|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
3-416 |
4.53e-153 |
|
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: 439.20 E-value: 4.53e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 3 PFTPTTIAPLAQQFGTPLWIYDADTITCQIAALR-LFD----IVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALA 77
Cdd:COG0019 11 TIEGVDLAELAEEYGTPLYVYDEAALRRNLRALReAFPgsgaKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 78 SGFTPGlhnghaDIVFTADLLDHATLARVVELNI-PVNCGSMDMLDQLGTV----NPGHPVWLRINPGFGHGYSKKTNTG 152
Cdd:COG0019 91 AGFPPE------RIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELaaelGKRAPVGLRVNPGVDAGTHEYISTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 153 GEHSKHGIWHGDLVRACEKIKSN-SLALQGLHMHIGSGV-DYTHLQEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQ 230
Cdd:COG0019 165 GKDSKFGIPLEDALEAYRRAAALpGLRLVGLHFHIGSQIlDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 231 TGEPTIDTANYFSLWNAtrhAVEQLLKHPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGA 310
Cdd:COG0019 245 EGDEPPDLEELAAAIKE---ALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPALYGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 311 YHGMELIHSDGtavNGLQLDTVVAGPLCESGDVFTQGdggvvlhRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAE 390
Cdd:COG0019 322 YHPIVPVGRPS---GAEAETYDVVGPLCESGDVLGKD-------RSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAE 391
|
410 420
....*....|....*....|....*.
gi 479993029 391 VLMENGEPRLIRRRQTVAELLALEAV 416
Cdd:COG0019 392 VLVDDGEARLIRRRETYEDLLASEVL 417
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
12-414 |
4.71e-146 |
|
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: 421.31 E-value: 4.71e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 12 LAQQFGTPLWIYDADTITCQIAALRLFD----IVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhng 87
Cdd:TIGR01048 19 LAQEFGTPLYVYDEDTIRRRFRAYKEAFggrsLVCYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPP----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 88 hADIVFTADLLDHATLARVVELNIPVNCGSMDMLDQLGTVNPGH----PVWLRINPGFGHGYSKKTNTGGEHSKHGIWHG 163
Cdd:TIGR01048 94 -EKIVFSGNGKSRAELERALELGICINVDSFSELERLNEIAPELgkkaRISLRVNPGVDAKTHPYISTGLKDSKFGIDVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 164 DLVRACEK-IKSNSLALQGLHMHIGSGVDYTHLQEVCGAML-KLVEVVnAQGLDLHAISAGGGLSVPYQTGEPTIDTANY 241
Cdd:TIGR01048 173 EALEAYLYaLQLPHLELVGIHCHIGSQITDLSPFVEAAEKVvKLAESL-AEGIDLEFLDLGGGLGIPYTPEEEPPDLSEY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 242 FSLWNATRHAvEQLLKHPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELIhsdg 321
Cdd:TIGR01048 252 AQAILNALEG-YADLGLDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPALYGAYHHIIVL---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 322 TAVNGLQLDTV-VAGPLCESGDVFTQGdggvvlhRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVLMENGEPRL 400
Cdd:TIGR01048 327 NRTNDAPTEVAdVVGPVCESGDVLAKD-------RELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARL 399
|
410
....*....|....
gi 479993029 401 IRRRQTVAELLALE 414
Cdd:TIGR01048 400 IRRRETYEDLWALE 413
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
16-392 |
8.72e-145 |
|
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: 416.50 E-value: 8.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 16 FGTPLWIYDADTITCQIAALR-LFD----IVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghAD 90
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKeAFSgpgfKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPP------ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 91 IVFTADLLDHATLARVVELNI-PVNCGSMDMLDQLGTVNP----GHPVWLRINPGFGHGYSKKTNTGGEHSKHGIWHGDL 165
Cdd:cd06828 75 IVFTGNGKSDEELELALELGIlRINVDSLSELERLGEIAPelgkGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 166 VRACEKIK-SNSLALQGLHMHIGSGV-DYTHLQEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQTGEPTIDTANYFS 243
Cdd:cd06828 155 LEAYRRAKeLPGLKLVGLHCHIGSQIlDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDEPLDIEEYAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 244 LWNAtrhAVEQLLK--HPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELIHSDG 321
Cdd:cd06828 235 AIAE---ALKELCEggPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPG 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479993029 322 TavnGLQLDTVVAGPLCESGDVFTQgdggvvlHRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVL 392
Cdd:cd06828 312 E---GETEKVDVVGPICESGDVFAK-------DRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVL 372
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
20-372 |
4.61e-103 |
|
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent decarboxylases act on ornithine, lysine, arginine and related substrates.
