYVAIDGGMSDNPRPITYQSVYRAVVANK 376
Cdd:PRK08961 723 DAGLAEVKAQH------PGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVR-RVGLETGMNSLIRPALYGAYHEIVNLSR 795
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297078214 377 ISSPLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVVA 441
Cdd:PRK08961 796 LDEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
71-328 |
2.68e-53 |
|
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: 179.01 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 71 TLRSACQQYRDAFKQYykgesQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHNNNKSREELI 150
Cdd:pfam02784 3 SIERRHRRWKKALPRI-----KPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 151 FATEAGCT-IVVDNWHELRTLVEIVESAnspsvhpRLLLRLTPGIECHTHEYirtgqlDSKFGFDPNELEELFTFVSKQS 229
Cdd:pfam02784 78 YALEVGVGcVTVDNVDELEKLARLAPEA-------RVLLRIKPDDSAATCPL------SSKFGADLDEDVEALLEAAKLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 230 FLNCVGLHAHIGSQIFERQPH----RDLAALMVQWlreaAKYGLKLTELNVGGGLGIKYIESDDPPSIEEWVKPICEVIQ 305
Cdd:pfam02784 145 NLQVVGVSFHVGSGCTDAEAFvlalEDARGVFDQG----AELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINEALE 220
|
250 260
....*....|....*....|...
gi 1297078214 306 EACAVenLPLPKLLCEPGRSLIA 328
Cdd:pfam02784 221 EYFPG--DPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
62-440 |
3.25e-51 |
|
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: 177.63 E-value: 3.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 62 SPLYILDEKTLRSACQQYrdafkQYYKGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQA--GVNPEKIYL 139
Cdd:cd06840 12 GPCYVYDLETVRARARQV-----SALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 140 HNNNKSREELIFATEAGCTIVVDNWHELRTLVEIVESAnspsvhpRLLLRLTPGIECHTHEYIRTGQLDSKFGFDPNELE 219
Cdd:cd06840 87 TPNFAARSEYEQALELGVNVTVDNLHPLREWPELFRGR-------EVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 220 ELFTfVSKQSFLNCVGLHAHIGSQIFERqphrDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYIESDDPPSIEEWVKP 299
Cdd:cd06840 160 EARD-LAKKAGIIVIGLHAHSGSGVEDT----DHWARHGDYLASLARHFPAVRILNVGGGLGIPEAPGGRPIDLDALDAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 300 ICEVIQEacavenLPLPKLLCEPGRSLIATACVTAYTIGSSKVIPEIRtYVAIDGGMSDNPRPITYQSVYRAVVANKISS 379
Cdd:cd06840 235 LAAAKAA------HPQYQLWMEPGRFIVAESGVLLARVTQIKHKDGVR-FVGLETGMNSLIRPALYGAYHEIVNLSRLDE 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1297078214 380 PLTQTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYNRLPRPAAVVV 440
Cdd:cd06840 308 PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
61-440 |
2.09e-48 |
|
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: 169.98 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 61 GSPLYILDEKTLRSACQQYRDAFKQyykgeSQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLH 140
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPR-----VRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 141 NNNKSREELIFATEAGCTI-VVDNWHELRTLVEIVESAnspsvhpRLLLRLT---PGIEChtheyirtgQLDSKFGFDPN 216
Cdd:cd00622 76 NPCKSISDIRYAAELGVRLfTFDSEDELEKIAKHAPGA-------KLLLRIAtddSGALC---------PLSRKFGADPE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 217 ELEELFTfVSKQSFLNCVGLHAHIGSQIFERQPHRDlAALMVQWL-REAAKYGLKLTELNVGGGLGIKYIEsdDPPSIEE 295
Cdd:cd00622 140 EARELLR-RAKELGLNVVGVSFHVGSQCTDPSAYVD-AIADAREVfDEAAELGFKLKLLDIGGGFPGSYDG--VVPSFEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 296 wvkpICEVIQEACAvENLP--LPKLLCEPGRSLIATACVTAYT-IGSSKVIPEIRTY-VAIDGG--------MSDNPRPI 363
