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Conserved domains on  [gi|559158804|gb|AHB01286|]
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ornithine decarboxylase [Brucella ceti TE10759-12]

Protein Classification

type III PLP-dependent enzyme( domain architecture ID 10089786)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme similar to Selenomonas ruminantium lysine/ornithine decarboxylase, and human ornithine decarboxylase and antizyme inhibitor 2

CATH:  3.20.20.10
EC:  4.1.1.-
Gene Ontology:  GO:0003824
PubMed:  15189147|8690703
SCOP:  4003520

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 16-377 0e+00

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: 511.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  16 EGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKK 95
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  96 ERDIARAFDLGIRLYAVDCVEEVEKIARVAPGSRVFCRVLTDGEGAEWPLSRKFGCVPAMAKDVLRRAKALGLDAYGVSF 175
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 176 HVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYGMAIFDALSRHFGNRIPETIIEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDEGVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 256 RGMVGNAGVIKTEVVLVSRKADNDNVRWVYLDIGKFGGLAETMDEAIRYQIVTPHDG---SETEPCVLAGPTCDSADVLY 332
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGgrdGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 559158804 333 EktPYPLPVSLTIGDEILIEGTGAYTTTYSAVaFNGFEPLRSYVI 377
Cdd:cd00622  321 E--DVLLPEDLAVGDWLLFENMGAYTTAYAST-FNGFPPPKIVYV 362
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 16-377 0e+00

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: 511.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  16 EGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKK 95
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  96 ERDIARAFDLGIRLYAVDCVEEVEKIARVAPGSRVFCRVLTDGEGAEWPLSRKFGCVPAMAKDVLRRAKALGLDAYGVSF 175
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 176 HVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYGMAIFDALSRHFGNRIPETIIEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDEGVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 256 RGMVGNAGVIKTEVVLVSRKADNDNVRWVYLDIGKFGGLAETMDEAIRYQIVTPHDG---SETEPCVLAGPTCDSADVLY 332
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGgrdGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 559158804 333 EktPYPLPVSLTIGDEILIEGTGAYTTTYSAVaFNGFEPLRSYVI 377
Cdd:cd00622  321 E--DVLLPEDLAVGDWLLFENMGAYTTAYAST-FNGFPPPKIVYV 362
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 19-355 2.35e-109

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: 323.67  E-value: 2.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   19 CLVVDTDVVRENYQGFEKAL-PYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKER 97
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   98 DIARAFDLGIRLYAVDCVEEVEKIARVAPG--SRVFCRVLTDGEGAE-----WPLSRKFGCVPAMAKDVLRRAKALGLDA 170
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGThkistGGLSSKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  171 YGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDV-PTAQAYGMAIFDALSRHFGNRIpE 249
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPpPDFEEYAAAIREALDEYFPPDL-E 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  250 TIIEPGRGMVGNAGVIKTEVVLVSrkaDNDNVRWVYLDIGKFGGLAETMDEAIRYQIVTPHDGS-ETEPCVLAGPTCDSA 328
Cdd:pfam00278 240 IIAEPGRYLVANAGVLVTRVIAVK---TGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEgPLETYDVVGPTCESG 316

                         330       340
                  ....*....|....*....|....*..
gi 559158804  329 DVLYEKtpYPLPVsLTIGDEILIEGTG 355
Cdd:pfam00278 317 DVLAKD--RELPE-LEVGDLLAFEDAG 340
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 18-369 2.98e-83

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: 259.70  E-value: 2.98e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQGFEKALPYS--RIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKK 95
Cdd:COG0019   27 PLYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  96 ERDIARAFDLGIRLYAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAE------WPLSRKFGCVPAMAKDVLRRAKA 165
Cdd:COG0019  107 EEELEEALELGVGHINVDSLSELERLAELAAELgkraPVGLRVNPGVDAGTheyistGGKDSKFGIPLEDALEAYRRAAA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 166 L-GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKD--VPTAQAYGMAIFDALSRH 242
Cdd:COG0019  187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGdePPDLEELAAAIKEALEEL 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 243 FGNRiPETIIEPGRGMVGNAGVIKTEVvlVSRKaDNDNVRWVYLDigkfGGLAETMDEAI---RYQI--VTPHDGSETEP 317
Cdd:COG0019  267 CGLG-PELILEPGRALVGNAGVLLTRV--LDVK-ENGGRRFVIVD----AGMNDLMRPALygaYHPIvpVGRPSGAEAET 338

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 559158804 318 CVLAGPTCDSADVLYEktPYPLPvSLTIGDEILIEGTGAYTTTYSAvAFNGF 369
Cdd:COG0019  339 YDVVGPLCESGDVLGK--DRSLP-PLEPGDLLAFLDAGAYGFSMAS-NYNGR 386
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 18-357 8.77e-58

