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Conserved domains on  [gi|1386806211|ref|NP_001349943|]
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antizyme inhibitor 1 isoform 4 [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 ...
 1-252 1.24e-176

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 cd06831:

Pssm-ID: 469695  Cd Length: 394  Bit Score: 492.44  E-value: 1.24e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEE 80
Cdd:cd06831   143 MKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  81 VNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASK 160
Cdd:cd06831   223 VNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASK 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 161 LSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMM 240
Cdd:cd06831   303 LSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMM 382

                         250
                  ....*....|..
gi 1386806211 241 SFSDWYEMQDAG 252
Cdd:cd06831   383 SFSDWYEMQDAG 394
 
Name Accession Description Interval E-value
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 1-252 1.24e-176

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: 492.44  E-value: 1.24e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEE 80
Cdd:cd06831   143 MKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  81 VNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASK 160
Cdd:cd06831   223 VNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASK 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 161 LSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMM 240
Cdd:cd06831   303 LSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMM 382

                         250
                  ....*....|..
gi 1386806211 241 SFSDWYEMQDAG 252
Cdd:cd06831   383 SFSDWYEMQDAG 394
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-218 3.97e-69

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: 217.35  E-value: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF-----TGTE 75
Cdd:pfam00278 137 SKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPP 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  76 FQLEEVNHVISPLLDIYFPEgsGVKIISEPGSYYVSSAFTLAVNIIAKKVVENdkfpsgvektgsdepAFMYYMNDGVYG 155
Cdd:pfam00278 217 PDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMND 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386806211 156 SFASKLSEDLNTIPEVhkKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMG 218
Cdd:pfam00278 280 LFRPALYDAYHPIPVV--KEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 2-237 5.56e-21

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: 91.75  E-value: 5.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF------TGT 74
Cdd:COG0019   169 KFGIPLEDALEAYRRAAALPgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  75 EFQLEEVNHVISPLLDIYFpeGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFpsgvektgsdepafmYY----MN 150
Cdd:COG0019   249 PPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRF---------------VIvdagMN 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 151 DGV----YGSFasklsedlNTIPEVHKkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPS 226
Cdd:COG0019   312 DLMrpalYGAY--------HPIVPVGR--PSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMAS 381

                         250
                  ....*....|.
gi 1386806211 227 AFNDFQRPAIY 237
Cdd:COG0019   382 NYNGRPRPAEV 392
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
2-234 1.94e-05

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 45.84  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQvyvHALSDARCVFDMAGEIGfTMNMLDIGGGFT------GTE 75
Cdd:PRK08961  641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEP 716

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  76 FQLEEVNHVISPLLDIYfpegSGVKIISEPGSYYVSSAFTLavniIAK--KVVENDKFP-SGVEkTGsdepafmyyMND- 151
Cdd:PRK08961  717 FDLDALDAGLAEVKAQH----PGYQLWIEPGRYLVAEAGVL----LARvtQVKEKDGVRrVGLE-TG---------MNSl 778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 152 ---GVYGSF-----ASKLSEdlntipevhkkykedEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFH 223
Cdd:PRK08961  779 irpALYGAYheivnLSRLDE---------------PAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYS 843

                         250
                  ....*....|.
gi 1386806211 224 EPSAFNdfQRP 234
Cdd:PRK08961  844 MSSTYN--LRE 852
 
Name Accession Description Interval E-value
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 1-252 1.24e-176

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: 492.44  E-value: 1.24e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEE 80
Cdd:cd06831   143 MKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  81 VNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASK 160
Cdd:cd06831   223 VNHVIRPLLDVYFPEGSGIQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASK 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 161 LSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMM 240
Cdd:cd06831   303 LSEKLNTTPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMM 382

                         250
                  ....*....|..
gi 1386806211 241 SFSDWYEMQDAG 252
Cdd:cd06831   383 SFSDWYEMQDAG 394
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 1-239 9.69e-107

