NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498359334|ref|WP_010673490|]
View 

MULTISPECIES: type III PLP-dependent enzyme [Aeromonas]

Protein Classification

type III PLP-dependent enzyme( domain architecture ID 10089786)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme similar to Selenomonas ruminantium lysine/ornithine decarboxylase, and human ornithine decarboxylase and antizyme inhibitor 2

CATH:  3.20.20.10
EC:  4.1.1.-
Gene Ontology:  GO:0003824
PubMed:  15189147|8690703
SCOP:  4003520

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 18-370 2.60e-162

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: 459.27  E-value: 2.60e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  18 GSPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKR 97
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  98 DSDIRYALEFGCTVFVYDNPLELEKFLPYKDEVKLLLRVSFPNPETKVDLSKKFGCTPEQALPLLQLAQAKGIKVMGLSF 177
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 178 HVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGEFDIDGFCAPIREALAKLPAT--VQKIAEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDegVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 256 RFISAPAMTSVSSVMGKAHRGD---KIWYYLDDGLYGSYNGQLYDHVTYPVST---PYAHGELHNAVLSGPTCDSVDVIR 329
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDddrERWYYLNDGVYGSFNEILFDHIRYPPRVlkdGGRDGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 498359334 330 DSIMLP-DLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd00622  321 EDVLLPeDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 18-370 2.60e-162

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: 459.27  E-value: 2.60e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  18 GSPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKR 97
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  98 DSDIRYALEFGCTVFVYDNPLELEKFLPYKDEVKLLLRVSFPNPETKVDLSKKFGCTPEQALPLLQLAQAKGIKVMGLSF 177
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 178 HVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGEFDIDGFCAPIREALAKLPAT--VQKIAEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDegVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 256 RFISAPAMTSVSSVMGKAHRGD---KIWYYLDDGLYGSYNGQLYDHVTYPVST---PYAHGELHNAVLSGPTCDSVDVIR 329
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDddrERWYYLNDGVYGSFNEILFDHIRYPPRVlkdGGRDGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 498359334 330 DSIMLP-DLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd00622  321 EDVLLPeDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 21-349 7.14e-99

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 297.09  E-value: 7.14e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   21 LLLLDKAAVRKQYRALAAAL-PDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDS 99
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  100 DIRYALEFGCTVFVYDNPLELEKFLPYKDE--VKLLLRVSfPNPETKVD------LSKKFGCTPEQALPLLQLAQAKGIK 171
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRIN-PDVDAGTHkistggLSSKFGIDLEDAPELLALAKELGLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  172 VMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE-FDIDGFCAPIREALAK-LPATVQ 249
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPpPDFEEYAAAIREALDEyFPPDLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  250 KIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDGLYGSYNGQLYDHVTY-PVSTPYAHGELHNAVLSGPTCDSVDVI 328
Cdd:pfam00278 240 IIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPiPVVKEPGEGPLETYDVVGPTCESGDVL 319

                         330       340
                  ....*....|....*....|.
gi 498359334  329 RDSIMLPDLEIGELVVGRVMG 349
Cdd:pfam00278 320 AKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 9-374 4.26e-86

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: 267.01  E-value: 4.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   9 DYRQLVEQFGSPLLLLDKAAVRKQYRALAAALP--DVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRP 86
Cdd:COG0019   16 DLAELAEEYGTPLYVYDEAALRRNLRALREAFPgsGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  87 GRCIHTHPIKRDSDIRYALEFGCTVFVYDNPLELEKFLP----YKDEVKLLLRVsfpNPETKVDLSK---------KFGC 153
Cdd:COG0019   96 ERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLRV---NPGVDAGTHEyistggkdsKFGI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 154 TPEQALPLLQLA-QAKGIKVMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE--FDI 230
Cdd:COG0019  173 PLEDALEAYRRAaALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGDepPDL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 231 DGFCAPIREALAKLPATVQKIA-EPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------LYGSYngqlydhvtY 301
Cdd:COG0019  253 EELAAAIKEALEELCGLGPELIlEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGmndlmrpaLYGAY---------H 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498359334 302 PVS--TPYAHGELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILILDSAQ 374
Cdd:COG0019  324 PIVpvGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE 398
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
18-371 1.99e-30

