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Conserved domains on  [gi|658132468|ref|NP_001280714|]
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antizyme inhibitor 2 [Camelus ferus]

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

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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 ...
 40-396 1.36e-175

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


:

Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 496.25  E-value: 1.36e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  40 AFFVADLGAVVRKHFCFLKCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPSAKMVLSIATDDSHSLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 200 GSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPGVE-GAKMRFDEIASVINSALDLYFPEGcGVDILAKLGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 279 YYVTSAFTLAVSIIGKKEVLLDQPGREedtgsapktivYHLHEGVYGIFNSVLFDNTCPTPISQKKPSTEQPVYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 658132468 359 PVVDGCDCVAEGLWLPQ-LHVGDWLVFENMGAYTVGVGS 396
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYAS 349
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-396 1.36e-175

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 496.25  E-value: 1.36e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  40 AFFVADLGAVVRKHFCFLKCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPSAKMVLSIATDDSHSLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 200 GSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPGVE-GAKMRFDEIASVINSALDLYFPEGcGVDILAKLGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 279 YYVTSAFTLAVSIIGKKEVLLDQPGREedtgsapktivYHLHEGVYGIFNSVLFDNTCPTPISQKKPSTEQPVYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 658132468 359 PVVDGCDCVAEGLWLPQ-LHVGDWLVFENMGAYTVGVGS 396
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYAS 349
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 41-388 7.59e-114

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: 338.31  E-value: 7.59e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468   41 FFVADLGAVVRKHFCFLKCL-PRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPS--AKMVLSIATD---DSHSLS--RLNLKFGASLKSCRHLLENAKRDHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKIStgGLSSKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  193 VGVSFHIGSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPG--VEGAKMRFDEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIpyRDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  271 DILAKLGRYYVTSAFTLAVSIIGKKEvlldqpgreedtgSAPKTIVYhLHEGVYGIFNSVLFDNTCPTPIsqKKPSTEQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 658132468  351 VYSSSLWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 61-391 5.42e-48

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: 169.94  E-value: 5.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  61 PRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVRLLSFDNEMEL 140
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 141 AKVVKSHPSAKMVLSIA----------TDDSHSLSRLNLKFGASLKSCRHLLENAKR-DHVEVVGVSFHIGSGCPDPQAF 209
Cdd:COG0019  130 ERLAELAAELGKRAPVGlrvnpgvdagTHEYISTGGKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPF 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 210 AKSisdARLVFEMGAEL---GHRMHILDLGGGFpGV----EGAKMRFDEIASVINSALDLYFpeGCGVDILAKLGRYYVT 282
Cdd:COG0019  210 EEA---LERLLELAEELrelGIDLEWLDLGGGL-GIpyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRALVG 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 283 SAFTLAVSIIGKKEVlldqpgreedtgsAPKTIVY-------HLHEGVYGIFNSVLFDNtcptpisqKKPSTEQPVYssS 355
Cdd:COG0019  284 NAGVLLTRVLDVKEN-------------GGRRFVIvdagmndLMRPALYGAYHPIVPVG--------RPSGAEAETY--D 340

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 658132468 356 LWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAYT 391
Cdd:COG0019  341 VVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYG 376
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 1.82e-10

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 63.18  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  66 FYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIIYASPCKQIAQIKYAAKHGVrLLSFDNEMELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 144 VKSHPSAKMVLSI--ATDDSH----SLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHIGSGCPDPQAFaksisdaR 217
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHW-------R 681

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658132468 218 LVFEMGAELGHRM---HILDLGGGFPGVEGAKMR---FDEIASVINSALDLYfPegcGVDILAKLGRYYVTSA 284
Cdd:PRK08961 682 RMADELASFARRFpdvRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-396 1.36e-175

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily is composed mainly of eukaryotic ornithine decarboxylases (ODC, EC 4.1.1.17) and ODC-like enzymes from prokaryotes represented by Vibrio vulnificus LysineOrnithine decarboxylase. These are fold type III PLP-dependent enzymes that differ from most bacterial ODCs which are fold type I PLP-dependent enzymes. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. Members of this subfamily contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity. Also members of this subfamily are proteins with homology to ODC but do not possess any catalytic activity, the Antizyme inhibitor (AZI) and ODC-paralogue (ODC-p). AZI binds to the regulatory protein Antizyme with a higher affinity than ODC and prevents ODC degradation. ODC-p is a novel ODC-like protein, present only in mammals, that is specifically exressed in the brain and testes. ODC-p may function as a tissue-specific antizyme inhibitory protein.


