|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
9-385 |
4.07e-135 |
|
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: 392.20 E-value: 4.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 9 LHRIAERYSTPTYVYDLDAIGDRVARLRAALPT--AELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEG 86
Cdd:COG0019 17 LAELAEEYGTPLYVYDEAALRRNLRALREAFPGsgAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGELRLALAAGFPPE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 87 RILLGGPRQDPPLVAAA--WGVGWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPRTHEHLATGAARSKFGMPFGE 163
Cdd:COG0019 97 RIVFSGNGKSEEELEEAleLGVGHINVDSLSELERLAELAAELGKRaPVGLRVNPGVDAGTHEYISTGGKDSKFGIPLED 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 164 LAALGAAL----GEHLAGFHVHIGSQITELGAYEPVFAQLGALLTRFPHA----DTLDLGGGFAVP------GFALPEFS 229
Cdd:COG0019 177 ALEAYRRAaalpGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELgidlEWLDLGGGLGIPytegdePPDLEELA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 230 ARVRAFLAQVPFR--RLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQHPVRVLGAA-DGAS 305
Cdd:COG0019 257 AAIKEALEELCGLgpELILEPGRALVGNAGVLLTRVLDVKENGGRRfVIVDAGMNDLMRPALYGAYHPIVPVGRPsGAEA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 306 GSADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVVAGGEVRLARRRETPDDLVQLEL 385
Cdd:COG0019 337 ETYDVVGPLCESGDVLGKDRSLPPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEARLIRRRETYEDLLASEV 416
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
16-363 |
5.18e-116 |
|
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: 342.16 E-value: 5.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 16 YSTPTYVYDLDAIGDRVARLRAALPTAELL--YAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGG- 92
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKicYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 93 --PRQDPPLvAAAWGVGWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPRTHEHLATGAARSKFGMPFGEL-AALG 168
Cdd:cd06828 81 gkSDEELEL-ALELGILRINVDSLSELERLGEIAPELGKGaPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQAlEAYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 169 AALGEH---LAGFHVHIGSQITELGAY----EPVFAQLGALLTRFPHADTLDLGGGFAVP------GFALPEFSARVRA- 234
Cdd:cd06828 160 RAKELPglkLVGLHCHIGSQILDLEPFveaaEKLLDLAAELRELGIDLEFLDLGGGLGIPyrdedePLDIEEYAEAIAEa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 235 ---FLAQVPFRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQHPVRVLGAAD-GASGSAD 309
Cdd:cd06828 240 lkeLCEGGPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTfVGVDAGMNDLIRPALYGAYHEIVPVNKPGeGETEKVD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502941680 310 LDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVV 363
Cdd:cd06828 320 VVGPICESGDVFAKDRELPEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
9-385 |
3.55e-111 |
|
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: 331.18 E-value: 3.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 9 LHRIAERYSTPTYVYDLDAIGDRVARLRAALPTAELL-YAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGR 87
Cdd:TIGR01048 16 LLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSLVcYAVKANSNLAVLRLLAELGSGFDVVSGGELYRALAAGFPPEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 88 ILLGGPRQDPPLVAAAWGVG-WVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPRTHEHLATGAARSKFGMPFGEL- 164
Cdd:TIGR01048 96 IVFSGNGKSRAELERALELGiCINVDSFSELERLNEIAPELGKKaRISLRVNPGVDAKTHPYISTGLKDSKFGIDVEEAl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 165 -AALGAALGEHL--AGFHVHIGSQITELGAYEPVFAQLGALLTRFP---HADTLDLGGGFAVP---GFALPEFSARVRAF 235
Cdd:TIGR01048 176 eAYLYALQLPHLelVGIHCHIGSQITDLSPFVEAAEKVVKLAESLAegiDLEFLDLGGGLGIPytpEEEPPDLSEYAQAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 236 LAQV-------PFRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQHPVRVLGA-ADGASG 306
Cdd:TIGR01048 256 LNALegyadlgLDPKLILEPGRSIVANAGVLLTRVGFVKETGSRNfVIVDAGMNDLIRPALYGAYHHIIVLNRtNDAPTE 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502941680 307 SADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVVAGGEVRLARRRETPDDLVQLEL 385
Cdd:TIGR01048 336 VADVVGPVCESGDVLAKDRELPEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARLIRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
21-342 |
1.18e-98 |
|
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: 296.71 E-value: 1.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 21 YVYDLDAIGDRVARLRAAL-PTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQDPPL 99
Cdd:pfam00278 2 YVYDLATLRRNYRRWKAALpPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTDSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 100 VAAA--WGVGWVSLDNPSQWRGWQRFAAREGApRFLLRLNPGLDPRTHeHLATGAARSKFGMP---FGELAALGAALGEH 174
Cdd:pfam00278 82 IRYAleAGVLCFNVDSEDELEKIAKLAPELVA-RVALRINPDVDAGTH-KISTGGLSSKFGIDledAPELLALAKELGLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 175 LAGFHVHIGSQITELGAYEPVFAQLGAL---LTRFPHA-DTLDLGGGFAVP-----GFALPEFSARVRAFLAQV--PFRR 243
Cdd:pfam00278 160 VVGVHFHIGSQITDLEPFVEALQRARELfdrLRELGIDlKLLDIGGGFGIPyrdepPPDFEEYAAAIREALDEYfpPDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 244 LLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQHPVRVLGA-ADGASGSADLDGPLCENADRL 321
Cdd:pfam00278 240 IIAEPGRYLVANAGVLVTRVIAVKTGGGKTfVIVDAGMNDLFRPALYDAYHPIPVVKEpGEGPLETYDVVGPTCESGDVL 319
|
330 340
....*....|....*....|.
gi 502941680 322 ARGVALPALTPGTLLAVEQAG 342
Cdd:pfam00278 320 AKDRELPELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
18-363 |
1.84e-84 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.
Pssm-ID: 143485 [Multi-domain] Cd Length: 368 Bit Score: 261.47 E-value: 1.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 18 TPTYVYDLDAIGDRVARLRAALPT-AELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQD 96
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPSgVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 97 PPLV--AAAWGVGWVSLDNPSQWRGWQRFAAREG-APRFLLRLNPGLDPRTHEHlATGAARSKFGMPFGELAALGAALGE 173
Cdd:cd06810 81 VSEIeaALASGVDHIVVDSLDELERLNELAKKLGpKARILLRVNPDVSAGTHKI-STGGLKSKFGLSLSEARAALERAKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 174 H---LAGFHVHIGSQITELGAYEPVFAQLGALLTRFPHAD----TLDLGGGFAVP----GFALPEFSARVRAFLAQ---- 238
Cdd:cd06810 160 LdlrLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGfpleMLDLGGGLGIPydeqPLDFEEYAALINPLLKKyfpn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 239 VPFRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPAL-YGAQHPVRVLGAA--DGASGSADLDGPL 314
Cdd:cd06810 240 DPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFfAVVDGGMNHSFRPALaYDAYHPITPLKAPgpDEPLVPATLAGPL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502941680 315 CENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVV 363
Cdd:cd06810 320 CDSGDVIGRDRLLPELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
5-363 |
8.66e-70 |
|
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: 223.47 E-value: 8.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 5 RAALLhRIAERYStPTYVYDLDAIGDRVARLRAALPTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRA--G 82
Cdd:cd06840 1 RDALL-RLAPDVG-PCYVYDLETVRARARQVSALKAVDSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 83 FPEGRILLGGPRQDPPLVAAAWGVG-WVSLDNPSQWRGW-QRFAAREgaprFLLRLNPGLDPRTHEHLATGAARSKFGMP 160
Cdd:cd06840 79 LDPRRVLFTPNFAARSEYEQALELGvNVTVDNLHPLREWpELFRGRE----VILRIDPGQGEGHHKHVRTGGPESKFGLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 161 ---FGELAALGAALGEHLAGFHVHIGSQITELGAYEPVFAQLGALLTRFPHADTLDLGGGFAVP------GFALPEFSAR 231
Cdd:cd06840 155 vdeLDEARDLAKKAGIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHFPAVRILNVGGGLGIPeapggrPIDLDALDAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 232 VRAFLAQVPFRRLLLEPGRFLVAESGVLLTRVLHVKEGP-VRHVIADAGMADLLRPALYGAQHPVRVLGAAD-GASGSAD 309
Cdd:cd06840 235 LAAAKAAHPQYQLWMEPGRFIVAESGVLLARVTQIKHKDgVRFVGLETGMNSLIRPALYGAYHEIVNLSRLDePPAGNAD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502941680 310 LDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVV 363
Cdd:cd06840 315 VVGPICESGDVLGRDRLLPETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
5-364 |
7.21e-69 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 232.28 E-value: 7.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 5 RAALLHRIAERysTPTYVYDLDAIGDRVARLRAALPTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAgFP 84
Cdd:PRK08961 492 RARLLTLSDAG--SPCYVYHLPTVRARARALAALAAVDQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFEL-FP 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 85 E---GRILLGGPRQDPPLVAAAWGVG-WVSLDNPSQWRGW-QRFAAREgaprFLLRLNPGLDPRTHEHLATGAARSKFGM 159
Cdd:PRK08961 569 ElspERVLFTPNFAPRAEYEAAFALGvTVTLDNVEPLRNWpELFRGRE----VWLRIDPGHGDGHHEKVRTGGKESKFGL 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 160 P---FGELAALGAALGEHLAGFHVHIGSQITELGAYEPVFAQLGALLTRFPHADTLDLGGGFAVP------GFALPEFSA 230
Cdd:PRK08961 645 SqtrIDEFVDLAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPDVRTIDLGGGLGIPesagdePFDLDALDA 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 231 RVRAFLAQVPFRRLLLEPGRFLVAESGVLLTRVLHVKE-GPVRHVIADAGMADLLRPALYGAQHPVRVLGAADG-ASGSA 308
Cdd:PRK08961 725 GLAEVKAQHPGYQLWIEPGRYLVAEAGVLLARVTQVKEkDGVRRVGLETGMNSLIRPALYGAYHEIVNLSRLDEpAAGTA 804
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502941680 309 DLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVVA 364
Cdd:PRK08961 805 DVVGPICESSDVLGKRRRLPATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
12-363 |
3.33e-66 |
|
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: 214.77 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 12 IAERYSTPTYVYDLDAIGDRVARLRAALPTA-ELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILL 90
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAALPPAiEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKILF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 91 GGP-RQDPPLVAA-AWGVGWVSLDNPSQWRGWQRFAAREG-APRFLLRLNPGLDPRTHEHLATGAArSKFGMP----FGE 163
Cdd:cd06839 81 AGPgKSDAELRRAiEAGIGTINVESLEELERIDALAEEHGvVARVALRINPDFELKGSGMKMGGGP-SQFGIDveelPAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 164 LAALGAALGEHLAGFHVHIGSQITELGAYEPVFAQLGALLTRFPHA-----DTLDLGGGFAVPGFA------LPEFSARV 232
Cdd:cd06839 160 LARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLAEElglplEFLDLGGGFGIPYFPgetpldLEALGAAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 233 RAFLAQVPFR----RLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQH-----PVRVLGAAD 302
Cdd:cd06839 240 AALLAELGDRlpgtRVVLELGRYLVGEAGVYVTRVLDRKVSRGETfLVTDGGMHHHLAASGNFGQVlrrnyPLAILNRMG 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502941680 303 G-ASGSADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGF-AMASNYASSLRPAEVVV 363
Cdd:cd06839 320 GeERETVTVVGPLCTPLDLLGRNVELPPLEPGDLVAVLQSGAYGLsASPLAFLSHPAPAEVLV 382
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
18-379 |
1.07e-50 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 174.98 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 18 TPTYVYDLDAIGDRVARLRAALPTAELL--YAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQ 95
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALEGLRSIigYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 96 DPP--LVAAAWGVgWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPRTHEHLATGAARSKFGMPFGELAALGAALG 172
Cdd:PLN02537 98 LLEdlVLAAQEGV-FVNVDSEFDLENIVEAARIAGKKvNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 173 EH-----LAGFHVHIGSQITELGayepVFAQLGALLTRFP--------HADTLDLGGGFAV----PGFALP---EFSARV 232
Cdd:PLN02537 177 AHpnelkLVGAHCHLGSTITKVD----IFRDAAVLMVNYVdeiraqgfELSYLNIGGGLGIdyyhAGAVLPtprDLIDTV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 233 RAFLAQVPFRrLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGA-QHPVRVLGAADGASGSA-D 309
Cdd:PLN02537 253 RELVLSRDLT-LIIEPGRSLIANTCCFVNRVTGVKTNGTKNfIVIDGSMAELIRPSLYDAyQHIELVSPPPPDAEVSTfD 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502941680 310 LDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPAEVVVA-GGEVRLARRRETPDD 379
Cdd:PLN02537 332 VVGPVCESADFLGKDRELPTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEeDGSITKIRHAETFDD 402
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
12-366 |
5.02e-49 |
|
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: 169.75 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 12 IAERYSTPTYVYDLDAIGDRVARLRAAL----PTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGR 87
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFkkryPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 88 ILLGGPRQDPP--LVAAAWGvGWVSLDNPSQWRGWQRFAAREGA-PRFLLRLNpgldprtheHLATGAARSKFGMPFGEL 164
Cdd:cd06841 81 IIFNGPYKSKEelEKALEEG-ALINIDSFDELERILEIAKELGRvAKVGIRLN---------MNYGNNVWSRFGFDIEEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 165 AALGAALGEH-------LAGFHVHIGSQITELGAYEPVFAQLGALLTRF--PHADTLDLGGGFAV---------PGFALP 226
Cdd:cd06841 151 GEALAALKKIqesknlsLVGLHCHVGSNILNPEAYSAAAKKLIELLDRLfgLELEYLDLGGGFPAktplslaypQEDTVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 227 EFSARVRAFLAQV--------PFRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRHV-IADAGMADLLRPALYgaQHPVRV 297
Cdd:cd06841 231 DPEDYAEAIASTLkeyyankeNKPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIaVTDAGINNIPTIFWY--HHPILV 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502941680 298 L--GAADGASGSADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYgFAMASNYASSLRPAEVVVAGG 366
Cdd:cd06841 309 LrpGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPLNVGDILAIRNVGAY-NMTQSNQFIRPRPAVYLIDNN 378
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
18-351 |
2.63e-45 |
|
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: 159.58 E-value: 2.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 18 TPTYVYDLDAIGDRVARLRAALPTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGP-RQD 96
Cdd:cd00622 2 TPFLVVDLGDVVRKYRRWKKALPRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPcKSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 97 PPLVAAAW-GVGWVSLDNPSQWRGWQRFAarEGApRFLLRL---NPGldprthehlatgaARSKFGMPFG-------ELA 165
Cdd:cd00622 82 SDIRYAAElGVRLFTFDSEDELEKIAKHA--PGA-KLLLRIatdDSG-------------ALCPLSRKFGadpeearELL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 166 ALGAALGEHLAGFHVHIGSQITELGAYEP-------VFAQLGALLtrfPHADTLDLGGGF----AVPGFALPEFSARVRA 234
Cdd:cd00622 146 RRAKELGLNVVGVSFHVGSQCTDPSAYVDaiadareVFDEAAELG---FKLKLLDIGGGFpgsyDGVVPSFEEIAAVINR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 235 FLAQVPFR---RLLLEPGRFLVAESGVLLTRVLHVKE----GPVRHVIADAGMADLLRPALYGAQH-PVRVL--GAADGA 304
Cdd:cd00622 223 ALDEYFPDegvRIIAEPGRYLVASAFTLAVNVIAKRKrgddDRERWYYLNDGVYGSFNEILFDHIRyPPRVLkdGGRDGE 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502941680 305 SGSADLDGPLCENADRLARGVALPA-LTPGTLLAVEQAGAYGFAMASN 351
Cdd:cd00622 303 LYPSSLWGPTCDSLDVIYEDVLLPEdLAVGDWLLFENMGAYTTAYAST 350
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
22-359 |
9.49e-42 |
|
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: 150.62 E-value: 9.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 22 VYDLDAIGDRVARLRAALPTAEL-LYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQDPPLV 100
Cdd:cd06836 7 LYDLDGFRALVARLTAAFPAPVLhTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 101 AAAWGVG-WVSLDNPSQwrgWQRFAA-----REGAPRFLLRLNPGLDPRTHEHLATGAARSKFGMPFGELA--ALGAALG 172
Cdd:cd06836 87 REALELGvAINIDNFQE---LERIDAlvaefKEASSRIGLRVNPQVGAGKIGALSTATATSKFGVALEDGArdEIIDAFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 173 EH--LAGFHVHIGSQITEL-------GAYEPVFAQLGALLTRfPHADTLDLGGGFAVpGFA----LPEFSARVRAFLAQV 239
Cdd:cd06836 164 RRpwLNGLHVHVGSQGCELsllaegiRRVVDLAEEINRRVGR-RQITRIDIGGGLPV-NFEsediTPTFADYAAALKAAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 240 P-----FRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRHV-IADAGMADLLRPALYGAQHPVRVLG------AADGASGS 307
Cdd:cd06836 242 PelfdgRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIaITHAGAQVATRTAYAPDDWPLRVTVfdangePKTGPEVV 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502941680 308 ADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPA 359
Cdd:cd06836 322 TDVAGPCCFAGDVLAKERALPPLEPGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
19-345 |
2.56e-41 |
|
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: 149.35 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 19 PTYVYDLDAIGDRVARLRAALPT-AELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAgFPEGRILLGGPRQDP 97
Cdd:cd06843 3 CAYVYDLAALRAHARALRASLPPgCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 98 PLVAAA--WGVGWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPRTHEHLATGAARSKFGMPFGELAALGAALGE- 173
Cdd:cd06843 82 SELAQAlaQGVERIHVESELELRRLNAVARRAGRTaPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 174 ---HLAGFHVHIGS-------QITELGAY---EPVFAQLGALltrfpHADTLDLGGGFAVP------GFALPEFSARVRA 234
Cdd:cd06843 162 pniRLRGFHFHLMShnldaaaHLALVKAYletARQWAAEHGL-----DLDVVNVGGGIGVNyadpeeQFDWAGFCEGLDQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 235 FLAQ-VPFRRLLLEPGRFLVAESGVLLTRVLHVKEGPVRH-VIADAGMADLLRPALYGAQHPVRVLGAAD---------G 303
Cdd:cd06843 237 LLAEyEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWfAVLRGGTHHFRLPAAWGHNHPFSVLPVEEwpypwprpsV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502941680 304 ASGSADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYG 345
Cdd:cd06843 317 RDTPVTLVGQLCTPKDVLARDVPVDRLRAGDLVVFPLAGAYG 358
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
28-250 |
2.77e-27 |
|
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: 107.40 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 28 IGDRVARLRAALPT-AELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQDPPLV--AAAW 104
Cdd:cd06808 1 IRHNYRRLREAAPAgITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELedAAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 105 GVGWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNPGLDPrthehlatgaarSKFGMPFGELAALGAALGEH----LAGFH 179
Cdd:cd06808 81 GVIVVTVDSLEELEKLEEAALKAGPPaRVLLRIDTGDEN------------GKFGVRPEELKALLERAKELphlrLVGLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502941680 180 VHIGSQITELGAYEPVFAQLGALL----TRFPHADTLDLGGGFAVPGFALPEfsarvraflaqvPFRRLLLEPGR 250
Cdd:cd06808 149 THFGSADEDYSPFVEALSRFVAALdqlgELGIDLEQLSIGGSFAILYLQELP------------LGTFIIVEPGR 211
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
25-254 |
2.55e-25 |
|
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: 102.74 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 25 LDAIGDRVARLRAALPTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQDPPLV--AA 102
Cdd:pfam02784 1 LGSIERRHRRWKKALPRIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLryAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 103 AWGVGWVSLDNPSQWRGWQRFAARegaPRFLLRLNPGLDPRTHEHlatgaaRSKFGMPFGEL--AALGAALGEHL--AGF 178
Cdd:pfam02784 81 EVGVGCVTVDNVDELEKLARLAPE---ARVLLRIKPDDSAATCPL------SSKFGADLDEDveALLEAAKLLNLqvVGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 179 HVHIGSQITELGAY-------EPVFAQLGALLTRFPHadtLDLGGGFAV------PGFALPEFSARVRAFLAQV----PF 241
Cdd:pfam02784 152 SFHVGSGCTDAEAFvlaledaRGVFDQGAELGFNLKI---LDLGGGFGVdytegeEPLDFEEYANVINEALEEYfpgdPG 228
|
250
....*....|...
gi 502941680 242 RRLLLEPGRFLVA 254
Cdd:pfam02784 229 VTIIAEPGRYFVA 241
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
9-344 |
5.81e-21 |
|
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: 93.86 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 9 LHRIAERYSTPTYVYDLDAIGDRVARLRAALPTA----ELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFP 84
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHgvdgRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 85 EGRILLGGPRQDPPLVAAAWGVG-WVSLDNPSQWRGWQRFAAREGAP--RFLLRLNPglDPRTHehlatgaaRSKFGMPF 161
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGaTIAVDSLDELDRLLALARGYTTGpaRVLLRLSP--FPASL--------PSRFGMPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 162 GELAALGAALGE-----HLAGFHVHIG--SQITELGAYEPVFAQLGALLTRFPHADTLDLGGGFAV-------------- 220
Cdd:cd06842 151 AEVRTALERLAQlrervRLVGFHFHLDgySAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVsyladaaeweafla 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 221 ----------PGFALPEFSARVRAFLAQVPF----------RRLL----------------------LEPGRFLVAESGV 258
Cdd:cd06842 231 altealygygRPLTWRNEGGTLRGPDDFYPYgqplvaadwlRAILsaplpqgrtiaerlrdngitlaLEPGRALLDQCGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 259 LLTRVLHVKE-GPVRHVIADAGMAD---------LLRPALYGAQHPVRvlgaaDGASGSADLDGPLCENADRLA-RGVAL 327
Cdd:cd06842 311 TVARVAFVKQlGDGNHLIGLEGNSFsacefssefLVDPLLIPAPEPTT-----DGAPIEAYLAGASCLESDLITrRKIPF 385
|
410
....*....|....*...
gi 502941680 328 PAL-TPGTLLAVEQAGAY 344
Cdd:cd06842 386 PRLpKPGDLLVFPNTAGY 403
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
149-268 |
4.75e-12 |
|
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: 66.83 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 149 ATGAARSKFGMPFGELAAL-----GAALGEHLAGFHVHIGSQITELGAYEP-------VFAQLGALltrFPHADTLDLGG 216
Cdd:cd06830 156 ESGGDRSKFGLTASEILEVveklkEAGMLDRLKLLHFHIGSQITDIRRIKSalreaarIYAELRKL---GANLRYLDIGG 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 217 GFAVP------------GFALPEFSARVRAFL------AQVPFRRLLLEPGRFLVAESGVLLTRVLHVKE 268
Cdd:cd06830 233 GLGVDydgsrsssdssfNYSLEEYANDIVKTVkeicdeAGVPHPTIVTESGRAIVAHHSVLIFEVLGVKR 302
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
109-294 |
2.66e-09 |
|
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: 57.95 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 109 VSLDNPSQWRGWQRFAAREGAPRfLLRLNPGLDPRTHEhLATGAAR-SKFGMPfgeLAALGAALGEHLAGFHVHI----- 182
Cdd:cd06829 93 IIFNSLSQLERFKDRAKAAGISV-GLRINPEYSEVETD-LYDPCAPgSRLGVT---LDELEEEDLDGIEGLHFHTlceqd 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 183 -GSQITELGAYEPVFAQLgalltrFPHADTLDLGGG--FAVPGFALPEFSARVRAFLAQVPFRrLLLEPGRFLVAESGVL 259
Cdd:cd06829 168 fDALERTLEAVEERFGEY------LPQLKWLNLGGGhhITRPDYDVDRLIALIKRFKEKYGVE-VYLEPGEAVALNTGYL 240
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502941680 260 LTRVLHVKEGPVRHVIADAG----MADLL----RPALYGAQHP 294
Cdd:cd06829 241 VATVLDIVENGMPIAILDASatahMPDVLempyRPPIRGAGEP 283
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
21-359 |
1.16e-07 |
|
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: 53.31 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 21 YVYDLDAIGDRVARLRAALPTAELLYAVKANPCGAVLRHLAAAGLGAEVISVGELARARRAGFPEGRILLGGPRQDPPLV 100
Cdd:cd06831 16 FVGDLGKIVKKHSQWQTVMAQIKPFYTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 101 --AAAWGVGWVSLDNPSQWRgwqRFAAREGAPRFLLrlnpgldprtheHLATGA--ARSKFGMPFG-------ELAALGA 169
Cdd:cd06831 96 kyAAKVGVNIMTCDNEIELK---KIARNHPNAKLLL------------HIATEDniGGEEMNMKFGttlkncrHLLECAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 170 ALGEHLAGFHVHIGSQITELGAY-------EPVFAQLGALLTRFphaDTLDLGGGFAVPGFALPEFSARVRAFLaQVPFR 242
Cdd:cd06831 161 ELDVQIVGVKFHVSSSCKEYQTYvhalsdaRCVFDMAEEFGFKM---NMLDIGGGFTGSEIQLEEVNHVIRPLL-DVYFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 243 -----RLLLEPGRFLVAESGVLLTRVLHVKEGPVRHVIADAGMAdllrpalyGAQHPVRVLGAADGASGS---------- 307
Cdd:cd06831 237 egsgiQIIAEPGSYYVSSAFTLAVNVIAKKAVENDKHLSSVEKN--------GSDEPAFVYYMNDGVYGSfasklsekln 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502941680 308 -----------------ADLDGPLCENADRLARGVALPALTPGTLLAVEQAGAYGFAMASNYASSLRPA 359
Cdd:cd06831 309 ttpevhkkykedeplftSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGAGSLHEPSTFNDFQRPA 377
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
24-174 |
2.02e-06 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 48.37 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 24 DLDAIGDRVARLRAALPTAELLYAV-KANPCGA----VLRHLAAAG---LGaeVISVGELARARRAGFPEGRILLGGPRQ 95
Cdd:pfam01168 2 DLDALRHNLRRLRRRAGPGAKLMAVvKANAYGHgaveVARALLEGGadgFA--VATLDEALELREAGITAPILVLGGFPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 96 DPPLVAAAWGVgWVSLDNPSQWRGWQRFAAREGAP-RFLLRLNpgldprthehlaTGAARSkfGMPFGELAALGAALGEH 174
Cdd:pfam01168 80 EELALAAEYDL-TPTVDSLEQLEALAAAARRLGKPlRVHLKID------------TGMGRL--GFRPEEALALLARLAAL 144
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
19-174 |
9.48e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family 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. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 37.86 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 19 PTYVY-DLDAIGDRVARLRAALPTAELLYAV-KAN-------PCGAVLRHLAAAGLGaeVISVGELARARRAGfPEGRIL 89
Cdd:cd00430 1 RTWAEiDLDALRHNLRVIRRLLGPGTKIMAVvKADayghgavEVAKALEEAGADYFA--VATLEEALELREAG-ITAPIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502941680 90 -LGGPRQDPPLVAAAWGVgWVSLDNPSQWRGWQRFAAREGAPrfllrlnpgldPRTHEHLATGAARskFGMPFGELAALG 168
Cdd:cd00430 78 vLGGTPPEEAEEAIEYDL-TPTVSSLEQAEALSAAAARLGKT-----------LKVHLKIDTGMGR--LGFRPEEAEELL 143
|
....*.
gi 502941680 169 AALGEH 174
Cdd:cd00430 144 EALKAL 149
|
|
| |
