|
Name |
Accession |
Description |
Interval |
E-value |
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
9-417 |
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: 575.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 9 RNDVLHAEGVALPALAERFGTPLYVYSKAALTSAYQAYAKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGEL 88
Cdd:COG0019 6 RDGELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGAKVLYAVKANSNLAVLRLLAEEGLGADVVSGGEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 89 ARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVFCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYISTGL 168
Cdd:COG0019 86 RLALAAGFPPERIVFSGNGKSEEELEEALELGVGHINVDSLSELERLAELAAELGKRAPVGLRVNPGVDAGTHEYISTGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 169 RGNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTD 248
Cdd:COG0019 166 KDSKFGIPLEDALEAYRRAAALPGLRLVGLHFHIGSQILDLEPFEEALERLLELAEELRELGIDLEWLDLGGGLGIPYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 249 -ETPPDITAFATTLLDHIAKRGHGHRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGI 327
Cdd:COG0019 246 gDEPPDLEELAAAIKEALEELCGLGPELILEPGRALVGNAGVLLTRVLDVKENGGRRFVIVDAGMNDLMRPALYGAYHPI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 328 DPVERRAVDG-VIYDVVGPVCESGDWLGHDRAL-AIAPGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMVDGNEAYLVRER 405
Cdd:COG0019 326 VPVGRPSGAEaETYDVVGPLCESGDVLGKDRSLpPLEPGDLLAFLDAGAYGFSMASNYNGRPRPAEVLVDDGEARLIRRR 405
|
410
....*....|..
gi 1736826776 406 ETVESLFAGERL 417
Cdd:COG0019 406 ETYEDLLASEVL 417
|
|
| lysA |
TIGR01048 |
diaminopimelate decarboxylase; This family consists of diaminopimelate decarboxylase, an ... |
7-416 |
0e+00 |
|
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: 539.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 7 SYRNDVLHAEGVALPALAERFGTPLYVYSKAALTSAYQAYAKACEGRNAaVHYAAKANSNLAVLGVFAKLGAGFDIVSAG 86
Cdd:TIGR01048 3 ENEDGELFIEGVPLLELAQEFGTPLYVYDEDTIRRRFRAYKEAFGGRSL-VCYAVKANSNLAVLRLLAELGSGFDVVSGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 87 ELARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVfCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYIST 166
Cdd:TIGR01048 82 ELYRALAAGFPPEKIVFSGNGKSRAELERALELGI-CINVDSFSELERLNEIAPELGKKARISLRVNPGVDAKTHPYIST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 167 GLRGNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEaAGISLHHIDVGGGLGITY 246
Cdd:TIGR01048 161 GLKDSKFGIDVEEALEAYLYALQLPHLELVGIHCHIGSQITDLSPFVEAAEKVVKLAESLA-EGIDLEFLDLGGGLGIPY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 247 TDET-PPDITAFATTLLDHIAKRGHGHR--QVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEA 323
Cdd:TIGR01048 240 TPEEePPDLSEYAQAILNALEGYADLGLdpKLILEPGRSIVANAGVLLTRVGFVKETGSRNFVIVDAGMNDLIRPALYGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 324 YHGIDPVER-RAVDGVIYDVVGPVCESGDWLGHDRALAIA-PGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMVDGNEAYL 401
Cdd:TIGR01048 320 YHHIIVLNRtNDAPTEVADVVGPVCESGDVLAKDRELPEVePGDLLAVFDAGAYGFSMSSNYNSRPRPAEVLVDGGQARL 399
|
410
....*....|....*
gi 1736826776 402 VRERETVESLFAGER 416
Cdd:TIGR01048 400 IRRRETYEDLWALEV 414
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
27-394 |
0e+00 |
|
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: 531.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 27 FGTPLYVYSKAALTSAYQAYAKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGV 106
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFSGPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFTGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 107 GKHADEMRYALEKNVFCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYISTGLRGNKFGVAYEEAFDAYRA 186
Cdd:cd06828 81 GKSDEELELALELGILRINVDSLSELERLGEIAPELGKGAPVALRVNPGVDAGTHPYISTGGKDSKFGIPLEQALEAYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 187 AAAMPNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTDE-TPPDITAFATTLLDHI 265
Cdd:cd06828 161 AKELPGLKLVGLHCHIGSQILDLEPFVEAAEKLLDLAAELRELGIDLEFLDLGGGLGIPYRDEdEPLDIEEYAEAIAEAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 266 AKRGHGHR--QVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGIDPVERRAVDG-VIYDV 342
Cdd:cd06828 241 KELCEGGPdlKLIIEPGRYIVANAGVLLTRVGYVKETGGKTFVGVDAGMNDLIRPALYGAYHEIVPVNKPGEGEtEKVDV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1736826776 343 VGPVCESGDWLGHDRALA-IAPGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMV 394
Cdd:cd06828 321 VGPICESGDVFAKDRELPeVEEGDLLAIHDAGAYGYSMSSNYNSRPRPAEVLV 373
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
31-373 |
1.17e-150 |
|
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: 430.37 E-value: 1.17e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 31 LYVYSKAALTSAYQAYAKACEGRnAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGKHA 110
Cdd:pfam00278 1 FYVYDLATLRRNYRRWKAALPPR-VKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 111 DEMRYALEKNVFCFNVESRPELDRLNDVAgqAGKRARVSLRVNPNVDAKTHpYISTGLRGNKFGVAYEEAFDAYRAAAAM 190
Cdd:pfam00278 80 SEIRYALEAGVLCFNVDSEDELEKIAKLA--PELVARVALRINPDVDAGTH-KISTGGLSSKFGIDLEDAPELLALAKEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 191 pNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTDETPPDITAFATTLLDHIAKRGH 270
Cdd:pfam00278 157 -GLNVVGVHFHIGSQITDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDEPPPDFEEYAAAIREALDEYFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 271 GHRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGIdPVER--RAVDGVIYDVVGPVCE 348
Cdd:pfam00278 236 PDLEIIAEPGRYLVANAGVLVTRVIAVKTGGGKTFVIVDAGMNDLFRPALYDAYHPI-PVVKepGEGPLETYDVVGPTCE 314
|
330 340
....*....|....*....|....*.
gi 1736826776 349 SGDWLGHDRAL-AIAPGDLLAIRSAG 373
Cdd:pfam00278 315 SGDVLAKDRELpELEVGDLLAFEDAG 340
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
29-394 |
4.55e-111 |
|
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: 330.81 E-value: 4.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 29 TPLYVYSKAALTSAYQAYaKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGK 108
Cdd:cd06810 1 TPFYVYDLDIIRAHYAAL-KEALPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGPAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 109 HADEMRYALEKNVFCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHpYISTGLRGNKFGVAYEEAFDAYRAAA 188
Cdd:cd06810 80 SVSEIEAALASGVDHIVVDSLDELERLNELAKKLGPKARILLRVNPDVSAGTH-KISTGGLKSKFGLSLSEARAALERAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 189 AMpNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTDETPP--DITAFATTLLDHIA 266
Cdd:cd06810 159 EL-DLRLVGLHFHVGSQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDfeEYAALINPLLKKYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 267 KRGHGHRqVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAM-YEAYHGIDPVERRAVDG--VIYDVV 343
Cdd:cd06810 238 PNDPGVT-LILEPGRYIVAQAGVLVTRVVAVKVNGGRFFAVVDGGMNHSFRPALaYDAYHPITPLKAPGPDEplVPATLA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1736826776 344 GPVCESGDWLGHDRAL-AIAPGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMV 394
Cdd:cd06810 317 GPLCDSGDVIGRDRLLpELEVGDLLVFEDMGAYGFSESSNFNSHPRPAEYLV 368
|
|
| PLN02537 |
PLN02537 |
diaminopimelate decarboxylase |
29-409 |
2.27e-98 |
|
diaminopimelate decarboxylase
Pssm-ID: 178152 [Multi-domain] Cd Length: 410 Bit Score: 299.79 E-value: 2.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 29 TPLYVYSKAALTSAYQAYAKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGK 108
Cdd:PLN02537 18 RPFYLYSKPQITRNYEAYKEALEGLRSIIGYAIKANNNLKILEHLRELGCGAVLVSGNELRLALRAGFDPTRCIFNGNGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 109 HADEMRYALEKNVFcFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYISTGLRGNKFGVAYEEAFDAYRAAA 188
Cdd:PLN02537 98 LLEDLVLAAQEGVF-VNVDSEFDLENIVEAARIAGKKVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDAVK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 189 AMPN-LEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITY--TDETPPDITAFATTLLDHI 265
Cdd:PLN02537 177 AHPNeLKLVGAHCHLGSTITKVDIFRDAAVLMVNYVDEIRAQGFELSYLNIGGGLGIDYyhAGAVLPTPRDLIDTVRELV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 266 AKRGhghRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGIDPVERRAVDGVI--YDVV 343
Cdd:PLN02537 257 LSRD---LTLIIEPGRSLIANTCCFVNRVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPPPPDAEVstFDVV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736826776 344 GPVCESGDWLGHDRALAI-APGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMV-DGNEAYLVRERETVE 409
Cdd:PLN02537 334 GPVCESADFLGKDRELPTpPKGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVeEDGSITKIRHAETFD 401
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
23-394 |
1.60e-82 |
|
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: 258.29 E-value: 1.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 23 LAERFGTPLYVYSKAALTSAYQAYAKACeGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAV 102
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAAL-PPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEKIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 103 FSGVGKHADEMRYALEKNVFCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKtHPYISTGLRGNKFGVAYEEAFD 182
Cdd:cd06839 80 FAGPGKSDAELRRAIEAGIGTINVESLEELERIDALAEEHGVVARVALRINPDFELK-GSGMKMGGGPSQFGIDVEELPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 183 AYRAAAAMPNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKL-EAAGISLHHIDVGGGLGITYTD-ETPPDITAFATT 260
Cdd:cd06839 159 VLARIAALPNLRFVGLHIYPGTQILDADALIEAFRQTLALALRLaEELGLPLEFLDLGGGFGIPYFPgETPLDLEALGAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 261 LLDHIAKRG--HGHRQVLFEPGRSLVGNAGVLLTRVEFLK--HGETknFAIVDAAMNDLAR-------------PAMYEA 323
Cdd:cd06839 239 LAALLAELGdrLPGTRVVLELGRYLVGEAGVYVTRVLDRKvsRGET--FLVTDGGMHHHLAasgnfgqvlrrnyPLAILN 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736826776 324 YHGIDPVERravdgviYDVVGPVCESGDWLGHDRALAIA-PGDLLAIRSAGAYGFTMS-SNYNTRPRAAEVMV 394
Cdd:cd06839 317 RMGGEERET-------VTVVGPLCTPLDLLGRNVELPPLePGDLVAVLQSGAYGLSASpLAFLSHPAPAEVLV 382
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
57-285 |
4.68e-68 |
|
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: 215.99 E-value: 4.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 57 VHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVFCFNVESRPELDRLN 136
Cdd:pfam02784 20 PFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGVGCVTVDNVDELEKLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 137 DVAgqagKRARVSLRVNPNVDAKTHPYistglrGNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHIGSQITEISPYLDAT 216
Cdd:pfam02784 100 RLA----PEARVLLRIKPDDSAATCPL------SSKFGADLDEDVEALLEAAKLLNLQVVGVSFHVGSGCTDAEAFVLAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736826776 217 DKVLDLVEKLEAAGISLHHIDVGGGLGITYTDETPP-DITAFATTLLDHIAK--RGHGHRQVLFEPGRSLVG 285
Cdd:pfam02784 170 EDARGVFDQGAELGFNLKILDLGGGFGVDYTEGEEPlDFEEYANVINEALEEyfPGDPGVTIIAEPGRYFVA 241
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
23-397 |
9.34e-65 |
|
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: 212.12 E-value: 9.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 23 LAERFGTPLYVYSKAALTSAYQAYAKACEGR--NAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKR 100
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRypNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 101 AVFSGVGKHADEMRYALEKNVFcFNVESRPELDRLNDVAGQAGKRARVSLRVNPNvdakTHPYISTglrgnKFGVAYEEA 180
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGAL-INIDSFDELERILEIAKELGRVAKVGIRLNMN----YGNNVWS-----RFGFDIEEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 181 FDAYRA---AAAMPNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEklEAAGISLHHIDVGGGL-------GITYTDET 250
Cdd:cd06841 151 GEALAAlkkIQESKNLSLVGLHCHVGSNILNPEAYSAAAKKLIELLD--RLFGLELEYLDLGGGFpaktplsLAYPQEDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 251 PPDITAFA----TTLLDHIAKRGHgHRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYeaYHG 326
Cdd:cd06841 229 VPDPEDYAeaiaSTLKEYYANKEN-KPKLILEPGRALVDDAGYLLGRVVAVKNRYGRNIAVTDAGINNIPTIFWY--HHP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736826776 327 IDPVERRAVDGVI--YDVVGPVCESGDWLGHDRAL-AIAPGDLLAIRSAGAYGFTMSSNYnTRPRAAEVMVDGN 397
Cdd:cd06841 306 ILVLRPGKEDPTSknYDVYGFNCMESDVLFPNVPLpPLNVGDILAIRNVGAYNMTQSNQF-IRPRPAVYLIDNN 378
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
14-395 |
1.77e-62 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 216.10 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 14 HAEGVALPALAERfGTPLYVYSKAALTsayqAYAKACEGRNA--AVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARV 91
Cdd:PRK08961 489 HAERARLLTLSDA-GSPCYVYHLPTVR----ARARALAALAAvdQRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 92 IAA--GGDPKRAVFSGVGKHADEMRYALEKNVFcFNVESRPELDRLNDVAgqAGKRarVSLRVNPNVDAKTHPYISTGLR 169
Cdd:PRK08961 564 FELfpELSPERVLFTPNFAPRAEYEAAFALGVT-VTLDNVEPLRNWPELF--RGRE--VWLRIDPGHGDGHHEKVRTGGK 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 170 GNKFGVAYEEAFDAYRAAAAMpNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGIslhhIDVGGGLGITYTDE 249
Cdd:PRK08961 639 ESKFGLSQTRIDEFVDLAKTL-GITVVGLHAHLGSGIETGEHWRRMADELASFARRFPDVRT----IDLGGGLGIPESAG 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 250 TPP-DITAFATTLLDhiAKRGHGHRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGID 328
Cdd:PRK08961 714 DEPfDLDALDAGLAE--VKAQHPGYQLWIEPGRYLVAEAGVLLARVTQVKEKDGVRRVGLETGMNSLIRPALYGAYHEIV 791
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736826776 329 PVER-RAVDGVIYDVVGPVCESGDWLGHDRAL-AIAPGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMVD 395
Cdd:PRK08961 792 NLSRlDEPAAGTADVVGPICESSDVLGKRRRLpATAEGDVILIANAGAYGYSMSSTYNLREPAREVVLD 860
|
|
| PLPDE_III_Bif_AspK_DapDC |
cd06840 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bifunctional Aspartate Kinase ... |
30-394 |
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: 203.05 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 30 PLYVYSKAALTsayqAYAKACEGRNA--AVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAA--GGDPKRAVFSG 105
Cdd:cd06840 13 PCYVYDLETVR----ARARQVSALKAvdSLFYAIKANPHPDVLRTLEEAGLGFECVSIGELDLVLKLfpDLDPRRVLFTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 106 VGKHADEMRYALEKNVFC-----FNVESRPELDRlndvagqagkRARVSLRVNPNVDAKTHPYISTGLRGNKFGVAYEEA 180
Cdd:cd06840 89 NFAARSEYEQALELGVNVtvdnlHPLREWPELFR----------GREVILRIDPGQGEGHHKHVRTGGPESKFGLDVDEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 181 FDAYRAAAAMpNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGIslhhIDVGGGLGITYTDETPP-DITAFAT 259
Cdd:cd06840 159 DEARDLAKKA-GIIVIGLHAHSGSGVEDTDHWARHGDYLASLARHFPAVRI----LNVGGGLGIPEAPGGRPiDLDALDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 260 TLLDhiAKRGHGHRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGIDPVERRAVDG-V 338
Cdd:cd06840 234 ALAA--AKAAHPQYQLWMEPGRFIVAESGVLLARVTQIKHKDGVRFVGLETGMNSLIRPALYGAYHEIVNLSRLDEPPaG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1736826776 339 IYDVVGPVCESGDWLGHDRAL-AIAPGDLLAIRSAGAYGFTMSSNYNTRPRAAEVMV 394
Cdd:cd06840 312 NADVVGPICESGDVLGRDRLLpETEEGDVILIANAGAYGFCMASTYNLREPAEEVVL 368
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
32-380 |
1.09e-54 |
|
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: 185.56 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 32 YVYSKAALtSAYQAYAKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDpKRAVFSGVGKHAD 111
Cdd:cd06843 5 YVYDLAAL-RAHARALRASLPPGCELFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAAVPD-APLIFGGPGKTDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 112 EMRYALEKNVFCFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYISTGLRGNKFGVAYEEAFDAYRAAAAMP 191
Cdd:cd06843 83 ELAQALAQGVERIHVESELELRRLNAVARRAGRTAPVLLRVNLALPDLPSSTLTMGGQPTPFGIDEADLPDALELLRDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 192 NLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAA-GISLHHIDVGGGLGITYTD-ETPPDITAFATTLLDHIAKRG 269
Cdd:cd06843 163 NIRLRGFHFHLMSHNLDAAAHLALVKAYLETARQWAAEhGLDLDVVNVGGGIGVNYADpEEQFDWAGFCEGLDQLLAEYE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 270 HGhRQVLFEPGRSLVGNAGVLLTRVEFLKHGETKNFAIVDAAMNDLARPAMYEAYHGI---------DPVERRAVDGVIY 340
Cdd:cd06843 243 PG-LTLRFECGRYISAYCGYYVTEVLDLKRSHGEWFAVLRGGTHHFRLPAAWGHNHPFsvlpveewpYPWPRPSVRDTPV 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1736826776 341 DVVGPVCESGDWLGHD-RALAIAPGDLLAIRSAGAYGFTMS 380
Cdd:cd06843 322 TLVGQLCTPKDVLARDvPVDRLRAGDLVVFPLAGAYGWNIS 362
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
60-390 |
7.96e-48 |
|
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: 167.57 E-value: 7.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 60 AAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVfCFNVESRPELDRLND-V 138
Cdd:cd06836 33 AVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAKTRAELREALELGV-AINIDNFQELERIDAlV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 139 AGQAGKRARVSLRVNPNVDAKTHPYISTGLRGNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHIGSQITEISPYLDATDK 218
Cdd:cd06836 112 AEFKEASSRIGLRVNPQVGAGKIGALSTATATSKFGVALEDGARDEIIDAFARRPWLNGLHVHVGSQGCELSLLAEGIRR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 219 VLDLVEKLEAAGISLH--HIDVGGGLGITY-TDETPPDITAFATTLLDHIAKRGHGHRQVLFEPGRSLVGNAGVLLTRVE 295
Cdd:cd06836 192 VVDLAEEINRRVGRRQitRIDIGGGLPVNFeSEDITPTFADYAAALKAAVPELFDGRYQLVTEFGRSLLAKCGTIVSRVE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 296 FLKHGETKNFAIVDAAMNDLARPA-MYEAYH----GIDPV-ERRAVDGVIYDVVGPVCESGDWLGHDRAL-AIAPGDLLA 368
Cdd:cd06836 272 YTKSSGGRRIAITHAGAQVATRTAyAPDDWPlrvtVFDANgEPKTGPEVVTDVAGPCCFAGDVLAKERALpPLEPGDYVA 351
|
330 340
....*....|....*....|..
gi 1736826776 369 IRSAGAYGFTMSSNYNTRPRAA 390
Cdd:cd06836 352 VHDTGAYYFSSHSSYNSLPRPA 373
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
28-384 |
4.79e-46 |
|
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: 162.28 E-value: 4.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 28 GTPLYVYSKAALTSAYQAYAKACegRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVG 107
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKAL--PRVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFANPC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 108 KHADEMRYALEKNVFCFNVESRPELDRLNDVAgqagKRARVSLRVNPNVDAKTHPYistglrGNKFGVAYEEAFDAYRAA 187
Cdd:cd00622 79 KSISDIRYAAELGVRLFTFDSEDELEKIAKHA----PGAKLLLRIATDDSGALCPL------SRKFGADPEEARELLRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 188 AAMpNLEVVGIDCHIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYtDETPPDITAFATTLLDHIAK 267
Cdd:cd00622 149 KEL-GLNVVGVSFHVGSQCTDPSAYVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSY-DGVVPSFEEIAAVINRALDE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 268 -RGHGHRQVLFEPGRSLVGNAGVLLTRVeflkHGETKNFAIVDAAM---ND-----LARpAMYEAYHG-IDPVERRAVDG 337
Cdd:cd00622 227 yFPDEGVRIIAEPGRYLVASAFTLAVNV----IAKRKRGDDDRERWyylNDgvygsFNE-ILFDHIRYpPRVLKDGGRDG 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1736826776 338 VIYDVV--GPVCESGDWLGHDRAL--AIAPGDLLAIRSAGAYGFTMSSNYN 384
Cdd:cd00622 302 ELYPSSlwGPTCDSLDVIYEDVLLpeDLAVGDWLLFENMGAYTTAYASTFN 352
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
43-255 |
1.28e-45 |
|
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: 156.71 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 43 YQAYAKACeGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVF 122
Cdd:cd06808 5 YRRLREAA-PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 123 CFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAkthpyistglrgNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHI 202
Cdd:cd06808 84 VVTVDSLEELEKLEEAALKAGPPARVLLRIDTGDEN------------GKFGVRPEELKALLERAKELPHLRLVGLHTHF 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1736826776 203 GSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTDETPPDIT 255
Cdd:cd06808 152 GSADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTF 204
|
|
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
20-375 |
6.93e-25 |
|
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: 105.81 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 20 LPALAERFGTPLYVYSK-------AALTSAYQAYakaceGRNAAVHYAAKANSNLAVLGVFAKLGAGFDIVSAGELARVI 92
Cdd:cd06842 1 LVALVEAYGSPLNVLFPqtfreniAALRAVLDRH-----GVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 93 AAGGDPKRAVFSGVGKHADEMRYALEKNVfCFNVESRPELDRLND-VAGQAGKRARVSLRVNPnvDAKTHPyistglrgN 171
Cdd:cd06842 76 AAGVRGDRIVATGPAKTDEFLWLAVRHGA-TIAVDSLDELDRLLAlARGYTTGPARVLLRLSP--FPASLP--------S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 172 KFGVAYEE-AFDAYRAAAAMPNLEVVGIDCHIGSqiTEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITYTD-- 248
Cdd:cd06842 145 RFGMPAAEvRTALERLAQLRERVRLVGFHFHLDG--YSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLAda 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 249 ------------------------------ETPPDITAFATTL-----LDHI-AKRGHGHRQV-----------LFEPGR 281
Cdd:cd06842 223 aeweaflaaltealygygrpltwrneggtlRGPDDFYPYGQPLvaadwLRAIlSAPLPQGRTIaerlrdngitlALEPGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 282 SLVGNAGVLLTRVEFLKHGETKNfAIVDAAMNDL-ARPAMYEAYhgIDPV-------ERRAVDGVIYdVVGPVCESGDWL 353
Cdd:cd06842 303 ALLDQCGLTVARVAFVKQLGDGN-HLIGLEGNSFsACEFSSEFL--VDPLlipapepTTDGAPIEAY-LAGASCLESDLI 378
|
410 420
....*....|....*....|....*
gi 1736826776 354 GHDRAL---AIAPGDLLAIRSAGAY 375
Cdd:cd06842 379 TRRKIPfprLPKPGDLLVFPNTAGY 403
|
|
| PLPDE_III_ADC |
cd06830 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase; This subfamily ... |
16-294 |
3.91e-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: 67.60 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 16 EGVALPALAeRFGTPLyvysKAALTSAYQAYAKACEGRNAAVH----YAAKANSNLAVLGVFAKLG----AGFDIVSAGE 87
Cdd:cd06830 1 RGYGLPLLL-RFPDIL----RHRIERLNAAFAKAIEEYGYKGKyqgvYPIKVNQQREVVEEIVKAGkrynIGLEAGSKPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 88 LARVIAAGGDPKRAVFSGVGKHADEMRYALE-----KNVFcFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHP 162
Cdd:cd06830 76 LLAALALLKTPDALIICNGYKDDEYIELALLarklgHNVI-IVIEKLSELDLILELAKKLGVKPLLGVRIKLASKGSGKW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 163 YISTGLRGnKFGVAYEEAfdayraaaampnLEVVGI-------DC------HIGSQITEISPYLDATDKVLDLVEKLEAA 229
Cdd:cd06830 155 QESGGDRS-KFGLTASEI------------LEVVEKlkeagmlDRlkllhfHIGSQITDIRRIKSALREAARIYAELRKL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736826776 230 GISLHHIDVGGGLGITYtDETPP--------DITAFATTLLDHI----AKRGHGHRQVLFEPGRSLVGNAGVLLTRV 294
Cdd:cd06830 222 GANLRYLDIGGGLGVDY-DGSRSssdssfnySLEEYANDIVKTVkeicDEAGVPHPTIVTESGRAIVAHHSVLIFEV 297
|
|
| PLPDE_III_ODC_like_AZI |
cd06831 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase-like Antizyme ... |
59-294 |
2.14e-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: 52.54 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 59 YAAKANSNLAVLGVFAKLGAGFDIVSAGELARVIAAGGDPKRAVFSGVGKHADEMRYALEKNVFCFNVESRPELDRLndv 138
Cdd:cd06831 41 YTVRCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIYTNPCKQASQIKYAAKVGVNIMTCDNEIELKKI--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 139 agqagkrarvsLRVNPNvdAKTHPYIST-----GLRGN-KFGVAYEEAFDAYRAAAAMpNLEVVGIDCHIGSQITEISPY 212
Cdd:cd06831 118 -----------ARNHPN--AKLLLHIATednigGEEMNmKFGTTLKNCRHLLECAKEL-DVQIVGVKFHVSSSCKEYQTY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 213 LDATDK---VLDLVEKLeaaGISLHHIDVGGGLgiTYTDETPPDITAFATTLLDHIAKRGHGhRQVLFEPGRSLVGNAGV 289
Cdd:cd06831 184 VHALSDarcVFDMAEEF---GFKMNMLDIGGGF--TGSEIQLEEVNHVIRPLLDVYFPEGSG-IQIIAEPGSYYVSSAFT 257
|
....*
gi 1736826776 290 LLTRV 294
Cdd:cd06831 258 LAVNV 262
|
|
| PLPDE_III_CANSDC |
cd06829 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; ... |
29-379 |
1.40e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Carboxynorspermidine Decarboxylase; Carboxynorspermidine decarboxylase (CANSDC) catalyzes the decarboxylation of carboxynorspermidine, the last step in the biosynthesis of norspermidine. It is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Based on this similarity, CANSDC may require homodimer formation and the presence of the PLP cofactor for its catalytic activity.
Pssm-ID: 143502 [Multi-domain] Cd Length: 346 Bit Score: 49.86 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 29 TPLYVYSKAALTSAYQAYAKACEGRNAAVHYAAKANSNLAVLGVFAKLGAGfdiVSAGEL--ARVIAAGGDPKRAVFSgV 106
Cdd:cd06829 1 TPCYVLDEAKLRRNLEILKRVQERSGAKILLALKAFSMWSVFPLIREYLDG---TTASSLfeARLGREEFGGEVHTYS-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 107 GKHADEMRYALE-KNVFCFNveSRPELDRLNDVAgqAGKRARVSLRVNPNvdaktHPYISTGL-----RGNKFGVAYEEA 180
Cdd:cd06829 77 AYRDDEIDEILRlADHIIFN--SLSQLERFKDRA--KAAGISVGLRINPE-----YSEVETDLydpcaPGSRLGVTLDEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 181 FDAYraaaaMPNLEvvGIDCHIgsqITEISPylDATDKVLDLVEKLEAAGIS-LHHIDVGGGLGITYTDEtppDITAFAT 259
Cdd:cd06829 148 EEED-----LDGIE--GLHFHT---LCEQDF--DALERTLEAVEERFGEYLPqLKWLNLGGGHHITRPDY---DVDRLIA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 260 TLLDhiAKRGHGhRQVLFEPGRSLVGNAGVLLTRVEFLKHGEtKNFAIVDAA----MNDLA----RPAMYEAyhgIDPVE 331
Cdd:cd06829 213 LIKR--FKEKYG-VEVYLEPGEAVALNTGYLVATVLDIVENG-MPIAILDASatahMPDVLempyRPPIRGA---GEPGE 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1736826776 332 RravdGVIYDVVGPVCESGDWLGH---DRALAIapGDLLAIRSAGAYgfTM 379
Cdd:cd06829 286 G----AHTYRLGGNSCLAGDVIGDysfDEPLQV--GDRLVFEDMAHY--TM 328
|
|
| PRK05354 |
PRK05354 |
biosynthetic arginine decarboxylase; |
200-246 |
8.32e-06 |
|
biosynthetic arginine decarboxylase;
Pssm-ID: 235427 [Multi-domain] Cd Length: 634 Bit Score: 48.19 E-value: 8.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1736826776 200 CHIGSQITEISPYLDAtdkvldLVE------KLEAAGISLHHIDVGGGLGITY 246
Cdd:PRK05354 251 FHLGSQIANIRDIKTA------VREaarfyvELRKLGAPIQYLDVGGGLGVDY 297
|
|
| SpeA |
COG1166 |
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism]; |
119-246 |
4.43e-05 |
|
Arginine decarboxylase (spermidine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 440780 [Multi-domain] Cd Length: 633 Bit Score: 45.85 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 119 KNVFcFNVESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHPYISTGLRGnKFGVAYEEAfdayraaaampnLEVVG- 197
Cdd:COG1166 167 HKVI-IVIEKLSELELILEEAKELGVKPLIGVRVKLASKGSGKWQNSGGERS-KFGLSASEI------------LEVVEr 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736826776 198 ------IDC------HIGSQITEISPYLDAtdkvldLVE------KLEAAGISLHHIDVGGGLGITY 246
Cdd:COG1166 233 lkeagmLDClqllhfHLGSQIPNIRDIKRA------VREaarfyaELRKLGAPIEYLDVGGGLGVDY 293
|
|
| PLN02439 |
PLN02439 |
arginine decarboxylase |
127-291 |
4.43e-03 |
|
arginine decarboxylase
Pssm-ID: 215240 [Multi-domain] Cd Length: 559 Bit Score: 39.28 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 127 ESRPELDRLNDVAGQAGKRARVSLRVNPNVDAKTHpYISTGLRGNKFGVAYEEAfdayraaaampnLEVVG-------ID 199
Cdd:PLN02439 115 EQEEELDLVIEASQRLGVRPVIGVRAKLRTKHSGH-FGSTSGEKGKFGLTATEI------------VRVVRklrkegmLD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 200 C------HIGSQITEISPYLDATDKVLDLVEKLEAAGISLHHIDVGGGLGITY-------TD-ETPPDITAFATTLL--- 262
Cdd:PLN02439 182 ClqllhfHIGSQIPSTSLLKDGVSEAAQIYCELVRLGAPMRVIDIGGGLGIDYdgsksgsSDmSVAYSLEEYANAVVaav 261
|
170 180 190
....*....|....*....|....*....|
gi 1736826776 263 -DHIAKRGHGHRQVLFEPGRSLVGNAGVLL 291
Cdd:PLN02439 262 rDVCDRKGVKHPVICSESGRALVSHHSVLI 291
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
69-231 |
4.79e-03 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 38.36 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 69 VLGVFAKLGA-GFDIVSAGELARVIAAGGDPKRAVFSGVgkHADEMRYALEKNVFCFnVESRPELDRLNDVAGQAGKRAR 147
Cdd:pfam01168 39 VARALLEGGAdGFAVATLDEALELREAGITAPILVLGGF--PPEELALAAEYDLTPT-VDSLEQLEALAAAARRLGKPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736826776 148 VSLRVNpnvdakthpyisTGLrgNKFGVAYEEAFDAYRAAAAMPNLEVVGIDCHIGSQITEISPYLDA-TDKVLDLVEKL 226
Cdd:pfam01168 116 VHLKID------------TGM--GRLGFRPEEALALLARLAALPGLRLEGLMTHFACADEPDDPYTNAqLARFREAAAAL 181
|
....*
gi 1736826776 227 EAAGI 231
Cdd:pfam01168 182 EAAGL 186
|
|
| |
