|
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: 766.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 26 DNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPP 105
Cdd:cd06831 1 DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 106 ENIIYISPCKQVSQIKYAAKVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTLKNCRHLLECAK 185
Cdd:cd06831 81 ENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 186 ELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEEVNHVISPLLDIYFPEGSG 265
Cdd:cd06831 161 ELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 266 VKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYKED 345
Cdd:cd06831 241 IQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKED 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387629694 346 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMMSFSDWYEMQDAG 419
Cdd:cd06831 321 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG 394
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
37-406 |
2.49e-178 |
|
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: 502.41 E-value: 2.49e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 37 KNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQ 116
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 117 VSQIKYAAKVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTLKNCRHLLECAKELDVQIIGVKF 196
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 197 HVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQ----LEEVNHVISPLLDIYFPEGsGVKIISEP 272
Cdd:cd00622 161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvvpsFEEIAAVINRALDEYFPDE-GVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 273 GSYYVSSAFTLAVNIIAKKVVendkfpsgvektGSDEPAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSS 352
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKR------------GDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSS 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1387629694 353 LWGPSCDELDQIVESCLLPE-LNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYM 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 |
2.13e-136 |
|
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: 396.29 E-value: 2.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 38 NAFFVGDLGKIVKKHSQWQNV-VAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQ 116
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEAlPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 117 VSQIKYAAKVGVNILTCDNEIELKKIARNH----PNAKVLLHIATEDNIGGEEGNM-----KFGTTLKNCRHLLECAKEL 187
Cdd:cd06810 81 VSEIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSAGTHKISTgglksKFGLSLSEARAALERAKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 188 DVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGT----EFQLEEVNHVISPLLDIYFPEG 263
Cdd:cd06810 161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPydeqPLDFEEYAALINPLLKKYFPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 264 SGVKIISEPGSYYVSSAFTLAVNIIAKKVVENdkfpsgvektgsdepAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYK 343
Cdd:cd06810 241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGG---------------RFFAVVDGGMNHSFRPALAYDAYHPITPLKAPG 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387629694 344 EDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYM 406
Cdd:cd06810 306 PDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
40-385 |
9.99e-124 |
|
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: 362.96 E-value: 9.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 40 FFVGDLGKIVKKHSQWQNVVA-QIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVS 118
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALPpRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 119 QIKYAAKVGVNILTCDNEIELKKIARNHPN--AKVLLHIATEDNIGGEEGNM-----KFGTTLKNCRHLLECAKELDVQI 191
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 192 IGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF-----TGTEFQLEEVNHVISPLLDIYFPEgsGV 266
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 267 KIISEPGSYYVSSAFTLAVNIIAKKVVENdkfpsgvektgsdepAFMYYMNDGVYGSFASKLSEDLNTIPEVhkKYKEDE 346
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMNDLFRPALYDAYHPIPVV--KEPGEG 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 1387629694 347 PLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMG 385
Cdd:pfam00278 302 PLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
45-278 |
2.63e-115 |
|
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: 337.72 E-value: 2.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 45 LGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAA 124
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 125 KVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTL-KNCRHLLECAKELDVQIIGVKFHVSSACK 203
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 204 ESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFtGTEFQ-------LEEVNHVISPLLDIYFPEGSGVKIISEPGSYY 276
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeepldFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239
|
..
