NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119627876|gb|EAX07471|]
View 

arginine decarboxylase, isoform CRA_c [Homo sapiens]

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 ...
108-476 0e+00

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: 532.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 108 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 267
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 268 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 346
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 347 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 426
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119627876 427 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 476
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
108-476 0e+00

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: 532.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 108 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 267
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 268 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 346
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 347 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 426
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119627876 427 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 476
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
109-456 4.14e-116

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: 346.40  E-value: 4.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  109 FFVADLGAIVRKHFCFLKCL-PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LSLKFGVSLKSCRHLLENAKKHHVEV 260
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLSSKFGIDLEDAPELLALAKELGLNV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  261 VGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAKVRFEEIASVINSALDLYFPEgcGV 338
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  339 DIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGIFNSVLFDNICPTPIlqKKPSTEQP 418
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 119627876  419 LYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 456
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
129-466 4.18e-51

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: 179.96  E-value: 4.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 129 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 208
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 209 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 271
Cdd:COG0019  130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 272 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 348
Cdd:COG0019  204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 349 VTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSS 422
Cdd:COG0019  282 VGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETY 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 119627876 423 SLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 466
Cdd:COG0019  340 DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
134-464 9.40e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 70.88  E-value: 9.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 134 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 211
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 212 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 283
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 284 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsii 360
Cdd:PRK08961 688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV----------- 747
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 361 AKKEVLLDQPGREEENGSTSKTivyHLDEGVYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAE 437
Cdd:PRK08961 748 AEAGVLLARVTQVKEKDGVRRV---GLETGMNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGK 819
                        330       340
                 ....*....|....*....|....*..
gi 119627876 438 GLWLPQLHVGDWLVFDNMGAYTVGMGS 464
Cdd:PRK08961 820 RRRLPATAEGDVILIANAGAYGYSMSS 846
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
108-476 0e+00

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: 532.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 108 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 267
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 268 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 346
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 347 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 426
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119627876 427 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 476
Cdd:cd00622  311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
108-483 1.39e-143

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: 418.87  E-value: 1.39e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 108 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:cd06831   14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 267
Cdd:cd06831   94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 268 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEgakVRFEEIASVINSALDLYFPEGCGVDIFAELGRY 347
Cdd:cd06831  174 SSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSY 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 348 YVTSAFTVAVSIIAKKEVLLDQ-PGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 426
Cdd:cd06831  251 YVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWG 330
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119627876 427 PAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAW 483
Cdd:cd06831  331 PSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDW 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
109-456 4.14e-116

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: 346.40  E-value: 4.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  109 FFVADLGAIVRKHFCFLKCL-PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 187
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  188 QIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LSLKFGVSLKSCRHLLENAKKHHVEV 260
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLSSKFGIDLEDAPELLALAKELGLNV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  261 VGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAKVRFEEIASVINSALDLYFPEgcGV 338
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  339 DIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGIFNSVLFDNICPTPIlqKKPSTEQP 418
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 119627876  419 LYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 456
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
107-470 2.43e-102

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: 312.32  E-value: 2.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 107 AAFFVADLGAIVRKHFCFLKCLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQ 185
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 186 IAQIKYAAKHGIQLLSFDNEMELAKVV----KSHPSAKMVLCIATDDSH----SLSCLSL-KFGVSLKSCRHLLENAKKH 256
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSAgthkISTGGLKsKFGLSLSEARAALERAKEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 257 HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT-EGAKVRFEEIASVINSALDLYFPEG 335
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPyDEQPLDFEEYAALINPLLKKYFPND 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 336 CGVDIFAELGRYYVTSAFTVAVSIIAKKEVLldqpgreeengstsKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPST 415
Cdd:cd06810  241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNG--------------GRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119627876 416 EQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQ 470
Cdd:cd06810  307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHP 361
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
114-349 1.02e-97

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: 295.73  E-value: 1.02e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  114 LGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAA 193
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  194 KHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL-KSCRHLLENAKKHHVEVVGVSFHIGSGCP 272
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876  273 DPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFpGTE----GAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYY 348
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239

                  .
gi 119627876  349 V 349
Cdd:pfam02784 240 V 240
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
129-466 4.18e-51

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: 179.96  E-value: 4.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 129 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 208
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 209 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 271
Cdd:COG0019  130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 272 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 348
Cdd:COG0019  204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 349 VTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSS 422
Cdd:COG0019  282 VGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETY 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 119627876 423 SLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 466
Cdd:COG0019  340 DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
126-311 3.13e-46

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: 160.56  E-value: 3.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 126 KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNE 205
Cdd:cd06808   11 AAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 206 MELAKV----VKSHPSAKMVLCIATDDshslscLSLKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQS 280
Cdd:cd06808   91 EELEKLeeaaLKAGPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEA 164
                        170       180       190
                 ....*....|....*....|....*....|.
gi 119627876 281 IADARLVFEMGTELGHKMHVLDLGGGFPGTE 311
Cdd:cd06808  165 LSRFVAALDQLGELGIDLEQLSIGGSFAILY 195
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
109-464 9.93e-38