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 123.27  E-value: 1.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  18 GSPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQ--GVRPGRCIHTHPI 95
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNF 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  96 KRDSDIRYALEFGCTVFVyDN--PLELEKFLpYKDEvKLLLRVSFPNPE---TKVDLS---KKFGCTPEQALPLLQLAQA 167
Cdd:PRK08961 582 APRAEYEAAFALGVTVTL-DNvePLRNWPEL-FRGR-EVWLRIDPGHGDghhEKVRTGgkeSKFGLSQTRIDEFVDLAKT 658

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 168 KGIKVMGLSFHVGSQV---PHARRHvqaidaCREIMEQAWELGlKPWVLDIGGGFPVDYDGG--EFDIDGFCAPIREALA 242
Cdd:PRK08961 659 LGITVVGLHAHLGSGIetgEHWRRM------ADELASFARRFP-DVRTIDLGGGLGIPESAGdePFDLDALDAGLAEVKA 731

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 243 KLPAtVQKIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------LYGSYngqlYDHVTYPVSTPYAHGELHn 314
Cdd:PRK08961 732 QHPG-YQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGmnslirpaLYGAY----HEIVNLSRLDEPAAGTAD- 805

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359334 315 avLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILILD 371
Cdd:PRK08961 806 --VVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 18-370 2.60e-162

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: 459.27  E-value: 2.60e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  18 GSPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKR 97
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  98 DSDIRYALEFGCTVFVYDNPLELEKFLPYKDEVKLLLRVSFPNPETKVDLSKKFGCTPEQALPLLQLAQAKGIKVMGLSF 177
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 178 HVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGEFDIDGFCAPIREALAKLPAT--VQKIAEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDegVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 256 RFISAPAMTSVSSVMGKAHRGD---KIWYYLDDGLYGSYNGQLYDHVTYPVST---PYAHGELHNAVLSGPTCDSVDVIR 329
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDddrERWYYLNDGVYGSFNEILFDHIRYPPRVlkdGGRDGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 498359334 330 DSIMLP-DLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd00622  321 EDVLLPeDLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 21-349 7.14e-99

Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.


Pssm-ID: 459745 [Multi-domain]  Cd Length: 340  Bit Score: 297.09  E-value: 7.14e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   21 LLLLDKAAVRKQYRALAAAL-PDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDS 99
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  100 DIRYALEFGCTVFVYDNPLELEKFLPYKDE--VKLLLRVSfPNPETKVD------LSKKFGCTPEQALPLLQLAQAKGIK 171
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRIN-PDVDAGTHkistggLSSKFGIDLEDAPELLALAKELGLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  172 VMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE-FDIDGFCAPIREALAK-LPATVQ 249
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPpPDFEEYAAAIREALDEyFPPDLE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  250 KIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDGLYGSYNGQLYDHVTY-PVSTPYAHGELHNAVLSGPTCDSVDVI 328
Cdd:pfam00278 240 IIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPiPVVKEPGEGPLETYDVVGPTCESGDVL 319

                         330       340
                  ....*....|....*....|.
gi 498359334  329 RDSIMLPDLEIGELVVGRVMG 349
Cdd:pfam00278 320 AKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 19-370 3.16e-97

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: 293.83  E-value: 3.16e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  19 SPLLLLDKAAVRKQYRALAAALP-DVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKR 97
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  98 DSDIRYALEFGCTVFVYDNPLELEKFLPY----KDEVKLLLRVSFPNPETKV-----DLSKKFGCTPEQALPLLQLAQAK 168
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNELakklGPKARILLRVNPDVSAGTHkistgGLKSKFGLSLSEARAALERAKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 169 GIKVMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGEFDIDGFCAPIREALAKLPATV 248
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDFEEYAALINPLLKKYFPND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 249 QK---IAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDGLYGSYNGQLYDHVTYPV---STPYAHGELHNAVLSGPTC 322
Cdd:cd06810  241 PGvtlILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALAYDAYHPItplKAPGPDEPLVPATLAGPLC 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 498359334 323 DSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd06810  321 DSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 9-374 4.26e-86

