NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1776842982|ref|NP_001363653|]
View 

antizyme inhibitor 2 isoform 1 [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 ...
40-408 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: 530.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622     3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622    83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622   163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 358
Cdd:cd00622   242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1776842982 359 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 408
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 ...
40-408 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: 530.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622     3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622    83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622   163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 358
Cdd:cd00622   242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1776842982 359 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 408
Cdd:cd00622   311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
41-388 3.63e-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: 344.08  E-value: 3.63e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  41 FFVADLGAIVRKHFCFLKCL-PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LSLKFGVSLKSCRHLLENAKKHHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLSSKFGIDLEDAPELLALAKELGLNV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 193 VGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAKVRFEEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 271 DIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGIFNSVLFDNICPTPIlqKKPSTEQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1776842982 351 LYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
61-398 1.69e-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: 179.19  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  61 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 140
Cdd:COG0019    50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 141 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 203
Cdd:COG0019   130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 204 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 280
Cdd:COG0019   204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 281 VTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSS 354
Cdd:COG0019   282 VGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETY 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1776842982 355 SLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 398
Cdd:COG0019   340 DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-396 5.20e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 71.27  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  66 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 143
Cdd:PRK08961  530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 144 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 215
Cdd:PRK08961  609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 216 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsii 292
Cdd:PRK08961  688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV----------- 747
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 293 AKKEVLLDQPGREEENGStsktiVYH--LDEGVYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCV 367
Cdd:PRK08961  748 AEAGVLLARVTQVKEKDG-----VRRvgLETGMNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVL 817
                         330       340
                  ....*....|....*....|....*....
gi 1776842982 368 AEGLWLPQLHVGDWLVFDNMGAYTVGMGS 396
Cdd:PRK08961  818 GKRRRLPATAEGDVILIANAGAYGYSMSS 846
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
40-408 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: 530.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622     3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622    83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622   163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 358
Cdd:cd00622   242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWG 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1776842982 359 PAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGAYTVGMGSPFWGTQACHITY 408
Cdd:cd00622   311 PTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVY 361
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
40-415 5.93e-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: 414.63  E-value: 5.93e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd06831    14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd06831    94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEgakVRFEEIASVINSALDLYFPEGCGVDIFAELGRY 279
Cdd:cd06831   174 SSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSY 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 280 YVTSAFTVAVSIIAKKEVLLDQ-PGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWG 358
Cdd:cd06831   251 YVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWG 330
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776842982 359 PAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAW 415
Cdd:cd06831   331 PSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDW 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
41-388 3.63e-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: 344.08  E-value: 3.63e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  41 FFVADLGAIVRKHFCFLKCL-PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LSLKFGVSLKSCRHLLENAKKHHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLSSKFGIDLEDAPELLALAKELGLNV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 193 VGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAKVRFEEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPP--DL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 271 DIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGIFNSVLFDNICPTPIlqKKPSTEQP 350
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPV--VKEPGEGP 302
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1776842982 351 LYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 388
Cdd:pfam00278 303 LETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
39-402 8.57e-103

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: 311.16  E-value: 8.57e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  39 AAFFVADLGAIVRKHFCFLKCLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQ 117
Cdd:cd06810     1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 118 IAQIKYAAKHGIQLLSFDNEMELAKVV----KSHPSAKMVLCIATDDSH----SLSCLSL-KFGVSLKSCRHLLENAKKH 188
Cdd:cd06810    81 VSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSAgthkISTGGLKsKFGLSLSEARAALERAKEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 189 HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT-EGAKVRFEEIASVINSALDLYFPEG 267
Cdd:cd06810   161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPyDEQPLDFEEYAALINPLLKKYFPND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 268 CGVDIFAELGRYYVTSAFTVAVSIIAKKEVLldqpgreeengstsKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPST 347
Cdd:cd06810   241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNG--------------GRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1776842982 348 EQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQ 402
Cdd:cd06810   307 DEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHP 361
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
46-281 2.93e-98

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: 294.57  E-value: 2.93e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  46 LGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAA 125
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 126 KHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL-KSCRHLLENAKKHHVEVVGVSFHIGSGCP 204
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 205 DPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFpGTE----GAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYY 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239

