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Conserved domains on  [gi|563580285|ref|NP_001274117|]
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ornithine decarboxylase isoform 2 [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 ...
 1-279 2.00e-161

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: 455.03  E-value: 2.00e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFV 80
Cdd:cd00622   94 LFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  81 QAISDARCVFDMGAEVGFSMYLLDIGGGFPGSED-VKLKFEEITGVINPALDKYFPSDsGVRIIAEPGRYYVASAFTLAV 159
Cdd:cd00622  174 DAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAV 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 160 NIIAKKIVLKEQtgsddedesseQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVE 239
Cdd:cd00622  253 NVIAKRKRGDDD-----------RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYE 321

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 563580285 240 RCDLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 279
Cdd:cd00622  322 DVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 1-279 2.00e-161

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: 455.03  E-value: 2.00e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFV 80
Cdd:cd00622   94 LFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  81 QAISDARCVFDMGAEVGFSMYLLDIGGGFPGSED-VKLKFEEITGVINPALDKYFPSDsGVRIIAEPGRYYVASAFTLAV 159
Cdd:cd00622  174 DAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAV 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 160 NIIAKKIVLKEQtgsddedesseQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVE 239
Cdd:cd00622  253 NVIAKRKRGDDD-----------RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYE 321

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 563580285 240 RCDLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 279
Cdd:cd00622  322 DVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-258 2.42e-103

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: 306.72  E-value: 2.42e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285    1 MMTFDSEVELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGC 73
Cdd:pfam00278  92 CFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   74 TDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGS--EDVKLKFEEITGVINPALDKYFPSDsgVRIIAEPGRYYV 151
Cdd:pfam00278 172 TDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--LEIIAEPGRYLV 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  152 ASAFTLAVNIIAKKIvlkeqtgsddedesSEQTFMYYVNDGVYGSFNCILYDHAHVKPLlqKRPKPDEKYYSSSIWGPTC 231
Cdd:pfam00278 250 ANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTC 313

                         250       260
                  ....*....|....*....|....*..
gi 563580285  232 DGLDRIVERCDLPEMHVGDWMLFENMG 258
Cdd:pfam00278 314 ESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 3-295 1.37e-43

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: 154.54  E-value: 1.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   3 TFDSEVELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLRTSRLLLERAKEL-NIDVVGVSFHVGS 71
Cdd:COG0019  122 NVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAALpGLRLVGLHFHIGS 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  72 GCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALDKYFpsDSGVRIIAEPGR 148
Cdd:COG0019  202 QILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEELC--GLGPELILEPGR 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 149 YYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFmYYVNdgvyGSFNC----ILYD--HaHVKPLlqkRPKPDEKYY 222
Cdd:COG0019  280 ALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGayH-PIVPV---GRPSGAEAE 337

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 563580285 223 SSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPaWQLMQQFQNPD 295
Cdd:COG0019  338 TYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE-ARLIRRRETYE 409
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
40-274 3.91e-17

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 82.44  E-value: 3.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  40 KFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAisdARCVFDMGAEVGfSMYLLDIGGGFP---GSEDVK 116
Cdd:PRK08961 641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEP 716

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 117 LKFEeitgVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqtfMYYVndGVYGS 196
Cdd:PRK08961 717 FDLD----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETG 774

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 197 FNCI----LYDHAHVKPLLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgfQ 272
Cdd:PRK08961 775 MNSLirpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--L 850


                 ..
gi 563580285 273 RP 274
Cdd:PRK08961 851 RE 852
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 1-279 2.00e-161

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: 455.03  E-value: 2.00e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFV 80
Cdd:cd00622   94 LFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  81 QAISDARCVFDMGAEVGFSMYLLDIGGGFPGSED-VKLKFEEITGVINPALDKYFPSDsGVRIIAEPGRYYVASAFTLAV 159
Cdd:cd00622  174 DAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDgVVPSFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAV 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 160 NIIAKKIVLKEQtgsddedesseQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVE 239
Cdd:cd00622  253 NVIAKRKRGDDD-----------RERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYE 321

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 563580285 240 RCDLPE-MHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 279
Cdd:cd00622  322 DVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 1-290 9.29e-120

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: 350.30  E-value: 9.29e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFV 80
Cdd:cd06831  105 IMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  81 QAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEdvkLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVN 160
Cdd:cd06831  185 HALSDARCVFDMAEEFGFKMNMLDIGGGFTGSE---IQLEEVNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVN 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 161 IIAKKIVLKEQ-TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVE 239
Cdd:cd06831  262 VIAKKAVENDKhLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVE 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 563580285 240 RCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQ 290
Cdd:cd06831  342 SCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQD 392
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 1-279 3.44e-105

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.


