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Conserved domains on  [gi|685504961|ref|NP_001288755|]
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antizyme inhibitor 2 isoform 4 [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

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-353 4.98e-155

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: 440.01  E-value: 4.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504961 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQK-SKNHSPCYMS 353
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKdGGRDGELYPS 306
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-353 4.98e-155

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: 440.01  E-value: 4.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504961 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQK-SKNHSPCYMS 353
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKdGGRDGELYPS 306
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 46-281 7.85e-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: 289.95  E-value: 7.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961   46 LGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAA 125
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  126 KHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL-KSCRHLLENAKKHHVEVVGVSFHIGSGCP 204
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  205 DPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFpGTE----GAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYY 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239


                  .
gi 685504961  281 V 281
Cdd:pfam02784 240 V 240
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 61-297 6.98e-40

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: 145.68  E-value: 6.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  61 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 140
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 141 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 203
Cdd:COG0019  130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 204 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 280
Cdd:COG0019  204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281

                        250
                 ....*....|....*..
gi 685504961 281 VTSAFTVAVSIIAKKEV 297
Cdd:COG0019  282 VGNAGVLLTRVLDVKEN 298
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 2.84e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 71.27  E-value: 2.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  66 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 144 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 215
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504961 216 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVTSA 284
Cdd:PRK08961 688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 40-353 4.98e-155

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: 440.01  E-value: 4.98e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd00622    3 PFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKSIS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd00622   83 DIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGR 278
Cdd:cd00622  163 GSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGR 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504961 279 YYVTSAFTVAVSIIAKKEVLLDQPGREeengstsktivYHLDEGVYGIFNSVLFDNICPTPILQK-SKNHSPCYMS 353
Cdd:cd00622  242 YLVASAFTLAVNVIAKRKRGDDDRERW-----------YYLNDGVYGSFNEILFDHIRYPPRVLKdGGRDGELYPS 306
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 40-353 1.02e-116

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: 343.75  E-value: 1.02e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  40 AFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:cd06831   14 AFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQAS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHI 199
Cdd:cd06831   94 QIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 200 GSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEgakVRFEEIASVINSALDLYFPEGCGVDIFAELGRY 279
Cdd:cd06831  174 SSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSY 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504961 280 YVTSAFTVAVSIIAKKEVLLDQ-PGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTP-ILQKSKNHSPCYMS 353
Cdd:cd06831  251 YVSSAFTLAVNVIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPeVHKKYKEDEPLFTS 326
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 46-281 7.85e-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: 289.95  E-value: 7.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961   46 LGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAA 125
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  126 KHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSL-KSCRHLLENAKKHHVEVVGVSFHIGSGCP 204
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  205 DPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFpGTE----GAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYY 280
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYF 239


                  .
gi 685504961  281 V 281
Cdd:pfam02784 240 V 240
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 41-341 1.15e-97

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: 293.24  E-value: 1.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961   41 FFVADLGAIVRKHFCFLKCL-PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIA 119
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  120 QIKYAAKHGIQLLSFDNEMELAKVVKSHPS--AKMVLCIATD---DSHSLSC--LSLKFGVSLKSCRHLLENAKKHHVEV 192
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDvdaGTHKISTggLSSKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  193 VGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EGAKVRFEEIASVINSALDLYFPEgcGV 270
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504961  271 DIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVYGIFNSVLFDNICPTPIL 341
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMNDLFRPALYDAYHPIPVV 295
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 39-347 1.31e-79

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: 247.99  E-value: 1.31e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  39 AAFFVADLGAIVRKHFCFLKCLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQ 117
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEALPsGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 118 IAQIKYAAKHGIQLLSFDNEMELAKVV----KSHPSAKMVLCIATDDSH----SLSCLSL-KFGVSLKSCRHLLENAKKH 188
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNelakKLGPKARILLRVNPDVSAgthkISTGGLKsKFGLSLSEARAALERAKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 189 HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT-EGAKVRFEEIASVINSALDLYFPEG 267
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPyDEQPLDFEEYAALINPLLKKYFPND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 268 CGVDIFAELGRYYVTSAFTVAVSIIAKKEVLldqpgreeengstsKTIVYHLDEGVYGIFNSVLFDNICPTPILQKSKNH 347
Cdd:cd06810  241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNG--------------GRFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGP 306
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 58-243 9.54e-47