                  .
gi 1776842982 281 V 281
Cdd:pfam02784 240 V 240
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
61-398 1.69e-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: 179.19  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  61 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 140
Cdd:COG0019    50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 141 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 203
Cdd:COG0019   130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 204 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 280
Cdd:COG0019   204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 281 VTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYgifnsvlfDNICPT------PILQKKPSTEQPLYSS 354
Cdd:COG0019   282 VGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN--------DLMRPAlygayhPIVPVGRPSGAEAETY 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1776842982 355 SLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 398
Cdd:COG0019   340 DVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
58-243 1.10e-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: 1.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  58 KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNE 137
Cdd:cd06808    11 AAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 138 MELAKV----VKSHPSAKMVLCIATDDshslscLSLKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQS 212
Cdd:cd06808    91 EELEKLeeaaLKAGPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEA 164
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1776842982 213 IADARLVFEMGTELGHKMHVLDLGGGFPGTE 243
Cdd:cd06808   165 LSRFVAALDQLGELGIDLEQLSIGGSFAILY 195
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
41-396 9.33e-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: 141.47  E-value: 9.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  41 FFVADLGAIvRKHFCFLK---CLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQ 117
Cdd:cd06828     5 LYVYDEATI-RENYRRLKeafSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 118 IAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIA--------------TDDSHSLSclslKFGVSLKSCRHLLE 183
Cdd:cd06828    84 DEELELALELGILRINVDSLSELERLGEIAPELGKGAPVAlrvnpgvdagthpyISTGGKDS----KFGIPLEQALEAYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 184 NAKK-HHVEVVGVSFHIGSGCPDPQAYAQSiadARLVFEMGTEL---GHKMHVLDLGGGF--PGTEGAK-VRFEEIASVI 256
Cdd:cd06828   160 RAKElPGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgiPYRDEDEpLDIEEYAEAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 257 NSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVyHLDEGvygiFNsvlfDNIC 336
Cdd:cd06828   237 AEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKE-------------TGGKTFV-GVDAG----MN----DLIR 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776842982 337 PT------PILQKKPSTEQPLYSSSLWGPAvdgC---DCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 396
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 ...
41-398 1.07e-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: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  41 FFVADLGAIVRKHFCFL----KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCK 116
Cdd:cd06841     9 FFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 117 QIAQIKYAAKHG--IQLLSFDNEMELAKVVKSHP-SAKMVLCIATD-DSHSLSclslKFGVSLKSCRHLLENAKKH---- 188
Cdd:cd06841    89 SKEELEKALEEGalINIDSFDELERILEIAKELGrVAKVGIRLNMNyGNNVWS----RFGFDIEENGEALAALKKIqesk 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 189 HVEVVGVSFHIGSGCPDPQAYAQSIADarLVFEMGTELGHKMHVLDLGGGFPG---------TEGAKVRFEEIASVINSA 259
Cdd:cd06841   165 NLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktplslaypQEDTVPDPEDYAEAIAST 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 260 LDLYFPEGCG-VDIFAELGRYYVTSAFTVAVSIIAKKEVlldqPGREeengstsktiVYHLDEGvygIFNSVLFDNICPt 338
Cdd:cd06841   243 LKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNR----YGRN----------IAVTDAG---INNIPTIFWYHH- 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776842982 339 PILQKKPSTEQPLYSSS-LWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 398
Cdd:cd06841   305 PILVLRPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQF 365
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
41-390 1.34e-23

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: 101.90  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  41 FFVADLGAIvRKHFCFL-KCLPR-VRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQI 118
Cdd:cd06839     9 FYVYDRDRV-RERYAALrAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 119 AQIKYAAKHGIQLLSFDNEMELAKV----VKSHPSAKMVLCIATDDSHSLSCLSL-----KFGVS---LKSCRHLLENAk 186
Cdd:cd06839    88 AELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPDFELKGSGMKMgggpsQFGIDveeLPAVLARIAAL- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 187 kHHVEVVGvsFHI--GSGCPDPQAYAQSIADA-RLVFEMGTELGHKMHVLDLGGGF--P-GTEGAKVRFEEIASVINSAL 260
Cdd:cd06839   167 -PNLRFVG--LHIypGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFgiPyFPGETPLDLEALGAALAALL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 261 DLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIV-------YHLdeGVYGIFNSVLFD 333
Cdd:cd06839   244 AELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-------------SRGETFLvtdggmhHHL--AASGNFGQVLRR 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1776842982 334 NIcPTPILQKkpSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAY 390
Cdd:cd06839   309 NY-PLAILNR--MGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
68-394 4.16e-20