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: 314.05  E-value: 9.69e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQ--- 77
Cdd:cd00622   132 RKFGADPEEARELLRRAKELGLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvvp 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  78 -LEEVNHVISPLLDIYFPEGsGVKIISEPGSYYVSSAFTLAVNIIAKKVVendkfpsgvektGSDEPAFMYYMNDGVYGS 156
Cdd:cd00622   212 sFEEIAAVINRALDEYFPDE-GVRIIAEPGRYLVASAFTLAVNVIAKRKR------------GDDDRERWYYLNDGVYGS 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 157 FASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPE-LNVGDWLIFDNMGADSFHEPSAFNDFQRPA 235
Cdd:cd00622   279 FNEILFDHIRYPPRVLKDGGRDGELYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPK 358


                  ....
gi 1386806211 236 IYYM 239
Cdd:cd00622   359 IVYV 362
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 1-239 7.83e-86

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: 261.08  E-value: 7.83e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGT----EF 76
Cdd:cd06810   141 SKFGLSLSEARAALERAKELDLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPydeqPL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  77 QLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENdkfpsgvektgsdepAFMYYMNDGVYGS 156
Cdd:cd06810   221 DFEEYAALINPLLKKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGG---------------RFFAVVDGGMNHS 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 157 FASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAI 236
Cdd:cd06810   286 FRPALAYDAYHPITPLKAPGPDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAE 365


                  ...
gi 1386806211 237 YYM 239
Cdd:cd06810   366 YLV 368
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 1-218 3.97e-69

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: 217.35  E-value: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF-----TGTE 75
Cdd:pfam00278 137 SKFGIDLEDAPELLALAKELGLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPP 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  76 FQLEEVNHVISPLLDIYFPEgsGVKIISEPGSYYVSSAFTLAVNIIAKKVVENdkfpsgvektgsdepAFMYYMNDGVYG 155
Cdd:pfam00278 217 PDFEEYAAAIREALDEYFPP--DLEIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMND 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386806211 156 SFASKLSEDLNTIPEVhkKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMG 218
Cdd:pfam00278 280 LFRPALYDAYHPIPVV--KEPGEGPLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 1-111 6.69e-47

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: 157.06  E-value: 6.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTL-KNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFtGTEFQ-- 77
Cdd:pfam02784 124 SKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGF-GVDYTeg 202

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1386806211  78 -----LEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVS 111
Cdd:pfam02784 203 eepldFEEYANVINEALEEYFPGDPGVTIIAEPGRYFVA 241
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 2-237 5.56e-21

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: 91.75  E-value: 5.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGF------TGT 74
Cdd:COG0019   169 KFGIPLEDALEAYRRAAALPgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  75 EFQLEEVNHVISPLLDIYFpeGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFpsgvektgsdepafmYY----MN 150
Cdd:COG0019   249 PPDLEELAAAIKEALEELC--GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRF---------------VIvdagMN 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 151 DGV----YGSFasklsedlNTIPEVHKkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPS 226
Cdd:COG0019   312 DLMrpalYGAY--------HPIVPVGR--PSGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMAS 381

                         250
                  ....*....|.
gi 1386806211 227 AFNDFQRPAIY 237
Cdd:COG0019   382 NYNGRPRPAEV 392
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-106 6.08e-20

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: 85.45  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   1 MKFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLe 79
Cdd:cd06808   120 GKFGVRPEELKALLERAKELPhLRLVGLHTHFGSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQE- 198

                          90       100
                  ....*....|....*....|....*..
gi 1386806211  80 evnhvisplldiyfpEGSGVKIISEPG 106
Cdd:cd06808   199 ---------------LPLGTFIIVEPG 210
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 2-237 4.08e-13

