|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-357 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 602.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 3 AATAVIDRRALRHNLQQVRRQAPQSRLIAVVKANAYGHGLLETAHTLQDADCYGVARIGEALMLRSGGIVKPILLLEGFF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 83 CAEDLPVLVANNIETAVHSIEQLEALEQAELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSHFSR 162
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 163 ADEPESDATLKQIACFEQFARGKPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSGAEHGLQPAMTLKSSLIA 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 243 VREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPDAADKVGDEAV 322
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 746537223 323 LWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-357 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 601.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 1 MKAATAVIDRRALRHNLQQVRRQAPQ-SRLIAVVKANAYGHGLLETAHTLQ--DADCYGVARIGEALMLRSGGIVKPILL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPkSKLMAVVKANAYGHGAVEVAKTLLeaGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 78 LEGFFCAEDLPVLVANNIETAVHSIEQLEALEQAELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVAQpVNIM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 158 SHFSRADEPESDATLKQIACFEQFARGKPGQ----RSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSGAEHGLQPA 233
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKgkplRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 234 MTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPDA 313
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 746537223 314 ADKVGDEAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:PRK00053 320 QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
4-359 |
1.59e-180 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 504.64 E-value: 1.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 4 ATAVIDRRALRHNLQQVRRQA-PQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEG 80
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFcAEDLPVLVANNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMS 158
Cdd:COG0787 84 VP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGL-EVEGIMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 159 HFSRADEPESDATLKQIACFEQFARG------KPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDnGSGAEHGLQP 232
Cdd:COG0787 162 HFACADEPDHPFTAEQLERFEEAVAAlpaaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 313 AADKVGDEAVLWG-QALPVERIAACTGISAYELITKLTQRVAMEYIGD 359
Cdd:COG0787 321 PDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
1.75e-174 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 489.17 E-value: 1.75e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 2 KAATAVIDRRALRHNLQQVRRQ-APQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 79 EGFFcAEDLPVLVANNIETAVHSIEQLEALEQAELARP--VPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVAQPVNI 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 157 MSHFSRADEPESDATLKQIACFEQFARGKPGQ------RSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGS-GAEHG 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQnieppfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 230 LQPAMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDL 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 310 GPDAADKVGDEAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
6.24e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 253.69 E-value: 6.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 8 IDRRALRHNLQQVRRQA-PQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEGFfCA 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 85 EDLPVLVANNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSHFSR 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGL-RLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746537223 163 ADEPESDATLKQIACFEQFARGKPGQ------RSVAASGGTLLWPDAHNeWVRPGIILYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAglrppvVHLANSAAILLHPLHFD-MVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-356 |
3.10e-56 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 179.57 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPtGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 746537223 313 AADKVGDEAVLWG-QALPVERIAACTGISAYELITKLTQRVAMEY 356
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-357 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 602.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 3 AATAVIDRRALRHNLQQVRRQAPQSRLIAVVKANAYGHGLLETAHTLQDADCYGVARIGEALMLRSGGIVKPILLLEGFF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 83 CAEDLPVLVANNIETAVHSIEQLEALEQAELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSHFSR 162
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 163 ADEPESDATLKQIACFEQFARGKPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSGAEHGLQPAMTLKSSLIA 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 243 VREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPDAADKVGDEAV 322
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 746537223 323 LWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-357 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 601.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 1 MKAATAVIDRRALRHNLQQVRRQAPQ-SRLIAVVKANAYGHGLLETAHTLQ--DADCYGVARIGEALMLRSGGIVKPILL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPkSKLMAVVKANAYGHGAVEVAKTLLeaGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 78 LEGFFCAEDLPVLVANNIETAVHSIEQLEALEQAELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVAQpVNIM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 158 SHFSRADEPESDATLKQIACFEQFARGKPGQ----RSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSGAEHGLQPA 233
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKgkplRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 234 MTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPDA 313
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 746537223 314 ADKVGDEAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:PRK00053 320 QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
4-359 |
1.59e-180 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 504.64 E-value: 1.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 4 ATAVIDRRALRHNLQQVRRQA-PQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEG 80
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFcAEDLPVLVANNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMS 158
