|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
26-419 |
0e+00 |
|
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: 760.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 26 DNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSP 105
Cdd:cd06831 1 DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 106 ENIIYISPCKQVAQIKYAAKVGVNIMTCDNEVELKKISRNHPNAKVLLHIATEDAIGGEEGNMKFGTTLKNCRHLLECAK 185
Cdd:cd06831 81 ENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 186 ELDVQIIGVKFHVSSSCKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEYQLEEVNHVISPLLDIYFPEGSG 265
Cdd:cd06831 161 ELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 266 IKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFSSGVEKTGSDEPAFMYYMNDGVYGSFASKLSEDLNTVPEVHKKYKDD 345
Cdd:cd06831 241 IQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKED 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 683524034 346 EPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPTIYYMMSFSDWYEMQDAG 419
Cdd:cd06831 321 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG 394
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-406 |
4.87e-176 |
|
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: 496.63 E-value: 4.87e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 37 KNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 117 VAQIKYAAKVGVNIMTCDNEVELKKISRNHPNAKVLLHIATEDAIGGEEGNMKFGTTLKNCRHLLECAKELDVQIIGVKF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 197 HVSSSCKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEYQ----LEEVNHVISPLLDIYFPEGsGIKIISEP 272
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvvpsFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 273 GSYYVSSAFTLAVNIIAKKVVendkfssgvektGSDEPAFMYYMNDGVYGSFASKLSEDLNTVPEVHKKYKDDEPLFTSS 352
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKR------------GDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSS 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 683524034 353 LWGPSCDELDQIVENCLLPE-LNVGDWLIFDNMGADSFHEPSAFNDFQRPTIYYM 406
Cdd:cd00622 308 LWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
38-406 |
1.46e-133 |
|
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: 388.97 E-value: 1.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 38 NAFFVGDLGKIVKKHSQWQNV-VAQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQ 116
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAlPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 117 VAQIKYAAKVGVNIMTCDNEVELKKISRNH----PNAKVLLHIATEDAIGGEEGNM-----KFGTTLKNCRHLLECAKEL 187
Cdd:cd06810 81 VSEIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSAGTHKISTgglksKFGLSLSEARAALERAKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 188 DVQIIGVKFHVSSSCKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGT----EYQLEEVNHVISPLLDIYFPEG 263
Cdd:cd06810 161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPydeqPLDFEEYAALINPLLKKYFPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 264 SGIKIISEPGSYYVSSAFTLAVNIIAKKVVENdkfssgvektgsdepAFMYYMNDGVYGSFASKLSEDLNTVPEVHKKYK 343
Cdd:cd06810 241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGG---------------RFFAVVDGGMNHSFRPALAYDAYHPITPLKAPG 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 683524034 344 DDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPTIYYM 406
Cdd:cd06810 306 PDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-385 |
3.05e-121 |
|
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: 356.80 E-value: 3.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 40 FFVGDLGKIVKKHSQWQNVVA-QIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVA 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALPpRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 119 QIKYAAKVGVNIMTCDNEVELKKISRNHPN--AKVLLHIATEDAIGGEEGNM-----KFGTTLKNCRHLLECAKELDVQI 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 192 IGVKFHVSSSCKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF-----TGTEYQLEEVNHVISPLLDIYFPEgsGI 266
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 267 KIISEPGSYYVSSAFTLAVNIIAKKVVENdkfssgvektgsdepAFMYYMNDGVYGSFASKLSEDLNTVPEVhkKYKDDE 346
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMNDLFRPALYDAYHPIPVV--KEPGEG 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 683524034 347 PLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMG 385
Cdd:pfam00278 302 PLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
45-278 |
3.20e-112 |
|
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: 330.01 E-value: 3.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 45 LGKIVKKHSQWQNVVAQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVAQIKYAA 124
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 125 KVGVNIMTCDNEVELKKISRNHPNAKVLLHIATEDAIGGEEGNMKFGTTL-KNCRHLLECAKELDVQIIGVKFHVSSSCK 203
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 204 ESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFtGTEYQ-------LEEVNHVISPLLDIYFPEGSGIKIISEPGSYY 276
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeepldFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239
|
..