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: 68.44  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKEL----DVQIIGVKFHVSSACKESQVYVHALSDarcVFDMAGEI-GFTMNMLDIGGGFTG--- 73
Cdd:cd06841   142 RFGFDIEENGEALAALKKIqeskNLSLVGLHCHVGSNILNPEAYSAAAKK---LIELLDRLfGLELEYLDLGGGFPAktp 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  74 ---------TEFQLEE-VNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKvvendkfpsgvektgsdep 143
Cdd:cd06841   219 lslaypqedTVPDPEDyAEAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVK------------------- 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 144 afmyymndGVYGSFASKLSEDLNTIPEVH---------KKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIF 214
Cdd:cd06841   280 --------NRYGRNIAVTDAGINNIPTIFwyhhpilvlRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAI 351

                         250       260
                  ....*....|....*....|....*
gi 1386806211 215 DNMGADSFhepSAFNDF--QRPAIY 237
Cdd:cd06841   352 RNVGAYNM---TQSNQFirPRPAVY 373
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 2-235 1.64e-11

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: 63.66  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKELD-VQIIGVKFHVSSACKESQVYVHAlsdARCVFDMAGEI---GFTMNMLDIGGGF------ 71
Cdd:cd06828   146 KFGIPLEQALEAYRRAKELPgLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgipyrd 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  72 TGTEFQLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFpSGVEkTGsdepafmyyMND 151
Cdd:cd06828   223 EDEPLDIEEYAEAIAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTF-VGVD-AG---------MND 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 152 ----GVYGSF-----ASKlsedlntipevhkkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSF 222
Cdd:cd06828   292 lirpALYGAYheivpVNK---------------PGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGY 356

                         250
                  ....*....|...
gi 1386806211 223 HEPSAFNDFQRPA 235
Cdd:cd06828   357 SMSSNYNSRPRPA 369
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 53-219 3.42e-09

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: 56.83  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  53 DMAGEIGFTMNMLDIGGGF------TGTEFQLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVV 126
Cdd:cd06839   201 RLAEELGLPLEFLDLGGGFgipyfpGETPLDLEALGAALAALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKVS 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 127 ENDKF---PSGvektgsdepafmyyMND--GVYGSFASKLSEDLntiPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESC 201
Cdd:cd06839   281 RGETFlvtDGG--------------MHHhlAASGNFGQVLRRNY---PLAILNRMGGEERETVTVVGPLCTPLDLLGRNV 343

                         170
                  ....*....|....*...
gi 1386806211 202 LLPELNVGDWLIFDNMGA 219
Cdd:cd06839   344 ELPPLEPGDLVAVLQSGA 361
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 2-71 1.51e-05

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: 45.72  E-value: 1.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806211   2 KFGTTLKNCRHLLE-CAKELD-VQIIGVKFHVSSACKESQVyvHALSDARCVFDMAGEIGFTMNMLDIGGGF 71
Cdd:cd06842   145 RFGMPAAEVRTALErLAQLRErVRLVGFHFHLDGYSAAQRV--AALQECLPLIDRARALGLAPRFIDIGGGF 214
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
2-234 1.94e-05

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 45.84  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211   2 KFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQvyvHALSDARCVFDMAGEIGfTMNMLDIGGGFT------GTE 75
Cdd:PRK08961  641 KFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGIETGE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEP 716

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211  76 FQLEEVNHVISPLLDIYfpegSGVKIISEPGSYYVSSAFTLavniIAK--KVVENDKFP-SGVEkTGsdepafmyyMND- 151
Cdd:PRK08961  717 FDLDALDAGLAEVKAQH----PGYQLWIEPGRYLVAEAGVL----LARvtQVKEKDGVRrVGLE-TG---------MNSl 778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806211 152 ---GVYGSF-----ASKLSEdlntipevhkkykedEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFH 223
Cdd:PRK08961  779 irpALYGAYheivnLSRLDE---------------PAAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYS 843

                         250
                  ....*....|.
gi 1386806211 224 EPSAFNdfQRP 234
Cdd:PRK08961  844 MSSTYN--LRE 852
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 172-237 2.01e-03

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: 39.30  E-value: 2.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386806211 172 HKKYKEDePLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIY 237
Cdd:cd06836   311 NGEPKTG-PEVVTDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
 
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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