gi 1387629694 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 |
5.92e-63 |
|
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: 202.55 E-value: 5.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 48 IVKKHSQWQNVV-AQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKV 126
Cdd:cd06808 1 IRHNYRRLREAApAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 127 GVNILTCDNEIELKKIARNH----PNAKVLLHIATEDniggeeGNMKFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSA 201
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387629694 202 CKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLeevnhvisplldiyfpEGSGVKIISEPG 273
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQE----------------LPLGTFIIVEPG 210
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
40-404 |
2.73e-46 |
|
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: 165.32 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQV 117
Cdd:COG0019 28 LYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 118 SQIKYAAKVGVNILTCDNEIELKKIAR----NHPNAKVLL------HIATEDNI--GGEEGnmKFGTTLKNCRHLLECAK 185
Cdd:COG0019 108 EELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLrvnpgvDAGTHEYIstGGKDS--KFGIPLEDALEAYRRAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 186 ELD-VQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF------TGTEFQLEEVNHVISPLLDI 258
Cdd:COG0019 186 ALPgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDEPPDLEELAAAIKEALEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 259 YFpeGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFpsgvektgsdepafmYY----MNDGV----YGSFasklse 330
Cdd:COG0019 266 LC--GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRF---------------VIvdagMNDLMrpalYGAY------ 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387629694 331 dlNTIPEVHKkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIY 404
Cdd:COG0019 323 --HPIVPVGR--PSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEV 392
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
40-402 |
1.52e-32 |
|
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: 126.83 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQV 117
Cdd:cd06828 5 LYVYDEATIRENYRRLKEAFSGPgfKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 118 SQIKYAAKVGVNILTCDNEIELKKIARNHPN----AKVLL------------HIATedniGGEEGnmKFGTTLKNCRHLL 181
Cdd:cd06828 85 EELELALELGILRINVDSLSELERLGEIAPElgkgAPVALrvnpgvdagthpYIST----GGKDS--KFGIPLEQALEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 182 ECAKELD-VQIIGVKFHVSSACKESQVYVHAlsdARCVFDMAGEI---GFTMNMLDIGGGF------TGTEFQLEEVNHV 251
Cdd:cd06828 159 RRAKELPgLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgipyrdEDEPLDIEEYAEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 252 ISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFpSGVEkTGsdepafmyyMND----GVYGSF--- 324
Cdd:cd06828 236 IAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTF-VGVD-AG---------MNDlirpALYGAYhei 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 325 --ASKlsedlntipevhkkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPA 402
Cdd:cd06828 305 vpVNK---------------PGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPA 369
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
38-404 |
1.27e-28 |
|
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: 116.21 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 38 NAFFVGDLGKIVKKH--------SQWQNVVAQikpfYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENII 109
Cdd:cd06841 7 SPFFVFDEDALRENYrellgafkKRYPNVVIA----YSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 110 YISPCKQVSQIKYAAKVGVNIlTCDN--EIE-LKKIARNHpNAKVLLHIATEDNIGGeEGNMKFGTTLKNCRHLLECAKE 186
Cdd:cd06841 83 FNGPYKSKEELEKALEEGALI-NIDSfdELErILEIAKEL-GRVAKVGIRLNMNYGN-NVWSRFGFDIEENGEALAALKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 187 L----DVQIIGVKFHVSSACKESQVYVHALSDarcVFDMAGEI-GFTMNMLDIGGGFTG------------TEFQLEE-V 248
Cdd:cd06841 160 IqeskNLSLVGLHCHVGSNILNPEAYSAAAKK---LIELLDRLfGLELEYLDLGGGFPAktplslaypqedTVPDPEDyA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 249 NHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKvvendkfpsgvektgsdepafmyymndGVYGSFASKL 328
Cdd:cd06841 237 EAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVK---------------------------NRYGRNIAVT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 329 SEDLNTIPEVH---------KKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFhepSAFNDF- 398
Cdd:cd06841 290 DAGINNIPTIFwyhhpilvlRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNM---TQSNQFi 366
|
....*..
gi 1387629694 399 -QRPAIY 404
Cdd:cd06841 367 rPRPAVY 373
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
40-386 |
2.81e-25 |
|
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: 106.52 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 40 FFVGDLGKIVKKHSQWQNVVAQ-IKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVS 118
Cdd:cd06839 9 FYVYDRDRVRERYAALRAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 119 QIKYAAKVGVNILTCDNEIELKKIAR-----NHPnAKVLLHIATEDNIGGEEGNM-----KFG---TTLKNCRHLLECAK 185
