|
Name |
Accession |
Description |
Interval |
E-value |
| dadX |
PRK03646 |
catabolic alanine racemase; |
2-356 |
0e+00 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 713.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 2 TRPIQASLDLQALKQNLSIVRQAATHARVWSVVKANAYGHGIERIWSAIGATDGFALLNLEEAITLRERGWKGPILMLEG 81
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 82 FFHAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFA 161
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 162 EAEHPDGISGAMARIEQAAEGLECRRSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 241
Cdd:PRK03646 161 RADHPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 242 VQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPCPQAGIGTPVE 321
Cdd:PRK03646 241 VQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVE 320
|
330 340 350
....*....|....*....|....*....|....*
gi 16129153 322 LWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:PRK03646 321 LWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-356 |
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: 599.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 4 PIQASLDLQALKQNLSIVRQAATHARVWSVVKANAYGHGIERIWSAIGATDGFALLNLEEAITLRERGWKGPILMLEGFF 83
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 84 HAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFAEA 163
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 164 EHPD--GISGAMARIEQAAEGLECRRSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRdIANTGLRPVMTLSSEIIG 241
Cdd:cd06827 161 DEPDspGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 242 VQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPCPQAGIGTPVE 321
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 16129153 322 LWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-356 |
0e+00 |
|
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: 521.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 3 RPIQASLDLQALKQNLSIVR-QAATHARVWSVVKANAYGHGIERIWSAIGA--TDGFALLNLEEAITLRERGWKGPILML 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRnHIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 80 EGFFhAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAP--LDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGE-MTL 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLElEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 157 MSHFAEAEHP--DGISGAMARIEQAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRDIANTG 228
Cdd:TIGR00492 160 FSHFATADEPktGTTQKQIERFNSFLEGLKQQnieppfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 229 LRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDL 308
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16129153 309 TPCPQAGIGTPVELWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-356 |
1.88e-162 |
|
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: 458.80 E-value: 1.88e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 2 TRPIQASLDLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAI---GAtDGFALLNLEEAITLRERGWKGPIL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRAlAGPGAKLMAVVKADAYGHGAVEVARALleaGA-DGFAVATLEEALELREAGIDAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 78 MLEGFFhAQDLEIYDQHRLTTCVHSNWQLKALQNA--RLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMT 155
Cdd:COG0787 80 VLGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 156 LMSHFAEAEHPD--GISGAMARIEQAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQwrDIANT 227
Cdd:COG0787 159 IMSHFACADEPDhpFTAEQLERFEEAVAALPAAgldpplRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE--VAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 228 GLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVD 307
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16129153 308 LTPCPQAGIGTPVELWGKE-IKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:COG0787 317 VTDIPDVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-217 |
5.99e-72 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 223.26 E-value: 5.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 9 LDLQALKQNLSIVRQAATH-ARVWSVVKANAYGHGIERIWSAI--GATDGFALLNLEEAITLRERGWKGPILMLEGFfHA 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 86 QDLEIYDQHRLTTCVHSNWQLKALQNARLKA--PLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFAEA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLgkPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129153 164 EHPDGISGA--MARIEQAAEGLECR------RSLSNSAATLWHPeAHFDWVRPGIILYGASP 217
Cdd:pfam01168 160 DEPDDPYTNaqLARFREAAAALEAAglrppvVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
232-354 |
4.53e-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: 178.80 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 232 VMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPtGTPVLVDGVRTMTVGTVSMDMLAVDLTPC 311
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16129153 312 PQAGIGTPVELWGK-EIKIDDVAAAAGTVGYELMCALALRVPVV 354