Pssm-ID: 459745 [Multi-domain] Cd Length: 340 Bit Score: 309.03 E-value: 4.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 20 LWIYDADTITCQIAALR--LFDIVR--FAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVFTA 95
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKaaLPPRVKifYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDP------ERIVFAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 96 DLLDHATLARVVELNIP-VNCGSMDMLDQLGTVNPGH--PVWLRINPGFGHGYSKkTNTGGEHSKHGIWHGDLVRACEKI 172
Cdd:pfam00278 75 PGKTDSEIRYALEAGVLcFNVDSEDELEKIAKLAPELvaRVALRINPDVDAGTHK-ISTGGLSSKFGIDLEDAPELLALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 173 KSNSLALQGLHMHIGSGV-DYTHLQEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQTGEPTiDTANYFSLWNAtrhA 251
Cdd:pfam00278 154 KELGLNVVGVHFHIGSQItDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPP-DFEEYAAAIRE---A 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 252 VEQLLKHPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELIHSDGTAVnglQLDT 331
Cdd:pfam00278 230 LDEYFPPDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPIPVVKEPGEGP---LETY 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 479993029 332 VVAGPLCESGDVFTQgdggvvlHRSLPQAQVGDLLVLHDTG 372
Cdd:pfam00278 307 DVVGPTCESGDVLAK-------DRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
18-393 |
4.09e-98 |
|
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: 297.29 E-value: 4.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 18 TPLWIYDADTITCQIAALR--LFDIVR--FAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVF 93
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKeaLPSGVKlfYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPP------ERIIF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 94 TADLLDHATLARVVELNI-PVNCGSMDMLDQLGTV----NPGHPVWLRINPGFGHGySKKTNTGGEHSKHGIWHGDLVRA 168
Cdd:cd06810 75 TGPAKSVSEIEAALASGVdHIVVDSLDELERLNELakklGPKARILLRVNPDVSAG-THKISTGGLKSKFGLSLSEARAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 169 CEKIKSNSLALQGLHMHIGSGV-DYTHLQEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQTGEPTIDTanYFSLWNA 247
Cdd:cd06810 154 LERAKELDLRLVGLHFHVGSQIlDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDFEE--YAALINP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 248 TRhAVEQLLKHPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPAL-YGAYHGMELIHSDGTAVNG 326
Cdd:cd06810 232 LL-KKYFPNDPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPGPDEPL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479993029 327 LQldTVVAGPLCESGDVFTQgdggvvlHRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVLM 393
Cdd:cd06810 311 VP--ATLAGPLCDSGDVIGR-------DRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
19-393 |
1.34e-74 |
|
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: 236.95 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 19 PLWIYDADTITC---QIAALRLFDIVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASgfTPGLHNGHadIVFTA 95
Cdd:cd06840 13 PCYVYDLETVRArarQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKL--FPDLDPRR--VLFTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 96 DLLDHATLARVVELNIPVNCGSMDMLDQLGTVNPGHPVWLRINPGFGHGYSKKTNTGGEHSKHGIWHGDLVRACEKIKSN 175
Cdd:cd06840 89 NFAARSEYEQALELGVNVTVDNLHPLREWPELFRGREVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELDEARDLAKKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 176 SLALQGLHMHIGSGV-DYTHLQEVCGAMLKLVEvvnaQGLDLHAISAGGGLSVPYQTGEPTIDtanyFSLWNATRHAVEQ 254
Cdd:cd06840 169 GIIVIGLHAHSGSGVeDTDHWARHGDYLASLAR----HFPAVRILNVGGGLGIPEAPGGRPID----LDALDAALAAAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 255 LlkHP-VKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELIHSDGTAVNGLqldTVV 333
Cdd:cd06840 241 A--HPqYQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLSRLDEPPAGN---ADV 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 334 AGPLCESGDVFTQgdggvvlHRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVLM 393