Pssm-ID: 143485 [Multi-domain]  Cd Length: 368  Bit Score: 312.32  E-value: 3.44e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAH----PKAKLVLRIATDDSK-----AVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGS 71
Cdd:cd06810   94 HIVVDSLDELERLNELAkklgPKARILLRVNPDVSAgthkiSTGGLKSKFGLSLSEARAALERAKELDLRLVGLHFHVGS 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  72 GCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVK-LKFEEITGVINPALDKYFPSDSGVRIIAEPGRYY 150
Cdd:cd06810  174 QILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQpLDFEEYAALINPLLKKYFPNDPGVTLILEPGRYI 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 151 VASAFTLAVNIIAKKIVLKeqtgsddedesseqTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPT 230
Cdd:cd06810  254 VAQAGVLVTRVVAVKVNGG--------------RFFAVVDGGMNHSFRPALAYDAYHPITPLKAPGPDEPLVPATLAGPL 319

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 563580285 231 CDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 279
Cdd:cd06810  320 CDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-258 2.42e-103

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: 306.72  E-value: 2.42e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285    1 MMTFDSEVELMKVARAHP--KAKLVLRIATD-DSK----AVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGC 73
Cdd:pfam00278  92 CFNVDSEDELEKIAKLAPelVARVALRINPDvDAGthkiSTGGLSSKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   74 TDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGS--EDVKLKFEEITGVINPALDKYFPSDsgVRIIAEPGRYYV 151
Cdd:pfam00278 172 TDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPyrDEPPPDFEEYAAAIREALDEYFPPD--LEIIAEPGRYLV 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  152 ASAFTLAVNIIAKKIvlkeqtgsddedesSEQTFMYYVNDGVYGSFNCILYDHAHVKPLlqKRPKPDEKYYSSSIWGPTC 231
Cdd:pfam00278 250 ANAGVLVTRVIAVKT--------------GGGKTFVIVDAGMNDLFRPALYDAYHPIPV--VKEPGEGPLETYDVVGPTC 313

                         250       260
                  ....*....|....*....|....*..
gi 563580285  232 DGLDRIVERCDLPEMHVGDWMLFENMG 258
Cdd:pfam00278 314 ESGDVLAKDRELPELEVGDLLAFEDAG 340
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 1-152 6.19e-75

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: 230.63  E-value: 6.19e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285    1 MMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTS-RLLLERAKELNIDVVGVSFHVGSGCTDPETF 79
Cdd:pfam02784  86 CVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDvEALLEAAKLLNLQVVGVSFHVGSGCTDAEAF 165

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 563580285   80 VQAISDARCVFDMGAEVGFSMYLLDIGGGFpGSEDV----KLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVA 152
Cdd:pfam02784 166 VLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTegeePLDFEEYANVINEALEEYFPGDPGVTIIAEPGRYFVA 241
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 3-295 1.37e-43

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: 154.54  E-value: 1.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   3 TFDSEVELMKVARAHP----KAKLVLRIATD-DSK-----AVCRLSVKFGATLRTSRLLLERAKEL-NIDVVGVSFHVGS 71
Cdd:COG0019  122 NVDSLSELERLAELAAelgkRAPVGLRVNPGvDAGtheyiSTGGKDSKFGIPLEDALEAYRRAAALpGLRLVGLHFHIGS 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  72 GCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALDKYFpsDSGVRIIAEPGR 148
Cdd:COG0019  202 QILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGipyTEGDEPPDLEELAAAIKEALEELC--GLGPELILEPGR 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 149 YYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFmYYVNdgvyGSFNC----ILYD--HaHVKPLlqkRPKPDEKYY 222
Cdd:COG0019  280 ALVGNAGVLLTRVLDVK-------------ENGGRRF-VIVD----AGMNDlmrpALYGayH-PIVPV---GRPSGAEAE 337

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 563580285 223 SSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPaWQLMQQFQNPD 295
Cdd:COG0019  338 TYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGE-ARLIRRRETYE 409
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 1-274 1.86e-29

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: 115.66  E-value: 1.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAHP----KAKLVLRIATD-DSKAVCRLSV-----KFGATLRTSRLLLERAKEL-NIDVVGVSFHV 69
Cdd:cd06828   97 RINVDSLSELERLGEIAPelgkGAPVALRVNPGvDAGTHPYISTggkdsKFGIPLEQALEAYRRAKELpGLKLVGLHCHI 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  70 GSGCTDPETFVQAisdARCVFDMGAEV---GFSMYLLDIGGGFP---GSEDVKLKFEEITGVINPALDKYFPSDSGVRII 143
Cdd:cd06828  177 GSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLGipyRDEDEPLDIEEYAEAIAEALKELCEGGPDLKLI 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 144 AEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedESSEQTFMyyvndGVYGSFNCI----LYD--HaHVKPLLQKRPKP 217
Cdd:cd06828  254 IEPGRYIVANAGVLLTRVGYVK-------------ETGGKTFV-----GVDAGMNDLirpaLYGayH-EIVPVNKPGEGE 314

