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Conserved domains on  [gi|2508969895|ref|WP_283270320|]
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carboxynorspermidine decarboxylase [Stutzerimonas stutzeri]

Protein Classification

carboxynorspermidine decarboxylase( domain architecture ID 10160113)

carboxynorspermidine decarboxylase (also termed carboxyspermidine decarboxylase) catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine in a pyridoxal 5-phosphate (PLP)-dependent manner in arginine and proline metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
4-343 0e+00

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: 549.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQKFAGETHAYSVAWAD 83
Cdd:cd06829     1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGREEFGGEVHTYSPAYRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  84 DEIEEMVANCDKIIFNSIGQLERFAEATE--GTIRGLRVNPQVSSSDYLLADPARPFSRLGEHDPAKIEAVIGKISGFMF 161
Cdd:cd06829    81 DEIDEILRLADHIIFNSLSQLERFKDRAKaaGISVGLRINPEYSEVETDLYDPCAPGSRLGVTLDELEEEDLDGIEGLHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 162 HNNCENsSFELFDKMLSTIEERFGHLLEQVQWVSLGGGIHFTGEGYPLDAFCARLKAFSEKFGVQVYLEPGEAAITMSAS 241
Cdd:cd06829   161 HTLCEQ-DFDALERTLEAVEERFGEYLPQLKWLNLGGGHHITRPDYDVDRLIALIKRFKEKYGVEVYLEPGEAVALNTGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 242 LEVTVLDTLFNGKNLAVVDSSIEAHMLDLL--IYRLNAKMAPSGGE--HSYMVCGKSCLAGDIFGEYQFDRPLAIGDRLS 317
Cdd:cd06829   240 LVATVLDIVENGMPIAILDASATAHMPDVLemPYRPPIRGAGEPGEgaHTYRLGGNSCLAGDVIGDYSFDEPLQVGDRLV 319
                         330       340
                  ....*....|....*....|....*.
gi 2508969895 318 FIDAAGYTMVKKNWFNGLKMPSIVVK 343
Cdd:cd06829   320 FEDMAHYTMVKTNTFNGVRLPSIAIR 345
 
Name Accession Description Interval E-value
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
4-343 0e+00

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: 549.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQKFAGETHAYSVAWAD 83
Cdd:cd06829     1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGREEFGGEVHTYSPAYRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  84 DEIEEMVANCDKIIFNSIGQLERFAEATE--GTIRGLRVNPQVSSSDYLLADPARPFSRLGEHDPAKIEAVIGKISGFMF 161
Cdd:cd06829    81 DEIDEILRLADHIIFNSLSQLERFKDRAKaaGISVGLRINPEYSEVETDLYDPCAPGSRLGVTLDELEEEDLDGIEGLHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 162 HNNCENsSFELFDKMLSTIEERFGHLLEQVQWVSLGGGIHFTGEGYPLDAFCARLKAFSEKFGVQVYLEPGEAAITMSAS 241
Cdd:cd06829   161 HTLCEQ-DFDALERTLEAVEERFGEYLPQLKWLNLGGGHHITRPDYDVDRLIALIKRFKEKYGVEVYLEPGEAVALNTGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 242 LEVTVLDTLFNGKNLAVVDSSIEAHMLDLL--IYRLNAKMAPSGGE--HSYMVCGKSCLAGDIFGEYQFDRPLAIGDRLS 317
Cdd:cd06829   240 LVATVLDIVENGMPIAILDASATAHMPDVLemPYRPPIRGAGEPGEgaHTYRLGGNSCLAGDVIGDYSFDEPLQVGDRLV 319
                         330       340
                  ....*....|....*....|....*.
gi 2508969895 318 FIDAAGYTMVKKNWFNGLKMPSIVVK 343
Cdd:cd06829   320 FEDMAHYTMVKTNTFNGVRLPSIAIR 345
nspC TIGR01047
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. ...
2-360 1.03e-139

carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273414 [Multi-domain]  Cd Length: 379  Bit Score: 401.85  E-value: 1.03e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   2 IKTPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQKFAGETHAYSVAW 81
Cdd:TIGR01047   1 IPTPAFVLEEEKLRKNLEILESVQQQSGAKVLLALKGFAFWGAFPILREYLKGCTASGLWEAKLAKEEFGKEIHVYSPAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  82 ADDEIEEMVANCDKIIFNSIGQLERFAEATEG----TIRGLRVNPQVSSSDYLLADPARPFSRLGEHDPAKIEAVIGKIS 157
Cdd:TIGR01047  81 KEDDIPEIIPLADHIVFNSLAQWHRYRHKVQGknsaVKLGLRINPEYSEVPTDLYNPCGRFSRLGVQAKDFEEVLLDGIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 158 GFMFHNNCENSSfELFDKMLSTIEERFGHLLEQVQWVSLGGGIHFTGEGYPLDAFCARLKAFSEKFGVQVYLEPGEAAIT 237
Cdd:TIGR01047 161 GLHFHTLCEKDA-DALERTLEVIEEKFGEYLPQMKWVNFGGGHHITKKGYDVEKLIAVIKAFSERHGVQVILEPGEAIGW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 238 MSASLEVTVLDTLFNGKNLAVVDSSIEAHMLDLLIYR-----LNAKMAP--------SGGEHSYMVCGKSCLAGDIFGEY 304
Cdd:TIGR01047 240 QTGFLVASVVDIVENEKQIAILDVSFEAHMPDTLEMPyrpevLGARDPAtreneaqdKEGEFSYLLGGNTCLAGDVMGEY 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2508969895 305 QFDRPLAIGDRLSFIDAAGYTMVKKNWFNGLKMPSIVVKQLDGSVEVVREFDFNDY 360
Cdd:TIGR01047 320 AFDKPLKVGDKIVFLDMIHYTMVKNTTFNGVKLPSLGCLRAKGEFQMIRTFGYEDY 375
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
4-363 1.17e-99

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: 301.30  E-value: 1.17e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQK--FAGETHAYSVAW 81
Cdd:COG0019    26 TPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAgfPPERIVFSGNGK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  82 ADDEIEEMV-ANCDKIIFNSIGQLERFAEATEGTIR----GLRVNPQVSSSDYLLADPARPFSRLGEhDPAKIEAVIG-- 154
Cdd:COG0019   106 SEEELEEALeLGVGHINVDSLSELERLAELAAELGKrapvGLRVNPGVDAGTHEYISTGGKDSKFGI-PLEDALEAYRra 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 155 ------KISGFMFHNNCENSSFELFDKMLSTIEERFGHLLE---QVQWVSLGGGIHFT----GEGYPLDAFCARLKAFSE 221
Cdd:COG0019   185 aalpglRLVGLHFHIGSQILDLEPFEEALERLLELAEELRElgiDLEWLDLGGGLGIPytegDEPPDLEELAAAIKEALE 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 222 KF---GVQVYLEPGEAAITMSASLEVTVLDTLFN-GKNLAVVDSSIEAHMLDLLIYR----LNAKMAPSGGEHSYMVCGK 293
Cdd:COG0019   265 ELcglGPELILEPGRALVGNAGVLLTRVLDVKENgGRRFVIVDAGMNDLMRPALYGAyhpiVPVGRPSGAEAETYDVVGP 344
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2508969895 294 SCLAGDIFGEYQFDRPLAIGDRLSFIDAAGYTMVKKNWFNGLKMPSIVVKQlDGSVEVVREF-DFNDYLSS 363
Cdd:COG0019   345 LCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVD-DGEARLIRRReTYEDLLAS 414
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
7-321 6.60e-31