Cdd:COG0787 84 VP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGL-EVEGIMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 159 HFSRADEPESDATLKQIACFEQFARG------KPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDnGSGAEHGLQP 232
Cdd:COG0787 162 HFACADEPDHPFTAEQLERFEEAVAAlpaaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 313 AADKVGDEAVLWG-QALPVERIAACTGISAYELITKLTQRVAMEYIGD 359
Cdd:COG0787 321 PDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
1.75e-174 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 489.17 E-value: 1.75e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 2 KAATAVIDRRALRHNLQQVRRQ-APQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 79 EGFFcAEDLPVLVANNIETAVHSIEQLEALEQAELARP--VPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVAQPVNI 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 157 MSHFSRADEPESDATLKQIACFEQFARGKPGQ------RSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGS-GAEHG 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQnieppfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 230 LQPAMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDL 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 310 GPDAADKVGDEAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-357 |
6.64e-149 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 424.60 E-value: 6.64e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 4 ATAVIDRRALRHNLQQVRRQA-PQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEG 80
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALEEagADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFcAEDLPVLVANNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMS 158
Cdd:cd00430 82 TP-PEEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGL-ELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 159 HFSRADEPESDATLKQIACFEQF------ARGKPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDnGSGAEHGLQP 232
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEAlaeleeAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSP-EVKSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 746537223 313 AADKVGDEAVLWG----QALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:cd00430 319 PDVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-357 |
1.89e-141 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 405.27 E-value: 1.89e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 1 MKAATAVIDRRALRHNLQQVRRQAPQSRLIAVVKANAYGHGLLETAHTLQDADCYGVARIGEALMLRSGGIVKPILLLEG 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFCAEDLPVLVANNIETAVHSIEQLEALEQAELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVAQPVnIMSHF 160
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMT-LMSHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 161 SRADEPesDATLKQIACFEQFARGKPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSG-AEHGLQPAMTLKSS 239
Cdd:PRK03646 160 ARADHP--DGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDiANTGLRPVMTLSSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 240 LIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPDAADKVGD 319
Cdd:PRK03646 238 IIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGT 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 746537223 320 EAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYI 357
Cdd:PRK03646 318 PVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
6.24e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 253.69 E-value: 6.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 8 IDRRALRHNLQQVRRQA-PQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEGFfCA 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 85 EDLPVLVANNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSHFSR 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGL-RLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746537223 163 ADEPESDATLKQIACFEQFARGKPGQ------RSVAASGGTLLWPDAHNeWVRPGIILYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAglrppvVHLANSAAILLHPLHFD-MVRPGIALYGLSP 220
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
8-352 |
1.02e-83 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 259.94 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 8 IDRRALRHNLQQVRRQAP-QSRLIAVVKANAYGHGLLETAHTL--QDADCYGVARIGEALMLRSGGIVKPILLLEGFFCA 84
Cdd:PRK13340 45 ISPGAFRHNIKTLRSLLAnKSKVCAVMKADAYGHGIELLMPSIikANVPCIGIASNEEARRVRELGFTGQLLRVRSASPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 85 EdLPVLVANNIETAVHSIEQLEALEQ--AELARPVPVWMKLDT-GMHRLGVRPEQAEAFYQrlcACRNVAQP----VNIM 157
Cdd:PRK13340 125 E-IEQALRYDLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWE---ALRIATLPslgiVGIM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 158 SHFSRADEPESDATLKQiacFEQFARGKPGQRS---------VAASGGTLLWPDAHNEWVRPGIILYGvspldNGSGAEH 228
Cdd:PRK13340 201 THFPNEDEDEVRWKLAQ---FKEQTAWLIGEAGlkrekitlhVANSYATLNVPEAHLDMVRPGGILYG-----DRHPANT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 229 GLQPAMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVD 308
Cdd:PRK13340 273 EYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLMVD 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 309 LGPDAADKVGDEAVLWG----QALPVERIAACTGISAYELITKLTQRV 352
Cdd:PRK13340 353 VTDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYTAWGRTN 400
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
4-357 |
4.53e-80 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This subfamily is composed of Enterococcus gallinarum VanT and similar proteins. VanT is a membrane-bound serine racemase (EC 5.1.1.18) that is essential for vancomycin resistance in Enterococcus gallinarum. It converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. The C-terminal region of this protein contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, which is homologous to the fold type III PLP-dependent enzyme, bacterial alanine racemase (AR). AR 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. On the basis of this similarity, it has been suggested that dimer formation of VanT is required for its catalytic activity, and that it catalyzes the racemization of serine in a mechanistically similar manner to that of alanine by bacterial AR. Some biochemical evidence indicates that VanT also exhibits alanine racemase activity and plays a role in the racemization of L-alanine. VanT contains a unique N-terminal transmembrane domain, which may function as an L-serine transporter. VanT serine racemases are not related to eukaryotic serine racemases, which are fold type II PLP-dependent enzymes.