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 193.66  E-value: 8.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   18 PCLVVDTDVVRENYQGFEKALP-YSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKE 96
Cdd:TIGR01048  26 PLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   97 RDIARAFDLGIRLyAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAEWP------LSRKFGCVPAMAKDVLRRAKAL 166
Cdd:TIGR01048 106 AELERALELGICI-NVDSFSELERLNEIAPELgkkaRISLRVNPGVDAKTHPyistglKDSKFGIDVEEALEAYLYALQL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  167 -GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLAdEGIILRMVNMGGGFPTRYLK--DVPTAQAYGMAIFDALSRHF 243
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA-EGIDLEFLDLGGGLGIPYTPeeEPPDLSEYAQAILNALEGYA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  244 G-NRIPETIIEPGRGMVGNAGVIKTEVVLVSRkadNDNVRWVYLDIGkfgglaetMDEAIR---YQ------IVTPHDGS 313
Cdd:TIGR01048 264 DlGLDPKLILEPGRSIVANAGVLLTRVGFVKE---TGSRNFVIVDAG--------MNDLIRpalYGayhhiiVLNRTNDA 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 559158804  314 ETEPCVLAGPTCDSADVLYEKTPYPlpvSLTIGDEILIEGTGAY 357
Cdd:TIGR01048 333 PTEVADVVGPVCESGDVLAKDRELP---EVEPGDLLAVFDAGAY 373
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
10-377 1.19e-36

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 141.37  E-value: 1.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  10 LNTRRPEGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEA--GATPDRI 87
Cdd:PRK08961 496 LTLSDAGSPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  88 SYGNTIKKERDIARAFDLGIRLyAVDCVEEVEKIARVAPGSRVFCRV-LTDGEGAEWPLS-----RKFGCVPAMAKDVLR 161
Cdd:PRK08961 576 LFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNWPELFRGREVWLRIdPGHGDGHHEKVRtggkeSKFGLSQTRIDEFVD 654

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 162 RAKALGLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADegiiLRMVNMGGGFPTRYLKDVP--TAQAYGMAIFDAL 239
Cdd:PRK08961 655 LAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPD----VRTIDLGGGLGIPESAGDEpfDLDALDAGLAEVK 730

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 240 SRHFGNRIpetIIEPGRGMVGNAGVIKTEVVLVSRKadnDNVRWVYLDIGkfgglaetMDEAIR-------YQIV--TPH 310
Cdd:PRK08961 731 AQHPGYQL---WIEPGRYLVAEAGVLLARVTQVKEK---DGVRRVGLETG--------MNSLIRpalygayHEIVnlSRL 796

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158804 311 DGSETEPCVLAGPTCDSADVL-YEKtpyPLPVSLTiGDEILIEGTGAYTTTYSAvAFNGFEPLRSYVI 377
Cdd:PRK08961 797 DEPAAGTADVVGPICESSDVLgKRR---RLPATAE-GDVILIANAGAYGYSMSS-TYNLREPAREVVL 859
 
Name Accession Description Interval E-value
PLPDE_III_ODC cd00622
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ...
 16-377 0e+00

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: 511.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  16 EGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKK 95
Cdd:cd00622    1 ETPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPCKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  96 ERDIARAFDLGIRLYAVDCVEEVEKIARVAPGSRVFCRVLTDGEGAEWPLSRKFGCVPAMAKDVLRRAKALGLDAYGVSF 175
Cdd:cd00622   81 ISDIRYAAELGVRLFTFDSEDELEKIAKHAPGAKLLLRIATDDSGALCPLSRKFGADPEEARELLRRAKELGLNVVGVSF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 176 HVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYGMAIFDALSRHFGNRIPETIIEPG 255
Cdd:cd00622  161 HVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFEEIAAVINRALDEYFPDEGVRIIAEPG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 256 RGMVGNAGVIKTEVVLVSRKADNDNVRWVYLDIGKFGGLAETMDEAIRYQIVTPHDG---SETEPCVLAGPTCDSADVLY 332
Cdd:cd00622  241 RYLVASAFTLAVNVIAKRKRGDDDRERWYYLNDGVYGSFNEILFDHIRYPPRVLKDGgrdGELYPSSLWGPTCDSLDVIY 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 559158804 333 EktPYPLPVSLTIGDEILIEGTGAYTTTYSAVaFNGFEPLRSYVI 377
Cdd:cd00622  321 E--DVLLPEDLAVGDWLLFENMGAYTTAYAST-FNGFPPPKIVYV 362
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
 19-355 2.35e-109

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: 323.67  E-value: 2.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   19 CLVVDTDVVRENYQGFEKAL-PYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKER 97
Cdd:pfam00278   1 FYVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   98 DIARAFDLGIRLYAVDCVEEVEKIARVAPG--SRVFCRVLTDGEGAE-----WPLSRKFGCVPAMAKDVLRRAKALGLDA 170
Cdd:pfam00278  81 EIRYALEAGVLCFNVDSEDELEKIAKLAPElvARVALRINPDVDAGThkistGGLSSKFGIDLEDAPELLALAKELGLNV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  171 YGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDV-PTAQAYGMAIFDALSRHFGNRIpE 249
Cdd:pfam00278 161 VGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPpPDFEEYAAAIREALDEYFPPDL-E 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  250 TIIEPGRGMVGNAGVIKTEVVLVSrkaDNDNVRWVYLDIGKFGGLAETMDEAIRYQIVTPHDGS-ETEPCVLAGPTCDSA 328
Cdd:pfam00278 240 IIAEPGRYLVANAGVLVTRVIAVK---TGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEgPLETYDVVGPTCESG 316

                         330       340
                  ....*....|....*....|....*..
gi 559158804  329 DVLYEKtpYPLPVsLTIGDEILIEGTG 355
Cdd:pfam00278 317 DVLAKD--RELPE-LEVGDLLAFEDAG 340
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
 18-377 2.79e-83

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: 258.00  E-value: 2.79e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQGFEKALPY-SRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKE 96
Cdd:cd06810    2 PFYVYDLDIIRAHYAALKEALPSgVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKSV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  97 RDIARAFDLGIRLYAVDCVEEVEKIARVAPGS----RVFCRV-LTDGEGAEWP----LSRKFGCVPAMAKDVLRRAKALG 167
Cdd:cd06810   82 SEIEAALASGVDHIVVDSLDELERLNELAKKLgpkaRILLRVnPDVSAGTHKIstggLKSKFGLSLSEARAALERAKELD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 168 LDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYGMAIFDALSRHFGNRI 247
Cdd:cd06810  162 LRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDFEEYAALINPLLKKYFPNDP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 248 PETII-EPGRGMVGNAGVIKTEVVLVSrkaDNDNVRWVYLDIGKFGGLAETMDEAIRYQIVT---PHDGSETEPCVLAGP 323
Cdd:cd06810  242 GVTLIlEPGRYIVAQAGVLVTRVVAVK---VNGGRFFAVVDGGMNHSFRPALAYDAYHPITPlkaPGPDEPLVPATLAGP 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 559158804 324 TCDSADVLyekTPYPLPVSLTIGDEILIEGTGAYTTTYSaVAFNGFEPLRSYVI 377
Cdd:cd06810  319 LCDSGDVI---GRDRLLPELEVGDLLVFEDMGAYGFSES-SNFNSHPRPAEYLV 368
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 18-369 2.98e-83

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: 259.70  E-value: 2.98e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQGFEKALPYS--RIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKK 95
Cdd:COG0019   27 PLYVYDEAALRRNLRALREAFPGSgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPERIVFSGNGKS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  96 ERDIARAFDLGIRLYAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAE------WPLSRKFGCVPAMAKDVLRRAKA 165
Cdd:COG0019  107 EEELEEALELGVGHINVDSLSELERLAELAAELgkraPVGLRVNPGVDAGTheyistGGKDSKFGIPLEDALEAYRRAAA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 166 L-GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKD--VPTAQAYGMAIFDALSRH 242
Cdd:COG0019  187 LpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTEGdePPDLEELAAAIKEALEEL 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 243 FGNRiPETIIEPGRGMVGNAGVIKTEVvlVSRKaDNDNVRWVYLDigkfGGLAETMDEAI---RYQI--VTPHDGSETEP 317
Cdd:COG0019  267 CGLG-PELILEPGRALVGNAGVLLTRV--LDVK-ENGGRRFVIVD----AGMNDLMRPALygaYHPIvpVGRPSGAEAET 338

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 559158804 318 CVLAGPTCDSADVLYEktPYPLPvSLTIGDEILIEGTGAYTTTYSAvAFNGF 369
Cdd:COG0019  339 YDVVGPLCESGDVLGK--DRSLP-PLEPGDLLAFLDAGAYGFSMAS-NYNGR 386
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 18-357 2.65e-69

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: 221.97  E-value: 2.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQGFEKALPY--SRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISY-GNtIK 94
Cdd:cd06828    4 PLYVYDEATIRENYRRLKEAFSGpgFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFtGN-GK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  95 KERDIARAFDLGIRLYAVDCVEEVEKIARVAP----GSRVFCRV------------LTDGEGAewplsrKFGCVPAMAKD 158
Cdd:cd06828   83 SDEELELALELGILRINVDSLSELERLGEIAPelgkGAPVALRVnpgvdagthpyiSTGGKDS------KFGIPLEQALE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 159 VLRRAKAL-GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKD--VPTAQAYGMAI 235
Cdd:cd06828  157 AYRRAKELpGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEdePLDIEEYAEAI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 236 FDALSRHF-GNRIPETIIEPGRGMVGNAGVIKTEVVLVSRkadNDNVRWVYLDIGkfgglaetMDEAIR---YQ------ 305
Cdd:cd06828  237 AEALKELCeGGPDLKLIIEPGRYIVANAGVLLTRVGYVKE---TGGKTFVGVDAG--------MNDLIRpalYGayheiv 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 559158804 306 IVTPHDGSETEPCVLAGPTCDSADVLYEKtpYPLPvSLTIGDEILIEGTGAY 357
Cdd:cd06828  306 PVNKPGEGETEKVDVVGPICESGDVFAKD--RELP-EVEEGDLLAIHDAGAY 354
Orn_Arg_deC_N pfam02784
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ...
 27-260 1.02e-63

