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Conserved domains on  [gi|677283307|ref|NP_072107|]
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antizyme inhibitor 1 [Rattus norvegicus]

Protein Classification

PLPDE_III_ODC_like_AZI domain-containing protein( domain architecture ID 10160127)

PLPDE_III_ODC_like_AZI domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 26-419 0e+00

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: 770.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  26 DNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 105
Cdd:cd06831    1 DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 106 ENIIYTSPCKQASQIKYAAKVGVNIMTCDNEVELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAK 185
Cdd:cd06831   81 ENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELDVQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSG 265
Cdd:cd06831  161 ELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 266 IQIISEPGSYYVSSAFTLAVNIIAKKVVENDKLSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTVPEVHKKYKED 345
Cdd:cd06831  241 IQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKED 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677283307 346 EPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFMMSLSDWYEMQDAG 419
Cdd:cd06831  321 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG 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 ...
 26-419 0e+00

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: 770.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  26 DNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 105
Cdd:cd06831    1 DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 106 ENIIYTSPCKQASQIKYAAKVGVNIMTCDNEVELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAK 185
Cdd:cd06831   81 ENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELDVQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSG 265
Cdd:cd06831  161 ELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 266 IQIISEPGSYYVSSAFTLAVNIIAKKVVENDKLSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTVPEVHKKYKED 345
Cdd:cd06831  241 IQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKED 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677283307 346 EPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFMMSLSDWYEMQDAG 419
Cdd:cd06831  321 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG 394
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 40-385 5.95e-123

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: 361.03  E-value: 5.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307   40 FFVGDLGKIVKKHSQWQNVVA-QIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQAS 118
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALPpRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  119 QIKYAAKVGVNIMTCDNEVELKKIARNHPN--AKVLLHIATEDNIGGEDGNM-----KFGTTLKNCRHLLECAKELDVQI 191
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  192 IGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF-----TGTEIQLEEVNHVISPLLDIYFPEgsGI 266
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  267 QIISEPGSYYVSSAFTLAVNIIAKKVVENdklssgvekngsdepAFVYYMNDGVYGSFASKLSEDLNTVPEVhkKYKEDE 346
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMNDLFRPALYDAYHPIPVV--KEPGEG 301

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 677283307  347 PLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMG 385
Cdd:pfam00278 302 PLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 40-386 6.00e-46

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: 164.17  E-value: 6.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQA 117
Cdd:COG0019   28 LYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 118 SQIKYAAKVGVNIMTCDNEVELKKIAR----NHPNAKVLL------HIATEDNI--GGEDGnmKFGTTLKNCRHLLECAK 185
Cdd:COG0019  108 EELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLrvnpgvDAGTHEYIstGGKDS--KFGIPLEDALEAYRRAA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELD-VQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF------TGTEIQLEEVNHVISPLLDI 258
Cdd:COG0019  186 ALPgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDEPPDLEELAAAIKEALEE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 259 YFpeGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKlssgvekngsdepaFVYY---MNDGV----YGSF--ASKLS 329
Cdd:COG0019  266 LC--GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRR--------------FVIVdagMNDLMrpalYGAYhpIVPVG 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 677283307 330 EDlntvpevhkkykEDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:COG0019  330 RP------------SGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGA 374
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
59-386 6.23e-16

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 80.51  E-value: 6.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  59 VAQIKP----FYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQEL--GVSPENIIYTSPCKQASQIKYAAKVGVNImT 132
Cdd:PRK08961 520 LAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-T 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 133 CDNEVELKKIARNHPNAKVLLHIatedNIGGEDGN----------MKFGTTLKNCRHLLECAKELDVQIIGVKFHISSAC 202
Cdd:PRK08961 599 LDNVEPLRNWPELFRGREVWLRI----DPGHGDGHhekvrtggkeSKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGI 674

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 203 KEYQvyvHALSDARCVFDMAGEFGfTMNMLDIGGGFT------GTEIQLEEVNHVISPLLDIYfpegSGIQIISEPGSYY 276
Cdd:PRK08961 675 ETGE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEPFDLDALDAGLAEVKAQH----PGYQLWIEPGRYL 746