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: 142.62  E-value: 9.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 109 FFVADLGAIvRKHFCFLK---CLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQ 185
Cdd:cd06828    5 LYVYDEATI-RENYRRLKeafSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 186 IAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIA--------------TDDSHSLSclslKFGVSLKSCRHLLE 251
Cdd:cd06828   84 DEELELALELGILRINVDSLSELERLGEIAPELGKGAPVAlrvnpgvdagthpyISTGGKDS----KFGIPLEQALEAYR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 252 NAKK-HHVEVVGVSFHIGSGCPDPQAYAQSiadARLVFEMGTEL---GHKMHVLDLGGGF--PGTEGAK-VRFEEIASVI 324
Cdd:cd06828  160 RAKElPGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgiPYRDEDEpLDIEEYAEAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 325 NSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVyHLDEGvygiFNsvlfDNIC 404
Cdd:cd06828  237 AEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKE-------------TGGKTFV-GVDAG----MN----DLIR 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119627876 405 PT------PILQKKPSTEQPLYSSSLWGPAvdgC---DCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 464
Cdd:cd06828  295 PAlygayhEIVPVNKPGEGETEKVDVVGPI---CesgDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSS 360
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
109-466 2.64e-33

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: 130.46  E-value: 2.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 109 FFVADLGAIVRKHFCFL----KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCK 184
Cdd:cd06841    9 FFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 185 QIAQIKYAAKHG--IQLLSFDNEMELAKVVKSHP-SAKMVLCIATD-DSHSLSclslKFGVSLKSCRHLLENAKKH---- 256
Cdd:cd06841   89 SKEELEKALEEGalINIDSFDELERILEIAKELGrVAKVGIRLNMNyGNNVWS----RFGFDIEENGEALAALKKIqesk 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 257 HVEVVGVSFHIGSGCPDPQAYAQSIADarLVFEMGTELGHKMHVLDLGGGFPG---------TEGAKVRFEEIASVINSA 327
Cdd:cd06841  165 NLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktplslaypQEDTVPDPEDYAEAIAST 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 328 LDLYFPEGCG-VDIFAELGRYYVTSAFTVAVSIIAKKEVlldqPGREeengstsktiVYHLDEGvygIFNSVLFDNICPt 406
Cdd:cd06841  243 LKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNR----YGRN----------IAVTDAG---INNIPTIFWYHH- 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627876 407 PILQKKPSTEQPLYSSS-LWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 466
Cdd:cd06841  305 PILVLRPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQF 365
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
109-458 1.35e-22

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


Pssm-ID: 143506 [Multi-domain]  Cd Length: 382  Bit Score: 99.59  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 109 FFVADLGAIvRKHFCFL-KCLPR-VRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQI 186
Cdd:cd06839    9 FYVYDRDRV-RERYAALrAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 187 AQIKYAAKHGIQLLSFDNEMELAKV----VKSHPSAKMVLCIATDDSHSLSCLSL-----KFGVS---LKSCRHLLENAk 254
Cdd:cd06839   88 AELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPDFELKGSGMKMgggpsQFGIDveeLPAVLARIAAL- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 255 kHHVEVVGVSFHIGSGCPDPQAYAQSIADA-RLVFEMGTELGHKMHVLDLGGGF--P-GTEGAKVRFEEIASVINSALDL 330
Cdd:cd06839  167 -PNLRFVGLHIYPGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFgiPyFPGETPLDLEALGAALAALLAE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 331 YFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIV-------YHLdeGVYGIFNSVLFDNI 403
Cdd:cd06839  246 LGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-------------SRGETFLvtdggmhHHL--AASGNFGQVLRRNY 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119627876 404 cPTPILQKkpSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAY 458
Cdd:cd06839  311 -PLAILNR--MGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
136-462 1.77e-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: 90.15  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 136 AVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQlLSFDNEMELAKV---V 212
Cdd:cd06836   33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIdalV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 213 KSHPSAKMVLCI--------ATDDSHSLSCLSLKFGVSLK-SCRHLLENAKKHHVEVVGVSFHIGS-GCPDPQAyaqsIA 282
Cdd:cd06836  112 AEFKEASSRIGLrvnpqvgaGKIGALSTATATSKFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELSLL----AE 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 283 DARLVFEMGTELGHKM-----HVLDLGGGFP---GTEGAKVRFEEIASVINSALDLYFPEGCGVdiFAELGRYYVTSA-F 353
Cdd:cd06836  188 GIRRVVDLAEEINRRVgrrqiTRIDIGGGLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLLAKCgT 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 354 TVAVSIIAKK----EVLLDQPGREEENGSTSKTIVYHLDEGVYgifnsvlfdnicpTPILQKKPSTEQPlysSSLWGPAV 429
Cdd:cd06836  266 IVSRVEYTKSsggrRIAITHAGAQVATRTAYAPDDWPLRVTVF-------------DANGEPKTGPEVV---TDVAGPCC 329
                        330       340       350
                 ....*....|....*....|....*....|...
gi 119627876 430 DGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGM 462
Cdd:cd06836  330 FAGDVLAKERALPPLEPGDYVAVHDTGAYYFSS 362
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
111-308 6.18e-17