gi 683524034 277 VS 278
Cdd:pfam02784 240 VA 241
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
48-273 |
2.27e-61 |
|
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: 198.31 E-value: 2.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 48 IVKKHSQWQNVV-AQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVAQIKYAAKV 126
Cdd:cd06808 1 IRHNYRRLREAApAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 127 GVNIMTCDNEVELKKISRNH----PNAKVLLHIATEDaiggeeGNMKFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSS 201
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 683524034 202 CKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEYQLeevnhvisplldiyfpEGSGIKIISEPG 273
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQE----------------LPLGTFIIVEPG 210
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-404 |
1.84e-42 |
|
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: 154.92 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQV 117
Cdd:COG0019 28 LYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 118 AQIKYAAKVGVNIMTCDNEVELKKISR----NHPNAKVLLHIATE-DAIGGEEGNM-----KFGTTLKNCRHLLECAKEL 187
Cdd:COG0019 108 EELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLRVNPGvDAGTHEYISTggkdsKFGIPLEDALEAYRRAAAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 188 D-VQIIGVKFHVSSSCKESQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF------TGTEYQLEEVNHVISPLLDIYF 260
Cdd:COG0019 188 PgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDEPPDLEELAAAIKEALEELC 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 261 peGSGIKIISEPGSYYVSSAFTLAVNIIAKKVVENDKF----SSgvektgsdepafmyyMNDGV----YGSF--ASKLSE 330
Cdd:COG0019 268 --GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFvivdAG---------------MNDLMrpalYGAYhpIVPVGR 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 683524034 331 DlntvpevhkkykDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPTIY 404
Cdd:COG0019 331 P------------SGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEV 392
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
40-386 |
6.63e-30 |
|
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: 119.51 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQV 117
Cdd:cd06828 5 LYVYDEATIRENYRRLKEAFSGPgfKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 118 AQIKYAAKVGVNIMTCDNEVELKKISRNHPN----AKVLL------------HIATedaiGGEEGnmKFGTTLKNCRHLL 181
Cdd:cd06828 85 EELELALELGILRINVDSLSELERLGEIAPElgkgAPVALrvnpgvdagthpYIST----GGKDS--KFGIPLEQALEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 182 ECAKELD-VQIIGVKFHVSSSCKESQVYVHAlsdARCVFDMAGEF---GFTMNMLDIGGGFtGTEYQ-------LEEVNH 250
Cdd:cd06828 159 RRAKELPgLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGL-GIPYRdedepldIEEYAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 251 VISPLLDIYFPEGSGIKIISEPGSYYVSSAFTLAVNIIAKKVVENDKF---SSGvektgsdepafmyyMND----GVYGS 323
Cdd:cd06828 235 AIAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFvgvDAG--------------MNDlirpALYGA 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 683524034 324 F-----ASKlsedlntvpevhkkyKDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGA 386
Cdd:cd06828 301 YheivpVNK---------------PGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGA 353
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
38-401 |
1.98e-24 |
|
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: 104.27 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 38 NAFFVGDLGKIVKKH--------SQWQNVVAQikpfYTVKCNATPAVLEILAALGtGFA--CSnKTEIALVQELGVSPEN 107
