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Conserved domains on  [gi|1179685350|ref|NP_001337331|]
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antizyme inhibitor 2 isoform 5 [Homo sapiens]

Protein Classification

type III PLP-dependent enzyme domain-containing protein( domain architecture ID 469)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme domain-containing protein, similar to alanine racemase which catalyzes the interconversion of L-alanine and D-alanine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III super family cl00261
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-257 1.79e-117

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.


The actual alignment was detected with superfamily member cd00622:

Pssm-ID: 469695 [Multi-domain]  Cd Length: 362  Bit Score: 342.55  E-value: 1.79e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMH 80
Cdd:cd00622   115 LLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  81 VLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengs 159
Cdd:cd00622   195 LLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW----- 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 160 tsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGA 238
Cdd:cd00622   269 ------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGA 342

                         250
                  ....*....|....*....
gi 1179685350 239 YTVGMGSPFWGTQACHITY 257
Cdd:cd00622   343 YTTAYASTFNGFPPPKIVY 361
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 1-257 1.79e-117

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: 342.55  E-value: 1.79e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMH 80
Cdd:cd00622   115 LLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  81 VLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengs 159
Cdd:cd00622   195 LLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW----- 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 160 tsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGA 238
Cdd:cd00622   269 ------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGA 342

                         250
                  ....*....|....*....
gi 1179685350 239 YTVGMGSPFWGTQACHITY 257
Cdd:cd00622   343 YTTAYASTFNGFPPPKIVY 361
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 16-237 3.31e-67

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: 213.50  E-value: 3.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  16 LSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EG 93
Cdd:pfam00278 135 LSSKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  94 AKVRFEEIASVINSALDLYFPEgcGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVY 173
Cdd:pfam00278 215 PPPDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMN 278

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179685350 174 GIFNSVLFDNICPTPIlqKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 237
Cdd:pfam00278 279 DLFRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 19-247 1.00e-28

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: 114.09  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGA 94
Cdd:COG0019   169 KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  95 KVRFEEIASVINSALDLYFpeGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYg 174
Cdd:COG0019   249 PPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN- 311

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1179685350 175 ifnsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 247
Cdd:COG0019   312 -------DLMRPAlygayhPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
19-245 5.90e-08

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 53.93  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD--ARLVFEMGTelghkMHVLDLGGGFPGTEGAKV 96
Cdd:PRK08961  641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADelASFARRFPD-----VRTIDLGGGLGIPESAGD 714

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  97 R---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsiiAKKEVLLDQPGREEENGStsktiVYH--LDEG 171
Cdd:PRK08961  715 EpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV-----------AEAGVLLARVTQVKEKDG-----VRRvgLETG 774

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179685350 172 VYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 245
Cdd:PRK08961  775 MNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSS 846
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 1-257 1.79e-117

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: 342.55  E-value: 1.79e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMH 80
Cdd:cd00622   115 LLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  81 VLDLGGGFPGTE-GAKVRFEEIASVINSALDLYFPEGcGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREeengs 159
Cdd:cd00622   195 LLDIGGGFPGSYdGVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERW----- 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 160 tsktivYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQ-LHVGDWLVFDNMGA 238
Cdd:cd00622   269 ------YYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGA 342

                         250
                  ....*....|....*....
gi 1179685350 239 YTVGMGSPFWGTQACHITY 257
Cdd:cd00622   343 YTTAYASTFNGFPPPKIVY 361
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 1-264 1.67e-85

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: 262.09  E-value: 1.67e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMH 80
Cdd:cd06831   126 LLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  81 VLDLGGGFPGTEgakVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQ-PGREEENGS 159
Cdd:cd06831   206 MLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKhLSSVEKNGS 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 160 TSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAY 239
Cdd:cd06831   283 DEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAG 362