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: 119.90  E-value: 6.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   7 YLIDKQKLLGNLEKIayvRE--QSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQkfAG----ETHAYSVA 80
Cdd:pfam00278   2 YVYDLATLRRNYRRW---KAalPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALA--AGvdpeRIVFAGPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  81 WADDEIEEMV-ANCDKIIFNSIGQLERFAE-ATEGTIR-GLRVNPQVSSSDYLLAdPARPFSRLGEhDPAKIEAVIG--- 154
Cdd:pfam00278  77 KTDSEIRYALeAGVLCFNVDSEDELEKIAKlAPELVARvALRINPDVDAGTHKIS-TGGLSSKFGI-DLEDAPELLAlak 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 155 ----KISGFMFHNNCENSSFELFDKMLSTIEERFGHLLEQ---VQWVSLGGGIH---FTGEGYPLDAFCARLKAFSEKF- 223
Cdd:pfam00278 155 elglNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELgidLKLLDIGGGFGipyRDEPPPDFEEYAAAIREALDEYf 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 224 --GVQVYLEPGEAAITMSASLEVTVLDT-LFNGKNLAVVDSSIEAHMLDLL---IYRLNAKMAPSGGE-HSYMVCGKSCL 296
Cdd:pfam00278 235 ppDLEIIAEPGRYLVANAGVLVTRVIAVkTGGGKTFVIVDAGMNDLFRPALydaYHPIPVVKEPGEGPlETYDVVGPTCE 314
                         330       340
                  ....*....|....*....|....*.
gi 2508969895 297 AGDIFG-EYQFDrPLAIGDRLSFIDA 321
Cdd:pfam00278 315 SGDVLAkDRELP-ELEVGDLLAFEDA 339
 
Name Accession Description Interval E-value
PLPDE_III_CANSDC cd06829
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ...
4-343 0e+00

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: 549.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQKFAGETHAYSVAWAD 83
Cdd:cd06829     1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDGTTASSLFEARLGREEFGGEVHTYSPAYRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  84 DEIEEMVANCDKIIFNSIGQLERFAEATE--GTIRGLRVNPQVSSSDYLLADPARPFSRLGEHDPAKIEAVIGKISGFMF 161
Cdd:cd06829    81 DEIDEILRLADHIIFNSLSQLERFKDRAKaaGISVGLRINPEYSEVETDLYDPCAPGSRLGVTLDELEEEDLDGIEGLHF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 162 HNNCENsSFELFDKMLSTIEERFGHLLEQVQWVSLGGGIHFTGEGYPLDAFCARLKAFSEKFGVQVYLEPGEAAITMSAS 241
Cdd:cd06829   161 HTLCEQ-DFDALERTLEAVEERFGEYLPQLKWLNLGGGHHITRPDYDVDRLIALIKRFKEKYGVEVYLEPGEAVALNTGY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 242 LEVTVLDTLFNGKNLAVVDSSIEAHMLDLL--IYRLNAKMAPSGGE--HSYMVCGKSCLAGDIFGEYQFDRPLAIGDRLS 317
Cdd:cd06829   240 LVATVLDIVENGMPIAILDASATAHMPDVLemPYRPPIRGAGEPGEgaHTYRLGGNSCLAGDVIGDYSFDEPLQVGDRLV 319
                         330       340
                  ....*....|....*....|....*.
gi 2508969895 318 FIDAAGYTMVKKNWFNGLKMPSIVVK 343
Cdd:cd06829   320 FEDMAHYTMVKTNTFNGVRLPSIAIR 345
nspC TIGR01047
carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. ...
2-360 1.03e-139