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 563580285 218 DEKYyssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRP 274
Cdd:cd06828  315 TEKV---DVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRP 368
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-148 4.03e-29

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: 111.26  E-value: 4.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   1 MMTFDSEVELMKVARAH----PKAKLVLRIATDDskavcrLSVKFGATLRTSRLLLERAKELN-IDVVGVSFHVGSGCTD 75
Cdd:cd06808   84 VVTVDSLEELEKLEEAAlkagPPARVLLRIDTGD------ENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSADED 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 563580285  76 PETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLkfeeitgvinpaldkyfpsDSGVRIIAEPGR 148
Cdd:cd06808  158 YSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQEL-------------------PLGTFIIVEPGR 211
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
40-274 3.91e-17

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 82.44  E-value: 3.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  40 KFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAisdARCVFDMGAEVGfSMYLLDIGGGFP---GSEDVK 116
Cdd:PRK08961 641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRM---ADELASFARRFP-DVRTIDLGGGLGipeSAGDEP 716

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 117 LKFEeitgVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqtfMYYVndGVYGS 196
Cdd:PRK08961 717 FDLD----ALDAGLAEVKAQHPGYQLWIEPGRYLVAEAGVL----LARVTQVKEKDG------------VRRV--GLETG 774

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 197 FNCI----LYDHAHVKPLLQKRPKPdeKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgfQ 272
Cdd:PRK08961 775 MNSLirpaLYGAYHEIVNLSRLDEP--AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYN--L 850


                 ..
gi 563580285 273 RP 274
Cdd:PRK08961 851 RE 852
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 5-264 4.39e-17

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: 81.10  E-value: 4.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   5 DSEVELMKVARAHPK----AKLVLRIATDDSKAVCRLSV-----KFGATLRT-SRLLLERAKELNIDVVGVSFHVGSGCT 74
Cdd:cd06839  104 ESLEELERIDALAEEhgvvARVALRINPDFELKGSGMKMgggpsQFGIDVEElPAVLARIAALPNLRFVGLHIYPGTQIL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  75 DPETFVQAISDARCVF-DMGAEVGFSMYLLDIGGGF-----PGSEDvkLKFEEITGVINPALDKYFPSDSGVRIIAEPGR 148
Cdd:cd06839  184 DADALIEAFRQTLALAlRLAEELGLPLEFLDLGGGFgipyfPGETP--LDLEALGAALAALLAELGDRLPGTRVVLELGR 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 149 YYVASAFTLAVNIIAKKIvlkeqtgSDDEDesseqtfmYYVNDG-------VYGSFNCILYDHAHVKPLLQKRPKPDEKY 221
Cdd:cd06839  262 YLVGEAGVYVTRVLDRKV-------SRGET--------FLVTDGgmhhhlaASGNFGQVLRRNYPLAILNRMGGEERETV 326

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 563580285 222 yssSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAA 264
Cdd:cd06839  327 ---TVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLSA 366
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 9-277 8.61e-17

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: 80.38  E-value: 8.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   9 ELMKVARAHP-KAKLVLRIATDDSKAVcrLSvKFGATLRTSRLLLERAKEL----NIDVVGVSFHVGSGCTDPETFVQAI 83
Cdd:cd06841  113 RILEIAKELGrVAKVGIRLNMNYGNNV--WS-RFGFDIEENGEALAALKKIqeskNLSLVGLHCHVGSNILNPEAYSAAA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  84 SDarCVFDMGAEVGFSMYLLDIGGGFPGseDVKLKFEEITGVINPALDKYFPSDSGV------------RIIAEPGRYYV 151
Cdd:cd06841  190 KK--LIELLDRLFGLELEYLDLGGGFPA--KTPLSLAYPQEDTVPDPEDYAEAIASTlkeyyankenkpKLILEPGRALV 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 152 ASAFTLAVNIIAKKIVlkeqtgsddEDESSEQTfmyyvnDGVYGSFNCILYDHAHVKPLlqkRPKPDEKYYSSS-IWGPT 230
Cdd:cd06841  266 DDAGYLLGRVVAVKNR---------YGRNIAVT------DAGINNIPTIFWYHHPILVL---RPGKEDPTSKNYdVYGFN 327

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 563580285 231 CDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNgFQRPTIY 277
Cdd:cd06841  328 CMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFI-RPRPAVY 373
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 40-269 7.84e-11