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: 267.01  E-value: 4.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   9 DYRQLVEQFGSPLLLLDKAAVRKQYRALAAALP--DVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRP 86
Cdd:COG0019   16 DLAELAEEYGTPLYVYDEAALRRNLRALREAFPgsGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  87 GRCIHTHPIKRDSDIRYALEFGCTVFVYDNPLELEKFLP----YKDEVKLLLRVsfpNPETKVDLSK---------KFGC 153
Cdd:COG0019   96 ERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLRV---NPGVDAGTHEyistggkdsKFGI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 154 TPEQALPLLQLA-QAKGIKVMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE--FDI 230
Cdd:COG0019  173 PLEDALEAYRRAaALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGDepPDL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 231 DGFCAPIREALAKLPATVQKIA-EPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------LYGSYngqlydhvtY 301
Cdd:COG0019  253 EELAAAIKEALEELCGLGPELIlEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGmndlmrpaLYGAY---------H 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498359334 302 PVS--TPYAHGELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILILDSAQ 374
Cdd:COG0019  324 PIVpvGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE 398
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 17-370 3.40e-63

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: 206.57  E-value: 3.40e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  17 FGSPLLLLDKAAVRKQYRALAAAL--PDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHP 94
Cdd:cd06828    1 YGTPLYVYDEATIRENYRRLKEAFsgPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  95 IKRDSDIRYALEFGCTVFVYDNPLELEKF----LPYKDEVKLLLRVsfpNPETKVDLSK---------KFGCTPEQALPL 161
Cdd:cd06828   81 GKSDEELELALELGILRINVDSLSELERLgeiaPELGKGAPVALRV---NPGVDAGTHPyistggkdsKFGIPLEQALEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 162 LQLA-QAKGIKVMGLSFHVGSQVPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE--FDIDGFCAPIR 238
Cdd:cd06828  158 YRRAkELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDepLDIEEYAEAIA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 239 EALAKLPATVQK---IAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------LYGSYngqlydHVTYPVsTPY 307
Cdd:cd06828  238 EALKELCEGGPDlklIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGmndlirpaLYGAY------HEIVPV-NKP 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498359334 308 AHGELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd06828  311 GEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 27-260 4.58e-54

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: 178.63  E-value: 4.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   27 AAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDSDIRYALE 106
Cdd:pfam02784   2 GSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  107 FGCTVFVYDNPLELEKFLPYKDEVKLLLRVSFPNPETKVDLSKKFGCTPEQALP-LLQLAQAKGIKVMGLSFHVGSQVPH 185
Cdd:pfam02784  82 VGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDVEaLLEAAKLLNLQVVGVSFHVGSGCTD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  186 ARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGE--FDIDGFCAPIREALAKLPAT---VQKIAEPGRFISA 260
Cdd:pfam02784 162 AEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEepLDFEEYANVINEALEEYFPGdpgVTIIAEPGRYFVA 241
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 13-361 1.78e-47

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: 165.84  E-value: 1.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  13 LVEQFGSPLLLLDKAAVRKQYRALAAALPD-VRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIH 91
Cdd:cd06839    1 LADAYGTPFYVYDRDRVRERYAALRAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  92 THPIKRDSDIRYALEFGCTVFVYDNPLELEKFLPYKDE----VKLLLRVsfpNPETKVDLS--------KKFGCTPEQAL 159
Cdd:cd06839   81 AGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEhgvvARVALRI---NPDFELKGSgmkmgggpSQFGIDVEELP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 160 PLL-QLAQAKGIKVMGLSFHVGSQVPHA----RRHVQAIDACREIMEqawELGLKPWVLDIGGGFPVDYDGGE--FDIDG 232
Cdd:cd06839  158 AVLaRIAALPNLRFVGLHIYPGTQILDAdaliEAFRQTLALALRLAE---ELGLPLEFLDLGGGFGIPYFPGEtpLDLEA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 233 FCAPIREALAKLPATVQK---IAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDGL--YGSYNGQLYDHV--TYPVS- 304
Cdd:cd06839  235 LGAALAALLAELGDRLPGtrvVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMhhHLAASGNFGQVLrrNYPLAi 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498359334 305 -TPYAHGELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTwASASTFNF 361
Cdd:cd06839  315 lNRMGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYG-LSASPLAF 371
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 25-367 1.68e-45