Cdd:cd06839 89 ELRRAIEAGIGTINVESLEELERIDAlaeehGVV-ARVALRINPDFELKGSGMKMgggpsQFGidvEELPAVLARIAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 186 ELDvqIIGvkFHVSSAckeSQVY-VHALSDA-----RCVFDMAGEIGFTMNMLDIGGGF------TGTEFQLEEVNHVIS 253
Cdd:cd06839 168 NLR--FVG--LHIYPG---TQILdADALIEAfrqtlALALRLAEELGLPLEFLDLGGGFgipyfpGETPLDLEALGAALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 254 PLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKF---PSGvektgsdepafmyyMND--GVYGSFASKL 328
Cdd:cd06839 241 ALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVSRGETFlvtDGG--------------MHHhlAASGNFGQVL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387629694 329 SEDLntiPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGA 386
Cdd:cd06839 307 RRNY---PLAILNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGA 361
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
41-396 |
6.63e-16 |
|
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: 79.02 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 41 FVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQEL--GVPPENIIYISPCKQVS 118
Cdd:cd06840 15 YVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 119 QIKYAAKVGVNiLTCDNEIELkkiaRNHP----NAKVLLHIatedNIGGEEGN----------MKFGTTLKNCRHLLECA 184
Cdd:cd06840 95 EYEQALELGVN-VTVDNLHPL----REWPelfrGREVILRI----DPGQGEGHhkhvrtggpeSKFGLDVDELDEARDLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 185 KELDVQIIGVKFHVSSACKE----SQVYVHALSDARCVFDmageigftMNMLDIGGG------FTGTEFQLEEVNHVISP 254
Cdd:cd06840 166 KKAGIIVIGLHAHSGSGVEDtdhwARHGDYLASLARHFPA--------VRILNVGGGlgipeaPGGRPIDLDALDAALAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 255 LLDIYfpegSGVKIISEPGSYYVSSAFTLavniIAKkvVENDKFPSGVEKTGSDepAFMYYM-NDGVYGSF-----ASKL 328
Cdd:cd06840 238 AKAAH----PQYQLWMEPGRFIVAESGVL----LAR--VTQIKHKDGVRFVGLE--TGMNSLiRPALYGAYheivnLSRL 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387629694 329 SEdlntipevhkkykedEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFN 396
Cdd:cd06840 306 DE---------------PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
68-404 |
6.68e-16 |
|
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: 78.97 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 68 VKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVNIlTCDNEIELKKI---AR 144
Cdd:cd06836 34 VKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAI-NIDNFQELERIdalVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 145 NHPNAKVLLHIATEDNIG-GEEGNM-------KFGTTLKncrhllECAKEldvQII----------GVKFHV-SSACKES 205
Cdd:cd06836 113 EFKEASSRIGLRVNPQVGaGKIGALstatatsKFGVALE------DGARD---EIIdafarrpwlnGLHVHVgSQGCELS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 206 QvyvhALSDARCVFDMAGEIGFTM-----NMLDIGGGFtGTEFQLEEvnhvISPLLDIY-----------FPEGSGVkiI 269
Cdd:cd06836 184 L----LAEGIRRVVDLAEEINRRVgrrqiTRIDIGGGL-PVNFESED----ITPTFADYaaalkaavpelFDGRYQL--V 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 270 SEPGSYYVSSAFTLAvniiakkvvendkfpSGVE--KTGSDEPAFMYYMNDGVY--GSFASKLSEDLNTIPEVHKKYKED 345
Cdd:cd06836 253 TEFGRSLLAKCGTIV---------------SRVEytKSSGGRRIAITHAGAQVAtrTAYAPDDWPLRVTVFDANGEPKTG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387629694 346 ePLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIY 404
Cdd:cd06836 318 -PEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-401 |
2.60e-15 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 78.59 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 59 VAQIKP----FYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQEL--GVPPENIIYISPCKQVSQIKYAAKVGVNiLT 132
Cdd:PRK08961 520 LAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVT-VT 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 133 CDNEIELKKIARNHPNAKVLLHI--ATED------NIGGEEGnmKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKE 204
Cdd:PRK08961 599 LDNVEPLRNWPELFRGREVWLRIdpGHGDghhekvRTGGKES--KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIET 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 205 SQvyvHALSDARCVFDMAGEIGfTMNMLDIGGGFT------GTEFQLEEVNHVISPLLDIYfpegSGVKIISEPGSYYVS 278
Cdd:PRK08961 677 GE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEPFDLDALDAGLAEVKAQH----PGYQLWIEPGRYLVA 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 279 SAFTLavniIAK--KVVENDKFP-SGVEkTGsdepafmyyMND----GVYGSF-----ASKLSEdlntipevhkkykedE 346
Cdd:PRK08961 749 EAGVL----LARvtQVKEKDGVRrVGLE-TG---------MNSlirpALYGAYheivnLSRLDE---------------P 799
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1387629694 347 PLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNdfQRP 401
Cdd:PRK08961 800 AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--LRE 852
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
63-238 |
4.51e-15 |
|
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: 76.92 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 63 KPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVnILTCDNEIELKKI 142
Cdd:cd06842 39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 143 -----ARNHPNAKVLLHIATEDNiggeEGNMKFGTTLKNCRHLLE-CAKELD-VQIIGVKFHVSSACKESQvyVHALSDA 215
Cdd:cd06842 118 lalarGYTTGPARVLLRLSPFPA----SLPSRFGMPAAEVRTALErLAQLRErVRLVGFHFHLDGYSAAQR--VAALQEC 191
|
170 180
....*....|....*....|...