carboxynorspermidine decarboxylase; This protein is related to diaminopimelate decarboxylase. It is the last enzyme in norspermidine biosynthesis by an unusual pathway shown in Vibrio alginolyticus. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273414 [Multi-domain]  Cd Length: 379  Bit Score: 401.85  E-value: 1.03e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   2 IKTPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQKFAGETHAYSVAW 81
Cdd:TIGR01047   1 IPTPAFVLEEEKLRKNLEILESVQQQSGAKVLLALKGFAFWGAFPILREYLKGCTASGLWEAKLAKEEFGKEIHVYSPAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  82 ADDEIEEMVANCDKIIFNSIGQLERFAEATEG----TIRGLRVNPQVSSSDYLLADPARPFSRLGEHDPAKIEAVIGKIS 157
Cdd:TIGR01047  81 KEDDIPEIIPLADHIVFNSLAQWHRYRHKVQGknsaVKLGLRINPEYSEVPTDLYNPCGRFSRLGVQAKDFEEVLLDGIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 158 GFMFHNNCENSSfELFDKMLSTIEERFGHLLEQVQWVSLGGGIHFTGEGYPLDAFCARLKAFSEKFGVQVYLEPGEAAIT 237
Cdd:TIGR01047 161 GLHFHTLCEKDA-DALERTLEVIEEKFGEYLPQMKWVNFGGGHHITKKGYDVEKLIAVIKAFSERHGVQVILEPGEAIGW 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 238 MSASLEVTVLDTLFNGKNLAVVDSSIEAHMLDLLIYR-----LNAKMAP--------SGGEHSYMVCGKSCLAGDIFGEY 304
Cdd:TIGR01047 240 QTGFLVASVVDIVENEKQIAILDVSFEAHMPDTLEMPyrpevLGARDPAtreneaqdKEGEFSYLLGGNTCLAGDVMGEY 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2508969895 305 QFDRPLAIGDRLSFIDAAGYTMVKKNWFNGLKMPSIVVKQLDGSVEVVREFDFNDY 360
Cdd:TIGR01047 320 AFDKPLKVGDKIVFLDMIHYTMVKNTTFNGVKLPSLGCLRAKGEFQMIRTFGYEDY 375
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
4-363 1.17e-99

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: 301.30  E-value: 1.17e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQK--FAGETHAYSVAW 81
Cdd:COG0019    26 TPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAgfPPERIVFSGNGK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  82 ADDEIEEMV-ANCDKIIFNSIGQLERFAEATEGTIR----GLRVNPQVSSSDYLLADPARPFSRLGEhDPAKIEAVIG-- 154
Cdd:COG0019   106 SEEELEEALeLGVGHINVDSLSELERLAELAAELGKrapvGLRVNPGVDAGTHEYISTGGKDSKFGI-PLEDALEAYRra 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 155 ------KISGFMFHNNCENSSFELFDKMLSTIEERFGHLLE---QVQWVSLGGGIHFT----GEGYPLDAFCARLKAFSE 221
Cdd:COG0019   185 aalpglRLVGLHFHIGSQILDLEPFEEALERLLELAEELRElgiDLEWLDLGGGLGIPytegDEPPDLEELAAAIKEALE 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 222 KF---GVQVYLEPGEAAITMSASLEVTVLDTLFN-GKNLAVVDSSIEAHMLDLLIYR----LNAKMAPSGGEHSYMVCGK 293
Cdd:COG0019   265 ELcglGPELILEPGRALVGNAGVLLTRVLDVKENgGRRFVIVDAGMNDLMRPALYGAyhpiVPVGRPSGAEAETYDVVGP 344
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2508969895 294 SCLAGDIFGEYQFDRPLAIGDRLSFIDAAGYTMVKKNWFNGLKMPSIVVKQlDGSVEVVREF-DFNDYLSS 363
Cdd:COG0019   345 LCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVD-DGEARLIRRReTYEDLLAS 414
PLPDE_III_ODC_DapDC_like cd06810
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ...
4-342 1.08e-40