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: 158.25  E-value: 9.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  58 KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNE 137
Cdd:cd06808   11 AAPAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 138 MELAKV----VKSHPSAKMVLCIATDDshslscLSLKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQS 212
Cdd:cd06808   91 EELEKLeeaaLKAGPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEA 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 685504961 213 IADARLVFEMGTELGHKMHVLDLGGGFPGTE 243
Cdd:cd06808  165 LSRFVAALDQLGELGIDLEQLSIGGSFAILY 195
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 61-297 6.98e-40

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: 145.68  E-value: 6.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  61 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 140
Cdd:COG0019   50 SGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSEL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 141 AK---VVKSHPSAKMVLC-------------IATDDSHSlsclslKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGC 203
Cdd:COG0019  130 ERlaeLAAELGKRAPVGLrvnpgvdagtheyISTGGKDS------KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 204 PDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGAKVRFEEIASVINSALDLYFpeGCGVDIFAELGRYY 280
Cdd:COG0019  204 LDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDEPPDLEELAAAIKEALEELC--GLGPELILEPGRAL 281

                        250
                 ....*....|....*..
gi 685504961 281 VTSAFTVAVSIIAKKEV 297
Cdd:COG0019  282 VGNAGVLLTRVLDVKEN 298
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 61-281 7.29e-35

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: 131.07  E-value: 7.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  61 PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMEL 140
Cdd:cd06828   27 PGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSDEELELALELGILRINVDSLSEL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 141 AKVVKSHPSAKMVLCIA--------------TDDSHSLSclslKFGVSLKSCRHLLENAKK-HHVEVVGVSFHIGSGCPD 205
Cdd:cd06828  107 ERLGEIAPELGKGAPVAlrvnpgvdagthpyISTGGKDS----KFGIPLEQALEAYRRAKElPGLKLVGLHCHIGSQILD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 206 PQAYAQSiadARLVFEMGTEL---GHKMHVLDLGGGF--PGTEGAK-VRFEEIASVINSALDLYFPEGCGVDIFAELGRY 279
Cdd:cd06828  183 LEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgiPYRDEDEpLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRY 259


                 ..
gi 685504961 280 YV 281
Cdd:cd06828  260 IV 261
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 41-297 9.66e-25

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: 103.50  E-value: 9.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  41 FFVADLGAIVRKHFCFL----KCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCK 116
Cdd:cd06841    9 FFVFDEDALRENYRELLgafkKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPYK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 117 QIAQIKYAAKHG--IQLLSFDNEMELAKVVKSHP-SAKMVLCIATD-DSHSLSclslKFGVSLKSCRHLLENAKKH---- 188
Cdd:cd06841   89 SKEELEKALEEGalINIDSFDELERILEIAKELGrVAKVGIRLNMNyGNNVWS----RFGFDIEENGEALAALKKIqesk 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 189 HVEVVGVSFHIGSGCPDPQAYAQSIADarLVFEMGTELGHKMHVLDLGGGFPG---------TEGAKVRFEEIASVINSA 259
Cdd:cd06841  165 NLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktplslaypQEDTVPDPEDYAEAIAST 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 685504961 260 LDLYFPEGCG-VDIFAELGRYYVTSAFTVAVSIIAKKEV 297
Cdd:cd06841  243 LKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNR 281
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 41-296 2.40e-20

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: 91.12  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  41 FFVADLGAIvRKHFCFL-KCLPR-VRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQI 118
Cdd:cd06839    9 FYVYDRDRV-RERYAALrAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 119 AQIKYAAKHGIQLLSFDNEMELAKV----VKSHPSAKMVLCIATDDSHSLSCLSL-----KFGVS---LKSCRHLLENAk 186
Cdd:cd06839   88 AELRRAIEAGIGTINVESLEELERIdalaEEHGVVARVALRINPDFELKGSGMKMgggpsQFGIDveeLPAVLARIAAL- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 187 kHHVEVVGvsFHI--GSGCPDPQAYAQSIADA-RLVFEMGTELGHKMHVLDLGGGF--P-GTEGAKVRFEEIASVINSAL 260
Cdd:cd06839  167 -PNLRFVG--LHIypGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFgiPyFPGETPLDLEALGAALAALL 243

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 685504961 261 DLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKE 296
Cdd:cd06839  244 AELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV 279
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 68-288 5.07e-18

