|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
463-872 |
1.64e-170 |
|
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: 501.02 E-value: 1.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 463 CRDLVREFGSPVNVLNAGALPRNIDELVNAGKQMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVA 542
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 543 GERIILSAAIKPDRLLQLAISNGVVISADSRAEFDRIAALA---GDQAALVAPRVAPDPSlLPPTRFGERSAQW---AEH 616
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALArgyTTGPARVLLRLSPFPA-SLPSRFGMPAAEVrtaLER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 617 LSVPTPGVNVVGLHVHLHGYAAADRATALRECCELIDTLRACGHTPRFIDLGGGVPMSYIDSAEQWARYQDARAAVLDGY 696
Cdd:cd06842 160 LAQLRERVRLVGFHFHLDGYSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAEWEAFLAALTEALYGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 697 ADPFTWK-----ADPLSNTYPFHQSPVRGAWLKDVLSDG------VAQMLIDRGLRLHLEPGRSLLDGCGLILTEVAFVK 765
Cdd:cd06842 240 GRPLTWRneggtLRGPDDFYPYGQPLVAADWLRAILSAPlpqgrtIAERLRDNGITLALEPGRALLDQCGLTVARVAFVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 766 TRSDGLPLVGVAMNRTQCRTTSDDYLIDSLHITDgdtNNVDVDGDGLEAYLVGAYCIEDELILRRRIRFPRGVAPGDIIA 845
Cdd:cd06842 320 QLGDGNHLIGLEGNSFSACEFSSEFLVDPLLIPA---PEPTTDGAPIEAYLAGASCLESDLITRRKIPFPRLPKPGDLLV 396
|
410 420
....*....|....*....|....*..
gi 2486066021 846 IPNTAGYFMHILESASHQIPLATNVVW 872
Cdd:cd06842 397 FPNTAGYQMDFLESRFHRHPLPRRVVV 423
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
1-428 |
5.13e-60 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 211.74 E-value: 5.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 1 MKVAIIGGGPRGLWAAEELLelaRQRSADVDLHVYDD----GRGLAYDvTQPEEWLVNVRS---SIIRTQLGKFDDWLRD 73
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLL---RRAPEPLRITLFEPrpelGRGVAYS-TDSPEHLLNVPAgrmSAFPDDPDHFLRWLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 74 RGVETE-------YPPRRMVGEFLSDSWAALKQHIPRGCKLTEHTTHVEELAPDmesDGRWTIHGE-----RFDEVLLAT 141
Cdd:COG4529 82 NGARAApaidpdaFVPRRLFGEYLRERLAEALARAPAGVRLRHIRAEVVDLERD---DGGYRVTLAdgetlRADAVVLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 142 GHALSWPGALSPADIPnnvRLISSPYPASNLEGIGLQDRVLVRGAALTFIDITRAC----HPAVFIPVTRTGQLMTVKPN 217
Cdd:COG4529 159 GHPPPAPPPGLAAGSP---RYIADPWPPGALARIPPDARVLIIGTGLTAIDVVLSLaargHRGPITALSRRGLLPRAHPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 218 TAGLDLSDILDAGSKKIREVEDLSALRAVLDEVSQQVQQHAGVdddawglGVAWRDMY-------PSIVERASYEGRDSL 290
Cdd:COG4529 236 GAPLPLKFLTPEALEELPLFFAARTARDLLRALRADLAEAEAG-------GVDWRAVIdalrpvlQALWAALSAEERRRF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 291 VGFaeLAREMERVAFGPPPESAAYLNDLVEKGTVDIsHLGR--GDEPLADLVR--------ELDITVVIDAVIPPPGVVP 360
Cdd:COG4529 309 LRH--LRPYWDVHRHRMPPESAARLLALIAAGRLEV-LAGRleDIEAAEGGFVvtgagdgeTLEVDVVINATGPEPDLRR 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486066021 361 GT--LIGHLVEQGHARIRPGTRGLDVEPDGTVVG-----QQHLAAVGRMTEDVVLGNDTLSRtlhrvIPRWAQRV 428
Cdd:COG4529 386 DAdpLLRSLLARGLARPDPLGLGLDVDPDGRVLDadgraSPRLFALGPLARGTLWETTALPE-----IREQAAAL 455
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
455-852 |
4.61e-42 |
|
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: 159.16 E-value: 4.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 455 ELAADPGACRDLVREFGSPVNVLNAGALPRNIDELVNAGKQMGVdtHIFFARKANKALTFVDAVRDAGHGVDVASERELT 534
Cdd:COG0019 9 ELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGA--KVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 535 QVLDRGVAGERIILSAAIKPDRLLQLAISNGV-VISADSRAEFDRIAALAG--DQAALVAPRVAPDPSL---------LP 602
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAAelGKRAPVGLRVNPGVDAgtheyistgGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 603 PTRFGERSAQWAEHLSVP--TPGVNVVGLHVH-------LHGYAAAdrATALReccELIDTLRACGHTPRFIDLGGGVPM 673
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAaaLPGLRLVGLHFHigsqildLEPFEEA--LERLL---ELAEELRELGIDLEWLDLGGGLGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 674 SYIDsaeqwaryqDARAAVLDGYADPftwkadplsntypfhqspvrgawLKDVLSDgvaqmLIDRGLRLHLEPGRSLLDG 753
Cdd:COG0019 242 PYTE---------GDEPPDLEELAAA-----------------------IKEALEE-----LCGLGPELILEPGRALVGN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 754 CGLILTEVAFVKtRSDGLPLVGV--AMN---RtqcrttsdDYLIDSLHitdgDTNNVD-VDGDGLEAY-LVGAYCiE--D 824
Cdd:COG0019 285 AGVLLTRVLDVK-ENGGRRFVIVdaGMNdlmR--------PALYGAYH----PIVPVGrPSGAEAETYdVVGPLC-EsgD 350
|
410 420
....*....|....*....|....*...
gi 2486066021 825 elILRRRIRFPRgVAPGDIIAIPNTAGY 852
Cdd:COG0019 351 --VLGKDRSLPP-LEPGDLLAFLDAGAY 375
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
476-849 |
1.57e-35 |
|
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: 138.00 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 476 VLNAGALPRNIDELVNAgkqMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAAIKPD 555
Cdd:pfam00278 3 VYDLATLRRNYRRWKAA---LPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 556 RLLQLAISNGV-VISADSRAEFDRIAALAGDQAALVAPRVAPDPSL--------LPPTRFG------ERSAQWAEHLsvp 620
Cdd:pfam00278 80 SEIRYALEAGVlCFNVDSEDELEKIAKLAPELVARVALRINPDVDAgthkistgGLSSKFGidledaPELLALAKEL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 621 tpGVNVVGLHVHLhG---YAAADRATALRECCELIDTLRACGHTPRFIDLGGGVPMSYID-SAEQWARYQDARAAVLDGY 696
Cdd:pfam00278 157 --GLNVVGVHFHI-GsqiTDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDePPPDFEEYAAAIREALDEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 697 ADPftwkadplsntypfhqspvrgawlkdvlsdgvaqmlidrGLRLHLEPGRSLLDGCGLILTEVAFVKTrSDGLPLVGV 776
Cdd:pfam00278 234 FPP---------------------------------------DLEIIAEPGRYLVANAGVLVTRVIAVKT-GGGKTFVIV 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486066021 777 --AMNrtqcrTTSDDYLIDSLHITdgdtnNVDVDGDGLEAY---LVGAYCieDEL-ILRRRIRFPRgVAPGDIIAIPNT 849
Cdd:pfam00278 274 daGMN-----DLFRPALYDAYHPI-----PVVKEPGEGPLEtydVVGPTC--ESGdVLAKDRELPE-LEVGDLLAFEDA 339
|
|
| NAD_binding_9 |
pfam13454 |
FAD-NAD(P)-binding; |
4-143 |
3.18e-23 |
|
FAD-NAD(P)-binding;
Pssm-ID: 433222 [Multi-domain] Cd Length: 155 Bit Score: 96.96 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 4 AIIGGGPRGLWAAEELLELARQRsaDVDLHVYDD---GRGLAYDVTQPEEWLVNVRS---SIIRTQLGKFDDWLRDRGVE 77
Cdd:pfam13454 1 AIVGGGPSGLALLERLLARAPKR--PLEITLFDPsppGAGGVYRTDQSPEHLLNVPAsrmSLFPDDPPHFLEWLRARGAL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486066021 78 TE--------YPPRRMVGEFLSDSWAALKQHIPRGCKLTEHTTHVEELAPDmesDGRWTIHGE-----RFDEVLLATGH 143
Cdd:pfam13454 79 DEapgldpddFPPRALYGRYLRDRFEEALARAPAGVTVRVHRARVTDLRPR---GDGYRVLLAdgrtlAADAVVLATGH 154
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
411-873 |
2.84e-09 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 60.87 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 411 DTLSRTLH-RVIPRWAQRVINSasttPRHAHGIPPLTARIEPWAQELAADPGACRDLvrefGSPVNVLNAGALPRNIDEL 489
Cdd:PRK08961 449 DGLLPRLHaELIESGAMPVVFG----PRWREIFGSVRPRPTPWWHAERARLLTLSDA----GSPCYVYHLPTVRARARAL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 490 VNAGkqmGVDtHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDR--GVAGERIILSAAIKPDRLLQLAISNGVV 567
Cdd:PRK08961 521 AALA---AVD-QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVT 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 568 ISADSRAEFDRIAALAGDQAALVapRVAPD---------PSLLPPTRFGERSAQWAEHLSVP-TPGVNVVGLHVHLhGYA 637
Cdd:PRK08961 597 VTLDNVEPLRNWPELFRGREVWL--RIDPGhgdghhekvRTGGKESKFGLSQTRIDEFVDLAkTLGITVVGLHAHL-GSG 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 638 AADRATALRECCELIDTLRACGhTPRFIDLGGGVPMSYidSAEQWARYQDARAAVLDgyadpftwkadPLSNTYPfhqsp 717
Cdd:PRK08961 674 IETGEHWRRMADELASFARRFP-DVRTIDLGGGLGIPE--SAGDEPFDLDALDAGLA-----------EVKAQHP----- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 718 vrgawlkdvlsdgvaqmlidrGLRLHLEPGRSLLDGCGLILTEVAFVKTRsDGLPLVGV--AMNrTQCRTTsddyLIDSL 795
Cdd:PRK08961 735 ---------------------GYQLWIEPGRYLVAEAGVLLARVTQVKEK-DGVRRVGLetGMN-SLIRPA----LYGAY 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 796 HitdgDTNNV---DVDGDGLeAYLVGAYCiEDELILRRRIRFPrGVAPGDIIAIPNTAGYfMHILESASHQIPLATNVVW 872
Cdd:PRK08961 788 H----EIVNLsrlDEPAAGT-ADVVGPIC-ESSDVLGKRRRLP-ATAEGDVILIANAGAY-GYSMSSTYNLREPAREVVL 859
|
.
gi 2486066021 873 P 873
Cdd:PRK08961 860 D 860
|
|
| PRK09897 |
PRK09897 |
FAD-NAD(P)-binding protein; |
2-148 |
8.28e-06 |
|
FAD-NAD(P)-binding protein;
Pssm-ID: 182134 [Multi-domain] Cd Length: 534 Bit Score: 49.35 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 2 KVAIIGGGPRGLWAAEELLElaRQRSADVDLHVYDD--GRGLAY-DVTQPEEWLVNVRS----SIIRTQL----GKFDDW 70
Cdd:PRK09897 3 KIAIVGAGPTGIYTFFSLLQ--QQTPLSISIFEQADeaGVGMPYsDEENSKMMLANIASieipPIYCTYLewlqKQEDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 71 LRDRGVETE------YPPRRMVGEFLSDSWAAL-KQHIPRGCKLTEH-TTHVEELAPDMESDGRWTIHG---ERFDEVLL 139
Cdd:PRK09897 81 LQRYGVKKEtlhdrqFLPRILLGEYFRDQFLRLvDQARQQKFAVAVYeSCQVTDLQITNAGVMLATNQDlpsETFDLAVI 160
|
....*....
gi 2486066021 140 ATGHAlsWP 148
Cdd:PRK09897 161 ATGHV--WP 167
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_Y4yA_like |
cd06842 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Y4yA; This subfamily is composed of the ... |
463-872 |
1.64e-170 |
|
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: 501.02 E-value: 1.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 463 CRDLVREFGSPVNVLNAGALPRNIDELVNAGKQMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVA 542
Cdd:cd06842 1 LVALVEAYGSPLNVLFPQTFRENIAALRAVLDRHGVDGRVYFARKANKSLALVRAAAAAGIGVDVASLAELRQALAAGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 543 GERIILSAAIKPDRLLQLAISNGVVISADSRAEFDRIAALA---GDQAALVAPRVAPDPSlLPPTRFGERSAQW---AEH 616
Cdd:cd06842 81 GDRIVATGPAKTDEFLWLAVRHGATIAVDSLDELDRLLALArgyTTGPARVLLRLSPFPA-SLPSRFGMPAAEVrtaLER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 617 LSVPTPGVNVVGLHVHLHGYAAADRATALRECCELIDTLRACGHTPRFIDLGGGVPMSYIDSAEQWARYQDARAAVLDGY 696
Cdd:cd06842 160 LAQLRERVRLVGFHFHLDGYSAAQRVAALQECLPLIDRARALGLAPRFIDIGGGFPVSYLADAAEWEAFLAALTEALYGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 697 ADPFTWK-----ADPLSNTYPFHQSPVRGAWLKDVLSDG------VAQMLIDRGLRLHLEPGRSLLDGCGLILTEVAFVK 765
Cdd:cd06842 240 GRPLTWRneggtLRGPDDFYPYGQPLVAADWLRAILSAPlpqgrtIAERLRDNGITLALEPGRALLDQCGLTVARVAFVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 766 TRSDGLPLVGVAMNRTQCRTTSDDYLIDSLHITDgdtNNVDVDGDGLEAYLVGAYCIEDELILRRRIRFPRGVAPGDIIA 845
Cdd:cd06842 320 QLGDGNHLIGLEGNSFSACEFSSEFLVDPLLIPA---PEPTTDGAPIEAYLAGASCLESDLITRRKIPFPRLPKPGDLLV 396
|
410 420
....*....|....*....|....*..
gi 2486066021 846 IPNTAGYFMHILESASHQIPLATNVVW 872
Cdd:cd06842 397 FPNTAGYQMDFLESRFHRHPLPRRVVV 423
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
1-428 |
5.13e-60 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 211.74 E-value: 5.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 1 MKVAIIGGGPRGLWAAEELLelaRQRSADVDLHVYDD----GRGLAYDvTQPEEWLVNVRS---SIIRTQLGKFDDWLRD 73
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLL---RRAPEPLRITLFEPrpelGRGVAYS-TDSPEHLLNVPAgrmSAFPDDPDHFLRWLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 74 RGVETE-------YPPRRMVGEFLSDSWAALKQHIPRGCKLTEHTTHVEELAPDmesDGRWTIHGE-----RFDEVLLAT 141
Cdd:COG4529 82 NGARAApaidpdaFVPRRLFGEYLRERLAEALARAPAGVRLRHIRAEVVDLERD---DGGYRVTLAdgetlRADAVVLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 142 GHALSWPGALSPADIPnnvRLISSPYPASNLEGIGLQDRVLVRGAALTFIDITRAC----HPAVFIPVTRTGQLMTVKPN 217
Cdd:COG4529 159 GHPPPAPPPGLAAGSP---RYIADPWPPGALARIPPDARVLIIGTGLTAIDVVLSLaargHRGPITALSRRGLLPRAHPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 218 TAGLDLSDILDAGSKKIREVEDLSALRAVLDEVSQQVQQHAGVdddawglGVAWRDMY-------PSIVERASYEGRDSL 290
Cdd:COG4529 236 GAPLPLKFLTPEALEELPLFFAARTARDLLRALRADLAEAEAG-------GVDWRAVIdalrpvlQALWAALSAEERRRF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 291 VGFaeLAREMERVAFGPPPESAAYLNDLVEKGTVDIsHLGR--GDEPLADLVR--------ELDITVVIDAVIPPPGVVP 360
Cdd:COG4529 309 LRH--LRPYWDVHRHRMPPESAARLLALIAAGRLEV-LAGRleDIEAAEGGFVvtgagdgeTLEVDVVINATGPEPDLRR 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486066021 361 GT--LIGHLVEQGHARIRPGTRGLDVEPDGTVVG-----QQHLAAVGRMTEDVVLGNDTLSRtlhrvIPRWAQRV 428
Cdd:COG4529 386 DAdpLLRSLLARGLARPDPLGLGLDVDPDGRVLDadgraSPRLFALGPLARGTLWETTALPE-----IREQAAAL 455
|
|
| LysA |
COG0019 |
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ... |
455-852 |
4.61e-42 |
|
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: 159.16 E-value: 4.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 455 ELAADPGACRDLVREFGSPVNVLNAGALPRNIDELVNAGKQMGVdtHIFFARKANKALTFVDAVRDAGHGVDVASERELT 534
Cdd:COG0019 9 ELTIEGVDLAELAEEYGTPLYVYDEAALRRNLRALREAFPGSGA--KVLYAVKANSNLAVLRLLAEEGLGADVVSGGELR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 535 QVLDRGVAGERIILSAAIKPDRLLQLAISNGV-VISADSRAEFDRIAALAG--DQAALVAPRVAPDPSL---------LP 602
Cdd:COG0019 87 LALAAGFPPERIVFSGNGKSEEELEEALELGVgHINVDSLSELERLAELAAelGKRAPVGLRVNPGVDAgtheyistgGK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 603 PTRFGERSAQWAEHLSVP--TPGVNVVGLHVH-------LHGYAAAdrATALReccELIDTLRACGHTPRFIDLGGGVPM 673
Cdd:COG0019 167 DSKFGIPLEDALEAYRRAaaLPGLRLVGLHFHigsqildLEPFEEA--LERLL---ELAEELRELGIDLEWLDLGGGLGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 674 SYIDsaeqwaryqDARAAVLDGYADPftwkadplsntypfhqspvrgawLKDVLSDgvaqmLIDRGLRLHLEPGRSLLDG 753
Cdd:COG0019 242 PYTE---------GDEPPDLEELAAA-----------------------IKEALEE-----LCGLGPELILEPGRALVGN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 754 CGLILTEVAFVKtRSDGLPLVGV--AMN---RtqcrttsdDYLIDSLHitdgDTNNVD-VDGDGLEAY-LVGAYCiE--D 824
Cdd:COG0019 285 AGVLLTRVLDVK-ENGGRRFVIVdaGMNdlmR--------PALYGAYH----PIVPVGrPSGAEAETYdVVGPLC-EsgD 350
|
410 420
....*....|....*....|....*...
gi 2486066021 825 elILRRRIRFPRgVAPGDIIAIPNTAGY 852
Cdd:COG0019 351 --VLGKDRSLPP-LEPGDLLAFLDAGAY 375
|
|
| Orn_DAP_Arg_deC |
pfam00278 |
Pyridoxal-dependent decarboxylase, C-terminal sheet domain; These pyridoxal-dependent ... |
476-849 |
1.57e-35 |
|
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: 138.00 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 476 VLNAGALPRNIDELVNAgkqMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAAIKPD 555
Cdd:pfam00278 3 VYDLATLRRNYRRWKAA---LPPRVKIFYAVKANPNPAVLRLLAELGAGFDVASGGELERALAAGVDPERIVFAGPGKTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 556 RLLQLAISNGV-VISADSRAEFDRIAALAGDQAALVAPRVAPDPSL--------LPPTRFG------ERSAQWAEHLsvp 620
Cdd:pfam00278 80 SEIRYALEAGVlCFNVDSEDELEKIAKLAPELVARVALRINPDVDAgthkistgGLSSKFGidledaPELLALAKEL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 621 tpGVNVVGLHVHLhG---YAAADRATALRECCELIDTLRACGHTPRFIDLGGGVPMSYID-SAEQWARYQDARAAVLDGY 696
Cdd:pfam00278 157 --GLNVVGVHFHI-GsqiTDLEPFVEALQRARELFDRLRELGIDLKLLDIGGGFGIPYRDePPPDFEEYAAAIREALDEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 697 ADPftwkadplsntypfhqspvrgawlkdvlsdgvaqmlidrGLRLHLEPGRSLLDGCGLILTEVAFVKTrSDGLPLVGV 776
Cdd:pfam00278 234 FPP---------------------------------------DLEIIAEPGRYLVANAGVLVTRVIAVKT-GGGKTFVIV 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486066021 777 --AMNrtqcrTTSDDYLIDSLHITdgdtnNVDVDGDGLEAY---LVGAYCieDEL-ILRRRIRFPRgVAPGDIIAIPNT 849
Cdd:pfam00278 274 daGMN-----DLFRPALYDAYHPI-----PVVKEPGEGPLEtydVVGPTC--ESGdVLAKDRELPE-LEVGDLLAFEDA 339
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
472-855 |
7.06e-34 |
|
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: 133.97 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 472 SPVNVLNAGALPRNIDELVNAgkqMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAA 551
Cdd:cd06810 1 TPFYVYDLDIIRAHYAALKEA---LPSGVKLFYAVKANPNPHVLRTLAEAGTGFDVASKGELALALAAGVPPERIIFTGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 552 IKPDRLLQLAISNGV-VISADSRAEFDRIAALAG--DQAALVAPRVAPDPSLLP--------PTRFG-ERSAQWAEHLSV 619
Cdd:cd06810 78 AKSVSEIEAALASGVdHIVVDSLDELERLNELAKklGPKARILLRVNPDVSAGThkistgglKSKFGlSLSEARAALERA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 620 PTPGVNVVGLHVHL--HGYAAADRATALRECCELIDTLRACGHTPRFIDLGGGVPMSYIDSAEQWARYQDARAAVLDGYA 697
Cdd:cd06810 158 KELDLRLVGLHFHVgsQILDLETIVQALSDARELIEELVEMGFPLEMLDLGGGLGIPYDEQPLDFEEYAALINPLLKKYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 698 DPftwkadplsntypfhqspvrgawlkdvlsdgvaqmliDRGLRLHLEPGRSLLDGCGLILTEVAFVKTRSDG-LPLVGV 776
Cdd:cd06810 238 PN-------------------------------------DPGVTLILEPGRYIVAQAGVLVTRVVAVKVNGGRfFAVVDG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 777 AMNrTQCRT---TSDDYLIDSLHitdgdtnNVDVDGDGLEAYLVGAYCIEDELILRRRIRFPrgVAPGDIIAIPNTAGYF 853
Cdd:cd06810 281 GMN-HSFRPalaYDAYHPITPLK-------APGPDEPLVPATLAGPLCDSGDVIGRDRLLPE--LEVGDLLVFEDMGAYG 350
|
..
gi 2486066021 854 MH 855
Cdd:cd06810 351 FS 352
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
470-852 |
1.73e-32 |
|
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: 129.91 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 470 FGSPVNVLNAGALPRNIDELVNAGKqmGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILS 549
Cdd:cd06828 1 YGTPLYVYDEATIRENYRRLKEAFS--GPGFKICYAVKANSNLAILKLLAEEGLGADVVSGGELYRALKAGFPPERIVFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 550 AAIKPDRLLQLAISNGVV-ISADSRAEFDRIAALAGDQA--ALVAPRVAPDPSL---------LPPTRFG------ERSA 611
Cdd:cd06828 79 GNGKSDEELELALELGILrINVDSLSELERLGEIAPELGkgAPVALRVNPGVDAgthpyistgGKDSKFGipleqaLEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 612 QWAEHLsvptPGVNVVGLHVHLhG---------YAAADRAtalrecCELIDTLRACGHTPRFIDLGGGVPMSYIDsaeqw 682
Cdd:cd06828 159 RRAKEL----PGLKLVGLHCHI-GsqildlepfVEAAEKL------LDLAAELRELGIDLEFLDLGGGLGIPYRD----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 683 aryqDARAAVLDGYADPftwkadplsntypfhqspvrgawLKDVLSDGVAQMlidRGLRLHLEPGRSLLDGCGLILTEVA 762
Cdd:cd06828 223 ----EDEPLDIEEYAEA-----------------------IAEALKELCEGG---PDLKLIIEPGRYIVANAGVLLTRVG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 763 FVKtRSDGLPLVGV--AMNrtqcrttsDdyLI-----DSLH-IT------DGDTNNVDVdgdgleaylVGAYCiE--Del 826
Cdd:cd06828 273 YVK-ETGGKTFVGVdaGMN--------D--LIrpalyGAYHeIVpvnkpgEGETEKVDV---------VGPIC-EsgD-- 329
|
410 420
....*....|....*....|....*.
gi 2486066021 827 ILRRRIRFPRgVAPGDIIAIPNTAGY 852
Cdd:cd06828 330 VFAKDRELPE-VEEGDLLAIHDAGAY 354
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
466-854 |
2.17e-31 |
|
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: 126.99 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 466 LVREFGSPVNVLNAGALPRNIDELVNAGKQMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGER 545
Cdd:cd06841 1 LLESYGSPFFVFDEDALRENYRELLGAFKKRYPNVVIAYSYKTNYLPAICKILHEEGGYAEVVSAMEYELALKLGVPGKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 546 IILSAAIKPDRLLQLAISNGVVISADSRAEFDRIAALAGDQA--ALVAPRVAPDPSLLPPTRFGERSAQWAEHL-----S 618
Cdd:cd06841 81 IIFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGrvAKVGIRLNMNYGNNVWSRFGFDIEENGEALaalkkI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 619 VPTPGVNVVGLHVH---LHGYAAADRATALReCCELIDTLRacGHTPRFIDLGGGVPMsyiDSAEQWARYQDARAAVLDG 695
Cdd:cd06841 161 QESKNLSLVGLHCHvgsNILNPEAYSAAAKK-LIELLDRLF--GLELEYLDLGGGFPA---KTPLSLAYPQEDTVPDPED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 696 YADPFtwkADPLSNTYPfhqspvrgawlkdvlsDGVAQMlidrglRLHLEPGRSLLDGCGLILTEVAFVKTRSD------ 769
Cdd:cd06841 235 YAEAI---ASTLKEYYA----------------NKENKP------KLILEPGRALVDDAGYLLGRVVAVKNRYGrniavt 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 770 --GLPLVGVAMNRTQcrttsdDYLIDSLHITDGDTNNVDVdgdgleaylVGAYCIEDElILRRRIRFPRgVAPGDIIAIP 847
Cdd:cd06841 290 daGINNIPTIFWYHH------PILVLRPGKEDPTSKNYDV---------YGFNCMESD-VLFPNVPLPP-LNVGDILAIR 352
|
....*..
gi 2486066021 848 NTAGYFM 854
Cdd:cd06841 353 NVGAYNM 359
|
|
| NAD_binding_9 |
pfam13454 |
FAD-NAD(P)-binding; |
4-143 |
3.18e-23 |
|
FAD-NAD(P)-binding;
Pssm-ID: 433222 [Multi-domain] Cd Length: 155 Bit Score: 96.96 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 4 AIIGGGPRGLWAAEELLELARQRsaDVDLHVYDD---GRGLAYDVTQPEEWLVNVRS---SIIRTQLGKFDDWLRDRGVE 77
Cdd:pfam13454 1 AIVGGGPSGLALLERLLARAPKR--PLEITLFDPsppGAGGVYRTDQSPEHLLNVPAsrmSLFPDDPPHFLEWLRARGAL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486066021 78 TE--------YPPRRMVGEFLSDSWAALKQHIPRGCKLTEHTTHVEELAPDmesDGRWTIHGE-----RFDEVLLATGH 143
Cdd:pfam13454 79 DEapgldpddFPPRALYGRYLRDRFEEALARAPAGVTVRVHRARVTDLRPR---GDGYRVLLAdgrtlAADAVVLATGH 154
|
|
| PLPDE_III_Btrk_like |
cd06839 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Btrk Decarboxylase; This subfamily is ... |
466-852 |
2.75e-20 |
|
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: 93.81 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 466 LVREFGSPVNVLNAGALPRNIDELVNAgkqMGVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGER 545
Cdd:cd06839 1 LADAYGTPFYVYDRDRVRERYAALRAA---LPPAIEIYYSLKANPNPALVAHLRQLGDGAEVASAGELALALEAGVPPEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 546 IILSAAIKPDRLLQLAISNGVV-ISADSRAEFDRIAALAGDQA--ALVAPRVAPDPSLLP--------PTRFG--ERSAQ 612
Cdd:cd06839 78 ILFAGPGKSDAELRRAIEAGIGtINVESLEELERIDALAEEHGvvARVALRINPDFELKGsgmkmgggPSQFGidVEELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 613 WAEHLSVPTPGVNVVGLHVHL-------HGYAAADR---ATALRECCELidtlracGHTPRFIDLGGGVPMSYidsaeqw 682
Cdd:cd06839 158 AVLARIAALPNLRFVGLHIYPgtqildaDALIEAFRqtlALALRLAEEL-------GLPLEFLDLGGGFGIPY------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 683 arYQDARAAVLDGYADPFtwkADPLSNTYPFHQSPvrgawlkdvlsdgvaqmlidrglRLHLEPGRSLLDGCGLILTEVA 762
Cdd:cd06839 224 --FPGETPLDLEALGAAL---AALLAELGDRLPGT-----------------------RVVLELGRYLVGEAGVYVTRVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 763 FVKtRSDGLPLVgvamnrtqcrttsddylidslhITDGDTN--------------------NVDVDGDGLE--AYLVGAY 820
Cdd:cd06839 276 DRK-VSRGETFL----------------------VTDGGMHhhlaasgnfgqvlrrnyplaILNRMGGEERetVTVVGPL 332
|
410 420 430
....*....|....*....|....*....|...
gi 2486066021 821 CI-EDelILRRRIRFPRgVAPGDIIAIPNTAGY 852
Cdd:cd06839 333 CTpLD--LLGRNVELPP-LEPGDLVAVLQSGAY 362
|
|
| PLPDE_III_ODC |
cd00622 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Ornithine Decarboxylase; This subfamily ... |
471-852 |
5.17e-19 |
|
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: 89.86 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 471 GSPVNVLNAGALPRNIDELVNAGKqmgvDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSA 550
Cdd:cd00622 1 ETPFLVVDLGDVVRKYRRWKKALP----RVRPFYAVKCNPDPAVLRTLAALGAGFDCASKGEIELVLGLGVSPERIIFAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 551 AIKPDRLLQLAISNGV-VISADSRAEFDRIAALAGDqaALVAPRVAPDPS--LLP-PTRFG----------ERSAQWaeh 616
Cdd:cd00622 77 PCKSISDIRYAAELGVrLFTFDSEDELEKIAKHAPG--AKLLLRIATDDSgaLCPlSRKFGadpeearellRRAKEL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 617 lsvptpGVNVVGLHVHLhGYAAADR---ATALRECCELIDTLRACGHTPRFIDLGGGVPMSYIDSAEQwaryqdaraavL 693
Cdd:cd00622 152 ------GLNVVGVSFHV-GSQCTDPsayVDAIADAREVFDEAAELGFKLKLLDIGGGFPGSYDGVVPS-----------F 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 694 DGYAdpftwkadplsntypfhqspvrgawlkDVLSDGVAQMLIDRGLRLHLEPGRSLLDGCGLILTEVAFVKTRSDGLPL 773
Cdd:cd00622 214 EEIA---------------------------AVINRALDEYFPDEGVRIIAEPGRYLVASAFTLAVNVIAKRKRGDDDRE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 774 V------GV--AMNrtqCrtTSDDYLIDSLHItdgdTNNVDVDGDGLEAYLVGAYCieDEL-ILRRRIRFPRGVAPGDII 844
Cdd:cd00622 267 RwyylndGVygSFN---E--ILFDHIRYPPRV----LKDGGRDGELYPSSLWGPTC--DSLdVIYEDVLLPEDLAVGDWL 335
|
....*...
gi 2486066021 845 AIPNTAGY 852
Cdd:cd00622 336 LFENMGAY 343
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
502-765 |
2.66e-18 |
|
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: 87.72 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 502 IFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRgVAGERIILSAAIKPDRLLQLAISNGV-VISADSRAEFDRIA 580
Cdd:cd06843 29 LFYAIKANSDPPILRALAPHVDGFEVASGGEIAHVRAA-VPDAPLIFGGPGKTDSELAQALAQGVeRIHVESELELRRLN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 581 ALAGD--QAALVAPRVAPDPSLLP---------PTRFG--ERSAQWAEHLSVPTPGVNVVGLHVHL--HGYAAADRATAL 645
Cdd:cd06843 108 AVARRagRTAPVLLRVNLALPDLPsstltmggqPTPFGidEADLPDALELLRDLPNIRLRGFHFHLmsHNLDAAAHLALV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 646 RECCELIDTLRA-CGHTPRFIDLGGGVPMSYIDSAEQwaryqdaraavldgyadpFTWkadplsntypfhqspvrgawlk 724
Cdd:cd06843 188 KAYLETARQWAAeHGLDLDVVNVGGGIGVNYADPEEQ------------------FDW---------------------- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2486066021 725 DVLSDGVAQMLIDR--GLRLHLEPGRSLLDGCGLILTEVAFVK 765
Cdd:cd06843 228 AGFCEGLDQLLAEYepGLTLRFECGRYISAYCGYYVTEVLDLK 270
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
497-675 |
5.62e-16 |
|
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: 77.74 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 497 GVDTHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAAIKPDRLLQLAISNGV-VISADSRAE 575
Cdd:cd06808 13 PAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEDAAEQGViVVTVDSLEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 576 FDRIAALAGDQA--ALVAPRVAPDPSLLpptRFGERSAQWAEHLSV--PTPGVNVVGLHVHLhGYAAADRAT---ALREC 648
Cdd:cd06808 93 LEKLEEAALKAGppARVLLRIDTGDENG---KFGVRPEELKALLERakELPHLRLVGLHTHF-GSADEDYSPfveALSRF 168
|
170 180
....*....|....*....|....*..
gi 2486066021 649 CELIDTLRACGHTPRFIDLGGGVPMSY 675
Cdd:cd06808 169 VAALDQLGELGIDLEQLSIGGSFAILY 195
|
|
| Orn_Arg_deC_N |
pfam02784 |
Pyridoxal-dependent decarboxylase, pyridoxal binding domain; These pyridoxal-dependent ... |
502-681 |
1.31e-15 |
|
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: 77.32 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 502 IFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAAIKPDRLLQLAISNGV-VISADSRAEFDRIA 580
Cdd:pfam02784 20 PFYAVKCNSDPAVLRLLAELGTGFDCASKGELERVLAAGVPPERIIFANPCKQRSFLRYALEVGVgCVTVDNVDELEKLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 581 ALAGDQAALVapRVAPDPSL-LPP--TRFGERSAQWAEHL--SVPTPGVNVVGLHVHLhGYAAADR---ATALRECCELI 652
Cdd:pfam02784 100 RLAPEARVLL--RIKPDDSAaTCPlsSKFGADLDEDVEALleAAKLLNLQVVGVSFHV-GSGCTDAeafVLALEDARGVF 176
|
170 180
....*....|....*....|....*....
gi 2486066021 653 DTLRACGHTPRFIDLGGGVPMSYIDSAEQ 681
Cdd:pfam02784 177 DQGAELGFNLKILDLGGGFGVDYTEGEEP 205
|
|
| PLPDE_III_ODC_DapDC_like_1 |
cd06836 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Uncharacterized Proteins with ... |
474-854 |
1.63e-15 |
|
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: 79.36 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 474 VNVLNAGALPRNIDELVNAGKQMGVDThifFARKANKALTFVDAVRDAGHGVDVASERELTQVLDRGVAGERIILSAAIK 553
Cdd:cd06836 5 VGLYDLDGFRALVARLTAAFPAPVLHT---FAVKANPLVPVLRLLAEAGAGAEVASPGELELALAAGFPPERIVFDSPAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 554 PDRLLQLAISNGVVISADSRAEFDRIAAL---AGDQAALVAPRVAP--------DPSLLPPT-RFG----ERSAQWAEHL 617
Cdd:cd06836 82 TRAELREALELGVAINIDNFQELERIDALvaeFKEASSRIGLRVNPqvgagkigALSTATATsKFGvaleDGARDEIIDA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 618 SVPTPGVNvvGLHVHL--HGYA------AADRATALRECCELIDTLRACGhtprFIDLGGGVPMSYiDSAEQWARYQDAR 689
Cdd:cd06836 162 FARRPWLN--GLHVHVgsQGCElsllaeGIRRVVDLAEEINRRVGRRQIT----RIDIGGGLPVNF-ESEDITPTFADYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 690 AAVLdgyadpftwKADPLsntypfhqspvrgawlkdvlsdgvaqmLIDRGLRLHLEPGRSLLDGCGLILTEVAFVKTRSD 769
Cdd:cd06836 235 AALK---------AAVPE---------------------------LFDGRYQLVTEFGRSLLAKCGTIVSRVEYTKSSGG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 770 GLPLVGVAMNRTQCRTTsddYLIDS--LHITDGDTNNVDVDGDGLEAYLVGAYCIEDELILRRRIrFPRgVAPGDIIAIP 847
Cdd:cd06836 279 RRIAITHAGAQVATRTA---YAPDDwpLRVTVFDANGEPKTGPEVVTDVAGPCCFAGDVLAKERA-LPP-LEPGDYVAVH 353
|
....*..
gi 2486066021 848 NTAGYFM 854
Cdd:cd06836 354 DTGAYYF 360
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
411-873 |
2.84e-09 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 60.87 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 411 DTLSRTLH-RVIPRWAQRVINSasttPRHAHGIPPLTARIEPWAQELAADPGACRDLvrefGSPVNVLNAGALPRNIDEL 489
Cdd:PRK08961 449 DGLLPRLHaELIESGAMPVVFG----PRWREIFGSVRPRPTPWWHAERARLLTLSDA----GSPCYVYHLPTVRARARAL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 490 VNAGkqmGVDtHIFFARKANKALTFVDAVRDAGHGVDVASERELTQVLDR--GVAGERIILSAAIKPDRLLQLAISNGVV 567
Cdd:PRK08961 521 AALA---AVD-QRFYAIKANPHPAILRTLEEEGFGFECVSIGELRRVFELfpELSPERVLFTPNFAPRAEYEAAFALGVT 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 568 ISADSRAEFDRIAALAGDQAALVapRVAPD---------PSLLPPTRFGERSAQWAEHLSVP-TPGVNVVGLHVHLhGYA 637
Cdd:PRK08961 597 VTLDNVEPLRNWPELFRGREVWL--RIDPGhgdghhekvRTGGKESKFGLSQTRIDEFVDLAkTLGITVVGLHAHL-GSG 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 638 AADRATALRECCELIDTLRACGhTPRFIDLGGGVPMSYidSAEQWARYQDARAAVLDgyadpftwkadPLSNTYPfhqsp 717
Cdd:PRK08961 674 IETGEHWRRMADELASFARRFP-DVRTIDLGGGLGIPE--SAGDEPFDLDALDAGLA-----------EVKAQHP----- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 718 vrgawlkdvlsdgvaqmlidrGLRLHLEPGRSLLDGCGLILTEVAFVKTRsDGLPLVGV--AMNrTQCRTTsddyLIDSL 795
Cdd:PRK08961 735 ---------------------GYQLWIEPGRYLVAEAGVLLARVTQVKEK-DGVRRVGLetGMN-SLIRPA----LYGAY 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 796 HitdgDTNNV---DVDGDGLeAYLVGAYCiEDELILRRRIRFPrGVAPGDIIAIPNTAGYfMHILESASHQIPLATNVVW 872
Cdd:PRK08961 788 H----EIVNLsrlDEPAAGT-ADVVGPIC-ESSDVLGKRRRLP-ATAEGDVILIANAGAY-GYSMSSTYNLREPAREVVL 859
|
.
gi 2486066021 873 P 873
Cdd:PRK08961 860 D 860
|
|
| PRK09897 |
PRK09897 |
FAD-NAD(P)-binding protein; |
2-148 |
8.28e-06 |
|
FAD-NAD(P)-binding protein;
Pssm-ID: 182134 [Multi-domain] Cd Length: 534 Bit Score: 49.35 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 2 KVAIIGGGPRGLWAAEELLElaRQRSADVDLHVYDD--GRGLAY-DVTQPEEWLVNVRS----SIIRTQL----GKFDDW 70
Cdd:PRK09897 3 KIAIVGAGPTGIYTFFSLLQ--QQTPLSISIFEQADeaGVGMPYsDEENSKMMLANIASieipPIYCTYLewlqKQEDSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 71 LRDRGVETE------YPPRRMVGEFLSDSWAAL-KQHIPRGCKLTEH-TTHVEELAPDMESDGRWTIHG---ERFDEVLL 139
Cdd:PRK09897 81 LQRYGVKKEtlhdrqFLPRILLGEYFRDQFLRLvDQARQQKFAVAVYeSCQVTDLQITNAGVMLATNQDlpsETFDLAVI 160
|
....*....
gi 2486066021 140 ATGHAlsWP 148
Cdd:PRK09897 161 ATGHV--WP 167
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
505-590 |
2.91e-03 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 41.37 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486066021 505 ARKANKALTFVDAVRDAGHGVDVASERELTQVLD-RGVAGeriilsAAIKPDRLLQLAISNGVV-ISADSRAEFDRIAAL 582
Cdd:PRK13800 710 ALRAGDAALFAAALGDPDHRVRIEAVRALVSVDDvESVAG------AATDENREVRIAVAKGLAtLGAGGAPAGDAVRAL 783
|
....*...
gi 2486066021 583 AGDQAALV 590
Cdd:PRK13800 784 TGDPDPLV 791
|
|
| |