Cdd:cd06841 7 SPFFVFDEDALRENYrellgafkKRYPNVVIA----YSYKTNYLPAICKILHEEG-GYAevVS-AMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 108 IIYISPCKQVAQIKYAAKVGVNImTCDNEVELKK---ISRNHP-NAKVLLHIATEDaigGEEGNMKFGTTLKNCRHLLEC 183
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGALI-NIDSFDELERileIAKELGrVAKVGIRLNMNY---GNNVWSRFGFDIEENGEALAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 184 AKEL----DVQIIGVKFHVSSSCKESQVYVHALSDarcVFDMAGE-FGFTMNMLDIGGGFTG-----TEYQLEE------ 247
Cdd:cd06841 157 LKKIqeskNLSLVGLHCHVGSNILNPEAYSAAAKK---LIELLDRlFGLELEYLDLGGGFPAktplsLAYPQEDtvpdpe 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 248 --VNHVISPLLDIYFPEGSGIKIISEPGSYYVSSAFTLAVNIIAKKvvendkfssgvektgsdepafmyymndGVYGSFA 325
Cdd:cd06841 234 dyAEAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVK---------------------------NRYGRNI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 326 SKLSEDLNTVPEVH---------KKYKDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFhepSAFN 396
Cdd:cd06841 287 AVTDAGINNIPTIFwyhhpilvlRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNM---TQSN 363
|
....*
gi 683524034 397 DFQRP 401
Cdd:cd06841 364 QFIRP 368
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
40-386 |
2.49e-22 |
|
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: 98.05 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 40 FFVGDLGKIVKKHSQWQNVVAQ-IKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVA 118
Cdd:cd06839 9 FYVYDRDRVRERYAALRAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 119 QIKYAAKVGVNIMTCDNEVELKKISR-----NHPnAKVLLHIATEDAIGGEEGNM-----KFG---TTLKNCRHLLECAK 185
Cdd:cd06839 89 ELRRAIEAGIGTINVESLEELERIDAlaeehGVV-ARVALRINPDFELKGSGMKMgggpsQFGidvEELPAVLARIAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 186 ELDvqIIGVKFHVSSSCKESQVYV----HALSDARcvfDMAGEFGFTMNMLDIGGGF------TGTEYQLEEVNHVISPL 255
Cdd:cd06839 168 NLR--FVGLHIYPGTQILDADALIeafrQTLALAL---RLAEELGLPLEFLDLGGGFgipyfpGETPLDLEALGAALAAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 256 LDIYFPEGSGIKIISEPGSYYVSSAFTLAVNIIAKKVVENDKF---SSGvektgsdepafmyyMND--GVYGSFASKLSE 330
Cdd:cd06839 243 LAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFlvtDGG--------------MHHhlAASGNFGQVLRR 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 683524034 331 D--LNTVPEVhkkykDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGA 386
Cdd:cd06839 309 NypLAILNRM-----GGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGA 361
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
41-396 |
1.26e-14 |
|
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: 75.16 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 41 FVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQEL--GVSPENIIYISPCKQVA 118
Cdd:cd06840 15 YVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 119 QIKYAAKVGVNImTCDNEVELkkisRNHP----NAKVLL------------HIATedaiGGEEGnmKFGTTLKNCRHLLE 182
Cdd:cd06840 95 EYEQALELGVNV-TVDNLHPL----REWPelfrGREVILridpgqgeghhkHVRT----GGPES--KFGLDVDELDEARD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 183 CAKELDVQIIGVKFHVSSSCKE----SQVYVHALSDARcvfdmagEFGfTMNMLDIGGG------FTGTEYQLEEVNHVI 252
Cdd:cd06840 164 LAKKAGIIVIGLHAHSGSGVEDtdhwARHGDYLASLAR-------HFP-AVRILNVGGGlgipeaPGGRPIDLDALDAAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 253 SPLLDIYfpegSGIKIISEPGSYYVSSAFTLavniIAKkvVENDKFSSGVEKTGSDepAFMYYM-NDGVYGSFAS--KLS 329