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


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 62.45  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  40 KFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISD-ARCVFDMGAevgfsMYLLDIGGGFP---GSEDV 115
Cdd:cd06840  150 KFGLDVDELDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYlASLARHFPA-----VRILNVGGGLGipeAPGGR 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 116 KLKFEEITGVINpALDKYFPsdsGVRIIAEPGRYYVASAFTLavniIAKKIVLKEQTGsddedesseqTFMYYVNDGVYG 195
Cdd:cd06840  225 PIDLDALDAALA-AAKAAHP---QYQLWMEPGRFIVAESGVL----LARVTQIKHKDG----------VRFVGLETGMNS 286

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 563580285 196 SFNCILYDHAH-VKPLLQKRPkpdEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFN 269
Cdd:cd06840  287 LIRPALYGAYHeIVNLSRLDE---PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYN 358
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 5-110 1.33e-10

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: 61.89  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   5 DSEVELMKV-----ARAHPKAKLVLRIATDDSKAVCRlsvkFGATLRTSRLLLERAKELN--IDVVGVSFHVGSgcTDPE 77
Cdd:cd06842  109 DSLDELDRLlalarGYTTGPARVLLRLSPFPASLPSR----FGMPAAEVRTALERLAQLRerVRLVGFHFHLDG--YSAA 182

                         90       100       110
                 ....*....|....*....|....*....|...
gi 563580285  78 TFVQAISDARCVFDMGAEVGFSMYLLDIGGGFP 110
Cdd:cd06842  183 QRVAALQECLPLIDRARALGLAPRFIDIGGGFP 215
PLN02537 PLN02537
diaminopimelate decarboxylase
 5-279 6.66e-10

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 59.81  E-value: 6.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285   5 DSEVELMKVARAH----PKAKLVLRIATD-DSK-----AVCRLSVKFGatLRTSRL--LLE--RAKELNIDVVGVSFHVG 70
Cdd:PLN02537 115 DSEFDLENIVEAAriagKKVNVLLRINPDvDPQvhpyvATGNKNSKFG--IRNEKLqwFLDavKAHPNELKLVGAHCHLG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  71 SGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGfpgsedVKLKFEEiTGVINPAldkyfPSD-----------SG 139
Cdd:PLN02537 193 STITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGG------LGIDYYH-AGAVLPT-----PRDlidtvrelvlsRD 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 140 VRIIAEPGRYYVASAFTLAVNIIAKKivlkeqtgsddedesSEQTFMYYVNDGVYGSF-NCILYD-HAHVKplLQKRPKP 217
Cdd:PLN02537 261 LTLIIEPGRSLIANTCCFVNRVTGVK---------------TNGTKNFIVIDGSMAELiRPSLYDaYQHIE--LVSPPPP 323

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 563580285 218 DEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYV 279
Cdd:PLN02537 324 DAEVSTFDVVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWV 385
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
 215-277 1.26e-05

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which 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. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.


Pssm-ID: 143502 [Multi-domain]  Cd Length: 346  Bit Score: 46.39  E-value: 1.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 563580285 215 PKPDEKYYSSSIWGPTCDGLDRIVE-RCDLPeMHVGDWMLFENMGAYTVAAASTFNGFQRPTIY 277
Cdd:cd06829  281 GEPGEGAHTYRLGGNSCLAGDVIGDySFDEP-LQVGDRLVFEDMAHYTMVKTNTFNGVRLPSIA 343
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 64-277 1.89e-05

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: 45.85  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  64 GVSFHVGS-GCTDPetfvQAISDARCVFDMGAEVGFSMYL-----LDIGGGFP---GSEDVKLKFEEITGVINPALDKYF 134
Cdd:cd06836  170 GLHVHVGSqGCELS----LLAEGIRRVVDLAEEINRRVGRrqitrIDIGGGLPvnfESEDITPTFADYAAALKAAVPELF 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285 135 psDSGVRIIAEPGRYYVASA-FTLAVNIIAKKIVLKE----QTGSDDEDESSEQTFMYYVNDGVYGSfncilydHAHVKp 209
Cdd:cd06836  246 --DGRYQLVTEFGRSLLAKCgTIVSRVEYTKSSGGRRiaitHAGAQVATRTAYAPDDWPLRVTVFDA-------NGEPK- 315

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 563580285 210 llQKRPKPdekyysSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIY 277
Cdd:cd06836  316 --TGPEVV------TDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
51-146 2.34e-04

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 41.92  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563580285  51 LLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPAL 130
Cdd:COG1082   45 LRAALADHGLEISSLHAPGLNLAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELA 124

                         90
                 ....*....|....*.
gi 563580285 131 DKYfpSDSGVRIIAEP 146
Cdd:COG1082  125 ELA--EEAGVTLALEN 138
 
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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