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: 203.28  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   27 VRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKERDIARAFDLG 106
Cdd:pfam02784   4 IERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  107 IRLYAVDCVEEVEKIARVAPGSRVFCRVLTDGEGAEWPLSRKFGCVPAMAKDVLRR-AKALGLDAYGVSFHVGSQQTDLT 185
Cdd:pfam02784  84 VGCVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLSSKFGADLDEDVEALLEaAKLLNLQVVGVSFHVGSGCTDAE 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158804  186 AWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPT--AQAYGMAIFDALSRHF-GNRIPETIIEPGRGMVG 260
Cdd:pfam02784 164 AFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPldFEEYANVINEALEEYFpGDPGVTIIAEPGRYFVA 241
lysA TIGR01048
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ...
 18-357 8.77e-58

diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273415 [Multi-domain]  Cd Length: 414  Bit Score: 193.66  E-value: 8.77e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   18 PCLVVDTDVVRENYQGFEKALP-YSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKE 96
Cdd:TIGR01048  26 PLYVYDEDTIRRRFRAYKEAFGgRSLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEKIVFSGNGKSR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804   97 RDIARAFDLGIRLyAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAEWP------LSRKFGCVPAMAKDVLRRAKAL 166
Cdd:TIGR01048 106 AELERALELGICI-NVDSFSELERLNEIAPELgkkaRISLRVNPGVDAKTHPyistglKDSKFGIDVEEALEAYLYALQL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  167 -GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLAdEGIILRMVNMGGGFPTRYLK--DVPTAQAYGMAIFDALSRHF 243
Cdd:TIGR01048 185 pHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA-EGIDLEFLDLGGGLGIPYTPeeEPPDLSEYAQAILNALEGYA 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  244 G-NRIPETIIEPGRGMVGNAGVIKTEVVLVSRkadNDNVRWVYLDIGkfgglaetMDEAIR---YQ------IVTPHDGS 313
Cdd:TIGR01048 264 DlGLDPKLILEPGRSIVANAGVLLTRVGFVKE---TGSRNFVIVDAG--------MNDLIRpalYGayhhiiVLNRTNDA 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 559158804  314 ETEPCVLAGPTCDSADVLYEKTPYPlpvSLTIGDEILIEGTGAY 357
Cdd:TIGR01048 333 PTEVADVVGPVCESGDVLAKDRELP---EVEPGDLLAVFDAGAY 373
PLPDE_III_Btrk_like cd06839
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ...
 12-369 2.25e-49

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: 170.47  E-value: 2.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  12 TRRPEGPCLVVDTDVVRENYQGFEKALP-YSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYG 90
Cdd:cd06839    2 ADAYGTPFYVYDRDRVRERYAALRAALPpAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILFA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  91 NTIKKERDIARAFDLGIRLYAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAEWPLS-----RKFGCVPAMAKDVLR 161
Cdd:cd06839   82 GPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHgvvaRVALRINPDFELKGSGMKmgggpSQFGIDVEELPAVLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 162 RAKAL-GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADE-GIILRMVNMGGGFPTRYLK-----DVPtaqAYGMA 234
Cdd:cd06839  162 RIAALpNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEElGLPLEFLDLGGGFGIPYFPgetplDLE---ALGAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 235 IFDALSRhFGNRIPET--IIEPGRGMVGNAGVIKTEVvlVSRKADNDNvRWVYLDIG--KFGGLAETMDEAIR----YQI 306
Cdd:cd06839  239 LAALLAE-LGDRLPGTrvVLELGRYLVGEAGVYVTRV--LDRKVSRGE-TFLVTDGGmhHHLAASGNFGQVLRrnypLAI 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559158804 307 VTPHDGSETEPCVLAGPTCDSADVLYEKTPYPlpvSLTIGDEILIEGTGAYTTTYSAVAFNGF 369
Cdd:cd06839  315 LNRMGGEERETVTVVGPLCTPLDLLGRNVELP---PLEPGDLVAVLQSGAYGLSASPLAFLSH 374
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
 18-362 1.44e-45