Cdd:smart01005 80 PDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRV 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| dadX |
PRK03646 |
catabolic alanine racemase; |
2-356 |
0e+00 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 713.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 2 TRPIQASLDLQALKQNLSIVRQAATHARVWSVVKANAYGHGIERIWSAIGATDGFALLNLEEAITLRERGWKGPILMLEG 81
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 82 FFHAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFA 161
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 162 EAEHPDGISGAMARIEQAAEGLECRRSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 241
Cdd:PRK03646 161 RADHPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 242 VQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPCPQAGIGTPVE 321
Cdd:PRK03646 241 VQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVE 320
|
330 340 350
....*....|....*....|....*....|....*
gi 16129153 322 LWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:PRK03646 321 LWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-356 |
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: 599.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 4 PIQASLDLQALKQNLSIVRQAATHARVWSVVKANAYGHGIERIWSAIGATDGFALLNLEEAITLRERGWKGPILMLEGFF 83
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 84 HAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFAEA 163
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 164 EHPD--GISGAMARIEQAAEGLECRRSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRdIANTGLRPVMTLSSEIIG 241
Cdd:cd06827 161 DEPDspGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 242 VQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPCPQAGIGTPVE 321
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 16129153 322 LWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-356 |
0e+00 |
|
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: 521.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 3 RPIQASLDLQALKQNLSIVR-QAATHARVWSVVKANAYGHGIERIWSAIGA--TDGFALLNLEEAITLRERGWKGPILML 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRnHIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 80 EGFFhAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAP--LDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGE-MTL 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLElEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 157 MSHFAEAEHP--DGISGAMARIEQAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRDIANTG 228
Cdd:TIGR00492 160 FSHFATADEPktGTTQKQIERFNSFLEGLKQQnieppfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 229 LRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDL 308
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16129153 309 TPCPQAGIGTPVELWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-356 |
1.88e-162 |
|
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: 458.80 E-value: 1.88e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 2 TRPIQASLDLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAI---GAtDGFALLNLEEAITLRERGWKGPIL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRAlAGPGAKLMAVVKADAYGHGAVEVARALleaGA-DGFAVATLEEALELREAGIDAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 78 MLEGFFhAQDLEIYDQHRLTTCVHSNWQLKALQNA--RLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMT 155
Cdd:COG0787 80 VLGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 156 LMSHFAEAEHPD--GISGAMARIEQAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQwrDIANT 227
Cdd:COG0787 159 IMSHFACADEPDhpFTAEQLERFEEAVAALPAAgldpplRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE--VAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 228 GLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVD 307
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16129153 308 LTPCPQAGIGTPVELWGKE-IKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:COG0787 317 VTDIPDVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
3-356 |
2.56e-158 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 448.09 E-value: 2.56e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 3 RPIQASLDLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAI---GAtDGFALLNLEEAITLRERGWKGPILM 78
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLleaGA-DGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 79 LEGFFHAQDLEIYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMS 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 159 HFAEAEHPDG--ISGAMARIEQAAEGLE----CRRSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQwRDIANTGLRPV 232
Cdd:PRK00053 161 HFATADEPDNsyTEQQLNRFEAALAGLPgkgkPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 233 MTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPCP 312