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: 160.78  E-value: 1.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  25 DKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDSDIRYA 104
Cdd:cd06831   19 DLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 105 LEFGCTVFVYDNPLELEKFLPYKDEVKLLLRVSFPNPETKVDLSKKFGCTPEQALPLLQLAQAKGIKVMGLSFHVGSQVP 184
Cdd:cd06831   99 AKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 185 HARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFpvdyDGGEFDIDGFCAPIREAL-AKLP--ATVQKIAEPGRFISAP 261
Cdd:cd06831  179 EYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGF----TGSEIQLEEVNHVIRPLLdVYFPegSGIQIIAEPGSYYVSS 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 262 AMTSVSSVMGK--------AHRGDK-------IWYYLDDGLYGSYNGQLYDHV-TYP-VSTPYAHGE-LHNAVLSGPTCD 323
Cdd:cd06831  255 AFTLAVNVIAKkavendkhLSSVEKngsdepaFVYYMNDGVYGSFASKLSEKLnTTPeVHKKYKEDEpLFTSSLWGPSCD 334

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 498359334 324 SVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASI 367
Cdd:cd06831  335 ELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAI 378
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 13-372 1.18e-39

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: 144.71  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  13 LVEQFGSPLLLLDKAAVRKQYRALAAAL----PDVRLHYALK--PLPheAVVSVLKEEGACFDLATNGEVDLVRSQGVRP 86
Cdd:cd06841    1 LLESYGSPFFVFDEDALRENYRELLGAFkkryPNVVIAYSYKtnYLP--AICKILHEEGGYAEVVSAMEYELALKLGVPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  87 GRCIHTHPIKRDSDIRYALEFGCTVFVyDNPLELEKFLPYKDE----VKLLLRVSFPnpeTKVDLSKKFGCTPE---QAL 159
Cdd:cd06841   79 KRIIFNGPYKSKEELEKALEEGALINI-DSFDELERILEIAKElgrvAKVGIRLNMN---YGNNVWSRFGFDIEengEAL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 160 PLLQLAQ-AKGIKVMGLSFHVGSQVPHARRHVQAIDACREIMEQAweLGLKPWVLDIGGGFPVD------YDGGE--FDI 230
Cdd:cd06841  155 AALKKIQeSKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRL--FGLELEYLDLGGGFPAKtplslaYPQEDtvPDP 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 231 DGFCAPIREALAKL-PATVQK---IAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDdglyGSYNGQ----LYDHVTYP 302
Cdd:cd06841  233 EDYAEAIASTLKEYyANKENKpklILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTD----AGINNIptifWYHHPILV 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498359334 303 VStPYAHGELH-NAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFnFFPKASILILDS 372
Cdd:cd06841  309 LR-PGKEDPTSkNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQF-IRPRPAVYLIDN 377
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 29-256 9.37e-39

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: 137.84  E-value: 9.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  29 VRKQYRALAAALP-DVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDSDIRYALEF 107
Cdd:cd06808    1 IRHNYRRLREAAPaGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 108 GCTVFVYDNPLELEKF----LPYKDEVKLLLRVsfpNPEtkvDLSKKFGCTPEQALPLL-QLAQAKGIKVMGLSFHVGSQ 182
Cdd:cd06808   81 GVIVVTVDSLEELEKLeeaaLKAGPPARVLLRI---DTG---DENGKFGVRPEELKALLeRAKELPHLRLVGLHTHFGSA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498359334 183 VPHARRHVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYdggefdidgfcapireaLAKLPATVQKIAEPGR 256
Cdd:cd06808  155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILY-----------------LQELPLGTFIIVEPGR 211
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 11-370 4.99e-32