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: 147.07  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLgnlEKIAYVRE--QSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGR-QKFAGETHAYS-V 79
Cdd:cd06810     1 TPFYVYDLDIIR---AHYAALKEalPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALaAGVPPERIIFTgP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  80 AWADDEIEEMVA-NCDKIIFNSIGQLERFAEATEGTIR----GLRVNPQVSSSDYLLAdPARPFSRLGEhDPAKIEAVIG 154
Cdd:cd06810    78 AKSVSEIEAALAsGVDHIVVDSLDELERLNELAKKLGPkariLLRVNPDVSAGTHKIS-TGGLKSKFGL-SLSEARAALE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 155 -------KISGFMFHNNCENSSFELFDKMLST---IEERFGHLLEQVQWVSLGGG--IHFTGEGYPLDAFCARLKAFSEK 222
Cdd:cd06810   156 rakeldlRLVGLHFHVGSQILDLETIVQALSDareLIEELVEMGFPLEMLDLGGGlgIPYDEQPLDFEEYAALINPLLKK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 223 F-----GVQVYLEPGEAAITMSASLEVTVLDTLFN-GKNLAVVDSSIEAHMLDLLIYRLNAKM--APSGGEHS----YMV 290
Cdd:cd06810   236 YfpndpGVTLILEPGRYIVAQAGVLVTRVVAVKVNgGRFFAVVDGGMNHSFRPALAYDAYHPItpLKAPGPDEplvpATL 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2508969895 291 CGKSCLAGDIFGEYQFDRPLAIGDRLSFIDAAGYTMVKKNWFNGLKMPSIVV 342
Cdd:cd06810   316 AGPLCDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYL 367
Orn_DAP_Arg_deC pfam00278
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ...
7-321 6.60e-31

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: 119.90  E-value: 6.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   7 YLIDKQKLLGNLEKIayvRE--QSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQkfAG----ETHAYSVA 80
Cdd:pfam00278   2 YVYDLATLRRNYRRW---KAalPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALA--AGvdpeRIVFAGPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  81 WADDEIEEMV-ANCDKIIFNSIGQLERFAE-ATEGTIR-GLRVNPQVSSSDYLLAdPARPFSRLGEhDPAKIEAVIG--- 154
Cdd:pfam00278  77 KTDSEIRYALeAGVLCFNVDSEDELEKIAKlAPELVARvALRINPDVDAGTHKIS-TGGLSSKFGI-DLEDAPELLAlak 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 155 ----KISGFMFHNNCENSSFELFDKMLSTIEERFGHLLEQ---VQWVSLGGGIH---FTGEGYPLDAFCARLKAFSEKF- 223
Cdd:pfam00278 155 elglNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELgidLKLLDIGGGFGipyRDEPPPDFEEYAAAIREALDEYf 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 224 --GVQVYLEPGEAAITMSASLEVTVLDT-LFNGKNLAVVDSSIEAHMLDLL---IYRLNAKMAPSGGE-HSYMVCGKSCL 296
Cdd:pfam00278 235 ppDLEIIAEPGRYLVANAGVLVTRVIAVkTGGGKTFVIVDAGMNDLFRPALydaYHPIPVVKEPGEGPlETYDVVGPTCE 314
                         330       340
                  ....*....|....*....|....*.
gi 2508969895 297 AGDIFG-EYQFDrPLAIGDRLSFIDA 321
Cdd:pfam00278 315 SGDVLAkDRELP-ELEVGDLLAFEDA 339
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
4-341 2.29e-16