Cdd:cd06840 316 VGPICESGDVLGR-------DRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
17-394 |
6.37e-74 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 247.30 E-value: 6.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 17 GTPLWIYDADTITC---QIAALRLFDIVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASgfTPGLHNghADIVF 93
Cdd:PRK08961 502 GSPCYVYHLPTVRArarALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFEL--FPELSP--ERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 94 TADLLDHATLARVVELNIPVNCGSMDMLDQLGTVNPGHPVWLRINPGFGHGYSKKTNTGGEHSKHGIWHGDLVRACEKIK 173
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGVTVTLDNVEPLRNWPELFRGREVWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRIDEFVDLAK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 174 SNSLALQGLHMHIGSGV-DYTHLQEVCgamLKLVEVVNAQGlDLHAISAGGGLSVPYQTGEPTIDtanyFSLWNATRHAV 252
Cdd:PRK08961 658 TLGITVVGLHAHLGSGIeTGEHWRRMA---DELASFARRFP-DVRTIDLGGGLGIPESAGDEPFD----LDALDAGLAEV 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 253 EQLlkHP-VKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGME-LIHSDGTAVnglQLD 330
Cdd:PRK08961 730 KAQ--HPgYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEIVnLSRLDEPAA---GTA 804
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479993029 331 TVVaGPLCESGDVFTQGdggvvlhRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVLME 394
Cdd:PRK08961 805 DVV-GPICESSDVLGKR-------RRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
31-272 |
2.84e-53 |
|
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: 177.47 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 31 QIAALRLFD--IVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVFTADLLDHATLARVVE 108
Cdd:pfam02784 8 HRRWKKALPriKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPP------ERIIFANPCKQRSFLRYALE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 109 LNIP-VNCGSMDMLDQLGTVNPGHPVWLRINPGFGHGYSKKTntggehSKHGIWHGDLVRACEK-IKSNSLALQGLHMHI 186
Cdd:pfam02784 82 VGVGcVTVDNVDELEKLARLAPEARVLLRIKPDDSAATCPLS------SKFGADLDEDVEALLEaAKLLNLQVVGVSFHV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 187 GSGVD-----YTHLQEVCGAMLKLVEVvnaqGLDLHAISAGGGLSVPYQTGEPTIDTANYFSLWNAtrhAVEQLLKH--P 259
Cdd:pfam02784 156 GSGCTdaeafVLALEDARGVFDQGAEL----GFNLKILDLGGGFGVDYTEGEEPLDFEEYANVINE---ALEEYFPGdpG 228
|
250
....*....|...
gi 479993029 260 VKLEIEPGRYLMA 272
Cdd:pfam02784 229 VTIIAEPGRYFVA 241
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
18-406 |
2.24e-49 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 172.28 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 18 TPLWIYDADTITCQIAALR-----LFDIVRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPG--LHNGHAD 90
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKealegLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTrcIFNGNGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 91 ivftadLLDHATLArvVELNIPVNCGSMDMLDQLGTV----NPGHPVWLRINPGFG---HGYskkTNTGGEHSKHGIWHG 163
Cdd:PLN02537 98 ------LLEDLVLA--AQEGVFVNVDSEFDLENIVEAariaGKKVNVLLRINPDVDpqvHPY---VATGNKNSKFGIRNE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 164 DLVRACEKIKS--NSLALQGLHMHIGSGVDYTHL-QEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQTGEPTIDTAN 240
Cdd:PLN02537 167 KLQWFLDAVKAhpNELKLVGAHCHLGSTITKVDIfRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYYHAGAVLPTPR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 241 yfSLWNATRHAVeqlLKHPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELIHSD 320
Cdd:PLN02537 247 --DLIDTVRELV---LSRDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 321 GTAVNGLQLDTVvaGPLCESGDVFTQGdggvvlhRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIAEVLMEN-GEPR 399
Cdd:PLN02537 322 PPDAEVSTFDVV--GPVCESADFLGKD-------RELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEdGSIT 392
|
....*..