                         250       260
                  ....*....|....*....|....*
gi 1179685350 240 TVGMGSPFWGTQACHITYAMSRVAW 264
Cdd:cd06831   363 SLHEPSTFNDFQRPAIYYMMSFSDW 387
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 16-237 3.31e-67

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: 213.50  E-value: 3.31e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  16 LSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT--EG 93
Cdd:pfam00278 135 LSSKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  94 AKVRFEEIASVINSALDLYFPEgcGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVYhLDEGVY 173
Cdd:pfam00278 215 PPPDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKT-------------GGGKTFVI-VDAGMN 278

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179685350 174 GIFNSVLFDNICPTPIlqKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMG 237
Cdd:pfam00278 279 DLFRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 19-251 1.79e-61

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: 199.45  E-value: 1.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT-EGAKVR 97
Cdd:cd06810   142 KFGLSLSEARAALERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPyDEQPLD 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  98 FEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLldqpgreeengstsKTIVYHLDEGVYGIFN 177
Cdd:cd06810   222 FEEYAALINPLLKKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNG--------------GRFFAVVDGGMNHSFR 287

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179685350 178 SVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQ 251
Cdd:cd06810   288 PALAYDAYHPITPLKAPGPDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHP 361
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 1-130 2.64e-46

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: 156.29  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDSHSLSCLSLKFGVSL-KSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKM 79
Cdd:pfam02784 107 VLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNL 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1179685350  80 HVLDLGGGFpGTE----GAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYV 130
Cdd:pfam02784 187 KILDLGGGF-GVDytegEEPLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYFV 240
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 19-247 1.00e-28

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: 114.09  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGT---EGA 94
Cdd:COG0019   169 KFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPyteGDE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  95 KVRFEEIASVINSALDLYFpeGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVlldqpgreeengsTSKTIVYhLDEGVYg 174
Cdd:COG0019   249 PPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKEN-------------GGRRFVI-VDAGMN- 311

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1179685350 175 ifnsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPF 247
Cdd:COG0019   312 -------DLMRPAlygayhPIVPVGRPSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNY 383
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 19-245 1.87e-18

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: 84.46  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKK-HHVEVVGVSFHIGSGCPDPQAYAQSiadARLVFEMGTEL---GHKMHVLDLGGGF--PGTE 92
Cdd:cd06828   146 KFGIPLEQALEAYRRAKElPGLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgiPYRD 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  93 GAK-VRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIVyHLDEG 171
Cdd:cd06828   223 EDEpLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKE-------------TGGKTFV-GVDAG 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 172 vygiFNsvlfDNICPT------PILQKKPSTEQPLYSSSLWGPAvdgC---DCVAEGLWLPQLHVGDWLVFDNMGAYTVG 242
Cdd:cd06828   289 ----MN----DLIRPAlygayhEIVPVNKPGEGETEKVDVVGPI---CesgDVFAKDRELPEVEEGDLLAIHDAGAYGYS 357


                  ...
gi 1179685350 243 MGS 245
Cdd:cd06828   358 MSS 360
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 19-247 3.15e-18

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: 83.85  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKH----HVEVVGVSFHIGSGCPDPQAYAQSIADarLVFEMGTELGHKMHVLDLGGGFPG---- 90
Cdd:cd06841   142 RFGFDIEENGEALAALKKIqeskNLSLVGLHCHVGSNILNPEAYSAAAKK--LIELLDRLFGLELEYLDLGGGFPAktpl 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  91 -----TEGAKVRFEEIASVINSALDLYFPEGCG-VDIFAELGRYYVTSAFTVAVSIIAKKEVlldqPGREeengstskti 164
Cdd:cd06841   220 slaypQEDTVPDPEDYAEAIASTLKEYYANKENkPKLILEPGRALVDDAGYLLGRVVAVKNR----YGRN---------- 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 165 VYHLDEGvygIFNSVLFDNICPtPILQKKPSTEQPLYSSS-LWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGM 243
Cdd:cd06841   286 IAVTDAG---INNIPTIFWYHH-PILVLRPGKEDPTSKNYdVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQ 361