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: 124.08  E-value: 4.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  11 RQLVEQFGsPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRS--QGVRPGR 88
Cdd:cd06840    5 LRLAPDVG-PCYVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKlfPDLDPRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  89 CIHTHPIKRDSDIRYALEFGCTVFVyDN--PLELEKFLpYKDEvKLLLRVSFPNPE---TKVDLS---KKFGCTPEQALP 160
Cdd:cd06840   84 VLFTPNFAARSEYEQALELGVNVTV-DNlhPLREWPEL-FRGR-EVILRIDPGQGEghhKHVRTGgpeSKFGLDVDELDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 161 LLQLAQAKGIKVMGLSFHVGSQV---PHARRHVQAI-DACREIMEQAwelglkpwVLDIGGGFPVDY--DGGEFDIDGFC 234
Cdd:cd06840  161 ARDLAKKAGIIVIGLHAHSGSGVedtDHWARHGDYLaSLARHFPAVR--------ILNVGGGLGIPEapGGRPIDLDALD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 235 APIREALAKLPAtVQKIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDGLYGSYNGQLYDHVTYPVSTPYAHGELH- 313
Cdd:cd06840  233 AALAAAKAAHPQ-YQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLSRLDEPPAg 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359334 314 NAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILIL 370
Cdd:cd06840  312 NADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
18-371 1.99e-30

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 123.27  E-value: 1.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  18 GSPLLLLDKAAVRKQYRALAAALPDVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQ--GVRPGRCIHTHPI 95
Cdd:PRK08961 502 GSPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNF 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  96 KRDSDIRYALEFGCTVFVyDN--PLELEKFLpYKDEvKLLLRVSFPNPE---TKVDLS---KKFGCTPEQALPLLQLAQA 167
Cdd:PRK08961 582 APRAEYEAAFALGVTVTL-DNvePLRNWPEL-FRGR-EVWLRIDPGHGDghhEKVRTGgkeSKFGLSQTRIDEFVDLAKT 658

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 168 KGIKVMGLSFHVGSQV---PHARRHvqaidaCREIMEQAWELGlKPWVLDIGGGFPVDYDGG--EFDIDGFCAPIREALA 242
Cdd:PRK08961 659 LGITVVGLHAHLGSGIetgEHWRRM------ADELASFARRFP-DVRTIDLGGGLGIPESAGdePFDLDALDAGLAEVKA 731

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 243 KLPAtVQKIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------LYGSYngqlYDHVTYPVSTPYAHGELHn 314
Cdd:PRK08961 732 QHPG-YQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGmnslirpaLYGAY----HEIVNLSRLDEPAAGTAD- 805

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359334 315 avLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASILILD 371
Cdd:PRK08961 806 --VVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 11-242 1.36e-29

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: 118.13  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  11 RQLVEQFGSPLLLLDKAAVRKQYRALAAALP----DVRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRP 86
Cdd:cd06842    2 VALVEAYGSPLNVLFPQTFRENIAALRAVLDrhgvDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  87 GRCIHTHPIKRDSDIRYALEFGCTVFVyDNPLELEKFL-----PYKDEVKLLLRVS-FPNpetkvDLSKKFGCTPEQALP 160
Cdd:cd06842   82 DRIVATGPAKTDEFLWLAVRHGATIAV-DSLDELDRLLalargYTTGPARVLLRLSpFPA-----SLPSRFGMPAAEVRT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 161 LLQLAQ--AKGIKVMGLSFHVGSQVPHARrhVQAIDACREIMEQAWELGLKPWVLDIGGGFPVDYDGGEFDIDGFCAPIR 238
Cdd:cd06842  156 ALERLAqlRERVRLVGFHFHLDGYSAAQR--VAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAEWEAFLAALT 233


                 ....
gi 498359334 239 EALA 242
Cdd:cd06842  234 EALY 237
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 23-353 1.82e-28