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 277 VSSAFTLavniIAK--KVVENDKLS-SGVEK--NGSDEPAfvyymndgVYGSF-----ASKLSEdlntvpevhkkykedE 346
Cdd:PRK08961 747 VAEAGVL----LARvtQVKEKDGVRrVGLETgmNSLIRPA--------LYGAYheivnLSRLDE---------------P 799

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 677283307 347 PLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:PRK08961 800 AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGA 839
 
Name Accession Description Interval E-value
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 26-419 0e+00

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: 770.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  26 DNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 105
Cdd:cd06831    1 DNYIYEHTLTGKNAFFVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 106 ENIIYTSPCKQASQIKYAAKVGVNIMTCDNEVELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAK 185
Cdd:cd06831   81 ENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELDVQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSG 265
Cdd:cd06831  161 ELDVQIVGVKFHVSSSCKEYQTYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 266 IQIISEPGSYYVSSAFTLAVNIIAKKVVENDKLSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTVPEVHKKYKED 345
Cdd:cd06831  241 IQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKLNTTPEVHKKYKED 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 677283307 346 EPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFMMSLSDWYEMQDAG 419
Cdd:cd06831  321 EPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPAIYYMMSFSDWYEMQDAG 394
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 37-406 1.60e-174

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: 492.78  E-value: 1.60e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  37 KNAFFVGDLGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQ 116
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 117 ASQIKYAAKVGVNIMTCDNEVELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAKELDVQIIGVKF 196
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 197 HISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQ----LEEVNHVISPLLDIYFPEGsGIQIISEP 272
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGvvpsFEEIAAVINRALDEYFPDE-GVRIIAEP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 273 GSYYVSSAFTLAVNIIAKKVVendklssgveknGSDEPAFVYYMNDGVYGSFASKLSEDLNTVPEVHKKYKEDEPLFTSS 352
Cdd:cd00622  240 GRYLVASAFTLAVNVIAKRKR------------GDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGGRDGELYPSS 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 677283307 353 LWGPSCDELDQIVESCLLPE-LSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFM 406
Cdd:cd00622  308 LWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYASTFNGFPPPKIVYV 362
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 38-406 7.34e-133

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: 387.43  E-value: 7.34e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  38 NAFFVGDLGKIVKKHSQWQNV-VAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQ 116
Cdd:cd06810    1 TPFYVYDLDIIRAHYAALKEAlPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 117 ASQIKYAAKVGVNIMTCDNEVELKKIARNH----PNAKVLLHIATEDNIG-----GEDGNMKFGTTLKNCRHLLECAKEL 187
Cdd:cd06810   81 VSEIEAALASGVDHIVVDSLDELERLNELAkklgPKARILLRVNPDVSAGthkisTGGLKSKFGLSLSEARAALERAKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 188 DVQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGT----EIQLEEVNHVISPLLDIYFPEG 263
Cdd:cd06810  161 DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPydeqPLDFEEYAALINPLLKKYFPND 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 264 SGIQIISEPGSYYVSSAFTLAVNIIAKKVVENdklssgvekngsdepAFVYYMNDGVYGSFASKLSEDLNTVPEVHKKYK 343
Cdd:cd06810  241 PGVTLILEPGRYIVAQAGVLVTRVVAVKVNGG---------------RFFAVVDGGMNHSFRPALAYDAYHPITPLKAPG 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 677283307 344 EDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFM 406
Cdd:cd06810  306 PDEPLVPATLAGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 40-385 5.95e-123

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: 361.03  E-value: 5.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307   40 FFVGDLGKIVKKHSQWQNVVA-QIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQAS 118
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALPpRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  119 QIKYAAKVGVNIMTCDNEVELKKIARNHPN--AKVLLHIATEDNIGGEDGNM-----KFGTTLKNCRHLLECAKELDVQI 191
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGTHKISTgglssKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  192 IGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF-----TGTEIQLEEVNHVISPLLDIYFPEgsGI 266
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFgipyrDEPPPDFEEYAAAIREALDEYFPP--DL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  267 QIISEPGSYYVSSAFTLAVNIIAKKVVENdklssgvekngsdepAFVYYMNDGVYGSFASKLSEDLNTVPEVhkKYKEDE 346
Cdd:pfam00278 239 EIIAEPGRYLVANAGVLVTRVIAVKTGGG---------------KTFVIVDAGMNDLFRPALYDAYHPIPVV--KEPGEG 301