Cdd:cd00622 216 ----IAAVINRALD-EYFPdeGVRIIAEPGRYLVASAFTLAVNvIAKRKRGDDDRERwYYLNDGvygsfneiLFDHIRYP 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1297078214 364 tyqsvYRAVVANKISSPLtQTVTIAGKHCESGDILIKNALLPKT-EPGDILVVMGTGAYNYSMASNYNRLPRPAAVVV 440
Cdd:cd00622 291 -----PRVLKDGGRDGEL-YPSSLWGPTCDSLDVIYEDVLLPEDlAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
72-299 |
3.41e-38 |
|
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: 138.22 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 72 LRSACQQYRDAFKqyykGESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHNNNKSREELIF 151
Cdd:cd06808 1 IRHNYRRLREAAP----AGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 152 ATEAGC-TIVVDNWHELRTLVEIVESANSPSvhpRLLLRLTPGIEchtheyirtgqlDSKFGFDPNELEELFTFVSKQSF 230
Cdd:cd06808 77 AAEQGViVVTVDSLEELEKLEEAALKAGPPA---RVLLRIDTGDE------------NGKFGVRPEELKALLERAKELPH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1297078214 231 LNCVGLHAHIGSQIFERQPHRDLAALMVQWLREAAKYGLKLTELNVGGGLGIKYIeSDDPPSIEEWVKP 299
Cdd:cd06808 142 LRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYL-QELPLGTFIIVEP 209
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
64-436 |
1.19e-36 |
|
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: 138.68 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 64 LYILDEktLRSACQQYRDAFKQyykgesQVLY--ASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHN 141
Cdd:cd06836 7 LYDLDG--FRALVARLTAAFPA------PVLHtfAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 142 NNKSREELIFATEAGCTIVVDNWHELRTLVEIVESANSPSVhpRLLLRLTPGIECHTHEYIRTGQLDSKFG--FDPNELE 219
Cdd:cd06836 79 PAKTRAELREALELGVAINIDNFQELERIDALVAEFKEASS--RIGLRVNPQVGAGKIGALSTATATSKFGvaLEDGARD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 220 ELFTFVSKQSFLNCvgLHAHIGSQIFERQPHRDLAALMVQwLREA--AKYG-LKLTELNVGGGLGIKYIESDDPPSIEEW 296
Cdd:cd06836 157 EIIDAFARRPWLNG--LHVHVGSQGCELSLLAEGIRRVVD-LAEEinRRVGrRQITRIDIGGGLPVNFESEDITPTFADY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 297 VKpiceVIQEAcavenlpLPKL-------LCEPGRSLIATACVTAYTIgsskvipeirTYVAIDGGmsdnpRPITY---- 365
Cdd:cd06836 234 AA----ALKAA-------VPELfdgryqlVTEFGRSLLAKCGTIVSRV----------EYTKSSGG-----RRIAIthag 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 366 -----QSVY-------RAVVANKISSPLT---QTVTIAGKHCESGDILIKNALLPKTEPGDILVVMGTGAYNYSMASNYN 430
Cdd:cd06836 288 aqvatRTAYapddwplRVTVFDANGEPKTgpeVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYN 367
|
....*.
gi 1297078214 431 RLPRPA 436
Cdd:cd06836 368 SLPRPA 373
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
56-440 |
7.42e-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: 132.00 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 56 LVEQFGSPLYILDEKTLRSACQQYRDAFKQYYKgESQVLYASKAWNCLAVCAIAASEGLGIDVASGGELYTALQAGVNPE 135
Cdd:cd06842 4 LVEAYGSPLNVLFPQTFRENIAALRAVLDRHGV-DGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 136 KIYLHNNNKSREELIFATEAGCTIVVDNWHELRTLVEIVESANSPsvHPRLLLRLTPgiechtheyiRTGQLDSKFGFDP 215
Cdd:cd06842 83 RIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALARGYTTG--PARVLLRLSP----------FPASLPSRFGMPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 216 NELEELFTFVSK-QSFLNCVGLHAHIGSQifeRQPHRDLAAL-MVQWLREAAKYGLKLTELNVGGGLGIKYIESDD---- 289
Cdd:cd06842 151 AEVRTALERLAQlRERVRLVGFHFHLDGY---SAAQRVAALQeCLPLIDRARALGLAPRFIDIGGGFPVSYLADAAewea 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 290 ------------------------------------PPSIEEWVKPI----CEVIQEACAVENLPLPKLLCEPGRSLIAT 329
Cdd:cd06842 228 flaaltealygygrpltwrneggtlrgpddfypygqPLVAADWLRAIlsapLPQGRTIAERLRDNGITLALEPGRALLDQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 330 ACVTAYTIGSSKVIPEIRTYVAIDGGMSDN--------PRPITyqsvyraVVANKISSPLTQT-VTIAGKHCESGDILIK 400