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: 114.30  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  23 LLDKAAVRKQYRALAAALPD-VRLHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRpGRCIHTHPIKRDSDI 101
Cdd:cd06843    6 VYDLAALRAHARALRASLPPgCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPD-APLIFGGPGKTDSEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 102 RYALEFGCTVFVYDNPLELEKFLPYKDE----VKLLLRVsfpNPETKVDLSKK---------FGCTPEQALPLLQLAQA- 167
Cdd:cd06843   85 AQALAQGVERIHVESELELRRLNAVARRagrtAPVLLRV---NLALPDLPSSTltmggqptpFGIDEADLPDALELLRDl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 168 KGIKVMGLSFHVGSQVPHARRHVQAIDACREI---MEQAWELGLKpwVLDIGGGFPVDYDGGE--FDIDGFCAPIREALA 242
Cdd:cd06843  162 PNIRLRGFHFHLMSHNLDAAAHLALVKAYLETarqWAAEHGLDLD--VVNVGGGIGVNYADPEeqFDWAGFCEGLDQLLA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 243 KLPATVQKIAEPGRFISAPAMTSVSSVMGKAHRGDKiWYYLDDGlyGSYNGQL-----YDH--VTYPVST---PYAHGEL 312
Cdd:cd06843  240 EYEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGE-WFAVLRG--GTHHFRLpaawgHNHpfSVLPVEEwpyPWPRPSV 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 498359334 313 HNA--VLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTW 353
Cdd:cd06843  317 RDTpvTLVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYGW 359
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 22-368 8.43e-19

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: 87.06  E-value: 8.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  22 LLLDKAAVRKQYRALAAALPDVRLH-YALKPLPHEAVVSVLKEEGACFDLATNGEVDLVRSQGVRPGRCIHTHPIKRDSD 100
Cdd:cd06836    6 GLYDLDGFRALVARLTAAFPAPVLHtFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 101 IRYALEFGCTVFVyDNPLELEKFLPYKDEVK-----LLLRVsfpNPET---KVDL------SKKFGctpeqaLPLLQLAQ 166
Cdd:cd06836   86 LREALELGVAINI-DNFQELERIDALVAEFKeassrIGLRV---NPQVgagKIGAlstataTSKFG------VALEDGAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 167 AKGIKVM-------GLSFHVGSQ---VPharrhvQAIDACREIMEQAWELG-----LKPWVLDIGGGFPVDYDGGEFD-- 229
Cdd:cd06836  156 DEIIDAFarrpwlnGLHVHVGSQgceLS------LLAEGIRRVVDLAEEINrrvgrRQITRIDIGGGLPVNFESEDITpt 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 230 IDGFCAPIREALAKL-PATVQKIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG----LYGSYNGQLYdHVTYPVS 304
Cdd:cd06836  230 FADYAAALKAAVPELfDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGaqvaTRTAYAPDDW-PLRVTVF 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498359334 305 TPYAH---GELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFNFFPKASIL 368
Cdd:cd06836  309 DANGEpktGPEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
PLN02537 PLN02537
diaminopimelate decarboxylase
 3-360 2.58e-16

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 79.84  E-value: 2.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334   3 ETLVAQDYRQLVEQfgSPLLLLDKAAVRKQYRALAAALPDVR--LHYALKPLPHEAVVSVLKEEGACFDLATNGEVDLVR 80
Cdd:PLN02537   4 EGLRVQDIMESVEK--RPFYLYSKPQITRNYEAYKEALEGLRsiIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  81 SQGVRPGRCIHTHPIKRDSDIRYALEFGCTVFVyDNPLELEKFLPYK----DEVKLLLRVSfPNPETKV-------DLSK 149
Cdd:PLN02537  82 RAGFDPTRCIFNGNGKLLEDLVLAAQEGVFVNV-DSEFDLENIVEAAriagKKVNVLLRIN-PDVDPQVhpyvatgNKNS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 150 KFGCTPEQALPLLQLAQA--KGIKVMGLSFHVGSQVPHAR----RHVQAIDACREIMEQAWELGLkpwvLDIGGGFPVDY 223
Cdd:PLN02537 160 KFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKVDifrdAAVLMVNYVDEIRAQGFELSY----LNIGGGLGIDY 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 224 DGgefdiDGFCAP--------IREALAKLPATVqkIAEPGRFISAPAMTSVSSVMGKAHRGDKIWYYLDDG--------L 287
Cdd:PLN02537 236 YH-----AGAVLPtprdlidtVRELVLSRDLTL--IIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSmaelirpsL 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498359334 288 YGSYNgqlydHVTYpVSTPYAHGELHNAVLSGPTCDSVDVIRDSIMLPDLEIGELVVGRVMGAYTWASASTFN 360
Cdd:PLN02537 309 YDAYQ-----HIEL-VSPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYN 375
PLPDE_III_ADC cd06830
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ...
 15-336 8.87e-16