Cdd:cd06840 236 AAAKAAH----PQYQLWMEPGRFIVAESGVL----LAR--VTQIKHKDGVRFVGLE--TGMNSLiRPALYGAYHEivNLS 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 683524034 330 EDlntvpevhkkykDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFN 396
Cdd:cd06840 304 RL------------DEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
68-404 |
1.90e-14 |
|
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: 74.35 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 68 VKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVAQIKYAAKVGVNImTCDNEVELKKIS---R 144
Cdd:cd06836 34 VKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAI-NIDNFQELERIDalvA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 145 NHPNAKVLLHIATEDAIG-GEEGNM-------KFGTTLKncrhllECAKEldvQII----------GVKFHV-SSSCKES 205
Cdd:cd06836 113 EFKEASSRIGLRVNPQVGaGKIGALstatatsKFGVALE------DGARD---EIIdafarrpwlnGLHVHVgSQGCELS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 206 QvyvhALSDARCVFDMAGEFGFTM-----NMLDIGGG----FTGTE----YQlEEVNHVIS--PLLdiyFPEGSGikIIS 270
Cdd:cd06836 184 L----LAEGIRRVVDLAEEINRRVgrrqiTRIDIGGGlpvnFESEDitptFA-DYAAALKAavPEL---FDGRYQ--LVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 271 EPG-SYYVSSAFTLAvniiakkVVENDKFSSGVEKTGSDEPAFMYymndgVYGSFASKLSEDLNTVPEVHKKYKDDePLF 349
Cdd:cd06836 254 EFGrSLLAKCGTIVS-------RVEYTKSSGGRRIAITHAGAQVA-----TRTAYAPDDWPLRVTVFDANGEPKTG-PEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 683524034 350 TSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPTIY 404
Cdd:cd06836 321 VTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-401 |
9.67e-14 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 73.58 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 59 VAQIKP----FYTVKCNATPAVLEILAALGTGFACSNKTEIALVQEL--GVSPENIIYISPCKQVAQIKYAAKVGVNImT 132
Cdd:PRK08961 520 LAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-T 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 133 CDNEVELkkisRNHP----NAKVLL------------HIATedaiGGEEGnmKFGTTLKNCRHLLECAKELDVQIIGVKF 196
Cdd:PRK08961 599 LDNVEPL----RNWPelfrGREVWLridpghgdghheKVRT----GGKES--KFGLSQTRIDEFVDLAKTLGITVVGLHA 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 197 HVSSSCKESQvyvHALSDARCVFDMAGEFGfTMNMLDIGGGFT------GTEYQLEEVNHVISPLLDIYfpegSGIKIIS 270
Cdd:PRK08961 669 HLGSGIETGE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEPFDLDALDAGLAEVKAQH----PGYQLWI 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 271 EPGSYYVSSAFTLavniIAK--KVVENDKFS-SGVEkTGsdepafmyyMND----GVYGSF-----ASKLsedlntvpev 338
Cdd:PRK08961 741 EPGRYLVAEAGVL----LARvtQVKEKDGVRrVGLE-TG---------MNSlirpALYGAYheivnLSRL---------- 796
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 683524034 339 hkkykDDEPLFTSSLWGPSCDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNdfQRP 401
Cdd:PRK08961 797 -----DEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
63-238 |
2.56e-12 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.
Pssm-ID: 143509 [Multi-domain] Cd Length: 423 Bit Score: 68.06 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 63 KPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVAQIKYAAKVGVNImTCDNEVELKKI 142
Cdd:cd06842 39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGATI-AVDSLDELDRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 143 -----SRNHPNAKVLLHIATEDAiggeEGNMKFGTTLKNCRHLLE-CAKELD-VQIIGVKFHVSSSCKESQvyVHALSDA 215
Cdd:cd06842 118 lalarGYTTGPARVLLRLSPFPA----SLPSRFGMPAAEVRTALErLAQLRErVRLVGFHFHLDGYSAAQR--VAALQEC 191
|
170 180
....*....|....*....|...