Pssm-ID: 143498 [Multi-domain] Cd Length: 368 Bit Score: 249.19 E-value: 4.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 4 ATAVIDRRALRHNLQQVRRQAPQ-SRLIAVVKANAYGHGLLETAHTLQDA--DCYGVARIGEALMLRSGGIVKPILLLeG 80
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPStCKLMAVVKANAYGHGDVEVARVLEQIgiDFFAVATIDEGIRLREAGIKGEILIL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFCAEDLPVLVANNIETAVHSIEQLEALEQaeLARPVPVWMKLDTGMHRLGVRPEQAEAFyQRLCACRNVaQPVNIMSHF 160
Cdd:cd06825 81 YTPPVRAKELKKYSLTQTLISEAYAEELSK--YAVNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNL-KVSGIFSHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 161 SRADEPESDA---TLKQIACFEQF-----ARG-KPGQRSVAASGGTLLWPDAHNEWVRPGIILYGV--SPLDNgSGAEHG 229
Cdd:cd06825 157 CVSDSLDEDDiafTKHQIACFDQVladlkARGiEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVlsDPNDP-TKLGLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 230 LQPAMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRS-APTGTPILINGREVPIVGRVSMDMISVD 308
Cdd:cd06825 236 LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMVD 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 746537223 309 LG--PDAadKVGDEAVLWGQ----ALPVERIA--ACTgISAyELITKLTQRVAMEYI 357
Cdd:cd06825 316 VTdiPEV--KEGDTATLIGQdgdeELSADEVArnAHT-ITN-ELLSRIGERVKRIYK 368
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-359 |
1.43e-73 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 243.33 E-value: 1.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 8 IDRRALRHNLQQVR-RQAPQSRLIAVVKANAYGHGLLETAHTLQD--ADCYGVARIGEALMLRSGGIVKPILLLEgffcA 84
Cdd:PRK11930 464 INLNAIVHNLNYYRsKLKPETKIMCMVKAFAYGSGSYEIAKLLQEhrVDYLAVAYADEGVSLRKAGITLPIMVMN----P 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 85 E--DLPVLVANNIETAVHSIEQLEALEQAELARPV---PVWMKLDTGMHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSH 159
Cdd:PRK11930 540 EptSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGItgyPIHIKIDTGMHRLGFEPEDIPELARRLKKQPAL-KVRSVFSH 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 160 FSRADEPESDA-TLKQIACFE------QFARGKPGQRSVAASGGTLLWPDAHNEWVRPGIILYGVSPLDNGSGAehgLQP 232
Cdd:PRK11930 619 LAGSDDPDHDDfTRQQIELFDegseelQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQA---LRN 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGT-PILINGREVPIVGRVSMDMISVDLGp 311
Cdd:PRK11930 696 VSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDMCMIDVT- 774
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 746537223 312 DAADKVGDEAVLWGQALPVERIAACTGISAYELITKLTQRVAMEYIGD 359
Cdd:PRK11930 775 DIDAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-356 |
3.10e-56 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 179.57 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPtGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 746537223 313 AADKVGDEAVLWG-QALPVERIAACTGISAYELITKLTQRVAMEY 356
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
233-356 |
5.81e-56 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 178.71 E-value: 5.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 233 AMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLGPD 312
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 746537223 313 AADKVGDEAVLWGQ----ALPVERIAACTGISAYELITKLTQRVAMEY 356
Cdd:pfam00842 81 PEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-326 |
1.89e-47 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143499 [Multi-domain] Cd Length: 365 Bit Score: 164.44 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 8 IDRRALRHNLQQVRRQAP-QSRLIAVVKANAYGHGLLETAHTL--QDADCYGVARIGEALMLRSGGIVKPILLLEGFFCA 84
Cdd:cd06826 6 ISTGAFENNIKLLKKLLGgNTKLCAVMKADAYGHGIALVMPSIiaQNIPCVGITSNEEARVVREAGFTGKILRVRTATPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 85 EdLPVLVANNIETAVHSIEQLEAL-EQAE-LARPVPVWMKLDT-GMHRLGV--RPEQAEAFYQRLCACRNVaQPVNIMSH 159
Cdd:cd06826 86 E-IEDALAYNIEELIGSLDQAEQIdSLAKrHGKTLPVHLALNSgGMSRNGLelSTAQGKEDAVAIATLPNL-KIVGIMTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 160 FSRADEPESDATLKQiacFEQ-----FARGKPGQRSV----AASGGTLLWPDAHNEWVRPGIILYGVSPldngsgAEHGL 230
Cdd:cd06826 164 FPVEDEDDVRAKLAR---FNEdtawlISNAKLKREKItlhaANSFATLNVPEAHLDMVRPGGILYGDTP------PSPEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 231 QPAMTLKSSLIAVREHKAGEAVGYGGTWVSPRDTRLGVVAMGYGDGYPRSAPTGTPILINGREVPIVGRVSMDMISVDLG 310
Cdd:cd06826 235 KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVT 314
|
330
....*....|....*.