Cdd:cd06842 308 CGLTVARVAFVKQLGDGNHLIGLEGNSFSAcefsseflVDPLL-------IPAPEPTTDGAPIeAYLAGASCLESDLITR 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1297078214 401 NAL----LPKtePGDILVVMGTGAYN-YSMASNYNRLPRPAAVVV 440
Cdd:cd06842 381 RKIpfprLPK--PGDLLVFPNTAGYQmDFLESRFHRHPLPRRVVV 423
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
58-440 |
2.09e-22 |
|
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: 98.80 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 58 EQFGSPLYILDEKTLRSACQQYRDAFKQ-----YYKGESQVLYASKAwN--CLAVCAIAAS---EGLGIDVASGGELYTA 127
Cdd:cd06830 1 RGYGLPLLLRFPDILRHRIERLNAAFAKaieeyGYKGKYQGVYPIKV-NqqREVVEEIVKAgkrYNIGLEAGSKPELLAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 128 LQAGVNPEKIYLHNNNKSRE--ELIFATEAG---CTIVVDNWHELRTLVEIVESANspsVHPRLLLR--LTPGIECHTHE 200
Cdd:cd06830 80 LALLKTPDALIICNGYKDDEyiELALLARKLghnVIIVIEKLSELDLILELAKKLG---VKPLLGVRikLASKGSGKWQE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 201 yirTGQLDSKFGFDPNELEELFTFVSKQSFLNCVGL-HAHIGSQIferqphRDLAALmVQWLREAAKY-------GLKLT 272
Cdd:cd06830 157 ---SGGDRSKFGLTASEILEVVEKLKEAGMLDRLKLlHFHIGSQI------TDIRRI-KSALREAARIyaelrklGANLR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 273 ELNVGGGLGIKYIESDDPP------SIEEWVKPICEVIQEACAVENLPLPKLLCEPGRSLIATACVTAYTIGSskVIPEI 346
Cdd:cd06830 227 YLDIGGGLGVDYDGSRSSSdssfnySLEEYANDIVKTVKEICDEAGVPHPTIVTESGRAIVAHHSVLIFEVLG--VKRLA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 347 RTYVaIDGGMsdnprpitYQS---------VYRAVVANKISSPLTQTVTIAGKHCES--------GDILIKNAL-LPKTE 408
Cdd:cd06830 305 DWYF-CNFSL--------FQSlpdswaidqLFPIMPLHRLNEKPTRRAVLGDITCDSdgkidsfiDPPDILPTLpLHPLR 375
|
410 420 430
....*....|....*....|....*....|....
gi 1297078214 409 PGDI--LVVMGTGAYNYSMASNYNRLPRPAAVVV 440
Cdd:cd06830 376 KDEPyyLGFFLVGAYQEILGDLHNLFGDTNAVHV 409
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
92-435 |
1.39e-19 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 90.03 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 92 QVLYASKAWNCLAVCAIAASEGLGIDVASGGELytALQAGVNPEK-IYLHNNNKSREELIFATEAG-CTIVVDNWHELRT 169
Cdd:cd06843 28 ELFYAIKANSDPPILRALAPHVDGFEVASGGEI--AHVRAAVPDApLIFGGPGKTDSELAQALAQGvERIHVESELELRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 170 LVEIVESANSPSvhpRLLLRLTPGIECHTHEYIRTGQLDSKFGFDPNELEELFTFVSKQSFLNCVGLHAHIGSQIFERQP 249
Cdd:cd06843 106 LNAVARRAGRTA---PVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDLPNIRLRGFHFHLMSHNLDAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 250 HRDLAALMVQWLRE-AAKYGLKLTELNVGGGLGIKYiesDDPPSIEEWVKpICEVIQEACAvENLPLPKLLCEPGRSLIA 328
Cdd:cd06843 183 HLALVKAYLETARQwAAEHGLDLDVVNVGGGIGVNY---ADPEEQFDWAG-FCEGLDQLLA-EYEPGLTLRFECGRYISA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 329 tACvtAYTIgsSKVIpEI-----RTYVAIDGGMSDNPRPITYQ-----SVYRaVVANKISSP----LTQTVTIAGKHCES 394
Cdd:cd06843 258 -YC--GYYV--TEVL-DLkrshgEWFAVLRGGTHHFRLPAAWGhnhpfSVLP-VEEWPYPWPrpsvRDTPVTLVGQLCTP 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1297078214 395 GDILIKNALLPKTEPGDILVVMGTGAYNYSMaSNYNRL--PRP 435
Cdd:cd06843 331 KDVLARDVPVDRLRAGDLVVFPLAGAYGWNI-SHHDFLmhPHP 372
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
118-368 |
1.95e-13 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 72.46 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 118 VASGGELYTALQAGVNPEKI----YLHNNN--------KSRE--ELIF-ATEAG--CTIVVDNWHELRTLVEIVESANsp 180
Cdd:PRK05354 117 VASGKPYNLGLEAGSKPELMavlaLAGDPGalivcngyKDREyiRLALiGRKLGhkVFIVIEKLSELELILEEAKELG-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 181 sVHPRLLLRltpgiechtheyIR-----------TGQLDSKFGFDPNELEELFTFVSKQSFLNCVGL-HAHIGSQIFERQ 248