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 677283307  347 PLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMG 385
Cdd:pfam00278 302 PLETYDVVGPTCESGDVLAKDRELPELEVGDLLAFEDAG 340
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 45-278 1.96e-112

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: 330.40  E-value: 1.96e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307   45 LGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQASQIKYAA 124
Cdd:pfam02784   1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  125 KVGVNIMTCDNEVELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTL-KNCRHLLECAKELDVQIIGVKFHISSACK 203
Cdd:pfam02784  81 EVGVGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLdEDVEALLEAAKLLNLQVVGVSFHVGSGCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  204 EYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF----TGTEIQL--EEVNHVISPLLDIYFPEGSGIQIISEPGSYYV 277
Cdd:pfam02784 161 DAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFgvdyTEGEEPLdfEEYANVINEALEEYFPGDPGVTIIAEPGRYFV 240


                  .
gi 677283307  278 S 278
Cdd:pfam02784 241 A 241
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 48-252 8.25e-64

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: 204.86  E-value: 8.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  48 IVKKHSQWQNVV-AQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQASQIKYAAKV 126
Cdd:cd06808    1 IRHNYRRLREAApAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 127 GVNIMTCDNEVELKKIARNH----PNAKVLLHIATedniggEDGNMKFGTTLKNCRHLLECAKELD-VQIIGVKFHISSA 201
Cdd:cd06808   81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDT------GDENGKFGVRPEELKALLERAKELPhLRLVGLHTHFGSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 677283307 202 CKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVI 252
Cdd:cd06808  155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFI 205
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 40-386 6.00e-46

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: 164.17  E-value: 6.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQA 117
Cdd:COG0019   28 LYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKSE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 118 SQIKYAAKVGVNIMTCDNEVELKKIAR----NHPNAKVLL------HIATEDNI--GGEDGnmKFGTTLKNCRHLLECAK 185
Cdd:COG0019  108 EELEEALELGVGHINVDSLSELERLAElaaeLGKRAPVGLrvnpgvDAGTHEYIstGGKDS--KFGIPLEDALEAYRRAA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELD-VQIIGVKFHISSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGF------TGTEIQLEEVNHVISPLLDI 258
Cdd:COG0019  186 ALPgLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLgipyteGDEPPDLEELAAAIKEALEE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 259 YFpeGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKlssgvekngsdepaFVYY---MNDGV----YGSF--ASKLS 329
Cdd:COG0019  266 LC--GLGPELILEPGRALVGNAGVLLTRVLDVKENGGRR--------------FVIVdagMNDLMrpalYGAYhpIVPVG 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 677283307 330 EDlntvpevhkkykEDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:COG0019  330 RP------------SGAEAETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGA 374
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 40-386 3.17e-33

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: 128.76  E-value: 3.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  40 FFVGDLGKIVKKHSQWQNVVAQI--KPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQA 117
Cdd:cd06828    5 LYVYDEATIRENYRRLKEAFSGPgfKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGNGKSD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 118 SQIKYAAKVGVNIMTCDNEVELKKIARNHPN----AKVLL------------HIATedniGGEDGnmKFGTTLKNCRHLL 181
Cdd:cd06828   85 EELELALELGILRINVDSLSELERLGEIAPElgkgAPVALrvnpgvdagthpYIST----GGKDS--KFGIPLEQALEAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 182 ECAKELD-VQIIGVKFHISSACKEYQVYVHAlsdARCVFDMAGEF---GFTMNMLDIGGGF------TGTEIQLEEVNHV 251
Cdd:cd06828  159 RRAKELPgLKLVGLHCHIGSQILDLEPFVEA---AEKLLDLAAELrelGIDLEFLDLGGGLgipyrdEDEPLDIEEYAEA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 252 ISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKvvendklSSGVEK----NGSdepafvyyMND----GVYGS 323
Cdd:cd06828  236 IAEALKELCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVK-------ETGGKTfvgvDAG--------MNDlirpALYGA 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 677283307 324 F-----ASKlsedlntvpevhkkyKEDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:cd06828  301 YheivpVNK---------------PGEGETEKVDVVGPICESGDVFAKDRELPEVEEGDLLAIHDAGA 353
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 38-404 7.36e-28