gi 746537223 311 PDAADKVGDEAVLWGQ 326
Cdd:cd06826 315 DIPGVKAGDEVVLFGK 330
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-212 |
4.94e-36 |
|
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: 130.13 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 13 LRHNLQQVRRQAP-QSRLIAVVKANAYghglLETAHTLQD-ADCYGVARIGEALMLRSGGIV-KPILLLEGFFCAEDLPV 89
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANAN----PEVARTLAAlGTGFDVASLGEALLLRAAGIPpEPILFLGPCKQVSELED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 90 LVANN-IETAVHSIEQLEALEQA--ELARPVPVWMKLDTG--MHRLGVRPEQAEAFYQRLCACRNVaQPVNIMSHFSRAD 164
Cdd:cd06808 77 AAEQGvIVVTVDSLEELEKLEEAalKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHL-RLVGLHTHFGSAD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 746537223 165 EpESDATLKQIACFEQFARG------KPGQRSVAASGGTLLW---PDAHNEWVRPGI 212
Cdd:cd06808 156 E-DYSPFVEALSRFVAALDQlgelgiDLEQLSIGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
5-270 |
7.62e-13 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 68.62 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 5 TAVIDRRALRHNLQQVRRQAPQS--RLIAVVKAnaygHGLLETAHTLQDADCYG--VARIGEALMLRSGGIvKPILLLEG 80
Cdd:COG3616 10 ALVLDLDALERNIARMAARAAAHgvRLRPHGKT----HKSPELARRQLAAGAWGitVATLAEAEVLAAAGV-DDILLAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 81 FFCAEDLPVLVA-----NNIETAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRP-EQAEAFYQRLCACRNVaQ 152
Cdd:COG3616 85 LVGPAKLARLAAlaragARLTVLVDSVEQAEALAAAaaAAGRPLRVLVELDVGGGRTGVRPpEAALALARAIAASPGL-R 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 153 PVNIMSHFSRADEPESDATLKQIAcfEQFARgkpgqRSVAA---------------SGGTLLWPDAHNEW----VRPGII 213
Cdd:COG3616 164 LAGLMTYEGHIYGADDAEERRAAA--REELA-----RLAAAaealraaglpcpivsGGGTPTFDFVADLPgvteLRPGSY 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746537223 214 LYGvsPLDNGS-GAEHGLQPAMTLKSSLIAVreHKAGEAVGYGGTWVSPRD---TRLGVVA 270
Cdd:COG3616 237 VFH--DAGYYRyGVCFPFDPALSVLATVVSR--PEPGRAILDAGSKALSGDrgdDGLPVPL 293
|
|
| YhfX |
COG3457 |
Predicted amino acid racemase [Amino acid transport and metabolism]; |
1-322 |
1.94e-08 |
|
Predicted amino acid racemase [Amino acid transport and metabolism];
Pssm-ID: 442680 [Multi-domain] Cd Length: 356 Bit Score: 55.20 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 1 MKAATAVIDRRALRHNLQQVRRQAPQS--RLIAVVKANaygHGLLETAHTLQDADCYGVA--RIGEALMLRSGGIVKPIL 76
Cdd:COG3457 1 IPPPTLVIDLDKIRENARRLVELAAKHgiELYGVTKQF---GGNPEIAKALLDGGIKGIVdsRIKNLKKLKRAGIPHPGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 77 LL------EgffcAEDLpVLVANNIetAVHSIEQLEALEQA--ELARPVPVWMKLDTGMHRLGVRPEQAEAFYQRLCACR 148
Cdd:COG3457 78 LLripmlsE----VEEV-VRYADIS--LNSELETARALSEAakKQGKVHKVILMVDLGDLREGGFPEELVDTVEEILKLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 149 NVaQPVNIMSHFS--RADEPESD--ATLKQIAcfeQFARGKPGQRSVAASGGT-----LLwpdAHNEW------VRPG-I 212
Cdd:COG3457 151 GI-ELAGLGTNLPcfGGVLPTEEnlGTLLELA---ELLEAKFGIKLPIVSGGNstslpLL---AEGTLpkginhLRPGeA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 213 ILYGVSPLDN--GSGAEhglQPAMTLKSSLIavrEHKAGEAVGYGgtwvsprdtRLGVVAMG----YGD-GYPRSAptgt 285
Cdd:COG3457 224 LLLGTDPLNArpIPGLE---QDAFVLVAEII---ELKEKPSVPIG---------EIGRDAFGnapeFGDrGIRKRA---- 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 746537223 286 pILINGR-------------EVPIVGrVSMDMISVDLG-PDAADKVGDEAV 322