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: 160.51  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQGFEKAL----PYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTI 93
Cdd:cd06841    8 PFFVFDEDALRENYRELLGAFkkryPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKRIIFNGPY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  94 KKERDIARAFDLGIRLYaVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAEWplSRkFGCVPAMAKDVLRRAKALGLD 169
Cdd:cd06841   88 KSKEELEKALEEGALIN-IDSFDELERILEIAKELgrvaKVGIRLNMNYGNNVW--SR-FGFDIEENGEALAALKKIQES 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 170 AY----GVSFHVGSQQTDLTAWdralADAAAVFRTLADE--GIILRMVNMGGGFPTR--------YLKDVPTAQAYGMAI 235
Cdd:cd06841  164 KNlslvGLHCHVGSNILNPEAY----SAAAKKLIELLDRlfGLELEYLDLGGGFPAKtplslaypQEDTVPDPEDYAEAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 236 FDALSRHF--GNRIPETIIEPGRGMVGNAGVIKTEVVLVSRKADndnVRWVYLDIGKFggLAETMDEAIRYQIVTPHD-- 311
Cdd:cd06841  240 ASTLKEYYanKENKPKLILEPGRALVDDAGYLLGRVVAVKNRYG---RNIAVTDAGIN--NIPTIFWYHHPILVLRPGke 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 559158804 312 GSETEPCVLAGPTCDSADVLYEKTPYPlpvSLTIGDEILIEGTGAYTTTYS 362
Cdd:cd06841  315 DPTSKNYDVYGFNCMESDVLFPNVPLP---PLNVGDILAIRNVGAYNMTQS 362
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 27-256 2.78e-39

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: 138.99  E-value: 2.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  27 VRENYQGFEKALPY-SRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKERDIARAFDL 105
Cdd:cd06808    1 IRHNYRRLREAAPAgITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 106 GIRLYAVDCVEEVEKIARVA----PGSRVFCRVLTDGEgaewplSRKFGCVPAMAKDVLRRAKAL-GLDAYGVSFHVGSQ 180
Cdd:cd06808   81 GVIVVTVDSLEELEKLEEAAlkagPPARVLLRIDTGDE------NGKFGVRPEELKALLERAKELpHLRLVGLHTHFGSA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559158804 181 QTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPtaqaygmaifdalsrhfgnRIPETIIEPGR 256
Cdd:cd06808  155 DEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELP-------------------LGTFIIVEPGR 211
PRK08961 PRK08961
bifunctional aspartate kinase/diaminopimelate decarboxylase;
10-377 1.19e-36

bifunctional aspartate kinase/diaminopimelate decarboxylase;


Pssm-ID: 236358 [Multi-domain]  Cd Length: 861  Bit Score: 141.37  E-value: 1.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  10 LNTRRPEGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEA--GATPDRI 87
Cdd:PRK08961 496 LTLSDAGSPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERV 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  88 SYGNTIKKERDIARAFDLGIRLyAVDCVEEVEKIARVAPGSRVFCRV-LTDGEGAEWPLS-----RKFGCVPAMAKDVLR 161
Cdd:PRK08961 576 LFTPNFAPRAEYEAAFALGVTV-TLDNVEPLRNWPELFRGREVWLRIdPGHGDGHHEKVRtggkeSKFGLSQTRIDEFVD 654

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 162 RAKALGLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADegiiLRMVNMGGGFPTRYLKDVP--TAQAYGMAIFDAL 239
Cdd:PRK08961 655 LAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPD----VRTIDLGGGLGIPESAGDEpfDLDALDAGLAEVK 730

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 240 SRHFGNRIpetIIEPGRGMVGNAGVIKTEVVLVSRKadnDNVRWVYLDIGkfgglaetMDEAIR-------YQIV--TPH 310
Cdd:PRK08961 731 AQHPGYQL---WIEPGRYLVAEAGVLLARVTQVKEK---DGVRRVGLETG--------MNSLIRpalygayHEIVnlSRL 796

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559158804 311 DGSETEPCVLAGPTCDSADVL-YEKtpyPLPVSLTiGDEILIEGTGAYTTTYSAvAFNGFEPLRSYVI 377
Cdd:PRK08961 797 DEPAAGTADVVGPICESSDVLgKRR---RLPATAE-GDVILIANAGAYGYSMSS-TYNLREPAREVVL 859
PLPDE_III_ODC_like_AZI cd06831
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ...
 26-377 3.46e-33

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: 127.66  E-value: 3.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  26 VVRENYQgFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKERDIARAFDL 105
Cdd:cd06831   23 IVKKHSQ-WQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 106 GIRLYAVDCVEEVEKIARVAPGSRVFCRVLTDGEGAEWPLSRKFGCVPAMAKDVLRRAKALGLDAYGVSFHVGSQQTDLT 185
Cdd:cd06831  102 GVNIMTCDNEIELKKIARNHPNAKLLLHIATEDNIGGEEMNMKFGTTLKNCRHLLECAKELDVQIVGVKFHVSSSCKEYQ 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 186 AWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYGMAIFDALSRHFGNRIpetIIEPGRGMVGNA--- 262
Cdd:cd06831  182 TYVHALSDARCVFDMAEEFGFKMNMLDIGGGFTGSEIQLEEVNHVIRPLLDVYFPEGSGIQI---IAEPGSYYVSSAftl 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 263 --GVIKTEVV-------LVSRKADNDNVRWVYLDIGKFGGLAETMDEAIryqIVTP--HDGS-ETEPCV---LAGPTCDS 327
Cdd:cd06831  259 avNVIAKKAVendkhlsSVEKNGSDEPAFVYYMNDGVYGSFASKLSEKL---NTTPevHKKYkEDEPLFtssLWGPSCDE 335