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: 79.45  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895   4 TPYYLIDKQKLLGNLEKIAYVREQSGAKALLALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQ-KFAGETHAYS-VAW 81
Cdd:cd06828     3 TPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKaGFPPERIVFTgNGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  82 ADDEIEEMVANcDKIIFN--SIGQLERFAEATEGTIRG----LRVNPQVsssdyllaDParpfsrlGEH----------- 144
Cdd:cd06828    83 SDEELELALEL-GILRINvdSLSELERLGEIAPELGKGapvaLRVNPGV--------DA-------GTHpyistggkdsk 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 145 ---DPAKIEAVIG--------KISGFMFH---NNCENSSF-ELFDKMLSTIEErFGHLLEQVQWVSLGGG--IHFTGEGY 207
Cdd:cd06828   147 fgiPLEQALEAYRrakelpglKLVGLHCHigsQILDLEPFvEAAEKLLDLAAE-LRELGIDLEFLDLGGGlgIPYRDEDE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 208 PLD------AFCARLKAFSEKF-GVQVYLEPG-----EAAITMSaslevTVLDTLFNG-KNLAVVDSSieahMLDLL--- 271
Cdd:cd06828   226 PLDieeyaeAIAEALKELCEGGpDLKLIIEPGryivaNAGVLLT-----RVGYVKETGgKTFVGVDAG----MNDLIrpa 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508969895 272 IYR-----LNAKMAPSGGEHSYMVCGKSCLAGDIFGEyqfDRPL---AIGDRLSFIDAAGYTMVKKNWFNGLKMPSIV 341
Cdd:cd06828   297 LYGayheiVPVNKPGEGETEKVDVVGPICESGDVFAK---DRELpevEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEV 371
PLPDE_III_MccE_like cd06841
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ...
83-347 3.01e-09

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: 58.04  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  83 DDEIEEMVANCDKIIFNSIGQLERFAEATEGTIR----GLRVNPQVSSSdylladparPFSRLG--EHDPAKIEAVIGKI 156
Cdd:cd06841    90 KEELEKALEEGALINIDSFDELERILEIAKELGRvakvGIRLNMNYGNN---------VWSRFGfdIEENGEALAALKKI 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 157 S--------GFMFH-----NNCENSSfELFDKMLSTIEERFGHLLEqvqWVSLGGGIhFT-----GEGYPLDAF------ 212
Cdd:cd06841   161 QesknlslvGLHCHvgsniLNPEAYS-AAAKKLIELLDRLFGLELE---YLDLGGGF-PAktplsLAYPQEDTVpdpedy 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895 213 ----CARLKAFSEKFGVQ--VYLEPGEAAITMSASLEVTVLDTL-FNGKNLAVVDSSI----EAHMLDLLIYRLnaKMAP 281
Cdd:cd06841   236 aeaiASTLKEYYANKENKpkLILEPGRALVDDAGYLLGRVVAVKnRYGRNIAVTDAGInnipTIFWYHHPILVL--RPGK 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2508969895 282 SGGEHS-YMVCGKSCLAGD-IFGEYQFDrPLAIGDRLSFIDAAGYTMVKKNWFNgLKMPSIVVKQLDG 347
Cdd:cd06841   314 EDPTSKnYDVYGFNCMESDvLFPNVPLP-PLNVGDILAIRNVGAYNMTQSNQFI-RPRPAVYLIDNNG 379
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
19-199 8.33e-05

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: 43.08  E-value: 8.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  19 EKIAYVREQSGAKALL--ALKCFATWSVFDLMQQYMDGTTSSSLYELKLGRQkfAGETHAYSVAWA----DDEIEEMVAN 92
Cdd:cd06808     3 HNYRRLREAAPAGITLfaVVKANANPEVARTLAALGTGFDVASLGEALLLRA--AGIPPEPILFLGpckqVSELEDAAEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2508969895  93 CDkIIFNSIG--QLERFAEATEGTIRGLRVNPQVSSSDYLladparpfSRLGEHD---PAKIEAVIG----KISGFMFH- 162
Cdd:cd06808    81 GV-IVVTVDSleELEKLEEAALKAGPPARVLLRIDTGDEN--------GKFGVRPeelKALLERAKElphlRLVGLHTHf 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2508969895 163 -NNCEN-SSFEL----FDKMLSTIEERFGHLLEqvqwVSLGGG 199
Cdd:cd06808   152 gSADEDySPFVEalsrFVAALDQLGELGIDLEQ----LSIGGS 190
 
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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