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: 84.37  E-value: 5.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  68 AVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQlLSFDNEMELAKV---V 144
Cdd:cd06836   33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVA-INIDNFQELERIdalV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 145 KSHPSAKMVLCI--------ATDDSHSLSCLSLKFGVSLK-SCRHLLENAKKHHVEVVGVSFHIGS-GCPDPQAyaqsIA 214
Cdd:cd06836  112 AEFKEASSRIGLrvnpqvgaGKIGALSTATATSKFGVALEdGARDEIIDAFARRPWLNGLHVHVGSqGCELSLL----AE 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 215 DARLVFEMGTELGHKM-----HVLDLGGGFP---GTEGAKVRFEEIASVINSALDLYFPEGCGVdiFAELGRYYVTSAFT 286
Cdd:cd06836  188 GIRRVVDLAEEINRRVgrrqiTRIDIGGGLPvnfESEDITPTFADYAAALKAAVPELFDGRYQL--VTEFGRSLLAKCGT 265


                 ..
gi 685504961 287 VA 288
Cdd:cd06836  266 IV 267
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 43-240 6.32e-18

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the hypothetical Rhizobium sp. protein Y4yA and similar uncharacterized bacterial proteins. These proteins are homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Proteins in this subfamily may function as PLP-dependent decarboxylases.


Pssm-ID: 143509 [Multi-domain]  Cd Length: 423  Bit Score: 84.23  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  43 VADLGAIVRKHFcfLKClprvRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIK 122
Cdd:cd06842   24 IAALRAVLDRHG--VDG----RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLW 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 123 YAAKHGIqLLSFDNEMELAKVVK-----SHPSAKMVLCIATDDSHSLSclslKFGVSLKSCRHLLENAKKH--HVEVVGV 195
Cdd:cd06842   98 LAVRHGA-TIAVDSLDELDRLLAlargyTTGPARVLLRLSPFPASLPS----RFGMPAAEVRTALERLAQLreRVRLVGF 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 685504961 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 ...
 64-284 1.72e-13

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: 70.93  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  64 RPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELA 141
Cdd:cd06840   37 SLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARSEYEQALELGVNV-TVDNLHPLR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 142 KVVKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIAD 215
Cdd:cd06840  116 EWPELFRGREVILRIdpGQGEGHhkhvRTGGPESKFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDY 195

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504961 216 -ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVRFEEIASVINS--ALDLYFPegcGVDIFAELGRYYVTSA 284
Cdd:cd06840  196 lASLARHFPA-----VRILNVGGGLGIPEAPGGRPIDLDALDAAlaAAKAAHP---QYQLWMEPGRFIVAES 259
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
66-284 2.84e-13

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 71.27  E-value: 2.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  66 FYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHI--GIPASKIICANPCKQIAQIKYAAKHGIQLlSFDNEMELAKV 143
Cdd:PRK08961 530 FYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNW 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 144 VKSHPSAKMVLCI--ATDDSH----SLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD-- 215
Cdd:PRK08961 609 PELFRGREVWLRIdpGHGDGHhekvRTGGKESKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADel 687

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504961 216 ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR---FEEIASVINSALDLYfPegcGVDIFAELGRYYVTSA 284
Cdd:PRK08961 688 ASFARRFPD-----VRTIDLGGGLGIPESAGDEpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLVAEA 750
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 37-239 4.55e-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: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961  37 EVAAFfVADLGAIvRKHFCFLK-CLP-RVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGiPASKIICANP 114
Cdd:cd06843    1 PLCAY-VYDLAAL-RAHARALRaSLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV-PDAPLIFGGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 115 CKQIAQIKYAAKHGIQLLSFDNEMELAK---VVKSHPSAKMVLC---IATDDSHSlSCLSL-----KFGVSLKSCRHLLE 183
Cdd:cd06843   78 GKTDSELAQALAQGVERIHVESELELRRlnaVARRAGRTAPVLLrvnLALPDLPS-STLTMggqptPFGIDEADLPDALE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685504961 184 NAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFEMGTELGHKMHVLDLGGGF 239
Cdd:cd06843  157 LLRDLpNIRLRGFHFHLMSHNLDAAAHLALVKAyLETARQWAAEHGLDLDVVNVGGGI 214
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
171-272 3.41e-05

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 44.62  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504961 171 FGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFE 250
Cdd:COG1082   35 GDLDEADLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWD 114

                         90       100
                 ....*....|....*....|..
gi 685504961 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.
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