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16129153 313 QAGIGTPVELWGKEIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:PRK00053 320 QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
1-356 |
1.94e-123 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 361.25 E-value: 1.94e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 1 MTRPIQASLDLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAIGAT--DGFALLNLEEAITLRERGWKGPIL 77
Cdd:PRK13340 37 QPRNAWLEISPGAFRHNIKTLRSlLANKSKVCAVMKADAYGHGIELLMPSIIKAnvPCIGIASNEEARRVRELGFTGQLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 78 MLEGFfHAQDLEIYDQHRLTTCVHSNWQLKALQNARLKA--PLDIYLKVNS-GMNRLGFQPDRVLTVWQQLRA--MANVG 152
Cdd:PRK13340 117 RVRSA-SPAEIEQALRYDLEELIGDDEQAKLLAAIAKKNgkPIDIHLALNSgGMSRNGLDMSTARGKWEALRIatLPSLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 153 EMTLMSHFAEAEHpDGISGAMARIEQAAEGLECRRSL---------SNSAATLWHPEAHFDWVRPGIILYGAspsgqwRD 223
Cdd:PRK13340 196 IVGIMTHFPNEDE-DEVRWKLAQFKEQTAWLIGEAGLkrekitlhvANSYATLNVPEAHLDMVRPGGILYGD------RH 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 224 IANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDM 303
Cdd:PRK13340 269 PANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNT 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129153 304 LAVDLTPCPQAGIGTPVELWGK----EIKIDDVAAAAGTVGYELMCALALRVPVVTV 356
Cdd:PRK13340 349 LMVDVTDIPNVKPGDEVVLFGKqgnaEITVDEVEEASGTIFPELYTAWGRTNPRIYV 405
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-352 |
5.64e-120 |
|
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: 351.03 E-value: 5.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 7 ASLDLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAI---GAtDGFALLNLEEAITLRERGWKGPILMLeGF 82
Cdd:cd00430 4 AEIDLDALRHNLRVIRRlLGPGTKIMAVVKADAYGHGAVEVAKALeeaGA-DYFAVATLEEALELREAGITAPILVL-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 83 FHAQDLEIYDQHRLTTCVHSNWQLKALQNA--RLKAPLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVgEMT-LMSH 159
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGL-ELEgVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 160 FAEAEHPDGISGAM--ARIEQAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQWRDIAntGLRP 231
Cdd:cd00430 161 FATADEPDKAYTRRqlERFLEALAELEEAgippplKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL--GLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 232 VMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPC 311
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16129153 312 PQAGIGTPVELWGK----EIKIDDVAAAAGTVGYELMCALALRVP 352
Cdd:cd00430 319 PDVKVGDEVVLFGRqgdeEITAEELAELAGTINYEILCRISKRVP 363
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-217 |
5.99e-72 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 223.26 E-value: 5.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 9 LDLQALKQNLSIVRQAATH-ARVWSVVKANAYGHGIERIWSAI--GATDGFALLNLEEAITLRERGWKGPILMLEGFfHA 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 86 QDLEIYDQHRLTTCVHSNWQLKALQNARLKA--PLDIYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFAEA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLgkPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129153 164 EHPDGISGA--MARIEQAAEGLECR------RSLSNSAATLWHPeAHFDWVRPGIILYGASP 217
Cdd:pfam01168 160 DEPDDPYTNaqLARFREAAAALEAAglrppvVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
9-354 |
2.16e-63 |
|
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: 206.05 E-value: 2.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 9 LDLQALKQNLSIVrQAATHA--RVWSVVKANAYGHG---IERIWSAIGaTDGFALLNLEEAITLRERGWKGPILMLeGFF 83
Cdd:cd06825 6 IDLSALEHNVKEI-KRLLPStcKLMAVVKANAYGHGdveVARVLEQIG-IDFFAVATIDEGIRLREAGIKGEILIL-GYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 84 HAQDLEIYDQHRLTTCVHSNWQLKALqnARLKAPLDIYLKVNSGMNRLGFQPDRVLTVwQQLRAMANVGEMTLMSHFAEA 163
Cdd:cd06825 83 PPVRAKELKKYSLTQTLISEAYAEEL--SKYAVNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNLKVSGIFSHLCVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 164 EH--PDGISGAMARIE---QAAEGLECR------RSLSNSAATLWHPEAHFDWVRPGIILYGaSPSGQWRDIANT-GLRP 231
Cdd:cd06825 160 DSldEDDIAFTKHQIAcfdQVLADLKARgievgkIHIQSSYGILNYPDLKYDYVRPGILLYG-VLSDPNDPTKLGlDLRP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 232 VMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRH-APTGTPVLVDGVRTMTVGTVSMDMLAVDLTP 310
Cdd:cd06825 239 VLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMVDVTD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16129153 311 CPQAGIGTPVELWGK----EIKIDDVAAAAGTVGYELMCALALRVPVV 354
Cdd:cd06825 319 IPEVKEGDTATLIGQdgdeELSADEVARNAHTITNELLSRIGERVKRI 366
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
10-351 |
4.10e-58 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 201.34 E-value: 4.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 10 DLQALKQNLSIVRQAAT-HARVWSVVKANAYG------------HGIERIwsAIGATDgfallnleEAITLRERGWKGPI 76