Pssm-ID: 143482 [Multi-domain]  Cd Length: 362  Bit Score: 496.25  E-value: 1.36e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  40 AFFVADLGAVVRKHFCFLKCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPSAKMVLSIATDDSHSLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 200 GSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPGVE-GAKMRFDEIASVINSALDLYFPEGcGVDILAKLGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 279 YYVTSAFTLAVSIIGKKEVLLDQPGREedtgsapktivYHLHEGVYGIFNSVLFDNTCPTPISQKKPSTEQPVYSSSLWG 358
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 658132468 359 PVVDGCDCVAEGLWLPQ-LHVGDWLVFENMGAYTVGVGS 396
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYAS 349
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 40-415 6.61e-137

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: 399.22  E-value: 6.61e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  40 AFFVADLGAVVRKHFCFLKCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:cd06831   14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPSAKMVLSIATDDSHSLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHI 199
Cdd:cd06831   94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 200 GSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPGVEgakMRFDEIASVINSALDLYFPEGCGVDILAKLGRY 279
Cdd:cd06831  174 SSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSY 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 280 YVTSAFTLAVSIIGKKEVLLDQ--PGREEDTGSAPkTIVYHLHEGVYGIFNSVLFDNTCPTPISQKKPSTEQPVYSSSLW 357
Cdd:cd06831  251 YVSSAFTLAVNVIAKKAVENDKhlSSVEKNGSDEP-AFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLW 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658132468 358 GPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAYTVGVGSLLRGAQTCRITYAMSRVAW 415
Cdd:cd06831  330 GPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDW 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 41-388 7.59e-114

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: 338.31  E-value: 7.59e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468   41 FFVADLGAVVRKHFCFLKCL-PRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  120 QIKYAAKHGVRLLSFDNEMELAKVVKSHPS--AKMVLSIATD---DSHSLS--RLNLKFGASLKSCRHLLENAKRDHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKIStgGLSSKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  193 VGVSFHIGSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPG--VEGAKMRFDEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIpyRDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  271 DILAKLGRYYVTSAFTLAVSIIGKKEvlldqpgreedtgSAPKTIVYhLHEGVYGIFNSVLFDNTCPTPIsqKKPSTEQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 658132468  351 VYSSSLWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 46-281 5.84e-100

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: 299.20  E-value: 5.84e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468   46 LGAVVRKHFCFLKCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAA 125
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  126 KHGVRLLSFDNEMELAKVVKSHPSAKMVLSIATDDSHSLSRLNLKFGASL-KSCRHLLENAKRDHVEVVGVSFHIGSGCP 204
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  205 DPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFpGVE----GAKMRFDEIASVINSALDLYFPEGCGVDILAKLGRYY 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239


                  .
gi 658132468  281 V 281
Cdd:pfam02784 240 V 240
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 39-392 7.31e-96

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: 293.44  E-value: 7.31e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  39 AAFFVADLGAVVRKHFCFLKCLP-RVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQ 117
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 118 IAQIKYAAKHGVRLLSFDNEMELAKVV----KSHPSAKMVLSIATDDS-----HSLSRLNLKFGASLKSCRHLLENAKRD 188
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSagthkISTGGLKSKFGLSLSEARAALERAKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 189 HVEVVGVSFHIGSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPG-VEGAKMRFDEIASVINSALDLYFPEG 267
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIpYDEQPLDFEEYAALINPLLKKYFPND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 268 CGVDILAKLGRYYVTSAFTLAVSIIGKKEVlldqpgreedtgsaPKTIVYHLHEGVYGIFNSVLFDNTCPTPISQKKPST 347
Cdd:cd06810  241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVN--------------GGRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 658132468 348 EQPVYSSSLWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAYTV 392
Cdd:cd06810  307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGF 351
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 61-391 5.42e-48

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: 169.94  E-value: 5.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  61 PRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVRLLSFDNEMEL 140
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 141 AKVVKSHPSAKMVLSIA----------TDDSHSLSRLNLKFGASLKSCRHLLENAKR-DHVEVVGVSFHIGSGCPDPQAF 209
Cdd:COG0019  130 ERLAELAAELGKRAPVGlrvnpgvdagTHEYISTGGKDSKFGIPLEDALEAYRRAAAlPGLRLVGLHFHIGSQILDLEPF 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 210 AKSisdARLVFEMGAEL---GHRMHILDLGGGFpGV----EGAKMRFDEIASVINSALDLYFpeGCGVDILAKLGRYYVT 282
Cdd:COG0019  210 EEA---LERLLELAEELrelGIDLEWLDLGGGL-GIpyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRALVG 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 283 SAFTLAVSIIGKKEVlldqpgreedtgsAPKTIVY-------HLHEGVYGIFNSVLFDNtcptpisqKKPSTEQPVYssS 355
Cdd:COG0019  284 NAGVLLTRVLDVKEN-------------GGRRFVIvdagmndLMRPALYGAYHPIVPVG--------RPSGAEAETY--D 340