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 559158804 328 ADVLYEKTPYPlpvSLTIGDEILIEGTGAYTTTYSAvAFNGFE-PLRSYVI 377
Cdd:cd06831  336 LDQIVESCLLP---ELNVGDWLIFDNMGAGSLHEPS-TFNDFQrPAIYYMM 382
PLPDE_III_Bif_AspK_DapDC cd06840
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ...
 16-357 3.90e-33

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: 126.78  E-value: 3.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  16 EGPCLVVDTDVVRENYQGFEKALPYSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEA--GATPDRISYGNTI 93
Cdd:cd06840   11 VGPCYVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  94 KKERDIARAFDLGIRLyAVDCVEEVEKIARVAPGSRVFCRV-LTDGEGAEWPLS-----RKFGCVPAMAKDVLRRAKALG 167
Cdd:cd06840   91 AARSEYEQALELGVNV-TVDNLHPLREWPELFRGREVILRIdPGQGEGHHKHVRtggpeSKFGLDVDELDEARDLAKKAG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 168 LDAYGVSFHVGSQQTDLTAWDRALADAAavfrTLADEGIILRMVNMGGGFPTRYLKDVP--TAQAYGMAIFDALSRHFGN 245
Cdd:cd06840  170 IIVIGLHAHSGSGVEDTDHWARHGDYLA----SLARHFPAVRILNVGGGLGIPEAPGGRpiDLDALDAALAAAKAAHPQY 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 246 RIpetIIEPGRGMVGNAGVIKTEVVLVSRKadnDNVRWVYLDIGkfgglaetMDEAIR-------YQIV--TPHDGSETE 316
Cdd:cd06840  246 QL---WMEPGRFIVAESGVLLARVTQIKHK---DGVRFVGLETG--------MNSLIRpalygayHEIVnlSRLDEPPAG 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 559158804 317 PCVLAGPTCDSADVL-YEKtpyPLPVSLTiGDEILIEGTGAY 357
Cdd:cd06840  312 NADVVGPICESGDVLgRDR---LLPETEE-GDVILIANAGAY 349
PLPDE_III_ODC_DapDC_like_1 cd06836
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ...
 19-363 2.27e-23

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: 100.16  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  19 CLVVDTDVVRENYQGFEKALPYSRIF-YAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKER 97
Cdd:cd06836    5 VGLYDLDGFRALVARLTAAFPAPVLHtFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  98 DIARAFDLGIRLyAVDCVEEVEKI-ARVA----PGSRVFCRVLTD-GEGAEWPLS-----RKFGC-VPAMAKDVLRRAKA 165
Cdd:cd06836   85 ELREALELGVAI-NIDNFQELERIdALVAefkeASSRIGLRVNPQvGAGKIGALStatatSKFGVaLEDGARDEIIDAFA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 166 LGLDAYGVSFHVGSQQTDLTawdrALADAAAVFRTLADEgiILRMV--------NMGGGFPTRYLKDV--PTAQAYGMAI 235
Cdd:cd06836  164 RRPWLNGLHVHVGSQGCELS----LLAEGIRRVVDLAEE--INRRVgrrqitriDIGGGLPVNFESEDitPTFADYAAAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 236 FDALSRHFGNRIpETIIEPGRGMVGNAGVIKTEVVLVSRKAD----------NDNVRWVYLdigkfgglaeTMDEAIRYQ 305
Cdd:cd06836  238 KAAVPELFDGRY-QLVTEFGRSLLAKCGTIVSRVEYTKSSGGrriaithagaQVATRTAYA----------PDDWPLRVT 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158804 306 IVTPH---DGSETEPCVLAGPTCDSADVLYEKTPYPLpvsLTIGDEILIEGTGAYT-TTYSA 363
Cdd:cd06836  307 VFDANgepKTGPEVVTDVAGPCCFAGDVLAKERALPP---LEPGDYVAVHDTGAYYfSSHSS 365
PLPDE_III_Y4yA_like cd06842
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ...
 17-260 2.08e-22

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: 97.72  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  17 GPCLVVDTDVVRENYQGFEKALPY----SRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNT 92
Cdd:cd06842   10 SPLNVLFPQTFRENIAALRAVLDRhgvdGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRGDRIVATGP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  93 IKkerdiARAF-DLGIR---LYAVDCVEEVEKIARVAPGS-----RVFCRVLTDgegAEWPLSRkFGCVPAMAKDVLRRA 163
Cdd:cd06842   90 AK-----TDEFlWLAVRhgaTIAVDSLDELDRLLALARGYttgpaRVLLRLSPF---PASLPSR-FGMPAAEVRTALERL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 164 KALG--LDAYGVSFHVGSQQTDLTAwdRALADAAAVFRTLADEGIILRMVNMGGGFPTRYLKDVPTAQAYgmaiFDALSR 241
Cdd:cd06842  161 AQLRerVRLVGFHFHLDGYSAAQRV--AALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAEWEAF----LAALTE 234