Cdd:PRK11930 465 NLNAIVHNLNYYRSKLKpETKIMCMVKAFAYGsgsyeiakllqeHRVDYL--AVAYAD--------EGVSLRKAGITLPI 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 77 LMLEGFFHAQDLEIydQHRLTTCVHSNWQLKAL-QNARLKAPLD--IYLKVNSGMNRLGFQPDRVLTVWQQLRAMANVGE 153
Cdd:PRK11930 535 MVMNPEPTSFDTII--DYKLEPEIYSFRLLDAFiKAAQKKGITGypIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKV 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 154 MTLMSHFAEAEHPDGISGAMARIEQAAEGLECR---------RSLSNSAATLWHPEAHFDWVRPGIILYGASPSGQwrdi 224
Cdd:PRK11930 613 RSVFSHLAGSDDPDHDDFTRQQIELFDEGSEELqealgykpiRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGA---- 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 225 ANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGT-PVLVDGVRTMTVGTVSMDM 303
Cdd:PRK11930 689 GQQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDM 768
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16129153 304 LAVDLTPCPqAGIGTPVELWGKEIKIDDVAAAAGTVGYELMCALALRV 351
Cdd:PRK11930 769 CMIDVTDID-AKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRV 815
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
232-354 |
4.53e-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: 178.80 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 232 VMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPtGTPVLVDGVRTMTVGTVSMDMLAVDLTPC 311
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16129153 312 PQAGIGTPVELWGK-EIKIDDVAAAAGTVGYELMCALALRVPVV 354
Cdd:smart01005 80 PDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRV 123
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
232-354 |
1.04e-55 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 177.94 E-value: 1.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 232 VMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLAVDLTPC 311
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 16129153 312 PQAGIGTPVELWGK----EIKIDDVAAAAGTVGYELMCALALRVPVV 354
Cdd:pfam00842 81 PEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRV 127
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
10-343 |
3.46e-42 |
|
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: 150.57 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 10 DLQALKQNLSIVRQ-AATHARVWSVVKANAYGHGIERIWSAIGATD--GFALLNLEEAITLRERGWKGPILMLEGffhAQ 86
Cdd:cd06826 7 STGAFENNIKLLKKlLGGNTKLCAVMKADAYGHGIALVMPSIIAQNipCVGITSNEEARVVREAGFTGKILRVRT---AT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 87 DLEIYD--QHRLTTCVHSNWQLKALQN--ARLKAPLDIYLKVNS-GMNRLGFQpdrvLTVWQ---QLRAMANVGEMT--- 155
Cdd:cd06826 84 PSEIEDalAYNIEELIGSLDQAEQIDSlaKRHGKTLPVHLALNSgGMSRNGLE----LSTAQgkeDAVAIATLPNLKivg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 156 LMSHFAeAEHPDGISGAMARIEQ------AAEGLEcRRSL----SNSAATLWHPEAHFDWVRPGIILYGASPsgqwrdiA 225
Cdd:cd06826 160 IMTHFP-VEDEDDVRAKLARFNEdtawliSNAKLK-REKItlhaANSFATLNVPEAHLDMVRPGGILYGDTP-------P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 226 NTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARDEQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTMTVGTVSMDMLA 305
Cdd:cd06826 231 SPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVM 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16129153 306 VDLTPCPQAGIGTPVELWGK----EIKIDDVAAAAGTVGYEL 343
Cdd:cd06826 311 VDVTDIPGVKAGDEVVLFGKqggaEITAAEIEEGSGTILAEL 352
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
14-210 |
1.02e-18 |
|
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: 83.52 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 14 LKQNLSIVRQAA-THARVWSVVKANAYGHGIEriwSAIGATDGFALLNLEEAITLRERGWKG-PILMLEGFFHAQDLEIY 91
Cdd:cd06808 1 IRHNYRRLREAApAGITLFAVVKANANPEVAR---TLAALGTGFDVASLGEALLLRAAGIPPePILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129153 92 DQHRLTTC-VHSNWQLKALQNARLKA--PLDIYLKVNSG--MNRLGFQPDRVLTVWQQLRAMANVGEMTLMSHFAEA-EH 165
Cdd:cd06808 78 AEQGVIVVtVDSLEELEKLEEAALKAgpPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSAdED 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16129153 166 PDGISGAMARIEQAAEGLECR------RSLSNSAATLWH---PEAHFDWVRPGI 210
Cdd:cd06808 158 YSPFVEALSRFVAALDQLGELgidleqLSIGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
92-232 |
1.46e-04 |
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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: 43.07 E-value: 1.46e-04
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gi 16129153 92 DQHRLTTCVHSNWQLKALQNARLKA--PLDIYLKVNSGMNRLGFQ-PDRVLTVWQQLRAMANVGEMTLMSHFAEAEHPDG 168
Cdd:cd06820 94 ERVTLSVGVDSAEVARGLAEVAEGAgrPLEVLVEVDSGMNRCGVQtPEDAVALARAIASAPGLRFRGIFTYPGHSYAPGA 173
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90 100 110 120 130 140 150 160
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gi 16129153 169 ISGAM---ARIEQAAE------GLECRRSLSNSAATLWHPEAHF--DWVRPGIILYG-----ASPSGQWRDIANTGLRPV 232
Cdd:cd06820 174 LEEAAadeAEALLAAAgileeaGLEPPVVSGGSTPTLWRSHEVPgiTEIRPGTYIFNdasqvALGACTLDDCALTVLATV 253
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