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 658132468 356 LWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAYT 391
Cdd:COG0019  341 VVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYG 376
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 58-241 7.20e-45

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: 155.55  E-value: 7.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  58 KCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVRLLSFDNE 137
Cdd:cd06808   11 AAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 138 MELAKV----VKSHPSAKMVLSIATDDshslsrLNLKFGASLKSCRHLLENAKR-DHVEVVGVSFHIGSGCPDPQAFAKS 212
Cdd:cd06808   91 EELEKLeeaaLKAGPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKElPHLRLVGLHTHFGSADEDYSPFVEA 164

                        170       180
                 ....*....|....*....|....*....
gi 658132468 213 ISDARLVFEMGAELGHRMHILDLGGGFPG 241
Cdd:cd06808  165 LSRFVAALDQLGELGIDLEQLSIGGSFAI 193
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 61-390 2.35e-37

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: 140.31  E-value: 2.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  61 PRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVRLLSFDNEMEL 140
Cdd:cd06828   27 PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSEL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 141 AKVVKSHPSAKMVLSIA-------TDDSHSLSRLNL---KFGASLKSCRHLLENAKR-DHVEVVGVSFHIGSGCPDPQAF 209
Cdd:cd06828  107 ERLGEIAPELGKGAPVAlrvnpgvDAGTHPYISTGGkdsKFGIPLEQALEAYRRAKElPGLKLVGLHCHIGSQILDLEPF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 210 AKSisdARLVFEMGAEL---GHRMHILDLGGGFpGV----EGAKMRFDEIASVINSALDLYFPEGCGVDILAKLGRYYVT 282
Cdd:cd06828  187 VEA---AEKLLDLAAELrelGIDLEFLDLGGGL-GIpyrdEDEPLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVA 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 283 SAFTLAVSIIGKKEvlldqpgreedTGSapKTIVyhlheGVYGIFNsvlfDNTCP---------TPISQKKPSTEQPVys 353
Cdd:cd06828  263 NAGVLLTRVGYVKE-----------TGG--KTFV-----GVDAGMN----DLIRPalygayheiVPVNKPGEGETEKV-- 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 658132468 354 sSLWGPVvdgC---DCVAEGLWLPQLHVGDWLVFENMGAY 390
Cdd:cd06828  319 -DVVGPI---CesgDVFAKDRELPEVEEGDLLAIHDAGAY 354
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 41-392 7.14e-31

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: 122.37  E-value: 7.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  41 FFVADLGAVVRKHFCFL----KCLPRVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCK 116
Cdd:cd06841    9 FFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 117 QIAQIKYAAKHGVrLLSFDNEMELAKvvkshpsakmVLSIATDDSHSLS---RLNL--------KFGASLKSCRHLLENA 185
Cdd:cd06841   89 SKEELEKALEEGA-LINIDSFDELER----------ILEIAKELGRVAKvgiRLNMnygnnvwsRFGFDIEENGEALAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 186 KR----DHVEVVGVSFHIGSGCPDPQAFAKSISDarLVFEMGAELGHRMHILDLGGGFPGvegaKMR------------- 248
Cdd:cd06841  158 KKiqesKNLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPA----KTPlslaypqedtvpd 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 249 FDEIASVINSALDLYFPEGCGVDIL-AKLGRYYVTSAFTLAVSIIGKKEVlldqPGREEDTGSAPKTIVYHLHEgvygIF 327
Cdd:cd06841  232 PEDYAEAIASTLKEYYANKENKPKLiLEPGRALVDDAGYLLGRVVAVKNR----YGRNIAVTDAGINNIPTIFW----YH 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658132468 328 NSVLFDNTCPtpisQKKPSTEQPVYssslwGPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAYTV 392
Cdd:cd06841  304 HPILVLRPGK----EDPTSKNYDVY-----GFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNM 359
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 41-390 4.14e-25

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is composed of Bacillus circulans BtrK decarboxylase and similar proteins. These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. BtrK is presumed to function as a PLP-dependent decarboxylase involved in the biosynthesis of the aminoglycoside antibiotic butirosin. Homodimer formation and the presence of the PLP cofactor may be required for catalytic activity.