gi 479993029 400 LIRRRQT 406
Cdd:PLN02537 393 KIRHAET 399
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
12-392 |
1.64e-47 |
|
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: 166.62 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 12 LAQQFGTPLWIYDADTITCQIAALR-----LFDIvRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhn 86
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRaalppAIEI-YYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPP---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 87 ghADIVFTADLLDHATLARVVELNI-PVNCGSMDMLDQLGTVNPGH----PVWLRINPGFGHGYSKKTNTGGEhSKHGIW 161
Cdd:cd06839 76 --EKILFAGPGKSDAELRRAIEAGIgTINVESLEELERIDALAEEHgvvaRVALRINPDFELKGSGMKMGGGP-SQFGID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 162 HGDLVRACEKIKSN-SLALQGLHMHIGS-GVDYTHLQEVCGAMLKLV-EVVNAQGLDLHAISAGGGLSVPYQTGEPTIDT 238
Cdd:cd06839 153 VEELPAVLARIAALpNLRFVGLHIYPGTqILDADALIEAFRQTLALAlRLAEELGLPLEFLDLGGGFGIPYFPGETPLDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 239 ANYFSLWNATRHAVEQLLKHPvKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVrpALYGAYhGMEL-- 316
Cdd:cd06839 233 EALGAALAALLAELGDRLPGT-RVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMHHHL--AASGNF-GQVLrr 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 317 ---IHSDGTAVNGLQLDTVVAGPLCESGDVFtqGDGGvvlhrSLPQAQVGDLLVLHDTGAYGASMS-SNYNARPLIAEVL 392
Cdd:cd06839 309 nypLAILNRMGGEERETVTVVGPLCTPLDLL--GRNV-----ELPPLEPGDLVAVLQSGAYGLSASpLAFLSHPAPAEVL 381
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
43-389 |
6.56e-38 |
|
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: 140.99 E-value: 6.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 43 FAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVFTADLLDHATLARVVELNIPVNcgsMDMLD 122
Cdd:cd06836 32 FAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPP------ERIVFDSPAKTRAELREALELGVAIN---IDNFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 123 QLGTV--------NPGHPVWLRINPGFGHGYSKKTNTGGEHSKHGI----WHGDLVRacEKIKSNSLaLQGLHMHIGS-G 189
Cdd:cd06836 103 ELERIdalvaefkEASSRIGLRVNPQVGAGKIGALSTATATSKFGValedGARDEII--DAFARRPW-LNGLHVHVGSqG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 190 VDYTHLQEVCGAMLKLVEVVNAQGLDLHA--ISAGGGLSVPYqtgEPTIDTANYFSLWNATRHAVEQLLKHPVKLEIEPG 267
Cdd:cd06836 180 CELSLLAEGIRRVVDLAEEINRRVGRRQItrIDIGGGLPVNF---ESEDITPTFADYAAALKAAVPELFDGRYQLVTEFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 268 RYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVR----PALYgaYHGMELIHSDGTAVNGLQLDTVVAGPLCESGDV 343
Cdd:cd06836 257 RSLLAKCGTIVSRVEYTKSSGGRRIAITHAGAQVATRtayaPDDW--PLRVTVFDANGEPKTGPEVVTDVAGPCCFAGDV 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 479993029 344 ftqgdggVVLHRSLPQAQVGDLLVLHDTGAYGASMSSNYNARPLIA 389
Cdd:cd06836 335 -------LAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
12-396 |
1.25e-35 |
|
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: 134.70 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 12 LAQQFGTPLWIYDADTIT----CQIAALR-LFDIVRFAQ--KANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPGl 84
Cdd:cd06841 1 LLESYGSPFFVFDEDALRenyrELLGAFKkRYPNVVIAYsyKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 85 hnghaDIVFTADLLDHATLARVVELNIPVNCGSMDMLDQLGTVNPGH----PVWLRINpgfghgyskkTNTGGEH-SKHG 159
Cdd:cd06841 80 -----RIIFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELgrvaKVGIRLN----------MNYGNNVwSRFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 160 I---WHGDLVRACEKIK-SNSLALQGLHMHIGSGVDYthLQEVCGAMLKLVEVVN-AQGLDLHAISAGGG------LSVP 228
Cdd:cd06841 145 FdieENGEALAALKKIQeSKNLSLVGLHCHVGSNILN--PEAYSAAAKKLIELLDrLFGLELEYLDLGGGfpaktpLSLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 229 YQTGEPTIDTANYFslwnatRHAVEQLLKH-------PvKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFND 301
Cdd:cd06841 223 YPQEDTVPDPEDYA------EAIASTLKEYyankenkP-KLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 302 LvrPALYGAYHGMELIHSDgtAVNGLQLDTVVAGPLCesgdvfTQGDggvVLHRS--LPQAQVGDLLVLHDTGAYGASMS 379
Cdd:cd06841 296 I--PTIFWYHHPILVLRPG--KEDPTSKNYDVYGFNC------MESD---VLFPNvpLPPLNVGDILAIRNVGAYNMTQS 362
|
410
....*....|....*..
gi 479993029 380 SNYnARPLIAEVLMENG 396
Cdd:cd06841 363 NQF-IRPRPAVYLIDNN 378
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
41-268 |
9.06e-30 |
|
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: 114.72 E-value: 9.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 41 VRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVFTADLLDHATLARVVELN-IPVNCGSMD 119
Cdd:cd06808 18 LFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPP------EPILFLGPCKQVSELEDAAEQGvIVVTVDSLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 120 MLDQLGTVNPGHP----VWLRINPGFghgyskktntggEHSKHGIWHGDLVRACEKIKS-NSLALQGLHMHIGSGV-DYT 193
Cdd:cd06808 92 ELEKLEEAALKAGpparVLLRIDTGD------------ENGKFGVRPEELKALLERAKElPHLRLVGLHTHFGSADeDYS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479993029 194 HLQEVCGAMLKLVEVVNAQGLDLHAISAGGGLSVPYQtgeptidtanyfslwnatrhaveQLLKHPVKLEIEPGR 268
Cdd:cd06808 160 PFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYL-----------------------QELPLGTFIIVEPGR 211
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
17-383 |
5.30e-29 |
|
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: 116.05 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 17 GTPLWIYDADTITCQIAALR-LFDIVR--FAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTPglhnghADIVF 93
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKkALPRVRpfYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSP------ERIIF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 94 TADLLDHATLARVVELNIPV-NCGSMDMLDQLGTVNPGHPVWLRINPgfghgyskkTNTGGEHS---KHGIWHGDLVRAC 169
Cdd:cd00622 75 ANPCKSISDIRYAAELGVRLfTFDSEDELEKIAKHAPGAKLLLRIAT---------DDSGALCPlsrKFGADPEEARELL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 170 EKIKSNSLALQGLHMHIGSGVdyTHLQEVCGAMLK---LVEVVNAQGLDLHAISAGGGLSVPYQTGEPTIDtaNYFslwN 246
Cdd:cd00622 146 RRAKELGLNVVGVSFHVGSQC--TDPSAYVDAIADareVFDEAAELGFKLKLLDIGGGFPGSYDGVVPSFE--EIA---A 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 247 ATRHAVEQLLK-HPVKLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVM---VDAG----FNDlvrpALYGAYHGMELIH 318
Cdd:cd00622 219 VINRALDEYFPdEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRERwyyLNDGvygsFNE----ILFDHIRYPPRVL 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479993029 319 SDGTAvNGLQLDTVVAGPLCESGDVftqgdggVVLHRSLPQA-QVGDLLVLHDTGAYGASMSSNYN 383
Cdd:cd00622 295 KDGGR-DGELYPSSLWGPTCDSLDV-------IYEDVLLPEDlAVGDWLLFENMGAYTTAYASTFN 352
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
21-379 |
1.99e-21 |
|
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: 95.04 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 21 WIYDADTITCQIAALR--------LFdivrFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALAsgftpglHNGHADIV 92
Cdd:cd06843 5 YVYDLAALRAHARALRaslppgceLF----YAIKANSDPPILRALAPHVDGFEVASGGEIAHVRA-------AVPDAPLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 93 F-----TADLLDHAtLARVVELnipVNCGSMDMLDQLGTV----NPGHPVWLRINPGFGHGYSKKTNTGGEHSKHGIWHG 163
Cdd:cd06843 74 FggpgkTDSELAQA-LAQGVER---IHVESELELRRLNAVarraGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 164 DLVRACEKIK-SNSLALQGLHMHIGSG-VDYTHLQEVCGAMLKLVEVVNAQ-GLDLHAISAGGGLSVPYQTGEPTIDTAN 240
Cdd:cd06843 150 DLPDALELLRdLPNIRLRGFHFHLMSHnLDAAAHLALVKAYLETARQWAAEhGLDLDVVNVGGGIGVNYADPEEQFDWAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 241 YFSLWNATRHAVEQLLKhpvkLEIEPGRYLMAESGVLVTEVRATKQQGSNHFVMVDAGFNDLVRPALYGAYHGMELI--- 317
Cdd:cd06843 230 FCEGLDQLLAEYEPGLT----LRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFSVLpve 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479993029 318 -HSDGTAVNGLQLDTV-VAGPLCESGDvftqgdggvVLHRSLP--QAQVGDLLVLHDTGAYGASMS 379
Cdd:cd06843 306 eWPYPWPRPSVRDTPVtLVGQLCTPKD---------VLARDVPvdRLRAGDLVVFPLAGAYGWNIS 362
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
10-374 |
1.16e-16 |
|
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: 81.15 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 10 APLAQQFGTPLWIYDADTITCQIAALR-LFDI------VRFAQKANSNTHILRLMKQQGVVVDSVSLGEIERALASGFTP 82
Cdd:cd06842 2 VALVEAYGSPLNVLFPQTFRENIAALRaVLDRhgvdgrVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 83 glhnghADIVFTADLLDHATLARVVELNIPVNCGSMDMLDQLGTVNPGH-----PVWLRINPGFGHGyskktntggeHSK 157
Cdd:cd06842 82 ------DRIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALARGYttgpaRVLLRLSPFPASL----------PSR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 158 HGIWHGDLVRACEKIKS--NSLALQGLHMHIG--SGVDYTHLQEVCgamLKLVEVVNAQGLDLHAISAGGGLSVPY---- 229
Cdd:cd06842 146 FGMPAAEVRTALERLAQlrERVRLVGFHFHLDgySAAQRVAALQEC---LPLIDRARALGLAPRFIDIGGGFPVSYlada 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 230 ---------------------------QTGEPTIDTANYF--------------SLWNATRHAVEQLLKHPVKLEIEPGR 268
Cdd:cd06842 223 aeweaflaaltealygygrpltwrnegGTLRGPDDFYPYGqplvaadwlrailsAPLPQGRTIAERLRDNGITLALEPGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 269 YLMAESGVLVTEVRATKQQGS-NHFVMVD------AGFND--LVRPALYGAYHGMElihsDGTAVNGLqldtvVAGPLCE 339
Cdd:cd06842 303 ALLDQCGLTVARVAFVKQLGDgNHLIGLEgnsfsaCEFSSefLVDPLLIPAPEPTT----DGAPIEAY-----LAGASCL 373
|
410 420 430
....*....|....*....|....*....|....*...
gi 479993029 340 SGDVFTqgdggvvlHR--SLPQA-QVGDLLVLHDTGAY 374
Cdd:cd06842 374 ESDLIT--------RRkiPFPRLpKPGDLLVFPNTAGY 403
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
144-293 |
2.10e-11 |
|
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: 65.28 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 144 GYSKKTNTGGEHSKHGIWHGDLVRACEKIKSNSLA--LQGLHMHIGSGVDYTH-----LQEVCGAMLKLVevvnAQGLDL 216
Cdd:cd06830 150 GSGKWQESGGDRSKFGLTASEILEVVEKLKEAGMLdrLKLLHFHIGSQITDIRriksaLREAARIYAELR----KLGANL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 217 HAISAGGGLSVPY-QTGEPTIDTANY------FSLWNATRHAVEQL-LKHPVkLEIEPGRYLMAESGVLVTEVRATKQQG 288
Cdd:cd06830 226 RYLDIGGGLGVDYdGSRSSSDSSFNYsleeyaNDIVKTVKEICDEAgVPHPT-IVTESGRAIVAHHSVLIFEVLGVKRLA 304
|
....*
gi 479993029 289 SNHFV 293
Cdd:cd06830 305 DWYFC 309
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
150-281 |
4.56e-08 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 55.12 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 150 NTGGEHSKHGIWHGDLVRACEKIKSNSLA--LQGLHMHIGSGV----DYTH-LQEVC---------GAMLKLVEVvnaqg 213
Cdd:PRK05354 215 SSGGEKSKFGLSATEVLEAVERLREAGLLdcLQLLHFHLGSQIanirDIKTaVREAArfyvelrklGAPIQYLDV----- 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479993029 214 ldlhaisaGGGLSVPY-QTGEPTIDTANYfSLWNATRHAVEQL--------LKHPVkLEIEPGRYLMAESGVLVTEV 281
Cdd:PRK05354 290 --------GGGLGVDYdGTRSQSDSSVNY-SLQEYANDVVYTLkeiceehgVPHPT-IISESGRALTAHHAVLVFNV 356
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
128-374 |
1.86e-07 |
|
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: 52.55 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 128 NPGHPVWLRINPGFGHGYSKKTNTGGEHSKHGiwhgdlVRACEKIKSNSLALQGLHMHIGSGVDYTHLQEvcgaMLKLVE 207
Cdd:cd06829 110 AAGISVGLRINPEYSEVETDLYDPCAPGSRLG------VTLDELEEEDLDGIEGLHFHTLCEQDFDALER----TLEAVE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 208 VVNAQGLD-LHAISAGGGL---SVPYQTgEPTIDTANYFSlwnaTRHAVEqllkhpvkLEIEPGRYLMAESGVLVTEVRA 283
Cdd:cd06829 180 ERFGEYLPqLKWLNLGGGHhitRPDYDV-DRLIALIKRFK----EKYGVE--------VYLEPGEAVALNTGYLVATVLD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 284 TKQQGSNHfVMVDAGFN----DLV----RPALYGAYHGMELIHSdgtavnglqldTVVAGPLCESGDVFtqGDggvvlhR 355
Cdd:cd06829 247 IVENGMPI-AILDASATahmpDVLempyRPPIRGAGEPGEGAHT-----------YRLGGNSCLAGDVI--GD------Y 306
|
250 260
....*....|....*....|
gi 479993029 356 SLPQA-QVGDLLVLHDTGAY 374
Cdd:cd06829 307 SFDEPlQVGDRLVFEDMAHY 326
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
150-281 |
7.63e-07 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 51.25 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 150 NTGGEHSKHGIWHGDLVRACEKIKSNSL--ALQGLHMHIGSGVdyTHLQEVCGAMLKL----VEVVNAqGLDLHAISAGG 223
Cdd:COG1166 211 NSGGERSKFGLSASEILEVVERLKEAGMldCLQLLHFHLGSQI--PNIRDIKRAVREAarfyAELRKL-GAPIEYLDVGG 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 224 GLSVPYqTGEPTIDTA--NYfSLWNATRHAVEQL--------LKHPVkleI--EPGRYLMAESGVLVTEV 281
Cdd:COG1166 288 GLGVDY-DGSRSNSDSsmNY-SLQEYANDVVYAIkevcdeagVPHPT---IisESGRALTAHHSVLIFNV 352
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
151-281 |
3.08e-04 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 42.75 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479993029 151 TGGEHSKHGIWHGDLVRACEKIKSNSL--ALQGLHMHIGSGVDYTHL-----QEVCGAMLKLVEVvnaqGLDLHAISAGG 223
Cdd:PLN02439 153 TSGEKGKFGLTATEIVRVVRKLRKEGMldCLQLLHFHIGSQIPSTSLlkdgvSEAAQIYCELVRL----GAPMRVIDIGG 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479993029 224 GLSVPY---QTGEPTIDTAnyFSLWN-------ATRHAVEQL-LKHPVkLEIEPGRYLMAESGVLVTEV 281
Cdd:PLN02439 229 GLGIDYdgsKSGSSDMSVA--YSLEEyanavvaAVRDVCDRKgVKHPV-ICSESGRALVSHHSVLIFEA 294
|
|
| |