Cdd:COG3457 285 -ILAIGRqdvdpegltpidyGIEILG-ASSDHLILDVTdSKEDYKVGDTVV 333
|
|
| PLPDE_III_DSD |
cd06817 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase; This ... |
99-204 |
8.45e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase; This subfamily is composed of chicken D-serine dehydratase (DSD, EC 4.3.1.18) and similar eukaryotic proteins. Chicken DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. It is a fold type III PLP-dependent enzyme with similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as dimers 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. Experimental data suggest that chicken DSD also exists as dimers. Sequence comparison and biochemical experiments show that chicken DSD is distinct from the ubiquitous bacterial DSDs coded by dsdA gene, mammalian L-serine dehydratases (LSD) and mammalian serine racemase (SerRac), which are fold type II PLP-dependent enzymes.
Pssm-ID: 143491 [Multi-domain] Cd Length: 389 Bit Score: 47.33 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 99 VHSIEQLEALEQAEL---ARPVPVWMKLDTGMHRLGVRPE--QAEAFYQRLCACRNVAQPVNIMSH----FSRADEPESD 169
Cdd:cd06817 111 VDNPEQLDFLEQFQPlksGKKWSVFIKVDCGTHRAGVPPEseDAKELIQKLEKASEAVELFGFYSHaghsYSSRSAEDAK 190
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 746537223 170 ATLKQ-IAC---FEQFARGKPGQRSVAAS-GGTllwPDAH 204
Cdd:cd06817 191 EVLREeIEAvltAAKKLKSIQGDRKLTLSvGAT---PTAH 227
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
57-216 |
3.91e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR 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. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 45.15 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 57 VARIGEALMLRSGGiVKPILLLEGFFCAEDLPVLVA-----NNIETAVHSIEQLEALEQAELA--RPVPVWMKLDTGMHR 129
Cdd:cd07376 46 VATLAEAETFAEAG-VKDILMAYPLVGPAAIARLAGllrqeAEFHVLVDSPEALAALAAFAAAhgVRLRVMLEVDVGGHR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 130 LGVRPEQAEAFYQrlcACRNVAQP----VNIMSH---------FSRADEPESDATLKQIACFEQFARGKPGQRSVAASGG 196
Cdd:cd07376 125 SGVRPEEAAALAL---ADAVQASPglrlAGVMAYeghiygaggAREGAQARDQAVAAVRAAAAAAERGLACPTVSGGGTP 201
|
170 180
....*....|....*....|...
gi 746537223 197 TLLWP---DAHNEwVRPGIILYG 216
Cdd:cd07376 202 TYQLTagdRAVTE-LRAGSYVFM 223
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
95-243 |
3.64e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR 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. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143495 [Multi-domain] Cd Length: 361 Bit Score: 38.81 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 95 IETAVHSIEQLEALEQAELAR--PVPVWMKLDTGMHRLGVRPEQ-AEAFYQRLCACRNVaQPVNIM---SHFSRADEPE- 167
Cdd:cd06821 105 FSALVDDLEAAEALSAAAGSAglTLSVLLDVNTGMNRTGIAPGEdAEELYRAIATLPGL-VLAGLHaydGHHRNTDLAEr 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746537223 168 ---SDATLKQIACFEQFARGKPGQRSVAASGGTLLWP-DAHNEWVR--PGIILYGvsplDNGSGAEH---GLQPAMTLKS 238
Cdd:cd06821 184 eaaADAAYKPVLALREALEAAGLPVPELVAGGTPSFPfHAAYTDVEcsPGTFVLW----DAGYGSKLpdlGFKPAALVVT 259
|
....*
gi 746537223 239 SLIAV 243
Cdd:cd06821 260 RVISH 264
|
|
| |