                  ....
gi 1179685350 244 GSPF 247
Cdd:cd06841   362 SNQF 365
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-92 3.02e-15

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: 73.12  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350   1 MVLCIATDDshslscLSLKFGVSLKSCRHLLENAKKH-HVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKM 79
Cdd:cd06808   109 VLLRIDTGD------ENGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDL 182

                          90
                  ....*....|...
gi 1179685350  80 HVLDLGGGFPGTE 92
Cdd:cd06808   183 EQLSIGGSFAILY 195
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 37-239 2.16e-10

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: 60.69  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  37 HHVEVVGvsFHI--GSGCPDPQAYAQSIADA-RLVFEMGTELGHKMHVLDLGGGF--P-GTEGAKVRFEEIASVINSALD 110
Cdd:cd06839   167 PNLRFVG--LHIypGTQILDADALIEAFRQTlALALRLAEELGLPLEFLDLGGGFgiPyFPGETPLDLEALGAALAALLA 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 111 LYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEvlldqpgreeengSTSKTIV-------YHLdeGVYGIFNSVLFDN 183
Cdd:cd06839   245 ELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV-------------SRGETFLvtdggmhHHL--AASGNFGQVLRRN 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1179685350 184 IcPTPILQKkpSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAY 239
Cdd:cd06839   310 Y-PLAILNR--MGGEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAY 362
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
19-245 5.90e-08

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 53.93  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQsIAD--ARLVFEMGTelghkMHVLDLGGGFPGTEGAKV 96
Cdd:PRK08961  641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRR-MADelASFARRFPD-----VRTIDLGGGLGIPESAGD 714

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  97 R---FEEIASVINSALDLYfPegcGVDIFAELGRYYVtsaftvavsiiAKKEVLLDQPGREEENGStsktiVYH--LDEG 171
Cdd:PRK08961  715 EpfdLDALDAGLAEVKAQH-P---GYQLWIEPGRYLV-----------AEAGVLLARVTQVKEKDG-----VRRvgLETG 774

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179685350 172 VYGIFNSVLFD---NICPTPILqkkpsTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 245
Cdd:PRK08961  775 MNSLIRPALYGayhEIVNLSRL-----DEPAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSS 846
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 19-245 1.25e-07

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: 52.44  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  19 KFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIAD-ARLVFEMGTelghkMHVLDLGGGFPGTEGAKVR 97
Cdd:cd06840   150 KFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYlASLARHFPA-----VRILNVGGGLGIPEAPGGR 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  98 FEEIASVINS--ALDLYFPegcGVDIFAELGRYyvtsaftvavsIIAKKEVLLdqpGREEENGSTSKTIVYHLDEGVYGI 175
Cdd:cd06840   225 PIDLDALDAAlaAAKAAHP---QYQLWMEPGRF-----------IVAESGVLL---ARVTQIKHKDGVRFVGLETGMNSL 287

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350 176 FNSVLFDniCPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGS 245
Cdd:cd06840   288 IRPALYG--AYHEIVNLSRLDEPPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMAS 355
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 19-89 1.12e-06

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: 49.57  E-value: 1.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1179685350  19 KFGVSLKSCRHLLENAKKH--HVEVVGVSFHIGSGCPDPQAYAqsIADARLVFEMGTELGHKMHVLDLGGGFP 89
Cdd:cd06842   145 RFGMPAAEVRTALERLAQLreRVRLVGFHFHLDGYSAAQRVAA--LQECLPLIDRARALGLAPRFIDIGGGFP 215
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
20-121 2.84e-05

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 44.62  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179685350  20 FGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFE 99
Cdd:COG1082    35 GDLDEADLAELRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWD 114

                          90       100
                  ....*....|....*....|..
gi 1179685350 100 EIASVINSALDLYfpEGCGVDI 121
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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