gi 1387629694 216 RCVFDMAGEIGFTMNMLDIGGGF 238
Cdd:cd06842 192 LPLIDRARALGLAPRFIDIGGGF 214
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
64-406 |
3.17e-10 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 61.73 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 64 PFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVNIlTCDNEIELKKIA 143
Cdd:PLN02537 46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGVFV-NVDSEFDLENIV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 144 RNHPNA----KVLLHIATEDN------IGGEEGNMKFGTTLKNCRHLLECAKE--LDVQIIGVKFHVSSACKESQVYVHA 211
Cdd:PLN02537 125 EAARIAgkkvNVLLRINPDVDpqvhpyVATGNKNSKFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKVDIFRDA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 212 lsdARCVFDMAGEI---GFTMNMLDIGGGFtGTEFQ-----LEEVNHVISPLLDIYFPEgsGVKIISEPGSYYVSSAFTL 283
Cdd:PLN02537 205 ---AVLMVNYVDEIraqGFELSYLNIGGGL-GIDYYhagavLPTPRDLIDTVRELVLSR--DLTLIIEPGRSLIANTCCF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 284 AVNIiakkvvendkfpSGVEKTGSDEpaFMYymndgVYGSFASKLSEDL----NTIpEVHKKYKEDEPLFTSSLWGPSCD 359
Cdd:PLN02537 279 VNRV------------TGVKTNGTKN--FIV-----IDGSMAELIRPSLydayQHI-ELVSPPPPDAEVSTFDVVGPVCE 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1387629694 360 ELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYM 406
Cdd:PLN02537 339 SADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWV 385
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
60-275 |
2.64e-08 |
|
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: 55.75 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 60 AQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELgVPPENIIYISPCKQVSQIKYAAKVGVNILTCDNEIEL 139
Cdd:cd06843 25 PGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTDSELAQALAQGVERIHVESELEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 140 KKIARNHPNAKVLLHIATEDNIGGEEG-----NM-----KFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSACKESQVY 208
Cdd:cd06843 104 RRLNAVARRAGRTAPVLLRVNLALPDLpsstlTMggqptPFGIDEADLPDALELLRDLPnIRLRGFHFHLMSHNLDAAAH 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387629694 209 VHALSD-ARCVFDMAGEIGFTMNMLDIGGGF------TGTEFQLEEVNHVISPLLDIYFPegsGVKIISEPGSY 275
Cdd:cd06843 184 LALVKAyLETARQWAAEHGLDLDVVNVGGGIgvnyadPEEQFDWAGFCEGLDQLLAEYEP---GLTLRFECGRY 254
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
63-291 |
2.68e-05 |
|
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: 46.41 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 63 KPFYTVKCNSAPAVLEILAALGT----GFACSSKNEMALVQELGVPPENII---------YISpckqvsQIKYAAKVGVN 129
Cdd:cd06830 40 QGVYPIKVNQQREVVEEIVKAGKryniGLEAGSKPELLAALALLKTPDALIicngykddeYIE------LALLARKLGHN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 130 -ILTCDNEIELK---KIARNHpNAKVLLHI----ATE-----DNIGGEEGnmKFGTTLKNC---------RHLLECAKEL 187
Cdd:cd06830 114 vIIVIEKLSELDlilELAKKL-GVKPLLGVriklASKgsgkwQESGGDRS--KFGLTASEIlevveklkeAGMLDRLKLL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387629694 188 dvqiigvKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF----TGT--------EFQLEE-VNHVISP 254
Cdd:cd06830 191 -------HFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLgvdyDGSrsssdssfNYSLEEyANDIVKT 263
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387629694 255 LLDIYfpEGSGVK---IISEPGSYYVSSAFTLAVNIIAKK 291
Cdd:cd06830 264 VKEIC--DEAGVPhptIVTESGRAIVAHHSVLIFEVLGVK 301
|
|
| |