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: 83.08  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 111 VADLGAIVRKHFcfLKClprvRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIK 190
Cdd:cd06842   24 IAALRAVLDRHG--VDG----RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLW 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 191 YAAKHGIqLLSFDNEMELAKVVK-----SHPSAKMVLCIATDDSHSLSclslKFGVSLKSCRHLLENAKKH--HVEVVGV 263
Cdd:cd06842   98 LAVRHGA-TIAVDSLDELDRLLAlargyTTGPARVLLRLSPFPASLPS----RFGMPAAEVRTALERLAQLreRVRLVGF 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 119627876 264 SFHIGSGCPDPQAYAqsIADARLVFEMGTELGHKMHVLDLGGGFP 308
Cdd:cd06842  173 HFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
132-464 1.70e-14

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase/Diaminopimelate Decarboxylase; Bifunctional aspartate kinase/diaminopimelate decarboxylase (AspK/DapDC, EC 4.1.1.20/EC 2.7.2.4) typically exists in bacteria. These proteins contain an N-terminal AspK region and a C-terminal DapDC region, which contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, characteristic of fold type III PLP-dependent enzymes. Members of this subfamily have not been fully characterized. Based on their sequence, these proteins may catalyze both reactions catalyzed by AspK and DapDC. AspK catalyzes the phosphorylation of L-aspartate to produce 4-phospho-L-aspartate while DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine.


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 75.16  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 132 RPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELA 209
Cdd:cd06840   37 SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNV-TVDNLHPLR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 210 KVVKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIAD 283
Cdd:cd06840  116 EWPELFRGREVILRIdpGQGEGHhkhvRTGGPESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDY 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 284 -ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVRFEEIASVINS--ALDLYFPegcGVDIFAELGRYyvtsaftvavsII 360
Cdd:cd06840  196 lASLARHFPA-----VRILNVGGGLGIPEAPGGRPIDLDALDAAlaAAKAAHP---QYQLWMEPGRF-----------IV 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 361 AKKEVLLdqpGREEENGSTSKTIVYHLDEGVYGIFNSVLFDniCPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLW 440
Cdd:cd06840  257 AESGVLL---ARVTQIKHKDGVRFVGLETGMNSLIRPALYG--AYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRL 331
                        330       340
                 ....*....|....*....|....
gi 119627876 441 LPQLHVGDWLVFDNMGAYTVGMGS 464
Cdd:cd06840  332 LPETEEGDVILIANAGAYGFCMAS 355
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
134-464 9.40e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 70.88  E-value: 9.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 134 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 211
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 212 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 283
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 284 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsii 360
Cdd:PRK08961 688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV----------- 747
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 361 AKKEVLLDQPGREEENGSTSKTivyHLDEGVYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAE 437
Cdd:PRK08961 748 AEAGVLLARVTQVKEKDGVRRV---GLETGMNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGK 819
                        330       340
                 ....*....|....*....|....*..
gi 119627876 438 GLWLPQLHVGDWLVFDNMGAYTVGMGS 464
Cdd:PRK08961 820 RRRLPATAEGDVILIANAGAYGYSMSS 846
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
105-307 1.73e-08

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.


Pssm-ID: 143510 [Multi-domain]  Cd Length: 377  Bit Score: 56.52  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 105 EVAAFfVADLGAIvRKHFCFLK-CLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGiPASKIICANP 182
Cdd:cd06843    1 PLCAY-VYDLAAL-RAHARALRaSLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV-PDAPLIFGGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 183 CKQIAQIKYAAKHGIQLLSFDNEMELAK---VVKSHPSAKMVLC---IATDDSHSlSCLSL-----KFGVSLKSCRHLLE 251
Cdd:cd06843   78 GKTDSELAQALAQGVERIHVESELELRRlnaVARRAGRTAPVLLrvnLALPDLPS-STLTMggqptPFGIDEADLPDALE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119627876 252 NAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFEMGTELGHKMHVLDLGGGF 307
Cdd:cd06843  157 LLRDLpNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI 214
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
239-340 4.45e-05

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 45.00  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627876 239 FGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFE 318
Cdd:COG1082   35 GDLDEADLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWD 114
                         90       100
                 ....*....|....*....|..
gi 119627876 319 EIASVINSALDLYfpEGCGVDI 340
Cdd:COG1082  115 RLAERLRELAELA--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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH