|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
6-355 |
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: 620.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 6 RAEISSTALQNNLAVLRQQASSSQVMAVVKANGYGHGLLNVAHCLHTADGFGLARLEEALELREGGIKARLLLLEGFFRS 85
Cdd:cd06827 3 RATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 86 TDLPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAkPIHLMTHFACAD 165
Cdd:cd06827 83 DELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVA-SIVLMTHFACAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 166 EPDNHYTQVQMQTFNQLTADLPGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGDCGANHGLIPAMNLVSRLIAVR 245
Cdd:cd06827 162 EPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 246 EHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDAADQVGDDVLLW 325
Cdd:cd06827 242 ELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVELW 321
|
330 340 350
....*....|....*....|....*....|
gi 1273062169 326 GQALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:cd06827 322 GKGLPVDEVAAAAGTIGYELLCRLTPRVPR 351
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-356 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 584.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 1 MKPfPRAEISSTALQNNLAVLRQQA-SSSQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLL 77
Cdd:PRK00053 1 MRP-ATAEIDLDALRHNLRQIRKHApPKSKLMAVVKANAYGHGAVEVAKTLLEagADGFGVATLEEALELREAGITAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 78 LLEGFFRSTDLPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAKpIHL 157
Cdd:PRK00053 80 ILGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 158 MTHFACADEPDNHYTQVQMQTFNQLTADLPGF----RTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGDCGANHGLIP 233
Cdd:PRK00053 159 FSHFATADEPDNSYTEQQLNRFEAALAGLPGKgkplRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1273062169 314 AADQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAVC 356
Cdd:PRK00053 319 PQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRV 361
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-353 |
1.15e-176 |
|
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: 494.63 E-value: 1.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 6 RAEISSTALQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIKARLLLLEGF 82
Cdd:COG0787 5 WAEIDLDALRHNLRVLRALAGPgAKLMAVVKADAYGHGAVEVARALleAGADGFAVATLEEALELREAGIDAPILVLGGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 83 FRStDLPLLVEHDIDTVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVaKPIHLMTH 160
Cdd:COG0787 85 PPE-DLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGL-EVEGIMSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 161 FACADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPKSQGDWIRPGIALYGVSPvTGDCGANHGLIPA 234
Cdd:COG0787 163 FACADEPDHPFTAEQLERFEEAVAALPAagldppLRHLANSAAILRYPEAHFDMVRPGIALYGLSP-SPEVAADLGLKPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 235 MNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDA 314
Cdd:COG0787 242 MTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDIP 321
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1273062169 315 ADQVGDDVLLWG-QALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:COG0787 322 DVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRV 361
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-355 |
3.35e-148 |
|
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: 422.53 E-value: 3.35e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 7 AEISSTALQNNLAVLRQQ-ASSSQVMAVVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIKARLLLLEGFF 83
Cdd:TIGR00492 5 VEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLLGGFF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 84 RStDLPLLVEHDIDTVVHHESQIEMLEQAHLTKP--VTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAKPIHLMTHF 161
Cdd:TIGR00492 85 AE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIFSHF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 162 ACADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPKSQGDWIRPGIALYGVSPvTGDC--GANHGLIP 233
Cdd:TIGR00492 164 ATADEPKTGTTQKQIERFNSFLEGLKQqnieppFRHIANSAAILNWPESHFDMVRPGIILYGLYP-SADMsdGAPFGLKP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:TIGR00492 243 VLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPD 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1273062169 314 AADQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:TIGR00492 323 LQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPR 364
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-220 |
2.32e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 254.84 E-value: 2.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 9 ISSTALQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLLLLEGFfRS 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 86 TDLPLLVEHDIDTVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVaKPIHLMTHFAC 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGL-RLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1273062169 164 ADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPkSQGDWIRPGIALYGVSP 220
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAaglrppVVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
234-353 |
1.04e-59 |
|
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: 188.43 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPeGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1273062169 314 AADQVGDDVLLWG-QALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRV 120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
6-355 |
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: 620.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 6 RAEISSTALQNNLAVLRQQASSSQVMAVVKANGYGHGLLNVAHCLHTADGFGLARLEEALELREGGIKARLLLLEGFFRS 85
Cdd:cd06827 3 RATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 86 TDLPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAkPIHLMTHFACAD 165
Cdd:cd06827 83 DELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVA-SIVLMTHFACAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 166 EPDNHYTQVQMQTFNQLTADLPGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGDCGANHGLIPAMNLVSRLIAVR 245
Cdd:cd06827 162 EPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 246 EHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDAADQVGDDVLLW 325
Cdd:cd06827 242 ELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVELW 321
|
330 340 350
....*....|....*....|....*....|
gi 1273062169 326 GQALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:cd06827 322 GKGLPVDEVAAAAGTIGYELLCRLTPRVPR 351
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-356 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 584.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 1 MKPfPRAEISSTALQNNLAVLRQQA-SSSQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLL 77
Cdd:PRK00053 1 MRP-ATAEIDLDALRHNLRQIRKHApPKSKLMAVVKANAYGHGAVEVAKTLLEagADGFGVATLEEALELREAGITAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 78 LLEGFFRSTDLPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAKpIHL 157
Cdd:PRK00053 80 ILGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 158 MTHFACADEPDNHYTQVQMQTFNQLTADLPGF----RTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGDCGANHGLIP 233
Cdd:PRK00053 159 FSHFATADEPDNSYTEQQLNRFEAALAGLPGKgkplRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1273062169 314 AADQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAVC 356
Cdd:PRK00053 319 PQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRV 361
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-353 |
1.15e-176 |
|
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: 494.63 E-value: 1.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 6 RAEISSTALQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIKARLLLLEGF 82
Cdd:COG0787 5 WAEIDLDALRHNLRVLRALAGPgAKLMAVVKADAYGHGAVEVARALleAGADGFAVATLEEALELREAGIDAPILVLGGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 83 FRStDLPLLVEHDIDTVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVaKPIHLMTH 160
Cdd:COG0787 85 PPE-DLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGL-EVEGIMSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 161 FACADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPKSQGDWIRPGIALYGVSPvTGDCGANHGLIPA 234
Cdd:COG0787 163 FACADEPDHPFTAEQLERFEEAVAALPAagldppLRHLANSAAILRYPEAHFDMVRPGIALYGLSP-SPEVAADLGLKPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 235 MNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDA 314
Cdd:COG0787 242 MTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDIP 321
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1273062169 315 ADQVGDDVLLWG-QALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:COG0787 322 DVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRV 361
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-355 |
3.35e-148 |
|
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: 422.53 E-value: 3.35e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 7 AEISSTALQNNLAVLRQQ-ASSSQVMAVVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIKARLLLLEGFF 83
Cdd:TIGR00492 5 VEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLLGGFF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 84 RStDLPLLVEHDIDTVVHHESQIEMLEQAHLTKP--VTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAKPIHLMTHF 161
Cdd:TIGR00492 85 AE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIFSHF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 162 ACADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPKSQGDWIRPGIALYGVSPvTGDC--GANHGLIP 233
Cdd:TIGR00492 164 ATADEPKTGTTQKQIERFNSFLEGLKQqnieppFRHIANSAAILNWPESHFDMVRPGIILYGLYP-SADMsdGAPFGLKP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:TIGR00492 243 VLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPD 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1273062169 314 AADQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:TIGR00492 323 LQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPR 364
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
6-353 |
1.01e-142 |
|
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: 408.81 E-value: 1.01e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 6 RAEISSTALQNNLAVLRQQA-SSSQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLLLLEGF 82
Cdd:cd00430 3 WAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALEEagADYFAVATLEEALELREAGITAPILVLGGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 83 FRStDLPLLVEHDIDTVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVaKPIHLMTH 160
Cdd:cd00430 83 PPE-EAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGL-ELEGVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 161 FACADEPDNHYTQVQMQTFNQLTADL------PGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPvTGDCGANHGLIPA 234
Cdd:cd00430 161 FATADEPDKAYTRRQLERFLEALAELeeagipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYP-SPEVKSPLGLKPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 235 MNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDA 314
Cdd:cd00430 240 MSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1273062169 315 ADQVGDDVLLWG----QALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:cd00430 320 DVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRV 362
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-355 |
2.69e-142 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 407.19 E-value: 2.69e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 1 MKPFpRAEISSTALQNNLAVLRQQASSSQVMAVVKANGYGHGLLNVAHCLHTADGFGLARLEEALELREGGIKARLLLLE 80
Cdd:PRK03646 1 TRPI-QASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 81 GFFRSTDLPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVAKpIHLMTH 160
Cdd:PRK03646 80 GFFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGE-MTLMSH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 161 FACADEPDNhyTQVQMQTFNQLTADLPGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGDCG-ANHGLIPAMNLVS 239
Cdd:PRK03646 159 FARADHPDG--ISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDiANTGLRPVMTLSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 240 RLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQDAADQVG 319
Cdd:PRK03646 237 EIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIG 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1273062169 320 DDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:PRK03646 317 TPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPV 352
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-220 |
2.32e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 254.84 E-value: 2.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 9 ISSTALQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLLLLEGFfRS 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 86 TDLPLLVEHDIDTVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACENVaKPIHLMTHFAC 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGL-RLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1273062169 164 ADEPDNHYTQVQMQTFNQLTADLPG------FRTLANSAGALYWPkSQGDWIRPGIALYGVSP 220
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAaglrppVVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
7-353 |
2.39e-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: 249.96 E-value: 2.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 7 AEISSTALQNNLAVL-RQQASSSQVMAVVKANGYGHGLLNVAHCLHTA--DGFGLARLEEALELREGGIKARLLLLeGFF 83
Cdd:cd06825 4 LEIDLSALEHNVKEIkRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIgiDFFAVATIDEGIRLREAGIKGEILIL-GYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 84 RSTDLPLLVEHD-IDTVVHHESQIEMLEQAHltkPVTVWLKVDSGMHRLGVTPEQFTTVYARLAAcenvaKPIH---LMT 159
Cdd:cd06825 83 PPVRAKELKKYSlTQTLISEAYAEELSKYAV---NIKVHLKVDTGMHRLGESPEDIDSILAIYRL-----KNLKvsgIFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 160 HFA---CADEPDNHYTQVQMQTFNQLTADL------PGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPVTGD-CGANH 229
Cdd:cd06825 155 HLCvsdSLDEDDIAFTKHQIACFDQVLADLkargieVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPNDpTKLGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 230 GLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRN-APEGTPVWINGRRVPIVGRVSMDMLTV 308
Cdd:cd06825 235 DLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1273062169 309 DLGQDAADQVGDDVLLWGQ----ALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:cd06825 315 DVTDIPEVKEGDTATLIGQdgdeELSADEVARNAHTITNELLSRIGERV 363
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
7-355 |
5.30e-80 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 250.31 E-value: 5.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 7 AEISSTALQNNLAVLRQQA-SSSQVMAVVKANGYGHGLLNVAHCLHT--ADGFGLARLEEALELREGGIKARLLLLEGFF 83
Cdd:PRK13340 43 LEISPGAFRHNIKTLRSLLaNKSKVCAVMKADAYGHGIELLMPSIIKanVPCIGIASNEEARRVRELGFTGQLLRVRSAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 84 RStDLPLLVEHDIDTVVHHESQIEMLEQ--AHLTKPVTVWLKVDS-GMHRLGVTPEQFTTVY--ARLAACENVaKPIHLM 158
Cdd:PRK13340 123 PA-EIEQALRYDLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWeaLRIATLPSL-GIVGIM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 159 THFACADEPDnhyTQVQMQTFNQLTADLPGFRTL---------ANSAGALYWPKSQGDWIRPGIALYGVSPVtgdcgANH 229
Cdd:PRK13340 201 THFPNEDEDE---VRWKLAQFKEQTAWLIGEAGLkrekitlhvANSYATLNVPEAHLDMVRPGGILYGDRHP-----ANT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 230 GLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVD 309
Cdd:PRK13340 273 EYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLMVD 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1273062169 310 LGQDAADQVGDDVLLWG----QALPVEEVAEHIGTIAYELVTKL---TPRVAV 355
Cdd:PRK13340 353 VTDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYTAWgrtNPRIYV 405
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-353 |
2.25e-69 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 232.16 E-value: 2.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 8 EISSTALQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIkarllllegffr 84
Cdd:PRK11930 463 EINLNAIVHNLNYYRSKLKPeTKIMCMVKAFAYGSGSYEIAKLLqeHRVDYLAVAYADEGVSLRKAGI------------ 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 85 stDLPLLV----EHDIDTVVHHE------------SQIEMLEQAHLTKPvTVWLKVDSGMHRLGVTPEQFTTVYARLAAC 148
Cdd:PRK11930 531 --TLPIMVmnpePTSFDTIIDYKlepeiysfrlldAFIKAAQKKGITGY-PIHIKIDTGMHRLGFEPEDIPELARRLKKQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 149 ENVaKPIHLMTHFACADEPDNH-YTQVQMQTF----NQLTADL--PGFRTLANSAGALYWPKSQGDWIRPGIALYGVSPV 221
Cdd:PRK11930 608 PAL-KVRSVFSHLAGSDDPDHDdFTRQQIELFdegsEELQEALgyKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSAS 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 222 TGDcgaNHGLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGT-PVWINGRRVPIVGR 300
Cdd:PRK11930 687 GAG---QQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGN 763
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1273062169 301 VSMDMLTVDLGqDAADQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:PRK11930 764 ICMDMCMIDVT-DIDAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRV 815
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
234-353 |
1.04e-59 |
|
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: 188.43 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPeGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1273062169 314 AADQVGDDVLLWG-QALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRV 120
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
234-353 |
8.22e-59 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 186.03 E-value: 8.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 234 AMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGQD 313
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1273062169 314 AADQVGDDVLLWGQ----ALPVEEVAEHIGTIAYELVTKLTPRV 353
Cdd:pfam00842 81 PEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRV 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-355 |
4.30e-43 |
|
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: 152.88 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 8 EISSTALQNNLAVLRQQA-SSSQVMAVVKANGYGHGLLNV--AHCLHTADGFGLARLEEALELREGGIKARLLLLegffR 84
Cdd:cd06826 5 EISTGAFENNIKLLKKLLgGNTKLCAVMKADAYGHGIALVmpSIIAQNIPCVGITSNEEARVVREAGFTGKILRV----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 85 STD-------LPLLVEHDIDTVVHHESQIEMLEQAHLTKPVTVWLKvDSGMHRLGV--TPEQFTTVYARLAACENVaKPI 155
Cdd:cd06826 81 TATpseiedaLAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALN-SGGMSRNGLelSTAQGKEDAVAIATLPNL-KIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 156 HLMTHFACADEPDnhyTQVQMQTFNQLTADLPGFRTL---------ANSAGALYWPKSQGDWIRPGIALYGvspvtgDCG 226
Cdd:cd06826 159 GIMTHFPVEDEDD---VRAKLARFNEDTAWLISNAKLkrekitlhaANSFATLNVPEAHLDMVRPGGILYG------DTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 227 ANHGLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDML 306
Cdd:cd06826 230 PSPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1273062169 307 TVDLGQDAADQVGDDVLLWG-------QALPVEEVAEHIGTIAYELVTKLTPRVAV 355
Cdd:cd06826 310 MVDVTDIPGVKAGDEVVLFGkqggaeiTAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
14-213 |
3.43e-37 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 133.21 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 14 LQNNLAVLRQQASS-SQVMAVVKANGYGHGLLNVAHClhtADGFGLARLEEALELREGGIK-ARLLLLEGFFRSTDLPLL 91
Cdd:cd06808 1 IRHNYRRLREAAPAgITLFAVVKANANPEVARTLAAL---GTGFDVASLGEALLLRAAGIPpEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 92 VEH-DIDTVVHHESQIEMLEQAHLT--KPVTVWLKVDSG--MHRLGVTPEQFTTVYARLAACENVaKPIHLMTHFACADE 166
Cdd:cd06808 78 AEQgVIVVTVDSLEELEKLEEAALKagPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHL-RLVGLHTHFGSADE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1273062169 167 pDNHYTQVQMQTFNQLTADL------PGFRTLANSAGALYWPKSQG---DWIRPGI 213
Cdd:cd06808 157 -DYSPFVEALSRFVAALDQLgelgidLEQLSIGGSFAILYLQELPLgtfIIVEPGR 211
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|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
4-322 |
3.03e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing 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. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 48.31 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 4 FPRAEISSTALQNNLAVLRQQASSS--QVMAVVKANgygHGLLNVAHCLHTA--DGFGLARLEEALELREGGIKARLLLL 79
Cdd:cd06815 1 YPRLEINLSKIRHNAKVLVELCKSRgiEVTGVTKVV---CGDPEIAEALLEGgiTHLADSRIENLKKLKDLGISGPKMLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 80 EgffrstdLPLLveHDIDTVVHH--------ESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFTTVYARLAACE 149
Cdd:cd06815 78 R-------IPML--SEVEDVVKYadislnseLETIKALSEEakKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 150 NvakpIHLM---THFAC--ADEPDNHytqvQMQTFNQLTADLP---GFRTLANSAG---ALYWPKsQGDW------IRPG 212
Cdd:cd06815 149 G----IELVgigTNLGCygGVLPTEE----NMGKLVELKEEIEkefGIKLPIISGGnsaSLPLLL-KGELpgginqLRIG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 213 IALY-GVSPVTGDcganhgLIP-----AMNLVSRLIAVREhKANQPVG-YG-------CYWTAKQDTRLGVVAIGYGDgy 278
Cdd:cd06815 220 EAILlGRETTYNE------PIPglyqdAFTLEAEIIEIKE-KPSVPIGeIGldafgnkPEFEDRGIRKRAILAIGRQD-- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1273062169 279 prNAPEG-TPVwINGrrVPIVGRVSmDMLTVDLG-QDAADQVGDDV 322
Cdd:cd06815 291 --VDPDGlTPV-DNG--IEILGASS-DHLILDITdSDRDYKVGDEI 330
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
5-148 |
1.73e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; Low specificity D-threonine aldolase (Low specificity D-TA, EC 4.3.1.18), encoded by dtaAS gene from Arthrobacter sp. strain DK-38, is the prototype of this subfamily. Low specificity D-TAs are fold type III PLP-dependent enzymes that catalyze the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Members of this subfamily show 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 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: 143493 [Multi-domain] Cd Length: 358 Bit Score: 39.89 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 5 PRAEISS-------TALQNNLAVLRQQASSSQVMavVKANGYGHGLLNVAHCL--HTADGFGLARLEEALELREGGIK-- 73
Cdd:cd06819 1 PLAEIDTpalvldlDALERNIKRMAAFAKAHGVR--LRPHAKTHKCPAIARRQiaAGAVGVCCQKLSEAEVMAAAGIRdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273062169 74 ------------ARLLLLegfFRSTDLPLlvehdidtVVHHESQIEMLEQA--HLTKPVTVWLKVDSGMHRLGVTPEQFT 139
Cdd:cd06819 79 litnevvgpakiARLAAL---ARRAPLIV--------CVDHPDNVRALAAAavEAGVRLDVLVEIDVGQGRCGVPPGEAA 147
|
....*....
gi 1273062169 140 TVYARLAAC 148
Cdd:cd06819 148 LALARTIAA 156
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
89-151 |
1.95e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine Aldolase-like; This subfamily is composed of uncharacterized bacterial proteins with similarity to low specificity D-threonine aldolase (D-TA), which is a fold type III PLP-dependent enzyme that catalyzes the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Low specificity D-TAs show 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 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: 143494 [Multi-domain] Cd Length: 353 Bit Score: 39.61 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273062169 89 PLLVEHDIDTVVHHESQIEMLEQ--AHLTKPVTVWLKVDSGMHRLGV-TPEQFTTVYARLAACENV 151
Cdd:cd06820 91 ALAERVTLSVGVDSAEVARGLAEvaEGAGRPLEVLVEVDSGMNRCGVqTPEDAVALARAIASAPGL 156
|
|
| PLPDE_III_DSD |
cd06817 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase; This ... |
100-136 |
5.80e-03 |
|
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: 38.47 E-value: 5.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1273062169 100 VHHESQIEMLEQAHL---TKPVTVWLKVDSGMHRLGVTPE 136
Cdd:cd06817 111 VDNPEQLDFLEQFQPlksGKKWSVFIKVDCGTHRAGVPPE 150
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