Cdd:PRK05354 195 -VKPRLGVR------------ARlasqgsgkwqsSGGEKSKFGLSATEVLEAVERLREAGLLDCLQLlHFHLGSQIANIR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 249 PHRDlaALmvqwlREAAKY-------GLKLTELNVGGGLGIKY--IESDDPPSI----EEWVKPICEVIQEACAVENLPL 315
Cdd:PRK05354 262 DIKT--AV-----REAARFyvelrklGAPIQYLDVGGGLGVDYdgTRSQSDSSVnyslQEYANDVVYTLKEICEEHGVPH 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1297078214 316 PKLLCEPGRSLIAT-ACVTAYTIGSSKVIPEIRTYVAIdggmsDNPRPI-----TYQSV 368
Cdd:PRK05354 335 PTIISESGRALTAHhAVLVFNVLGVESQEYEEPPAPAE-----DAPPLLqnlweTYQEI 388
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
209-328 |
2.80e-12 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 68.96 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 209 SKFGFDPNELEELFTFVSKQSFLNCVGL-HAHIGSQIferqPH-RDLAALMvqwlREAAKY-------GLKLTELNVGGG 279
Cdd:COG1166 217 SKFGLSASEILEVVERLKEAGMLDCLQLlHFHLGSQI----PNiRDIKRAV----REAARFyaelrklGAPIEYLDVGGG 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1297078214 280 LGIKYiE---SDDPPSI----EEWVKPICEVIQEACAVENLPLPKLLCEPGRSLIA 328
Cdd:COG1166 289 LGVDY-DgsrSNSDSSMnyslQEYANDVVYAIKEVCDEAGVPHPTIISESGRALTA 343
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
110-382 |
3.21e-12 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 68.56 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 110 ASEGLGIDVASGGELYTALQ--AGVNPEKIYLHNNNKSREELIFATEA-----GCTIVVDNWHELRTLVEIVesaNSPSV 182
Cdd:PLN02439 56 SPFRFGLEAGSKPELLLAMSclCKGSPDAFLICNGYKDAEYVSLALLArklglNTVIVLEQEEELDLVIEAS---QRLGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 183 HPRLLLR--LTPGIECHTHEyirTGQLDSKFGFDPNELEELFTFVSKQSFLNCVGL-HAHIGSQIFERQPHRDLAALMVQ 259
Cdd:PLN02439 133 RPVIGVRakLRTKHSGHFGS---TSGEKGKFGLTATEIVRVVRKLRKEGMLDCLQLlHFHIGSQIPSTSLLKDGVSEAAQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 260 WLREAAKYGLKLTELNVGGGLGIKY-----IESDDPP--SIEEWVKPICEVIQEACAVENLPLPKLLCEPGRSLIATACV 332
Cdd:PLN02439 210 IYCELVRLGAPMRVIDIGGGLGIDYdgsksGSSDMSVaySLEEYANAVVAAVRDVCDRKGVKHPVICSESGRALVSHHSV 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1297078214 333 TAYTIGSSKVIPEIRTYVAID---GGMSDNPRpITYQSVYRAVVANKISSPLT 382
Cdd:PLN02439 290 LIFEAVSASKRGVPAADDDDQyllLGLTEELR-ADYENLYAAADRGDYEECLL 341
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
104-436 |
9.26e-06 |
|
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: 47.92 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 104 AVCAIAASEGLGIDVASGGELYTALQAGVNPEKIYLHNNNKSREELIFATEAGCTIVV-DNWHELRTLVEivesaNSPSV 182
Cdd:cd06831 50 AVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTcDNEIELKKIAR-----NHPNA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 183 hpRLLLRLTpgiechTHEYIRTGQLDSKFGFDPNELEELFTfVSKQSFLNCVGLHAHIGSQIFERQPHRDLAALMVQWLR 262
Cdd:cd06831 125 --KLLLHIA------TEDNIGGEEMNMKFGTTLKNCRHLLE-CAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 263 EAAKYGLKLTELNVGGGLGIKYIESDDPPSIeewVKPICEV-IQEACAVenlplpKLLCEPGRSLIATACVTAYTIGSSK 341
Cdd:cd06831 196 MAEEFGFKMNMLDIGGGFTGSEIQLEEVNHV---IRPLLDVyFPEGSGI------QIIAEPGSYYVSSAFTLAVNVIAKK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297078214 342 VIPEIRTYVAIDGGMSDNPRPI------TYQSVYRAVVANKISSPLTQ----------TVTIAGKHCESGDILIKNALLP 405
Cdd:cd06831 267 AVENDKHLSSVEKNGSDEPAFVyymndgVYGSFASKLSEKLNTTPEVHkkykedeplfTSSLWGPSCDELDQIVESCLLP 346
|
330 340 350
....*....|....*....|....*....|.
gi 1297078214 406 KTEPGDILVVMGTGAYNYSMASNYNRLPRPA 436
Cdd:cd06831 347 ELNVGDWLIFDNMGAGSLHEPSTFNDFQRPA 377
|
|
| |