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: 78.00  E-value: 8.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  15 EQFGSPLLL--LD--KAAVRKQYRALAAAL------PDVRLHYALKPLPHEAVVSVLKEEGACFDL----ATNGEVDLVR 80
Cdd:cd06830    1 RGYGLPLLLrfPDilRHRIERLNAAFAKAIeeygykGKYQGVYPIKVNQQREVVEEIVKAGKRYNIgleaGSKPELLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334  81 SQGVRPGRCIHTHPIKRDSDIRYALEFGC----TVFVYDNPLELEKFLPYKDE--VKLLL--RV-SFPNPETKVDLS--- 148
Cdd:cd06830   81 ALLKTPDALIICNGYKDDEYIELALLARKlghnVIIVIEKLSELDLILELAKKlgVKPLLgvRIkLASKGSGKWQESggd 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 149 -KKFGCTPEQALPLLQLAQAKGIK---VMgLSFHVGSQVPHARRHVQAIdacREIMEQAWEL-----GLKpwVLDIGGGF 219
Cdd:cd06830  161 rSKFGLTASEILEVVEKLKEAGMLdrlKL-LHFHIGSQITDIRRIKSAL---REAARIYAELrklgaNLR--YLDIGGGL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 220 PVDYDGG--------EFDIDGFCAPIREALAKLPATVQK-----IAEPGRFISAPAMTSVSSVMGKAHRGDkiWYYLDDG 286
Cdd:cd06830  235 GVDYDGSrsssdssfNYSLEEYANDIVKTVKEICDEAGVphptiVTESGRAIVAHHSVLIFEVLGVKRLAD--WYFCNFS 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498359334 287 LYGSYN-----GQLydhvtYPV-------STPYahgelHNAVLSGPTCDSVDVIRDSIMLPD 336
Cdd:cd06830  313 LFQSLPdswaiDQL-----FPImplhrlnEKPT-----RRAVLGDITCDSDGKIDSFIDPPD 364
SpeA COG1166
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
150-225 1.22e-05

Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 440780 [Multi-domain]  Cd Length: 633  Bit Score: 47.39  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 150 KFGCTPEQALPLLQLAQAKGikvMG-----LSFHVGSQVPHARRHVQAI-DACREIMEQAwELGLKPWVLDIGGGFPVDY 223
Cdd:COG1166  218 KFGLSASEILEVVERLKEAG---MLdclqlLHFHLGSQIPNIRDIKRAVrEAARFYAELR-KLGAPIEYLDVGGGLGVDY 293


                 ..
gi 498359334 224 DG 225
Cdd:COG1166  294 DG 295
PRK05354 PRK05354
biosynthetic arginine decarboxylase;
150-225 9.05e-05

biosynthetic arginine decarboxylase;


Pssm-ID: 235427 [Multi-domain]  Cd Length: 634  Bit Score: 44.34  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 150 KFGCTPEQALPLLQLAQAKGikvMG-----LSFHVGSQVPHARRHVQAI-DACR---EIMEqaweLGLKPWVLDIGGGFP 220
Cdd:PRK05354 222 KFGLSATEVLEAVERLREAG---LLdclqlLHFHLGSQIANIRDIKTAVrEAARfyvELRK----LGAPIQYLDVGGGLG 294


                 ....*
gi 498359334 221 VDYDG 225
Cdd:PRK05354 295 VDYDG 299
PLN02439 PLN02439
arginine decarboxylase
 150-225 2.90e-04

arginine decarboxylase


Pssm-ID: 215240 [Multi-domain]  Cd Length: 559  Bit Score: 42.75  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359334 150 KFGCTPEQALPLlqlaqAKGIKVMG-------LSFHVGSQVPharrhvqAIDACREIMEQAWE-------LGLKPWVLDI 215
Cdd:PLN02439 159 KFGLTATEIVRV-----VRKLRKEGmldclqlLHFHIGSQIP-------STSLLKDGVSEAAQiycelvrLGAPMRVIDI 226

                         90
                 ....*....|
gi 498359334 216 GGGFPVDYDG 225
Cdd:PLN02439 227 GGGLGIDYDG 236
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH