|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
69-478 |
0e+00 |
|
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: 537.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 69 AYRNGTLCAEQVPLEDIARRFGTPCYVYSRAAIEGAYGEFAQALHGRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGG 148
Cdd:COG0019 4 FARDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 149 ELARVLAAGGDPRKILFSGVGKTKEEIRLALEKNIHCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHPYIST 228
Cdd:COG0019 84 ELRLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHEYIST 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 229 GLRENKFGVAHRDAERLYAKAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRY 308
Cdd:COG0019 164 GGKDSKFGIPLEDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 309 RD-ETPRPVREFVAGALAALGDRRGS---VIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAWH 384
Cdd:COG0019 244 TEgDEPPDLEELAAAIKEALEELCGLgpeLILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPALYGAYH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 385 EVRTVREPESGAPGTvYDIVGPICETGDFLAKDRAL-TAREGDLLAVMSSGAYAMSMASNYNSRPRAAEVMVQGRAAELV 463
Cdd:COG0019 324 PIVPVGRPSGAEAET-YDVVGPLCESGDVLGKDRSLpPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEARLI 402
|
410
....*....|....*
gi 1671497599 464 RARESAEQLFALERI 478
Cdd:COG0019 403 RRRETYEDLLASEVL 417
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
89-455 |
5.11e-177 |
|
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: 500.86 E-value: 5.11e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 89 FGTPCYVYSRAAIEGAYGEFAQALHGRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGV 168
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 169 GKTKEEIRLALEKNIHCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHPYISTGLRENKFGVAHRDAERLYAK 248
Cdd:cd06828 81 GKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 249 AAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPRP-VREFVAGALAAL 327
Cdd:cd06828 161 AKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEDEPLdIEEYAEAIAEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 328 GD-----RRGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAWHEVRTVREPESGAPgTVYD 402
Cdd:cd06828 241 KElceggPDLKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGET-EKVD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1671497599 403 IVGPICETGDFLAKDRAL-TAREGDLLAVMSSGAYAMSMASNYNSRPRAAEVMV 455
Cdd:cd06828 320 VVGPICESGDVFAKDRELpEVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
70-477 |
1.58e-169 |
|
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: 483.72 E-value: 1.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 70 YRNGTLCAEQVPLEDIARRFGTPCYVYSRAAIEGAYGEFAQALHGRdAMLCYSVKANSNLAVLALLARLGAGFDIVSGGE 149
Cdd:TIGR01048 4 NEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGR-SLVCYAVKANSNLAVLRLLAELGSGFDVVSGGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 150 LARVLAAGGDPRKILFSGVGKTKEEIRLALEKNIhCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHPYISTG 229
Cdd:TIGR01048 83 LYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHPYISTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 230 LRENKFGVAHRDAERLYAKAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEaAGIRLRHLDLGGGIGIRYR 309
Cdd:TIGR01048 162 LKDSKFGIDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA-EGIDLEFLDLGGGLGIPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 310 DET-PRPVREFVAGALAALGDRRGS-----VIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAW 383
Cdd:TIGR01048 241 PEEePPDLSEYAQAILNALEGYADLgldpkLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPALYGAY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 384 HEVRTVREPEsGAPGTVYDIVGPICETGDFLAKDRAL-TAREGDLLAVMSSGAYAMSMASNYNSRPRAAEVMVQGRAAEL 462
Cdd:TIGR01048 321 HHIIVLNRTN-DAPTEVADVVGPVCESGDVLAKDRELpEVEPGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARL 399
|
410
....*....|....*
gi 1671497599 463 VRARESAEQLFALER 477
Cdd:TIGR01048 400 IRRRETYEDLWALEV 414
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
93-434 |
7.16e-141 |
|
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: 408.03 E-value: 7.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 93 CYVYSRAAIEGAYGEFAQALHGRdAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGKTK 172
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALPPR-VKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 173 EEIRLALEKNIHCINLESAAELERVAAVARELGrpAPVAFRVNPDVDARTHpYISTGLRENKFGVAHRDAERLYAKAAAM 252
Cdd:pfam00278 80 SEIRYALEAGVLCFNVDSEDELEKIAKLAPELV--ARVALRINPDVDAGTH-KISTGGLSSKFGIDLEDAPELLALAKEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 253 pALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPRPVREFVAGALAALGDRRG 332
Cdd:pfam00278 157 -GLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPDFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 333 S---VIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAWHEVrTVREPESGAPGTVYDIVGPICE 409
Cdd:pfam00278 236 PdleIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPI-PVVKEPGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*.
gi 1671497599 410 TGDFLAKDRAL-TAREGDLLAVMSSG 434
Cdd:pfam00278 315 SGDVLAKDRELpELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
91-455 |
3.97e-102 |
|
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: 310.00 E-value: 3.97e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 91 TPCYVYSRAAIEGAYGEFAQALHGRDAmLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGK 170
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEALPSGVK-LFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 171 TKEEIRLALEKNIHCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHpYISTGLRENKFGVAHRDAERLYAKAA 250
Cdd:cd06810 80 SVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLSLSEARAALERAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 251 AMPaLEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPRP--VREFVAGALAALG 328
Cdd:cd06810 159 ELD-LRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDFeeYAALINPLLKKYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 329 DRRG--SVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAW-HEVRTVREPESGAPGTVYDIVG 405
Cdd:cd06810 238 PNDPgvTLILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALAYDAyHPITPLKAPGPDEPLVPATLAG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1671497599 406 PICETGDFLAKDRALTA-REGDLLAVMSSGAYAMSMASNYNSRPRAAEVMV 455
Cdd:cd06810 318 PLCDSGDVIGRDRLLPElEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
75-471 |
2.26e-91 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 283.99 E-value: 2.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 75 LCAEQVPLEDIARRFG-TPCYVYSRAAIEGAYGEFAQALHGRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARV 153
Cdd:PLN02537 1 LYCEGLRVQDIMESVEkRPFYLYSKPQITRNYEAYKEALEGLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 154 LAAGGDPRKILFSGVGKTKEEIRLALEKNIHcINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHPYISTGLREN 233
Cdd:PLN02537 81 LRAGFDPTRCIFNGNGKLLEDLVLAAQEGVF-VNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 234 KFGVAHRDAERLYAKAAAMPA-LEVIGIGCHIGSQL--VDPAPLAAAVerLAALAGRIEAAGIRLRHLDLGGGIGIRYRD 310
Cdd:PLN02537 160 KFGIRNEKLQWFLDAVKAHPNeLKLVGAHCHLGSTItkVDIFRDAAVL--MVNYVDEIRAQGFELSYLNIGGGLGIDYYH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 311 E-----TPR----PVREFVAgalaalgDRRGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYD 381
Cdd:PLN02537 238 AgavlpTPRdlidTVRELVL-------SRDLTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMAELIRPSLYD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 382 AWHEVRTVREPESGAPGTVYDIVGPICETGDFLAKDRAL-TAREGDLLAVMSSGAYAMSMASNYNSRPRAAEVMVQ-GRA 459
Cdd:PLN02537 311 AYQHIELVSPPPPDAEVSTFDVVGPVCESADFLGKDRELpTPPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEeDGS 390
|
410
....*....|..
gi 1671497599 460 AELVRARESAEQ 471
Cdd:PLN02537 391 ITKIRHAETFDD 402
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
85-455 |
4.13e-76 |
|
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: 243.27 E-value: 4.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 85 IARRFGTPCYVYSRAAIEGAYGEFAQALHGRDAMLcYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKIL 164
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAALPPAIEIY-YSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 165 FSGVGKTKEEIRLALEKNIHCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARtHPYISTGLRENKFGVAHRDAER 244
Cdd:cd06839 80 FAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFELK-GSGMKMGGGPSQFGIDVEELPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 245 LYAKAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRI-EAAGIRLRHLDLGGGIGIRY-RDETP---RPVREF 319
Cdd:cd06839 159 VLARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLaEELGLPLEFLDLGGGFGIPYfPGETPldlEALGAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 320 VAGALAALGDRRGS--VIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLvrpaLYDAWHEVRTVR------- 390
Cdd:cd06839 239 LAALLAELGDRLPGtrVVLELGRYLVGEAGVYVTRVLDRKVSRGETFLVTDGGMHHH----LAASGNFGQVLRrnyplai 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671497599 391 EPESGAPGT-VYDIVGPICETGDFLAKDRAL-TAREGDLLAVMSSGAYAMSmAS--NYNSRPRAAEVMV 455
Cdd:cd06839 315 LNRMGGEEReTVTVVGPLCTPLDLLGRNVELpPLEPGDLVAVLQSGAYGLS-ASplAFLSHPAPAEVLV 382
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
92-455 |
2.05e-61 |
|
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: 204.59 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 92 PCYVYSRAAIEgAYGEFAQALHGRDAmLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAA--GGDPRKILFSGVG 169
Cdd:cd06840 13 PCYVYDLETVR-ARARQVSALKAVDS-LFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTPNF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 170 KTKEEIRLALEKNIHCI--NLESAAELErvaavarELGRPAPVAFRVNPDVDARTHPYISTGLRENKFGVAHRDAERLYA 247
Cdd:cd06840 91 AARSEYEQALELGVNVTvdNLHPLREWP-------ELFRGREVILRIDPGQGEGHHKHVRTGGPESKFGLDVDELDEARD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 248 KAAAMPAlEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAgirlRHLDLGGGIGIRYRDETPRPVREFVAGALAAL 327
Cdd:cd06840 164 LAKKAGI-IVIGLHAHSGSGVEDTDHWARHGDYLASLARHFPAV----RILNVGGGLGIPEAPGGRPIDLDALDAALAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 328 GDR--RGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAWHEVRTV-REPESGApgTVYDIV 404
Cdd:cd06840 239 KAAhpQYQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLsRLDEPPA--GNADVV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1671497599 405 GPICETGDFLAKDRALTA-REGDLLAVMSSGAYAMSMASNYNSRPRAAEVMV 455
Cdd:cd06840 317 GPICESGDVLGRDRLLPEtEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
90-455 |
9.67e-58 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 204.93 E-value: 9.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 90 GTPCYVYSRAAIEgaygEFAQALHGRDAM--LCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAA--GGDPRKILF 165
Cdd:PRK08961 502 GSPCYVYHLPTVR----ARARALAALAAVdqRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 166 SGVGKTKEEIRLALEKNIHcINLESAAELERVAAVARelGRPapVAFRVNPDVDARTHPYISTGLRENKFGVAHRDAERL 245
Cdd:PRK08961 578 TPNFAPRAEYEAAFALGVT-VTLDNVEPLRNWPELFR--GRE--VWLRIDPGHGDGHHEKVRTGGKESKFGLSQTRIDEF 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 246 YAkAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAgirlRHLDLGGGIGIRYRDETPRPVREFVAGALA 325
Cdd:PRK08961 653 VD-LAKTLGITVVGLHAHLGSGIETGEHWRRMADELASFARRFPDV----RTIDLGGGLGIPESAGDEPFDLDALDAGLA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 326 ALGDR--RGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDAWHE-VRTVREPESgaPGTVYD 402
Cdd:PRK08961 728 EVKAQhpGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEiVNLSRLDEP--AAGTAD 805
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1671497599 403 IVGPICETGDFLAKDRALTA-REGDLLAVMSSGAYAMSMASNYNSRPRAAEVMV 455
Cdd:PRK08961 806 VVGPICESSDVLGKRRRLPAtAEGDVILIANAGAYGYSMSSTYNLREPAREVVL 859
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
98-344 |
4.98e-56 |
|
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: 186.33 E-value: 4.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 98 RAAIEGAYGEFAQALHgrDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGKTKEEIRL 177
Cdd:pfam02784 1 LGSIERRHRRWKKALP--RIKPFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 178 ALEKNIHCINLESAAELERVAAVARElgrpAPVAFRVNPDVDARTHPYistglrENKFGVAHRDAERLYAKAAAMPALEV 257
Cdd:pfam02784 79 ALEVGVGCVTVDNVDELEKLARLAPE----ARVLLRIKPDDSAATCPL------SSKFGADLDEDVEALLEAAKLLNLQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 258 IGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPRPVREFVAGAL------AALGDRR 331
Cdd:pfam02784 149 VGVSFHVGSGCTDAEAFVLALEDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPLDFEEYANVInealeeYFPGDPG 228
|
250
....*....|...
gi 1671497599 332 GSVIFDPGRSMVG 344
Cdd:pfam02784 229 VTIIAEPGRYFVA 241
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
85-455 |
2.09e-52 |
|
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: 181.31 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 85 IARRFGTPCYVYSRAAIEGAYGEFAQALHGR--DAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRK 162
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRypNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 163 ILFSGVGKTKEEIRLALEKNIHcINLESAAELERVAAVARELGRPAPVAFRVNPDVdaRTHPYISTGLRENKFGvahrDA 242
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGAL-INIDSFDELERILEIAKELGRVAKVGIRLNMNY--GNNVWSRFGFDIEENG----EA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 243 ERLYAKAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIeaAGIRLRHLDLGGGIGIR--------YRDETPR 314
Cdd:cd06841 154 LAALKKIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLDRL--FGLELEYLDLGGGFPAKtplslaypQEDTVPD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 315 PVREF--VAGALAALGDRRGS---VIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPALYDawHEVRTV 389
Cdd:cd06841 232 PEDYAeaIASTLKEYYANKENkpkLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPTIFWYH--HPILVL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1671497599 390 REPESGAPGTVYDIVGPICETGDFLAKDRALTA-REGDLLAVMSSGAYAMSMASNYnSRPRAAEVMV 455
Cdd:cd06841 310 RPGKEDPTSKNYDVYGFNCMESDVLFPNVPLPPlNVGDILAIRNVGAYNMTQSNQF-IRPRPAVYLI 375
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
93-451 |
3.29e-49 |
|
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: 172.96 E-value: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 93 CYVYSRAAIEGAYGEFAQALHGrDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGKTK 172
Cdd:cd06836 5 VGLYDLDGFRALVARLTAAFPA-PVLHTFAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 173 EEIRLALEKNIHcINLESAAELERVAAVARELGRPA-PVAFRVNPDVDARTHPYISTGLRENKFGVAHRDAER-----LY 246
Cdd:cd06836 84 AELREALELGVA-INIDNFQELERIDALVAEFKEASsRIGLRVNPQVGAGKIGALSTATATSKFGVALEDGARdeiidAF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 247 AKAAAMPALEVigigcHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLR--HLDLGGGIGIRYRDETPRPVREFVAGAL 324
Cdd:cd06836 163 ARRPWLNGLHV-----HVGSQGCELSLLAEGIRRVVDLAEEINRRVGRRQitRIDIGGGLPVNFESEDITPTFADYAAAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 325 AA----LGDRRGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPA-LYDAWHEVRTVREPES---GA 396
Cdd:cd06836 238 KAavpeLFDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGGRRIAITHAGAQVATRTAyAPDDWPLRVTVFDANGepkTG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1671497599 397 PGTVYDIVGPICETGDFLAKDRALTARE-GDLLAVMSSGAYAMSMASNYNSRPRAA 451
Cdd:cd06836 318 PEVVTDVAGPCCFAGDVLAKERALPPLEpGDYVAVHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
92-437 |
5.45e-45 |
|
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: 161.29 E-value: 5.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 92 PCYVYSRAAIEgaygefAQALHGRDAM-----LCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRkILFS 166
Cdd:cd06843 3 CAYVYDLAALR------AHARALRASLppgceLFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPDAP-LIFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 167 GVGKTKEEIRLALEKNIHCINLESAAELERVAAVARELGRPAPVAFRVNPDVDARTHPYISTGLRENKFGVAHRDAERLY 246
Cdd:cd06843 76 GPGKTDSELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 247 AKAAAMPALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAA-GIRLRHLDLGGGIGIRYRD-ETPRPVREFVAG-- 322
Cdd:cd06843 156 ELLRDLPNIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEhGLDLDVVNVGGGIGVNYADpEEQFDWAGFCEGld 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 323 ALAALGDRRGSVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFLVVDAAMNDLVRPAlydAW---HEVRTVREPESGAP-- 397
Cdd:cd06843 236 QLLAEYEPGLTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPA---AWghnHPFSVLPVEEWPYPwp 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1671497599 398 -----GTVYDIVGPICETGDFLAKDRALTA-REGDLLAVMSSGAYA 437
Cdd:cd06843 313 rpsvrDTPVTLVGQLCTPKDVLARDVPVDRlRAGDLVVFPLAGAYG 358
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
90-445 |
7.11e-42 |
|
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: 152.65 E-value: 7.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 90 GTPCYVYSRAAIEGAYGEFAQALhgRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVG 169
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKAL--PRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 170 KTKEEIRLALEKNIHCINLESAAELERVAAVARElgrpAPVAFRVNPDVDARTHPyistgLReNKFGVAHRDAERLYAKA 249
Cdd:cd00622 79 KSISDIRYAAELGVRLFTFDSEDELEKIAKHAPG----AKLLLRIATDDSGALCP-----LS-RKFGADPEEARELLRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 250 AAMpALEVIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPrPVREF---VAGALAA 326
Cdd:cd00622 149 KEL-GLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVP-SFEEIaavINRALDE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 327 L-GDRRGSVIFDPGRSMVGNAGVLLTRVE---YVKPGEPRNFLVVDA----AMNDlvrpALYDAWH-EVRTVREPESGAP 397
Cdd:cd00622 227 YfPDEGVRIIAEPGRYLVASAFTLAVNVIakrKRGDDDRERWYYLNDgvygSFNE----ILFDHIRyPPRVLKDGGRDGE 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1671497599 398 GTVYDIVGPICETGDFLAKDRAL--TAREGDLLAVMSSGAYAMSMASNYN 445
Cdd:cd00622 303 LYPSSLWGPTCDSLDVIYEDVLLpeDLAVGDWLLFENMGAYTTAYASTFN 352
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
114-320 |
2.47e-37 |
|
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: 135.91 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 114 GRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGKTKEEIRLALEKNIHCINLESAAE 193
Cdd:cd06808 13 PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVIVVTVDSLEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 194 LERVAAVARELGRPAPVAFRVNPDVdarthpyistglRENKFGVAHRDAERLYAKAAAMPALEVIGIGCHIGSQLVDPAP 273
Cdd:cd06808 93 LEKLEEAALKAGPPARVLLRIDTGD------------ENGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSADEDYSP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1671497599 274 LAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRYRDETPRPVREFV 320
Cdd:cd06808 161 FVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFIIV 207
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
82-455 |
2.10e-24 |
|
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: 105.04 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 82 LEDIARRFGTPCYVYSRAAIEGAYGEFAQAL--HGRDAMLCYSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGD 159
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLdrHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 160 PRKILFSGVGKTKEEIRLALEKNIhCINLESAAELERVAA-VARELGRPAPVAFRVNPDVdarthpyistGLRENKFGVA 238
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLAlARGYTTGPARVLLRLSPFP----------ASLPSRFGMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 239 HRDAERLYAK-AAAMPALEVIGIGCHIGSqlVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLGGGIGIRY--------- 308
Cdd:cd06842 150 AAEVRTALERlAQLRERVRLVGFHFHLDG--YSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYladaaewea 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 309 -------------RDETPRPVREFV---------------AGALAALGD-------------RRGSVIF--DPGRSMVGN 345
Cdd:cd06842 228 flaaltealygygRPLTWRNEGGTLrgpddfypygqplvaADWLRAILSaplpqgrtiaerlRDNGITLalEPGRALLDQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 346 AGVLLTRVEYVKPGEPRNFLVVdAAMND----------LVRPALydawheVRTVREPESGAPGTVYdIVGPICETGDFLA 415
Cdd:cd06842 308 CGLTVARVAFVKQLGDGNHLIG-LEGNSfsacefssefLVDPLL------IPAPEPTTDGAPIEAY-LAGASCLESDLIT 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1671497599 416 KDRALTAR---EGDLLAVMSSGAYAM-SMASNYNSRPRAAEVMV 455
Cdd:cd06842 380 RRKIPFPRlpkPGDLLVFPNTAGYQMdFLESRFHRHPLPRRVVV 423
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
149-365 |
2.14e-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: 65.67 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 149 ELARVLAAGGDP-RKILFSGVgKTKEEIRLALE-----KNIhCINLESAAELERVAAVARELGRPAPVAFRVNPDVDART 222
Cdd:cd06830 75 ELLAALALLKTPdALIICNGY-KDDEYIELALLarklgHNV-IIVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 223 HPYISTGLREnKFGVAHRDAERLYAKAAAMPALE-VIGIGCHIGSQLVDPAPLAAAVERLAALAGRIEAAGIRLRHLDLG 301
Cdd:cd06830 153 KWQESGGDRS-KFGLTASEILEVVEKLKEAGMLDrLKLLHFHIGSQITDIRRIKSALREAARIYAELRKLGANLRYLDIG 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671497599 302 GGIGIRYrDETPRP--------VREFVA---GALAALGDRRG----SVIFDPGRSMVGNAGVLLTRVEYVKPGEPRNFL 365
Cdd:cd06830 232 GGLGVDY-DGSRSSsdssfnysLEEYANdivKTVKEICDEAGvphpTIVTESGRAIVAHHSVLIFEVLGVKRLADWYFC 309
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
151-298 |
4.92e-09 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 56.46 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 151 ARVLAAGGDPRKILFSGvGKTKEEIRLALEKNIHCInLESAAELERVAAVARELGRPAPVAFRVNpdvdarthpyisTGL 230
Cdd:pfam01168 59 ALELREAGITAPILVLG-GFPPEELALAAEYDLTPT-VDSLEQLEALAAAARRLGKPLRVHLKID------------TGM 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1671497599 231 reNKFGVAHRDAERLYAKAAAMPALEVIGIGCHIG-SQLVDPAPLAAAVERLAALAGRIEAAGIR--LRHL 298
Cdd:pfam01168 125 --GRLGFRPEEALALLARLAALPGLRLEGLMTHFAcADEPDDPYTNAQLARFREAAAALEAAGLRppVVHL 193
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
170-308 |
1.73e-06 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 50.50 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 170 KTKEEIRLAL--EK---NIHcINLESAAELERVAAVARELG-RPApVAFRVnpdvdaRTHPyISTGLREN------KFGV 237
Cdd:PRK05354 155 KDREYIRLALigRKlghKVF-IVIEKLSELELILEEAKELGvKPR-LGVRA------RLAS-QGSGKWQSsggeksKFGL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 238 AHRD----AERLyaKAAAMpalevigIGC------HIGSQLVDPAPLAAAV-ErlaalAGRIEA----AGIRLRHLDLGG 302
Cdd:PRK05354 226 SATEvleaVERL--REAGL-------LDClqllhfHLGSQIANIRDIKTAVrE-----AARFYVelrkLGAPIQYLDVGG 291
|
....*.
gi 1671497599 303 GIGIRY 308
Cdd:PRK05354 292 GLGVDY 297
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
156-298 |
5.31e-06 |
|
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: 48.65 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 156 AGGDPRKILFSGVgkTKEEIRLALEKNIHCInLESAAELERVAAVARELGRPAPVAFRVNpdvdarthpyisTGLreNKF 235
Cdd:cd00430 70 AGITAPILVLGGT--PPEEAEEAIEYDLTPT-VSSLEQAEALSAAAARLGKTLKVHLKID------------TGM--GRL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1671497599 236 GVAHRDAERLYAKAAAMPALEVIGIGCHIGSQLVDPAPLAAA-VERLAALAGRIEAAGIR--LRHL 298
Cdd:cd00430 133 GFRPEEAEELLEALKALPGLELEGVFTHFATADEPDKAYTRRqLERFLEALAELEEAGIPppLKHL 198
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
190-438 |
1.37e-03 |
|
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: 41.00 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 190 SAAELERVAAVARelGRPAPVAFRVNPDVDARTHPYISTGLRENKFGVAhrdaerlyAKAAAMPALEVI-GIGCHIGSQL 268
Cdd:cd06829 97 SLSQLERFKDRAK--AAGISVGLRINPEYSEVETDLYDPCAPGSRLGVT--------LDELEEEDLDGIeGLHFHTLCEQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 269 vDPAPLA---AAVE-RLAALAGRIEAagirlrhLDLGGGIGIRYRDetpRPVREFVAgALAALGDRRG-SVIFDPGRSMV 343
Cdd:cd06829 167 -DFDALErtlEAVEeRFGEYLPQLKW-------LNLGGGHHITRPD---YDVDRLIA-LIKRFKEKYGvEVYLEPGEAVA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 344 GNAGVLLTRV-EYVKPGEPrnFLVVDAA----MNDLV----RPALYDAwhevrtvrePESGAPGTVYDIVGPICETGDFL 414
Cdd:cd06829 235 LNTGYLVATVlDIVENGMP--IAILDASatahMPDVLempyRPPIRGA---------GEPGEGAHTYRLGGNSCLAGDVI 303
|
250 260
....*....|....*....|....*..
gi 1671497599 415 ---AKDRALtaREGDLLAVMSSGAYAM 438
Cdd:cd06829 304 gdySFDEPL--QVGDRLVFEDMAHYTM 328
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
151-298 |
3.76e-03 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 39.39 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 151 ARVLAAGGDPRKILFSGVGKTKEEIRLALEKNIHCI--NLESAAELERVaavarELGRPAPVafrvnpdvdartHPYIST 228
Cdd:PRK00053 66 ALELREAGITAPILILGGFFPAEDLPLIIAYNLTTAvhSLEQLEALEKA-----ELGKPLKV------------HLKIDT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 229 GLreNKFGVAHRDAERLYAKAAAMPALEVIGIGCHigsqlvdpapLAAA-----------VERLAALAGRIEAAGIRLRH 297
Cdd:PRK00053 129 GM--HRLGVRPEEAEAALERLLACPNVRLEGIFSH----------FATAdepdnsyteqqLNRFEAALAGLPGKGKPLRH 196
|
.
gi 1671497599 298 L 298
Cdd:PRK00053 197 L 197
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
121-303 |
4.19e-03 |
|
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: 39.45 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 121 YSVKANSNLAVLALLARLGAGFDIVSGGELARVLAAGGDPRKILFSGVGKTKEEIRLALEKNIHCINLESAAELERVAav 200
Cdd:cd06831 41 YTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKIA-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671497599 201 arelgrpapvafRVNPDVDARTHpyIST----GLREN--KFGVAHRDAERLYAKAAAMpALEVIGIGCHIGSQLVDPAPL 274
Cdd:cd06831 119 ------------RNHPNAKLLLH--IATedniGGEEMnmKFGTTLKNCRHLLECAKEL-DVQIVGVKFHVSSSCKEYQTY 183
|
170 180
....*....|....*....|....*....
gi 1671497599 275 AAAVERLAALAGRIEAAGIRLRHLDLGGG 303
Cdd:cd06831 184 VHALSDARCVFDMAEEFGFKMNMLDIGGG 212
|
|
| |