gi 683524034 216 RCVFDMAGEFGFTMNMLDIGGGF 238
Cdd:cd06842 192 LPLIDRARALGLAPRFIDIGGGF 214
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
64-406 |
9.70e-09 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 57.11 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 64 PFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELGVSPENIIYISPCKQVAQIKYAAKVGVNImTCDNEVELKKIS 143
Cdd:PLN02537 46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGVFV-NVDSEFDLENIV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 144 RNHPNA----KVLLHI------------ATEDAiggeegNMKFGTTLKNCRHLLECAKE--LDVQIIGVKFHVSSSCKES 205
Cdd:PLN02537 125 EAARIAgkkvNVLLRInpdvdpqvhpyvATGNK------NSKFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 206 QVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFtGTEYQ-----LEEVNHVISPLLDIYFPEgsGIKIISEPGSYYVSSA 280
Cdd:PLN02537 199 DIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGL-GIDYYhagavLPTPRDLIDTVRELVLSR--DLTLIIEPGRSLIANT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 281 FTLAVNIiakkvvendkfsSGVEKTGSDEpaFMYymndgVYGSFASKLSEDLNTV---PEVHKKYKDDEPLFTSSLWGPS 357
Cdd:PLN02537 276 CCFVNRV------------TGVKTNGTKN--FIV-----IDGSMAELIRPSLYDAyqhIELVSPPPPDAEVSTFDVVGPV 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 683524034 358 CDELDQIVENCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPTIYYM 406
Cdd:PLN02537 337 CESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWV 385
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
60-247 |
3.07e-07 |
|
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: 52.28 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 60 AQIKPFYTVKCNATPAVLEILAALGTGFACSNKTEIALVQELgvSPEN-IIYISPCKQVAQIKYAAKVGVNIMTCDNEVE 138
Cdd:cd06843 25 PGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA--VPDApLIFGGPGKTDSELAQALAQGVERIHVESELE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 139 LKKI----SRNHPNAKVLLHI--------ATEDAIGGEEgnMKFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSSCKES 205
Cdd:cd06843 103 LRRLnavaRRAGRTAPVLLRVnlalpdlpSSTLTMGGQP--TPFGIDEADLPDALELLRDLPnIRLRGFHFHLMSHNLDA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 683524034 206 QVYVHALSD-ARCVFDMAGEFGFTMNMLDIGGGFtGTEYQLEE 247
Cdd:cd06843 181 AAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI-GVNYADPE 222
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
63-291 |
5.27e-04 |
|
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: 42.17 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 63 KPFYTVKCNATPAVLEILAALGT----GFACSNKTEIALVQELGVSPENII---------YIspckqvAQIKYAAKVGVN 129
Cdd:cd06830 40 QGVYPIKVNQQREVVEEIVKAGKryniGLEAGSKPELLAALALLKTPDALIicngykddeYI------ELALLARKLGHN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 130 IM-TCDNEVELKKISR--NHPNAKVLLHI----ATEDAIGGEE---GNMKFGTTLKNC---------RHLLECAKELdvq 190
Cdd:cd06830 114 VIiVIEKLSELDLILElaKKLGVKPLLGVriklASKGSGKWQEsggDRSKFGLTASEIlevveklkeAGMLDRLKLL--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 683524034 191 iigvKFHVSSSCKESQVYVHALSDARCVF-DMAGEfGFTMNMLDIGGGF----TGT--------EYQLEE-VNHVISPLL 256
Cdd:cd06830 191 ----HFHIGSQITDIRRIKSALREAARIYaELRKL-GANLRYLDIGGGLgvdyDGSrsssdssfNYSLEEyANDIVKTVK 265
|
250 260 270
....*....|....*....|....*....|....*...
gi 683524034 257 DIYfpEGSGIK---IISEPGSYYVSSAFTLAVNIIAKK 291
Cdd:cd06830 266 EIC--DEAGVPhptIVTESGRAIVAHHSVLIFEVLGVK 301
|
|
| |