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: 91.69  E-value: 4.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  68 AVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQlLSFDNEMELAKV---V 144
Cdd:cd06836    33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIdalV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 145 KSHPSAKMVLCI--------ATDDSHSLSCLSLKFGVSLK-SCRHLLENAKKHHVEVVGVSFHIGS-GCPDPQAyaqsIA 214
Cdd:cd06836   112 AEFKEASSRIGLrvnpqvgaGKIGALSTATATSKFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELSLL----AE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 215 DARLVFEMGTELGHKM-----HVLDLGGGFP---GTEGAKVRFEEIASVINSALDLYFPEGCGVdiFAELGRYYVTSA-F 285
Cdd:cd06836   188 GIRRVVDLAEEINRRVgrrqiTRIDIGGGLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLLAKCgT 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 286 TVAVSIIAKK----EVLLDQPGREEENGSTSKTIVYHLDEGVYgifnsvlfdnicpTPILQKKPSTEQPlysSSLWGPAV 361
Cdd:cd06836   266 IVSRVEYTKSsggrRIAITHAGAQVATRTAYAPDDWPLRVTVF-------------DANGEPKTGPEVV---TDVAGPCC 329
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1776842982 362 DGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGM 394
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 ...
43-240 1.80e-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: 84.23  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  43 VADLGAIVRKHFcfLKClprvRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIK 122
Cdd:cd06842    24 IAALRAVLDRHG--VDG----RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLW 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 123 YAAKHGIqLLSFDNEMELAKVVK-----SHPSAKMVLCIATDDSHSLSclslKFGVSLKSCRHLLENAKKH--HVEVVGV 195
Cdd:cd06842    98 LAVRHGA-TIAVDSLDELDRLLAlargyTTGPARVLLRLSPFPASLPS----RFGMPAAEVRTALERLAQLreRVRLVGF 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1776842982 196 SFHIGSGCPDPQAYAqsIADARLVFEMGTELGHKMHVLDLGGGFP 240
Cdd:cd06842   173 HFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
64-396 8.29e-15

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: 75.55  E-value: 8.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  64 RPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELA 141
Cdd:cd06840    37 SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNV-TVDNLHPLR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 142 KVVKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIAD 215
Cdd:cd06840   116 EWPELFRGREVILRIdpGQGEGHhkhvRTGGPESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDY 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 216 -ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVRFEEIASVINS--ALDLYFPegcGVDIFAELGRYyvtsaftvavsII 292
Cdd:cd06840   196 lASLARHFPA-----VRILNVGGGLGIPEAPGGRPIDLDALDAAlaAAKAAHP---QYQLWMEPGRF-----------IV 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 293 AKKEVLLdqpGREEENGSTSKTIVYHLDEGVYGIFNSVLFDniCPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLW 372
Cdd:cd06840   257 AESGVLL---ARVTQIKHKDGVRFVGLETGMNSLIRPALYG--AYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRL 331
                         330       340
                  ....*....|....*....|....
gi 1776842982 373 LPQLHVGDWLVFDNMGAYTVGMGS 396
Cdd:cd06840   332 LPETEEGDVILIANAGAYGFCMAS 355
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-396 5.20e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 71.27  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  66 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 143
Cdd:PRK08961  530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 144 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 215
Cdd:PRK08961  609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 216 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsii 292
Cdd:PRK08961  688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV----------- 747
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 293 AKKEVLLDQPGREEENGStsktiVYH--LDEGVYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCV 367
Cdd:PRK08961  748 AEAGVLLARVTQVKEKDG-----VRRvgLETGMNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVL 817
                         330       340
                  ....*....|....*....|....*....
gi 1776842982 368 AEGLWLPQLHVGDWLVFDNMGAYTVGMGS 396
Cdd:PRK08961  818 GKRRRLPATAEGDVILIANAGAYGYSMSS 846
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
37-239 8.39e-09

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: 57.29  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982  37 EVAAFfVADLGAIvRKHFCFLK-CLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGiPASKIICANP 114
Cdd:cd06843     1 PLCAY-VYDLAAL-RAHARALRaSLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV-PDAPLIFGGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 115 CKQIAQIKYAAKHGIQLLSFDNEMELAK---VVKSHPSAKMVLC---IATDDSHSlSCLSL-----KFGVSLKSCRHLLE 183
Cdd:cd06843    78 GKTDSELAQALAQGVERIHVESELELRRlnaVARRAGRTAPVLLrvnLALPDLPS-STLTMggqptPFGIDEADLPDALE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1776842982 184 NAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFEMGTELGHKMHVLDLGGGF 239
Cdd:cd06843   157 LLRDLpNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI 214
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
171-272 5.01e-05

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 44.62  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842982 171 FGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFE 250
Cdd:COG1082    35 GDLDEADLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWD 114
                          90       100
                  ....*....|....*....|..
gi 1776842982 251 EIASVINSALDLYfpEGCGVDI 272
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