|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
30-390 |
1.97e-160 |
|
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: 455.03 E-value: 1.97e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 30 DQALNICDLSSLERKLRLWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRP 109
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 110 ASHLRYAKEQQVVNGTVDNEYEIYKLRKHYPDSNLIVRFKSEAKKALCPLGDKYGCDaEADAAALMLLAKALGLKVTGTS 189
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGAD-PEEARELLRRAKELGLNVVGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 190 FHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPGIDDEM---FEEIAQSVNTSVELRFPDKRIRIISEP 266
Cdd:cd00622 160 FHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVvpsFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 267 GRFFVEAAYTLICKVHAKREVRSKDgklDTMMYYLNDGIFGAFAGMFYYPEEVAPELYLDEAESLPKLKSVIWGPSCDAM 346
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDD---RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24586474 347 DKIS-DLLLP-NLNPGDLLGFRNMGAYTMPIASPFNGFDVPETRFF 390
Cdd:cd00622 317 DVIYeDVLLPeDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
38-271 |
1.98e-107 |
|
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: 315.76 E-value: 1.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 38 LSSLERKLRLWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAK 117
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 118 EQQVVNGTVDNEYEIYKLRKHYPDSNLIVRFKSEAKKALCPLGDKYGCDAEADAAALMLLAKALGLKVTGTSFHVGSGCS 197
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 198 EVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFpGIDDE------MFEEIAQSVNTSVELRFP-DKRIRIISEPGRFF 270
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeeplDFEEYANVINEALEEYFPgDPGVTIIAEPGRYF 239
|
.
gi 24586474 271 V 271
Cdd:pfam02784 240 V 240
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
35-382 |
4.54e-56 |
|
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: 189.59 E-value: 4.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 35 ICDLSSLERKLRLWHKLMPRI--EPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASH 112
Cdd:COG0019 30 VYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 113 LRYAKEQQV--VNgtVDNEYEIYKLRKHYPDSNLIVR----------FKSEAKKALCPLGDKYGCDAEADAAALMLLAKA 180
Cdd:COG0019 110 LEEALELGVghIN--VDSLSELERLAELAAELGKRAPvglrvnpgvdAGTHEYISTGGKDSKFGIPLEDALEAYRRAAAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 181 LGLKVTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFpGI---DDEM---FEEIAQSVNTSVElR 254
Cdd:COG0019 188 PGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGL-GIpytEGDEppdLEELAAAIKEALE-E 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 255 FPDKRIRIISEPGRFFV-EAAYtLICKVHAKREVRSKD-GKLDTMMyylNDGIFGAFAgMFYYPeeVAPelyLDEAESLP 332
Cdd:COG0019 266 LCGLGPELILEPGRALVgNAGV-LLTRVLDVKENGGRRfVIVDAGM---NDLMRPALY-GAYHP--IVP---VGRPSGAE 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24586474 333 KLKSVIWGPSCDAMDKI-SDLLLPNLNPGDLLGFRNMGAYTMPIASPFNGF 382
Cdd:COG0019 336 AETYDVVGPLCESGDVLgKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGR 386
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
21-380 |
8.01e-31 |
|
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: 121.63 E-value: 8.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 21 IEQADLEHLDQA----LNICDLSSLERKLRLWHKLMP-RIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLG 95
Cdd:TIGR01048 11 IEGVPLLELAQEfgtpLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 96 VSPERIIFAHPCRPASHLRYAKEQQV-VNgtVDNEYEIYKLRKHYPDSNLIVRF----------KSEAKKALCPLGDKYG 164
Cdd:TIGR01048 91 FPPEKIVFSGNGKSRAELERALELGIcIN--VDSFSELERLNEIAPELGKKARIslrvnpgvdaKTHPYISTGLKDSKFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 165 CDAEADAAALMLLAKALGLKVTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHkMELLDVGGGFpGI---DDEM-- 239
Cdd:TIGR01048 169 IDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGID-LEFLDLGGGL-GIpytPEEEpp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 240 -FEEIAQSVNTSVELRFPDKRI-RIISEPGRFFVEAAYTLICKVHAKREVRSKDGKL-DTMMyylNDGIFGAFAGMFYyp 316
Cdd:TIGR01048 247 dLSEYAQAILNALEGYADLGLDpKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIvDAGM---NDLIRPALYGAYH-- 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586474 317 eEVAPelyLDEAESLPKLKSVIWGPSCDAMDKIS-DLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:TIGR01048 322 -HIIV---LNRTNDAPTEVADVVGPVCESGDVLAkDRELPEVEPGDLLAVFDAGAYGFSMSSNYN 382
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-380 |
3.05e-20 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 92.84 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 59 YAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGL--GVSPERIIFAhpcrP--ASHLRYAKEQQV-VNGTVDNeyeIY 133
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFT----PnfAPRAEYEAAFALgVTVTLDN---VE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 134 KLRKH---YPDSNLIVRFK---------------SEAK--------KALCPLGDKYGcdaeadaaalmllakalgLKVTG 187
Cdd:PRK08961 604 PLRNWpelFRGREVWLRIDpghgdghhekvrtggKESKfglsqtriDEFVDLAKTLG------------------ITVVG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 188 TSFHVGSGCSEVEAYDR-AIEKAEnifkVGEMIGhKMELLDVGGGFP--------GIDdemFEEIAQSVnTSVELRFPDK 258
Cdd:PRK08961 666 LHAHLGSGIETGEHWRRmADELAS----FARRFP-DVRTIDLGGGLGipesagdePFD---LDALDAGL-AEVKAQHPGY 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 259 RIRIisEPGRFFVEAAYTLICKVhakREVRSKDG----KLDTMMYYLndgifgafagmfyypeeVAPELY--LDEAESLP 332
Cdd:PRK08961 737 QLWI--EPGRYLVAEAGVLLARV---TQVKEKDGvrrvGLETGMNSL-----------------IRPALYgaYHEIVNLS 794
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24586474 333 KLK------SVIWGPSCDAMDKIS-DLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:PRK08961 795 RLDepaagtADVVGPICESSDVLGkRRRLPATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
30-390 |
1.97e-160 |
|
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: 455.03 E-value: 1.97e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 30 DQALNICDLSSLERKLRLWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRP 109
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 110 ASHLRYAKEQQVVNGTVDNEYEIYKLRKHYPDSNLIVRFKSEAKKALCPLGDKYGCDaEADAAALMLLAKALGLKVTGTS 189
Cdd:cd00622 81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGAD-PEEARELLRRAKELGLNVVGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 190 FHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPGIDDEM---FEEIAQSVNTSVELRFPDKRIRIISEP 266
Cdd:cd00622 160 FHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVvpsFEEIAAVINRALDEYFPDEGVRIIAEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 267 GRFFVEAAYTLICKVHAKREVRSKDgklDTMMYYLNDGIFGAFAGMFYYPEEVAPELYLDEAESLPKLKSVIWGPSCDAM 346
Cdd:cd00622 240 GRYLVASAFTLAVNVIAKRKRGDDD---RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24586474 347 DKIS-DLLLP-NLNPGDLLGFRNMGAYTMPIASPFNGFDVPETRFF 390
Cdd:cd00622 317 DVIYeDVLLPeDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
38-271 |
1.98e-107 |
|
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: 315.76 E-value: 1.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 38 LSSLERKLRLWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAK 117
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 118 EQQVVNGTVDNEYEIYKLRKHYPDSNLIVRFKSEAKKALCPLGDKYGCDAEADAAALMLLAKALGLKVTGTSFHVGSGCS 197
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 198 EVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFpGIDDE------MFEEIAQSVNTSVELRFP-DKRIRIISEPGRFF 270
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeeplDFEEYANVINEALEEYFPgDPGVTIIAEPGRYF 239
|
.