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: 113.90  E-value: 7.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  38 NAFFVGDLGKIVKKH--------SQWQNVVAQikpfYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENII 109
Cdd:cd06841    7 SPFFVFDEDALRENYrellgafkKRYPNVVIA----YSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRII 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 110 YTSPCKQASQIKYAAKVGVNImTCDNEVELKK---IARNHpNAKVLLHIATEDNIGGeDGNMKFGTTLKNCRHLLECAKE 186
Cdd:cd06841   83 FNGPYKSKEELEKALEEGALI-NIDSFDELERileIAKEL-GRVAKVGIRLNMNYGN-NVWSRFGFDIEENGEALAALKK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 187 L----DVQIIGVKFHISSACKEYQVYVHALSDarcVFDMAGE-FGFTMNMLDIGGGFTG-TEIQLEE------------V 248
Cdd:cd06841  160 IqeskNLSLVGLHCHVGSNILNPEAYSAAAKK---LIELLDRlFGLELEYLDLGGGFPAkTPLSLAYpqedtvpdpedyA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 249 NHVISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKvvendklssgvekNGSDEPAFVyyMNDGVygsfaskl 328
Cdd:cd06841  237 EAIASTLKEYYANKENKPKLILEPGRALVDDAGYLLGRVVAVK-------------NRYGRNIAV--TDAGI-------- 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 329 sedlNTVPEVH---------KKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSdTQ 399
Cdd:cd06841  294 ----NNIPTIFwyhhpilvlRPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAYNMTQSNQFI-RP 368


                 ....*
gi 677283307 400 RPAIY 404
Cdd:cd06841  369 RPAVY 373
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 40-394 1.18e-25

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: 107.68  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  40 FFVGDLGKIVKKHSQWQNVVAQ-IKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQAS 118
Cdd:cd06839    9 FYVYDRDRVRERYAALRAALPPaIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFAGPGKSDA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 119 QIKYAAKVGVNIMTCDNEVELKKIAR-----NHPnAKVLLHIATEDNIGGEDGNM-----KFG---TTLKNCRHLLECAK 185
Cdd:cd06839   89 ELRRAIEAGIGTINVESLEELERIDAlaeehGVV-ARVALRINPDFELKGSGMKMgggpsQFGidvEELPAVLARIAALP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 186 ELDvqIIGvkFHI--------SSACKEYQVYVHALsdarcVFDMAGEFGFTMNMLDIGGGF------TGTEIQLEEVNHV 251
Cdd:cd06839  168 NLR--FVG--LHIypgtqildADALIEAFRQTLAL-----ALRLAEELGLPLEFLDLGGGFgipyfpGETPLDLEALGAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 252 ISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKVvendklSSGVekngsdepafVYYMNDG-------VYGSF 324
Cdd:cd06839  239 LAALLAELGDRLPGTRVVLELGRYLVGEAGVYVTRVLDRKV------SRGE----------TFLVTDGgmhhhlaASGNF 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 325 ASKLSEDLNTVPevHKKYKeDEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGAdslHGPSA 394
Cdd:cd06839  303 GQVLRRNYPLAI--LNRMG-GEERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGA---YGLSA 366
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
59-386 6.23e-16

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 80.51  E-value: 6.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  59 VAQIKP----FYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQEL--GVSPENIIYTSPCKQASQIKYAAKVGVNImT 132
Cdd:PRK08961 520 LAALAAvdqrFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVTV-T 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 133 CDNEVELKKIARNHPNAKVLLHIatedNIGGEDGN----------MKFGTTLKNCRHLLECAKELDVQIIGVKFHISSAC 202
Cdd:PRK08961 599 LDNVEPLRNWPELFRGREVWLRI----DPGHGDGHhekvrtggkeSKFGLSQTRIDEFVDLAKTLGITVVGLHAHLGSGI 674

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 203 KEYQvyvHALSDARCVFDMAGEFGfTMNMLDIGGGFT------GTEIQLEEVNHVISPLLDIYfpegSGIQIISEPGSYY 276
Cdd:PRK08961 675 ETGE---HWRRMADELASFARRFP-DVRTIDLGGGLGipesagDEPFDLDALDAGLAEVKAQH----PGYQLWIEPGRYL 746

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 277 VSSAFTLavniIAK--KVVENDKLS-SGVEK--NGSDEPAfvyymndgVYGSF-----ASKLSEdlntvpevhkkykedE 346
Cdd:PRK08961 747 VAEAGVL----LARvtQVKEKDGVRrVGLETgmNSLIRPA--------LYGAYheivnLSRLDE---------------P 799