Pssm-ID: 143506 [Multi-domain]  Cd Length: 382  Bit Score: 106.14  E-value: 4.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  41 FFVADLgAVVRKHFCFL-KCLPR-VRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQI 118
Cdd:cd06839    9 FYVYDR-DRVRERYAALrAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 119 AQIKYAAKHGVRLLSFDNEMELAKV----VKSHPSAKMVLSIATDDSHSLSRLNLKFGAS--------LKSCRHLLENak 186
Cdd:cd06839   88 AELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPDFELKGSGMKMGGGPSqfgidveeLPAVLARIAA-- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 187 RDHVEVVGVSFHIGSGCPDP----QAFAKSIsdaRLVFEMGAELGHRMHILDLGGGFpGV----EGAKMRFDEIASVINS 258
Cdd:cd06839  166 LPNLRFVGLHIYPGTQILDAdaliEAFRQTL---ALALRLAEELGLPLEFLDLGGGF-GIpyfpGETPLDLEALGAALAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 259 ALDLYFPEGCGVDILAKLGRYYVTSAFTLAVSIIGKKE-------VLldqpgreeDTGSapktivyHLHEGVYGIFNSVL 331
Cdd:cd06839  242 LLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVsrgetflVT--------DGGM-------HHHLAASGNFGQVL 306

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 658132468 332 FDNTCPTPISQKKPSTEQPVyssSLWGPVVDGCDCVAEGLWLPQLHVGDWLVFENMGAY 390
Cdd:cd06839  307 RRNYPLAILNRMGGEERETV---TVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 68-391 2.26e-21

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: 95.54  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  68 AVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVRLlSFDNEMELAKV---V 144
Cdd:cd06836   33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAI-NIDNFQELERIdalV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 145 KSHPSAKMVLSI--------ATDDSHSLSRLNLKFGASLK-SCRHLLENAKRDHVEVVGVSFHIGS-GCPDPQAfAKSIs 214
Cdd:cd06836  112 AEFKEASSRIGLrvnpqvgaGKIGALSTATATSKFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELSLL-AEGI- 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 215 daRLVFEMGAELGHRM-----HILDLGGGFP---GVEGAKMRFDEIASVINSALDLYFPEGCGVdiLAKLGRYYVTSAFT 286
Cdd:cd06836  190 --RRVVDLAEEINRRVgrrqiTRIDIGGGLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLLAKCGT 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 287 lAVSiigkkevlldqpgREEDTGSAPKTIVYHLHEGVYGIFNSVLFDNTCPTPI----SQKKPSTEQPVySSSLWGPVVD 362
Cdd:cd06836  266 -IVS-------------RVEYTKSSGGRRIAITHAGAQVATRTAYAPDDWPLRVtvfdANGEPKTGPEV-VTDVAGPCCF 330

                        330       340
                 ....*....|....*....|....*....
gi 658132468 363 GCDCVAEGLWLPQLHVGDWLVFENMGAYT 391
Cdd:cd06836  331 AGDVLAKERALPPLEPGDYVAVHDTGAYY 359
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 43-240 1.65e-18

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: 87.32  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  43 VADLGAVVRKHFcfLKClprvRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIIYASPCKQIAQIK 122
Cdd:cd06842   24 IAALRAVLDRHG--VDG----RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 123 YAAKHGVrLLSFDNEMELAKVVK-----SHPSAKMVLSIATDDSHSLSRlnlkFGASLKSCRHLLENAK--RDHVEVVGV 195
Cdd:cd06842   98 LAVRHGA-TIAVDSLDELDRLLAlargyTTGPARVLLRLSPFPASLPSR----FGMPAAEVRTALERLAqlRERVRLVGF 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 658132468 196 SFHIGSGCPDPQAFAksISDARLVFEMGAELGHRMHILDLGGGFP 240
Cdd:cd06842  173 HFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 64-390 1.64e-10

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: 62.45  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  64 RPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIIYASPCKQIAQIKYAAKHGVRlLSFDNEMELA 141
Cdd:cd06840   37 SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVN-VTVDNLHPLR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 142 KVVKSHPSAKMVLSI--ATDDSH----SLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHIGSGCPDPQAFAKSISD 215
Cdd:cd06840  116 EWPELFRGREVILRIdpGQGEGHhkhvRTGGPESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 216 -ARLVFEMGAelghrMHILDLGGGFPGVE---GAKMRFDEIASVInSALDLYFPegcGVDILAKLGRYYVTSAFTLAVSI 291
Cdd:cd06840  196 lASLARHFPA-----VRILNVGGGLGIPEapgGRPIDLDALDAAL-AAAKAAHP---QYQLWMEPGRFIVAESGVLLARV 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 292 IGKKEvlldqpgreedtgsAPKTIVYHLHEGVYGIFNSVLFDntCPTPISQKKPSTEQPVYSSSLWGPVVDGCDCVAEGL 371
Cdd:cd06840  267 TQIKH--------------KDGVRFVGLETGMNSLIRPALYG--AYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDR 330