gi 24586474 271 V 271
Cdd:pfam02784 240 V 240
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
33-369 |
5.42e-102 |
|
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: 305.56 E-value: 5.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 33 LNICDLSSLERKLRLWHK-LMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPAS 111
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAaLPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 112 HLRYAKEQQVVNGTVDNEYEIYKLRKHYPD--SNLIVRFK-----SEAKKALCPLGDKYGCDaEADAAALMLLAKALGLK 184
Cdd:pfam00278 81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINpdvdaGTHKISTGGLSSKFGID-LEDAPELLALAKELGLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 185 VTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPGIDDEM----FEEIAQSVNTSVELRFPDKrI 260
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEpppdFEEYAAAIREALDEYFPPD-L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 261 RIISEPGRFFVEAAYTLICKVHAKREVRSKdgkldtMMYYLNDGIFGAFAGMFY--YPEEVAPELYLDEAESlpklKSVI 338
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKTGGGK------TFVIVDAGMNDLFRPALYdaYHPIPVVKEPGEGPLE----TYDV 308
|
330 340 350
....*....|....*....|....*....|..
gi 24586474 339 WGPSCDAMDKIS-DLLLPNLNPGDLLGFRNMG 369
Cdd:pfam00278 309 VGPTCESGDVLAkDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
32-390 |
7.00e-79 |
|
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: 248.22 E-value: 7.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 32 ALNICDLSSLERKLRLWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPAS 111
Cdd:cd06831 14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 112 HLRYAKEQQVVNGTVDNEYEIYKLRKHYPDSNLIVRFKSEAKKALCPLGDKYGCdAEADAAALMLLAKALGLKVTGTSFH 191
Cdd:cd06831 94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGT-TLKNCRHLLECAKELDVQIVGVKFH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 192 VGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPGIDDEMfEEIAQSVNTSVELRFPDKR-IRIISEPGRFF 270
Cdd:cd06831 173 VSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQL-EEVNHVIRPLLDVYFPEGSgIQIIAEPGSYY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 271 VEAAYTLICKVHAKREVR-----SKDGKLDT----MMYYLNDGIFGAFAGMFYYPEEVAPELYLDEAESLPKLKSVIWGP 341
Cdd:cd06831 252 VSSAFTLAVNVIAKKAVEndkhlSSVEKNGSdepaFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWGP 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24586474 342 SCDAMDKISD-LLLPNLNPGDLLGFRNMGAYTMPIASPFNGFDVPETRFF 390
Cdd:cd06831 332 SCDELDQIVEsCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYM 381
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
32-385 |
1.75e-76 |
|
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: 241.05 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 32 ALNICDLSSLERKLRLWHK-LMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPA 110
Cdd:cd06810 2 PFYVYDLDIIRAHYAALKEaLPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 111 SHLRYAKEQQVVNGTVDNEYEIYKL----RKHYPDSNLIVRFKSEA-----KKALCPLGDKYGCDaEADAAALMLLAKAL 181
Cdd:cd06810 82 SEIEAALASGVDHIVVDSLDELERLnelaKKLGPKARILLRVNPDVsagthKISTGGLKSKFGLS-LSEARAALERAKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 182 GLKVTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPG--IDDEM-FEEIAQSVNTSVELRFP-D 257
Cdd:cd06810 161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIpyDEQPLdFEEYAALINPLLKKYFPnD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 258 KRIRIISEPGRFFVEAAYTLICKVHAKREVRSKDgkldtmMYYLNDGIFGAFAGMFYYPEEVAPELYLDEAESLPKLKSV 337
Cdd:cd06810 241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRF------FAVVDGGMNHSFRPALAYDAYHPITPLKAPGPDEPLVPAT 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24586474 338 IWGPSCDAMDKISDL-LLPNLNPGDLLGFRNMGAYTMPIASPFNGFDVP 385
Cdd:cd06810 315 LAGPLCDSGDVIGRDrLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRP 363
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
35-382 |
4.54e-56 |
|
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: 189.59 E-value: 4.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 35 ICDLSSLERKLRLWHKLMPRI--EPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASH 112
Cdd:COG0019 30 VYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 113 LRYAKEQQV--VNgtVDNEYEIYKLRKHYPDSNLIVR----------FKSEAKKALCPLGDKYGCDAEADAAALMLLAKA 180
Cdd:COG0019 110 LEEALELGVghIN--VDSLSELERLAELAAELGKRAPvglrvnpgvdAGTHEYISTGGKDSKFGIPLEDALEAYRRAAAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 181 LGLKVTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFpGI---DDEM---FEEIAQSVNTSVElR 254
Cdd:COG0019 188 PGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGL-GIpytEGDEppdLEELAAAIKEALE-E 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 255 FPDKRIRIISEPGRFFV-EAAYtLICKVHAKREVRSKD-GKLDTMMyylNDGIFGAFAgMFYYPeeVAPelyLDEAESLP 332
Cdd:COG0019 266 LCGLGPELILEPGRALVgNAGV-LLTRVLDVKENGGRRfVIVDAGM---NDLMRPALY-GAYHP--IVP---VGRPSGAE 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24586474 333 KLKSVIWGPSCDAMDKI-SDLLLPNLNPGDLLGFRNMGAYTMPIASPFNGF 382
Cdd:COG0019 336 AETYDVVGPLCESGDVLgKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGR 386
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
37-382 |
3.89e-40 |
|
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: 146.09 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 37 DLSSLERKLRLWHKLM--PRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLR 114
Cdd:cd06828 9 DEATIRENYRRLKEAFsgPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 115 YAKEQQVVNGTVDNEYEIYKLRKHYPDSNLIVR----------FKSEAKKALCPLGDKYGCDAEADAAALMLLAKALGLK 184
Cdd:cd06828 89 LALELGILRINVDSLSELERLGEIAPELGKGAPvalrvnpgvdAGTHPYISTGGKDSKFGIPLEQALEAYRRAKELPGLK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 185 VTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFpGI----DDEM--FEEIAQSVNTSV-ELRFPD 257
Cdd:cd06828 169 LVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGL-GIpyrdEDEPldIEEYAEAIAEALkELCEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 258 KRIRIISEPGRFFVEAAYTLICKVHAKREVRSKD-GKLDTMMyylNDGI----FGAfagmfYYPEEVApelyldEAESLP 332
Cdd:cd06828 248 PDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTfVGVDAGM---NDLIrpalYGA-----YHEIVPV------NKPGEG 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24586474 333 KLKSV-IWGPSCDAMDK-ISDLLLPNLNPGDLLGFRNMGAYTMPIASPFNGF 382
Cdd:cd06828 314 ETEKVdVVGPICESGDVfAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSR 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
41-252 |
2.08e-32 |
|
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: 121.27 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 41 LERKLRLWHKLMP-RIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAKEQ 119
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 120 QVVNGTVDNEYEIYKLR----KHYPDSNLIVRFKSEAKKAlcplgdKYGCDAEADAAALMLLAKALGLKVTGTSFHVGSG 195
Cdd:cd06808 81 GVIVVTVDSLEELEKLEeaalKAGPPARVLLRIDTGDENG------KFGVRPEELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24586474 196 CSEVEAYDRAIEKAENIFKVGEMIGHKMELLDVGGGFPGiddEMFEEIAQSVNTSVE 252
Cdd:cd06808 155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAI---LYLQELPLGTFIIVE 208
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
21-380 |
8.01e-31 |
|
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: 121.63 E-value: 8.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 21 IEQADLEHLDQA----LNICDLSSLERKLRLWHKLMP-RIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLG 95
Cdd:TIGR01048 11 IEGVPLLELAQEfgtpLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 96 VSPERIIFAHPCRPASHLRYAKEQQV-VNgtVDNEYEIYKLRKHYPDSNLIVRF----------KSEAKKALCPLGDKYG 164
Cdd:TIGR01048 91 FPPEKIVFSGNGKSRAELERALELGIcIN--VDSFSELERLNEIAPELGKKARIslrvnpgvdaKTHPYISTGLKDSKFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 165 CDAEADAAALMLLAKALGLKVTGTSFHVGSGCSEVEAYDRAIEKAENIFKVGEMIGHkMELLDVGGGFpGI---DDEM-- 239
Cdd:TIGR01048 169 IDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAEGID-LEFLDLGGGL-GIpytPEEEpp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 240 -FEEIAQSVNTSVELRFPDKRI-RIISEPGRFFVEAAYTLICKVHAKREVRSKDGKL-DTMMyylNDGIFGAFAGMFYyp 316
Cdd:TIGR01048 247 dLSEYAQAILNALEGYADLGLDpKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIvDAGM---NDLIRPALYGAYH-- 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586474 317 eEVAPelyLDEAESLPKLKSVIWGPSCDAMDKIS-DLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:TIGR01048 322 -HIIV---LNRTNDAPTEVADVVGPVCESGDVLAkDRELPEVEPGDLLAVFDAGAYGFSMSSNYN 382
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
26-379 |
8.42e-29 |
|
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: 115.44 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 26 LEHLDQALNICDLSSLERKLRLWHKLMPRIEPH----YAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERI 101
Cdd:cd06841 2 LESYGSPFFVFDEDALRENYRELLGAFKKRYPNvviaYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 102 IFAHPCRPASHLRYA-KEQQVVNgtVDNEYEIYKLRK----------------HYPDSNLIVRF---KSEAKKALCPLGD 161
Cdd:cd06841 82 IFNGPYKSKEELEKAlEEGALIN--IDSFDELERILEiakelgrvakvgirlnMNYGNNVWSRFgfdIEENGEALAALKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 162 KYGCDaeadaaalmllakalGLKVTGTSFHVGSGCSEVEAYDRAIEKAENIfkVGEMIGHKMELLDVGGGFPGIDDEM-- 239
Cdd:cd06841 160 IQESK---------------NLSLVGLHCHVGSNILNPEAYSAAAKKLIEL--LDRLFGLELEYLDLGGGFPAKTPLSla 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 240 ---------FEEIAQSVNTSVELRFPDK--RIRIISEPGRFFVEAAYTLICKVHAKREVRskdgklDTMMYYLNDGIFGA 308
Cdd:cd06841 223 ypqedtvpdPEDYAEAIASTLKEYYANKenKPKLILEPGRALVDDAGYLLGRVVAVKNRY------GRNIAVTDAGINNI 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24586474 309 FAgMFYYPEEVAPelyLDEAESLPKLKS-VIWGPSCDAMDKISD-LLLPNLNPGDLLGFRNMGAYTMPIASPF 379
Cdd:cd06841 297 PT-IFWYHHPILV---LRPGKEDPTSKNyDVYGFNCMESDVLFPnVPLPPLNVGDILAIRNVGAYNMTQSNQF 365
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
37-385 |
2.22e-28 |
|
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: 114.23 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 37 DLSSLERKLRLWHKLMPR-IEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRY 115
Cdd:cd06839 13 DRDRVRERYAALRAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDAELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 116 AKEQQVVNGTVDNEYEIYKL----RKHYPDSNLIVRFKS--EAKKALCPLGDK---YGCDAEADAAALMLLAKALGLKVT 186
Cdd:cd06839 93 AIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPdfELKGSGMKMGGGpsqFGIDVEELPAVLARIAALPNLRFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 187 GtsFHV--GSGCSEVEAYDRAIEKAENIFK-VGEMIGHKMELLDVGGGF-----PGIDDEMFEEIAQSVNTSVEL---RF 255
Cdd:cd06839 173 G--LHIypGTQILDADALIEAFRQTLALALrLAEELGLPLEFLDLGGGFgipyfPGETPLDLEALGAALAALLAElgdRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 256 PDKRIriISEPGRFFVEAAYTLICKVHAKREVRSKDgkldtmmYYLNDG---IFGAFAGMFY------YPEEVAPELYLD 326
Cdd:cd06839 251 PGTRV--VLELGRYLVGEAGVYVTRVLDRKVSRGET-------FLVTDGgmhHHLAASGNFGqvlrrnYPLAILNRMGGE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24586474 327 EAEslpklKSVIWGPSCDAMDKISD-LLLPNLNPGDLLGFRNMGAYTmPIASP--FNGFDVP 385
Cdd:cd06839 322 ERE-----TVTVVGPLCTPLDLLGRnVELPPLEPGDLVAVLQSGAYG-LSASPlaFLSHPAP 377
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
59-380 |
3.05e-20 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 92.84 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 59 YAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGL--GVSPERIIFAhpcrP--ASHLRYAKEQQV-VNGTVDNeyeIY 133
Cdd:PRK08961 531 YAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFT----PnfAPRAEYEAAFALgVTVTLDN---VE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 134 KLRKH---YPDSNLIVRFK---------------SEAK--------KALCPLGDKYGcdaeadaaalmllakalgLKVTG 187
Cdd:PRK08961 604 PLRNWpelFRGREVWLRIDpghgdghhekvrtggKESKfglsqtriDEFVDLAKTLG------------------ITVVG 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 188 TSFHVGSGCSEVEAYDR-AIEKAEnifkVGEMIGhKMELLDVGGGFP--------GIDdemFEEIAQSVnTSVELRFPDK 258
Cdd:PRK08961 666 LHAHLGSGIETGEHWRRmADELAS----FARRFP-DVRTIDLGGGLGipesagdePFD---LDALDAGL-AEVKAQHPGY 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 259 RIRIisEPGRFFVEAAYTLICKVhakREVRSKDG----KLDTMMYYLndgifgafagmfyypeeVAPELY--LDEAESLP 332
Cdd:PRK08961 737 QLWI--EPGRYLVAEAGVLLARV---TQVKEKDGvrrvGLETGMNSL-----------------IRPALYgaYHEIVNLS 794
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24586474 333 KLK------SVIWGPSCDAMDKIS-DLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:PRK08961 795 RLDepaagtADVVGPICESSDVLGkRRRLPATAEGDVILIANAGAYGYSMSSTYN 849
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
59-380 |
5.46e-18 |
|
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: 84.41 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 59 YAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGL--GVSPERIIFAhpcrP--ASHLRYAKEQQV-VNGTVDNeyeIY 133
Cdd:cd06840 40 YAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFT----PnfAARSEYEQALELgVNVTVDN---LH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 134 KLRKH---YPDSNLIVRF------------KSEAKKAlcplgdKYGCDaEADAAALMLLAKALGLKVTGTSFHVGSGCSE 198
Cdd:cd06840 113 PLREWpelFRGREVILRIdpgqgeghhkhvRTGGPES------KFGLD-VDELDEARDLAKKAGIIVIGLHAHSGSGVED 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 199 V----EAYDRAIEKAENIFKVgemighkmELLDVGGGF-----PGIDDEMFEEIAQSVnTSVELRFPDKRIRIisEPGRF 269
Cdd:cd06840 186 TdhwaRHGDYLASLARHFPAV--------RILNVGGGLgipeaPGGRPIDLDALDAAL-AAAKAAHPQYQLWM--EPGRF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 270 FVEAAYTLICKVhakREVRSKDGK----LDTMMYYL-NDGIFGAFagmfyypEEVAPELYLDEAeslPKLKSVIWGPSCD 344
Cdd:cd06840 255 IVAESGVLLARV---TQIKHKDGVrfvgLETGMNSLiRPALYGAY-------HEIVNLSRLDEP---PAGNADVVGPICE 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 24586474 345 AMDKIS-DLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:cd06840 322 SGDVLGrDRLLPETEEGDVILIANAGAYGFCMASTYN 358
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
60-380 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 60 AVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAKEQQV-VNgtVDNEYE---IYKL 135
Cdd:cd06836 33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVaIN--IDNFQElerIDAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 136 RKHYPDSNLIVRFKSEAKKALCPLGD--------KYGCDAEADAAALMLLAKALGLKVTGTSFHVGSGCSEVEAYDRAIE 207
Cdd:cd06836 111 VAEFKEASSRIGLRVNPQVGAGKIGAlstatatsKFGVALEDGARDEIIDAFARRPWLNGLHVHVGSQGCELSLLAEGIR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 208 KAENIFK-VGEMIG-HKMELLDVGGGFP-GIDDE----MFEEIAQSVNTSVELRFPDkRIRIISEPGRFFVEAAYTLICK 280
Cdd:cd06836 191 RVVDLAEeINRRVGrRQITRIDIGGGLPvNFESEditpTFADYAAALKAAVPELFDG-RYQLVTEFGRSLLAKCGTIVSR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 281 VhakrEVRSKDGKLDTMMYYlndgifgafAGMFYYPEEV-APELY------LDeAESLPKLKSV----IWGPSCDAMDKI 349
Cdd:cd06836 270 V----EYTKSSGGRRIAITH---------AGAQVATRTAyAPDDWplrvtvFD-ANGEPKTGPEvvtdVAGPCCFAGDVL 335
|
330 340 350
....*....|....*....|....*....|..
gi 24586474 350 -SDLLLPNLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:cd06836 336 aKERALPPLEPGDYVAVHDTGAYYFSSHSSYN 367
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
57-380 |
2.10e-11 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 64.81 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 57 PHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAKEQQV-VNgtVDNEYEIYKL 135
Cdd:PLN02537 46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGVfVN--VDSEFDLENI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 136 ----RKHYPDSNLIVRFKSEAKKALCPL------GDKYGC-DAEADAAALMLLAKALGLKVTGTSFHVGSGCSEVEAYDR 204
Cdd:PLN02537 124 veaaRIAGKKVNVLLRINPDVDPQVHPYvatgnkNSKFGIrNEKLQWFLDAVKAHPNELKLVGAHCHLGSTITKVDIFRD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 205 AIEKAENIFKVGEMIGHKMELLDVGGGFpGID----DEMFEEIAQSVNTSVELrFPDKRIRIISEPGRFFVEAAYTLICK 280
Cdd:PLN02537 204 AAVLMVNYVDEIRAQGFELSYLNIGGGL-GIDyyhaGAVLPTPRDLIDTVREL-VLSRDLTLIIEPGRSLIANTCCFVNR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 281 VHAkreVRSKDGK----LDTMMYYLndgIFGAFAGMFYYPEEVAPELYLDEAESLPklksvIWGPSCDAMDKI-SDLLLP 355
Cdd:PLN02537 282 VTG---VKTNGTKnfivIDGSMAEL---IRPSLYDAYQHIELVSPPPPDAEVSTFD-----VVGPVCESADFLgKDRELP 350
|
330 340
....*....|....*....|....*
gi 24586474 356 NLNPGDLLGFRNMGAYTMPIASPFN 380
Cdd:PLN02537 351 TPPKGAGLVVHDAGAYCMSMASTYN 375
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
57-233 |
6.85e-11 |
|
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: 63.43 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 57 PHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSPERIIFAHPCRPASHLRYAKEQQVVNgTVDNEYE---IY 133
Cdd:cd06842 40 VYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGATI-AVDSLDEldrLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 134 KLRKHYPD--SNLIVRFKSEAKKalcpLGDKYGCDAEADAAALMLLAKALGL-KVTGTSFHVGSGCSE--VEAYDRAIEk 208
Cdd:cd06842 119 ALARGYTTgpARVLLRLSPFPAS----LPSRFGMPAAEVRTALERLAQLRERvRLVGFHFHLDGYSAAqrVAALQECLP- 193
|
170 180
....*....|....*....|....*
gi 24586474 209 aenIFKVGEMIGHKMELLDVGGGFP 233
Cdd:cd06842 194 ---LIDRARALGLAPRFIDIGGGFP 215
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
37-135 |
1.39e-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: 56.14 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 37 DLSSLERKLR-LWHKLMPRIEPHYAVKCNDDPVVVKFLADLGTGFDCASKNELKLVLGLGVSpERIIFAHPCRPASHLRY 115
Cdd:cd06843 8 DLAALRAHARaLRASLPPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPD-APLIFGGPGKTDSELAQ 86
|
90 100
....*....|....*....|
gi 24586474 116 AKEQQVVNGTVDNEYEIYKL 135
Cdd:cd06843 87 ALAQGVERIHVESELELRRL 106
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
59-371 |
1.22e-06 |
|
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: 50.26 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 59 YAVKCNDDPVVVKFLADLGT----GFDCASKNELKLVLGLGVSPERIIFahpC---------RPASHLRYAKEQQVVngT 125
Cdd:cd06830 43 YPIKVNQQREVVEEIVKAGKryniGLEAGSKPELLAALALLKTPDALII---CngykddeyiELALLARKLGHNVII--V 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 126 VDNEYEIYKL----RKHYPDSNLIVRFKSEAK-----KALCPLGDKYGcdaeadAAALMLLAKALGLKVTGTS------- 189
Cdd:cd06830 118 IEKLSELDLIlelaKKLGVKPLLGVRIKLASKgsgkwQESGGDRSKFG------LTASEILEVVEKLKEAGMLdrlkllh 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 190 FHVGSGCSEVEAYDRAIEKAENIF----KVGEmighKMELLDVGGGFpGID----------------DEMFEEIAQSVNT 249
Cdd:cd06830 192 FHIGSQITDIRRIKSALREAARIYaelrKLGA----NLRYLDIGGGL-GVDydgsrsssdssfnyslEEYANDIVKTVKE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 250 SVELR---FPDkrirIISEPGRFFVEAAYTLICKVHAKREVRSKdgkldtmmYYLNDGIFGAFAGMF----YYPeeVAPE 322
Cdd:cd06830 267 ICDEAgvpHPT----IVTESGRAIVAHHSVLIFEVLGVKRLADW--------YFCNFSLFQSLPDSWaidqLFP--IMPL 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586474 323 LYLDEAeslPKLKSVIWGPSCDAMDKIS----------DLLLPNLNPGD--LLGFRNMGAY 371
Cdd:cd06830 333 HRLNEK---PTRRAVLGDITCDSDGKIDsfidppdilpTLPLHPLRKDEpyYLGFFLVGAY 390
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
185-385 |
6.43e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.
Pssm-ID: 143502 [Multi-domain] Cd Length: 346 Bit Score: 41.38 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 185 VTGTSFHVGsgC-SEVEAYDRAIEKAENIFkvGEMIgHKMELLDVGGGF----PGIDDEMFEEIAQsvntsvelRFPDKR 259
Cdd:cd06829 155 IEGLHFHTL--CeQDFDALERTLEAVEERF--GEYL-PQLKWLNLGGGHhitrPDYDVDRLIALIK--------RFKEKY 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 260 -IRIISEPGRFFVEAAYTLICKVhakrevrskdgkLDTMMYYLNDGIFGAFA--------GMFYYPEevapelYLDEAES 330
Cdd:cd06829 222 gVEVYLEPGEAVALNTGYLVATV------------LDIVENGMPIAILDASAtahmpdvlEMPYRPP------IRGAGEP 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24586474 331 LPKLKSV-IWGPSCDAMDKISDLLLPN-LNPGDLLGFRNMGAYTMPIASPFNGFDVP 385
Cdd:cd06829 284 GEGAHTYrLGGNSCLAGDVIGDYSFDEpLQVGDRLVFEDMAHYTMVKTNTFNGVRLP 340
|
|
| nspC |
TIGR01047 |
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. ... |
185-385 |
2.74e-03 |
|
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 273414 [Multi-domain] Cd Length: 379 Bit Score: 39.38 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 185 VTGTSFHvgSGC-SEVEAYDRAIEKAENIFkvGEMIGhKMELLDVGGGF----PGIDDEMFEEIAQSvntsvelrFPDKR 259
Cdd:TIGR01047 159 IEGLHFH--TLCeKDADALERTLEVIEEKF--GEYLP-QMKWVNFGGGHhitkKGYDVEKLIAVIKA--------FSERH 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586474 260 -IRIISEPGRFFVEAAYTLICKV---------HAKREVRSKDGKLDTMMYYLNDGIFGAfagmfyypeEVAPELYLDEAE 329
Cdd:TIGR01047 226 gVQVILEPGEAIGWQTGFLVASVvdivenekqIAILDVSFEAHMPDTLEMPYRPEVLGA---------RDPATRENEAQD 296
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24586474 330 SLPKLKSVIWGPSCDAMDKISDLLLPN-LNPGDLLGFRNMGAYTMPIASPFNGFDVP 385
Cdd:TIGR01047 297 KEGEFSYLLGGNTCLAGDVMGEYAFDKpLKVGDKIVFLDMIHYTMVKNTTFNGVKLP 353
|
|
| |