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 677283307 347 PLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:PRK08961 800 AAGTADVVGPICESSDVLGKRRRLPATAEGDVILIANAGA 839
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 41-386 1.33e-15

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


Pssm-ID: 143507 [Multi-domain]  Cd Length: 368  Bit Score: 77.86  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  41 FVGDLGKIVKKHSQWQNVVAQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQEL--GVSPENIIYTSPCKQAS 118
Cdd:cd06840   15 YVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNFAARS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 119 QIKYAAKVGVNImTCDNEVELkkiaRNHP----NAKVLLHIatedNIGGEDGN----------MKFGTTLKNCRHLLECA 184
Cdd:cd06840   95 EYEQALELGVNV-TVDNLHPL----REWPelfrGREVILRI----DPGQGEGHhkhvrtggpeSKFGLDVDELDEARDLA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 185 KELDVQIIGVKFHISSACKE---YQVYVHALSDArcvfdmAGEFGfTMNMLDIGGG------FTGTEIQLEEVNHVISPL 255
Cdd:cd06840  166 KKAGIIVIGLHAHSGSGVEDtdhWARHGDYLASL------ARHFP-AVRILNVGGGlgipeaPGGRPIDLDALDAALAAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 256 LDIYfpegSGIQIISEPGSYYVSSAFTLavniIAKkvVENDKLSSGVEKNGSDEPafvyyMND----GVYGSF-----AS 326
Cdd:cd06840  239 KAAH----PQYQLWMEPGRFIVAESGVL----LAR--VTQIKHKDGVRFVGLETG-----MNSlirpALYGAYheivnLS 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 327 KLSEdlntvpevhkkykedEPLFTSSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGA 386
Cdd:cd06840  304 RLDE---------------PPAGNADVVGPICESGDVLGRDRLLPETEEGDVILIANAGA 348
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 63-238 4.22e-14

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: 73.83  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  63 KPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQASQIKYAAKVGVNImTCDNEVELKKI 142
Cdd:cd06842   39 RVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGPAKTDEFLWLAVRHGATI-AVDSLDELDRL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 143 -----ARNHPNAKVLLHIATEDNiggeDGNMKFGTTLKNCRHLLE-CAKELD-VQIIGVKFHISSACKEYQvyVHALSDA 215
Cdd:cd06842  118 lalarGYTTGPARVLLRLSPFPA----SLPSRFGMPAAEVRTALErLAQLRErVRLVGFHFHLDGYSAAQR--VAALQEC 191

                        170       180
                 ....*....|....*....|...
gi 677283307 216 RCVFDMAGEFGFTMNMLDIGGGF 238
Cdd:cd06842  192 LPLIDRARALGLAPRFIDIGGGF 214
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 68-404 8.30e-14

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: 72.43  E-value: 8.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  68 VKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQASQIKYAAKVGVNImTCDNEVELKKI---AR 144
Cdd:cd06836   34 VKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGVAI-NIDNFQELERIdalVA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 145 NHPNAKVLLHIATEDNIGGED-GNM-------KFGTTLKncrhllECAKEldvQIIGV--------KFHISSACKEYQVY 208
Cdd:cd06836  113 EFKEASSRIGLRVNPQVGAGKiGALstatatsKFGVALE------DGARD---EIIDAfarrpwlnGLHVHVGSQGCELS 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 209 vHALSDARCVFDMAGEFGFTM-----NMLDIGGG----FTGTEIQ---LEEVNHVIS--PLLdiyFPEGSgiQIISEPGS 274
Cdd:cd06836  184 -LLAEGIRRVVDLAEEINRRVgrrqiTRIDIGGGlpvnFESEDITptfADYAAALKAavPEL---FDGRY--QLVTEFGR 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 275 YYVSSAFTLAvniiakkvvendklsSGVE--KNGSDEPAFVYYMNDGVY--GSFASKLSEDLNTVPEVHKKYKEDePLFT 350
Cdd:cd06836  258 SLLAKCGTIV---------------SRVEytKSSGGRRIAITHAGAQVAtrTAYAPDDWPLRVTVFDANGEPKTG-PEVV 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 677283307 351 SSLWGPSCDELDQIVESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIY 404
Cdd:cd06836  322 TDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPAVY 375
PLN02537 PLN02537
diaminopimelate decarboxylase
 64-406 7.48e-12