                        330
                 ....*....|....*....
gi 658132468 372 WLPQLHVGDWLVFENMGAY 390
Cdd:cd06840  331 LLPETEEGDVILIANAGAY 349
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 37-242 1.76e-10

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: 62.30  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  37 EVAAFfVADLGAVvRKHFCFLK-CLP-RVRPFYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHIgVPASKIIYASP 114
Cdd:cd06843    1 PLCAY-VYDLAAL-RAHARALRaSLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 115 CKQIAQIKYAAKHGVRLLSFDNEMELAK---VVKSHPSAKMVL---SIATDDSHSlSRLNL-----KFG---ASLKSCRH 180
Cdd:cd06843   78 GKTDSELAQALAQGVERIHVESELELRRlnaVARRAGRTAPVLlrvNLALPDLPS-STLTMggqptPFGideADLPDALE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658132468 181 LLENAkrDHVEVVGVSFHIGSGCPDPQAFAKSISD-ARLVFEMGAELGHRMHILDLGGGFpGV 242
Cdd:cd06843  157 LLRDL--PNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI-GV 216
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 1.82e-10

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 63.18  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  66 FYAVKCNSSSGVLKVLAELGLGFSCANKAEMELVQHI--GVPASKIIYASPCKQIAQIKYAAKHGVrLLSFDNEMELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGV-TVTLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 144 VKSHPSAKMVLSI--ATDDSH----SLSRLNLKFGASLKSCRHLLENAKRDHVEVVGVSFHIGSGCPDPQAFaksisdaR 217
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHW-------R 681

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658132468 218 LVFEMGAELGHRM---HILDLGGGFPGVEGAKMR---FDEIASVINSALDLYfPegcGVDILAKLGRYYVTSA 284
Cdd:PRK08961 682 RMADELASFARRFpdvRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
PLN02537 PLN02537
diaminopimelate decarboxylase
 15-396 6.17e-09

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 57.88  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  15 EGFSTQDLLEeltlgasqatKDEVAAFFVADLGAVVRKHFCFLKCLPRVR--PFYAVKCNSSSGVLKVLAELGLGFSCAN 92
Cdd:PLN02537   4 EGLRVQDIME----------SVEKRPFYLYSKPQITRNYEAYKEALEGLRsiIGYAIKANNNLKILEHLRELGCGAVLVS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468  93 KAEMELVQHIGVPASKIIYASPCKQIAQIKYAAKHGVrLLSFDNEMELAKVV----KSHPSAKMVLSIATD---DSH--- 162
Cdd:PLN02537  74 GNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGV-FVNVDSEFDLENIVeaarIAGKKVNVLLRINPDvdpQVHpyv 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 163 SLSRLNLKFGASLKSCRHLLENAKR--DHVEVVGVSFHIGSGCPDPQAFaksiSDARLVF-----EMGAElGHRMHILDL 235
Cdd:PLN02537 153 ATGNKNSKFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKVDIF----RDAAVLMvnyvdEIRAQ-GFELSYLNI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 236 GGGFpGVE----GAKMrfDEIASVINSALDLYFPEgcGVDILAKLGRYYVTSAFTLAVSIIGKKE------VLLDqpgre 305
Cdd:PLN02537 228 GGGL-GIDyyhaGAVL--PTPRDLIDTVRELVLSR--DLTLIIEPGRSLIANTCCFVNRVTGVKTngtknfIVID----- 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 306 edtGSAPKTIvyhlHEGVYGIFNSVLFdntcptpisQKKPSTEQPVYSSSLWGPVVDGCDCVAEGLWLPQLHVGDWLVFE 385
Cdd:PLN02537 298 ---GSMAELI----RPSLYDAYQHIEL---------VSPPPPDAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVH 361

                        410
                 ....*....|.
gi 658132468 386 NMGAYTVGVGS 396
Cdd:PLN02537 362 DAGAYCMSMAS 372
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
172-272 3.67e-04

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 41.92  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658132468 172 GASLKSCRHLLENAkrdHVEVVGVSFHIGSGCPDPQAFAKSISDARLVFEMGAELGHRMHILDLGGGFPGVEGAKMRFDE 251
Cdd:COG1082   39 EADLAELRAALADH---GLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDR 115

                         90       100
                 ....*....|....*....|.
gi 658132468 252 IASVINSALDLYfpEGCGVDI 272
Cdd:COG1082  116 LAERLRELAELA--EEAGVTL 134
 
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.
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