                        250       260
                 ....*....|....*....|
gi 559158804 242 -HFGNRIPETIIEPGRGMVG 260
Cdd:cd06842  235 aLYGYGRPLTWRNEGGTLRG 254
PLPDE_III_PvsE_like cd06843
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ...
 21-274 3.11e-20

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: 90.80  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  21 VVDTDVVRENYQGFEKALP-YSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGatPD-RISYGNTIKKERD 98
Cdd:cd06843    6 VYDLAALRAHARALRASLPpGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAV--PDaPLIFGGPGKTDSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  99 IARAFDLGIRLYAVDCVEEVEKIARVAP--GSR--VFCRVLTDGEGAewPLSR--------KFGCVPAMAKDVLRRAKAL 166
Cdd:cd06843   84 LAQALAQGVERIHVESELELRRLNAVARraGRTapVLLRVNLALPDL--PSSTltmggqptPFGIDEADLPDALELLRDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 167 -GLDAYGVSFHVGSQQTDLTAWDRALADAAAVFRTLADE-GIILRMVNMGGGFPTRYLKdvPTAQaygmaiFD--ALSRH 242
Cdd:cd06843  162 pNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEhGLDLDVVNVGGGIGVNYAD--PEEQ------FDwaGFCEG 233

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 559158804 243 FGNRIPET------IIEPGRGMVGNAGVIKTEVVLVSR 274
Cdd:cd06843  234 LDQLLAEYepgltlRFECGRYISAYCGYYVTEVLDLKR 271
PLN02537 PLN02537
diaminopimelate decarboxylase
 27-357 1.81e-16

diaminopimelate decarboxylase


Pssm-ID: 178152 [Multi-domain]  Cd Length: 410  Bit Score: 80.22  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  27 VRENYQGFEKALP--YSRIFYAVKANPAPEILRLLASLGSSFDTASVAEIEMALEAGATPDRISYGNTIKKERDIARAFD 104
Cdd:PLN02537  28 ITRNYEAYKEALEglRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGKLLEDLVLAAQ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 105 LGIrLYAVDCVEEVEKIARVAPGS----RVFCRVLTDGEGAEWPL------SRKFGCVPAMAKDVLRRAKA--LGLDAYG 172
Cdd:PLN02537 108 EGV-FVNVDSEFDLENIVEAARIAgkkvNVLLRINPDVDPQVHPYvatgnkNSKFGIRNEKLQWFLDAVKAhpNELKLVG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 173 VSFHVGSQQTDLTAWdralADAAAVFRTLADE----GIILRMVNMGGGFPTRYLKD---VPTAqaygMAIFDALSRHFGN 245
Cdd:PLN02537 187 AHCHLGSTITKVDIF----RDAAVLMVNYVDEiraqGFELSYLNIGGGLGIDYYHAgavLPTP----RDLIDTVRELVLS 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 246 RIPETIIEPGRGMVGNAGVIKTEVVLVSrkaDNDNVRWVYLDigkfgglaETMDEAIR------YQ----IVTPHDGSET 315
Cdd:PLN02537 259 RDLTLIIEPGRSLIANTCCFVNRVTGVK---TNGTKNFIVID--------GSMAELIRpslydaYQhielVSPPPPDAEV 327

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 559158804 316 EPCVLAGPTCDSADVLYEKTPYPLPVSltiGDEILIEGTGAY 357
Cdd:PLN02537 328 STFDVVGPVCESADFLGKDRELPTPPK---GAGLVVHDAGAY 366
PLPDE_III_ADC cd06830
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ...
 28-357 4.27e-14

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: 72.99  E-value: 4.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  28 RENYQGfekalPYsRIFYAVKANPAPEILRLLASLGSSFD----TASVAEIEMALEAGATPDRISYGNTIKKE---RDIA 100
Cdd:cd06830   32 EYGYKG-----KY-QGVYPIKVNQQREVVEEIVKAGKRYNigleAGSKPELLAALALLKTPDALIICNGYKDDeyiELAL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 101 RAFDLGIRLYAV-DCVEEVEKIARVAP--------GSRVfcRVLTDGEGaEW----PLSRKFGCVPAMAKDVLRRAKALG 167
Cdd:cd06830  106 LARKLGHNVIIViEKLSELDLILELAKklgvkpllGVRI--KLASKGSG-KWqesgGDRSKFGLTASEILEVVEKLKEAG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 168 LdayGVS-----FHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGGGFPTRY---LKDVPTAQAYGMAIF-DA 238
Cdd:cd06830  183 M---LDRlkllhFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIGGGLGVDYdgsRSSSDSSFNYSLEEYaND 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 239 LSRHFG-----NRIPE-TII-EPGRGMVGNAGVIKTEVVLVSRKADndnvrWVYLDIGKFGGLAETMdeAIRyQ--IVTP 309
Cdd:cd06830  260 IVKTVKeicdeAGVPHpTIVtESGRAIVAHHSVLIFEVLGVKRLAD-----WYFCNFSLFQSLPDSW--AID-QlfPIMP 331