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 66.74  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  64 PFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTSPCKQASQIKYAAKVGVNImTCDNEVELKKIA 143
Cdd:PLN02537  46 IGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQEGVFV-NVDSEFDLENIV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 144 RNHPNA----KVLLHIATEDN------IGGEDGNMKFGTTLKNCRHLLECAKE--LDVQIIGVKFHISSACKEYQVYVHA 211
Cdd:PLN02537 125 EAARIAgkkvNVLLRINPDVDpqvhpyVATGNKNSKFGIRNEKLQWFLDAVKAhpNELKLVGAHCHLGSTITKVDIFRDA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 212 LSDARCVFDMAGEFGFTMNMLDIGGG----FTGTEIQLEEVNHVISPLLDIYFPEgsGIQIISEPGSYYVSSAFTLAVNI 287
Cdd:PLN02537 205 AVLMVNYVDEIRAQGFELSYLNIGGGlgidYYHAGAVLPTPRDLIDTVRELVLSR--DLTLIIEPGRSLIANTCCFVNRV 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 288 iakkvvendklsSGVEKNGSDEpaFVYymndgVYGSFASKLSEDLNTV---PEVHKKYKEDEPLFTSSLWGPSCDELDQI 364
Cdd:PLN02537 283 ------------TGVKTNGTKN--FIV-----IDGSMAELIRPSLYDAyqhIELVSPPPPDAEVSTFDVVGPVCESADFL 343

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 677283307 365 VESCLLPELSVGDWLIFDNMGADSLHGPSAFSDTQRPAIYFM 406
Cdd:PLN02537 344 GKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWV 385
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 60-238 1.85e-08

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.


Pssm-ID: 143510 [Multi-domain]  Cd Length: 377  Bit Score: 56.14  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  60 AQIKPFYMVKCNSTPAVLEILAALGTGFACSSKNEMALVQELgvSPEN-IIYTSPCKQASQIKYAAKVGVNIMTCDNEVE 138
Cdd:cd06843   25 PGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA--VPDApLIFGGPGKTDSELAQALAQGVERIHVESELE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 139 LKKIARNHPNAKVLLHIATEDNIGGEDG-----NM-----KFGTTLKNCRHLLECAKELD-VQIIGVKFHISS----ACK 203
Cdd:cd06843  103 LRRLNAVARRAGRTAPVLLRVNLALPDLpsstlTMggqptPFGIDEADLPDALELLRDLPnIRLRGFHFHLMShnldAAA 182

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 677283307 204 EYQVYVHALSDARcvfDMAGEFGFTMNMLDIGGGF 238
Cdd:cd06843  183 HLALVKAYLETAR---QWAAEHGLDLDVVNVGGGI 214
PLPDE_III_ADC cd06830
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ...
 63-291 1.58e-04

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC 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. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.


Pssm-ID: 143503 [Multi-domain]  Cd Length: 409  Bit Score: 43.71  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307  63 KPFYMVKCNSTPAVLEILAALGT----GFACSSKNEMALVQELGVSPENIIYTSPCKQASQIK---YAAKVGVNIM-TCD 134
Cdd:cd06830   40 QGVYPIKVNQQREVVEEIVKAGKryniGLEAGSKPELLAALALLKTPDALIICNGYKDDEYIElalLARKLGHNVIiVIE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 135 NEVELK---KIARNHpNAKVLLHI----ATE-----DNIGGEDGnmKFGTTLKNC---------RHLLECAKELdvqiig 193
Cdd:cd06830  120 KLSELDlilELAKKL-GVKPLLGVriklASKgsgkwQESGGDRS--KFGLTASEIlevveklkeAGMLDRLKLL------ 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677283307 194 vKFHISSACKEYQVYVHALSDARCVF-DMAGEfGFTMNMLDIGGGF----TGTEIQ--------LEE-VNHVISPLLDIY 259
Cdd:cd06830  191 -HFHIGSQITDIRRIKSALREAARIYaELRKL-GANLRYLDIGGGLgvdyDGSRSSsdssfnysLEEyANDIVKTVKEIC 268

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 677283307 260 fpEGSGI---QIISEPGSYYVSSAFTLAVNIIAKK 291
Cdd:cd06830  269 --DEAGVphpTIVTESGRAIVAHHSVLIFEVLGVK 301
 
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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