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 310 ---HDGSETEPCVLAGPTCDSADVlYEKTPYPLPVSLTIGDEILIEG---------TGAY 357
Cdd:cd06830  332 lhrLNEKPTRRAVLGDITCDSDGK-IDSFIDPPDILPTLPLHPLRKDepyylgfflVGAY 390
Dsd1 COG3616
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
11-215 1.32e-12

D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];


Pssm-ID: 442834 [Multi-domain]  Cd Length: 357  Bit Score: 68.24  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  11 NTRRPEGPCLVVDTDVVREN---YQGFEKALPySRIFYAVKANPAPEILRLLASLGSS-FDTASVAEIEMALEAGAtpDR 86
Cdd:COG3616    2 NLADLDTPALVLDLDALERNiarMAARAAAHG-VRLRPHGKTHKSPELARRQLAAGAWgITVATLAEAEVLAAAGV--DD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  87 ISYGNTIKKERDIARAFDL---GIRLY-AVDCVEEVEKIARVAPGSRVFCRVLTD-GEGAewplsRKFGCVP-AMAKDVL 160
Cdd:COG3616   79 ILLAYPLVGPAKLARLAALaraGARLTvLVDSVEQAEALAAAAAAAGRPLRVLVElDVGG-----GRTGVRPpEAALALA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 559158804 161 RRAKAL------GLDAY-GVSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNMGG 215
Cdd:COG3616  154 RAIAASpglrlaGLMTYeGHIYGADDAEERRAAAREELARLAAAAEALRAAGLPCPIVSGGG 215
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
 172-368 7.81e-06

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.


Pssm-ID: 143502 [Multi-domain]  Cd Length: 346  Bit Score: 47.16  E-value: 7.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 172 GVSFHVGSQQtDLTAWDRALADAAAVFRTLADEgiiLRMVNMGGG-FPTRYLKDVPTAqaygMAIFDALSRHFGNRIpet 250
Cdd:cd06829  157 GLHFHTLCEQ-DFDALERTLEAVEERFGEYLPQ---LKWLNLGGGhHITRPDYDVDRL----IALIKRFKEKYGVEV--- 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 251 IIEPGRGMVGNAGVIKTEVvlvsrkadndnvrwvyLDIGKFGglaetMDEAI-----------------RYQIVTPHDGS 313
Cdd:cd06829  226 YLEPGEAVALNTGYLVATV----------------LDIVENG-----MPIAIldasatahmpdvlempyRPPIRGAGEPG 284

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 559158804 314 ETEPCV-LAGPTCDSADVLYEktpYPLPVSLTIGDEILIEGTGAYT---TTYsavaFNG 368
Cdd:cd06829  285 EGAHTYrLGGNSCLAGDVIGD---YSFDEPLQVGDRLVFEDMAHYTmvkTNT----FNG 336
PLPDE_III_D-TA cd06821
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ...
 18-125 1.78e-04

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR 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. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.


Pssm-ID: 143495 [Multi-domain]  Cd Length: 361  Bit Score: 43.05  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804  18 PCLVVDTDVVRENYQG-FEKALPYSRIFYAVKANPAPEILRLLASLG-SSFDTASVAEIEMALEAGATPDRISYGNT-IK 94
Cdd:cd06821   10 PALAVYPDRIEENIRRmIRMAGDPQRLRPHVKTHKMAEIVRLQLEAGiTKFKCATIAEAEMLAEAGAPDVLLAYPLVgPN 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 559158804  95 KER--DIARAFDlGIRLYA-VDCVEEVEKIARVA 125
Cdd:cd06821   90 IERflELAKKYP-GTRFSAlVDDLEAAEALSAAA 122
PLN02439 PLN02439
arginine decarboxylase
 136-270 3.98e-04

arginine decarboxylase


Pssm-ID: 215240 [Multi-domain]  Cd Length: 559  Bit Score: 42.37  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559158804 136 TDGEGAewplsrKFG-CVPAMAKDVLRRAKALGLDAYG-VSFHVGSQQTDLTAWDRALADAAAVFRTLADEGIILRMVNM 213
Cdd:PLN02439 153 TSGEKG------KFGlTATEIVRVVRKLRKEGMLDCLQlLHFHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDI 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559158804 214 GGGFPTRY------LKDVPTaqAYGM---------AIFDALSRhfgNRIPETII--EPGRGMVGNAGVIKTEVV 270
Cdd:PLN02439 227 GGGLGIDYdgsksgSSDMSV--AYSLeeyanavvaAVRDVCDR---KGVKHPVIcsESGRALVSHHSVLIFEAV 295
 
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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