|
Name |
Accession |
Description |
Interval |
E-value |
| dadX |
PRK03646 |
catabolic alanine racemase; |
2-355 |
0e+00 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 2 SRPIQASLDLQALRHNLEVVRRAAPRSRVWSVVKANAYGHGLDRVWSALGATDGFAMLNLEEAILLRERGWKGPILMLEG 81
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 82 FFHADELPLFDKYRLTTSVHSNWQLKALAEAKLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFA 161
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 162 DADRPDGIDAAMVRIEQAAEGIDAPRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRDIATSGLQPVMTLKSEIIG 241
Cdd:PRK03646 161 RADHPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 242 VQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCPQAGIGSPVE 321
Cdd:PRK03646 241 VQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVE 320
|
330 340 350
....*....|....*....|....*....|....
gi 495163301 322 LWGNEIKIDDVAAACGTIGYELMCALAPRVPVST 355
Cdd:PRK03646 321 LWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-353 |
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: 595.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 4 PIQASLDLQALRHNLEVVRRAAPRSRVWSVVKANAYGHGLDRVWSALGATDGFAMLNLEEAILLRERGWKGPILMLEGFF 83
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 84 HADELPLFDKYRLTTSVHSNWQLKALAEAKLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFADA 163
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 164 DRPD--GIDAAMVRIEQAAEGIDAPRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRdIATSGLQPVMTLKSEIIG 241
Cdd:cd06827 161 DEPDspGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 242 VQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCPQAGIGSPVE 321
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|..
gi 495163301 322 LWGNEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPR 351
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-352 |
7.27e-167 |
|
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: 469.97 E-value: 7.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 2 SRPIQASLDLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL---GAtDGFAMLNLEEAILLRERGWKGPIL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRaLAGPGAKLMAVVKADAYGHGAVEVARALleaGA-DGFAVATLEEALELREAGIDAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 78 MLEGFFhADELPLFDKYRLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQIT 155
Cdd:COG0787 80 VLGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 156 LMAHFADADRPD--GIDAAMVRIEQAAEGIDA------PRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQwrDIATS 227
Cdd:COG0787 159 IMSHFACADEPDhpFTAEQLERFEEAVAALPAagldppLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE--VAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 228 GLQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVD 307
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 495163301 308 LTPCPQAGIGSPVELWG-NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:COG0787 317 VTDIPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVP 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-353 |
2.63e-161 |
|
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: 455.66 E-value: 2.63e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 3 RPIQASLDLQALRHNLEVVRR-AAPRSRVWSVVKANAYGHGLDRVWSALGA--TDGFAMLNLEEAILLRERGWKGPILML 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNhIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 80 EGFFhADELPLFDKYRLTTSVHSNWQLKALAEAKLNAP--LDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQIT-L 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEgI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 157 MAHFADADRP--DGIDAAMVRIEQAAEG-----IDAP-RSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRDIATSG 228
Cdd:TIGR00492 160 FSHFATADEPktGTTQKQIERFNSFLEGlkqqnIEPPfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 229 LQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDL 308
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 495163301 309 TPCPQAGIGSPVELWGNEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPR 364
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-217 |
8.49e-75 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 230.19 E-value: 8.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 9 LDLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL--GATDGFAMLNLEEAILLRERGWKGPILMLEGFfHA 85
Cdd:pfam01168 1 IDLDALRHNLRRLRrRAGPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 86 DELPLFDKYRLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFADA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163301 164 DRPD--GIDAAMVRIEQAAEGIDA------PRSLANSAAALWHPqAHFDWVRPGIVLYGASP 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 ... |
232-352 |
8.90e-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: 185.73 E-value: 8.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 232 VMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPdGTPVLVDGVRTGIVGTVSMDMLAVDLTPC 311
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495163301 312 PQAGIGSPVELWG-NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVP 121
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| dadX |
PRK03646 |
catabolic alanine racemase; |
2-355 |
0e+00 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 2 SRPIQASLDLQALRHNLEVVRRAAPRSRVWSVVKANAYGHGLDRVWSALGATDGFAMLNLEEAILLRERGWKGPILMLEG 81
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 82 FFHADELPLFDKYRLTTSVHSNWQLKALAEAKLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFA 161
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 162 DADRPDGIDAAMVRIEQAAEGIDAPRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRDIATSGLQPVMTLKSEIIG 241
Cdd:PRK03646 161 RADHPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 242 VQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCPQAGIGSPVE 321
Cdd:PRK03646 241 VQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVE 320
|
330 340 350
....*....|....*....|....*....|....
gi 495163301 322 LWGNEIKIDDVAAACGTIGYELMCALAPRVPVST 355
Cdd:PRK03646 321 LWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-353 |
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: 595.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 4 PIQASLDLQALRHNLEVVRRAAPRSRVWSVVKANAYGHGLDRVWSALGATDGFAMLNLEEAILLRERGWKGPILMLEGFF 83
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 84 HADELPLFDKYRLTTSVHSNWQLKALAEAKLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFADA 163
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 164 DRPD--GIDAAMVRIEQAAEGIDAPRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRdIATSGLQPVMTLKSEIIG 241
Cdd:cd06827 161 DEPDspGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 242 VQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCPQAGIGSPVE 321
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|..
gi 495163301 322 LWGNEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPR 351
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-352 |
7.27e-167 |
|
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: 469.97 E-value: 7.27e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 2 SRPIQASLDLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL---GAtDGFAMLNLEEAILLRERGWKGPIL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRaLAGPGAKLMAVVKADAYGHGAVEVARALleaGA-DGFAVATLEEALELREAGIDAPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 78 MLEGFFhADELPLFDKYRLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQIT 155
Cdd:COG0787 80 VLGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 156 LMAHFADADRPD--GIDAAMVRIEQAAEGIDA------PRSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQwrDIATS 227
Cdd:COG0787 159 IMSHFACADEPDhpFTAEQLERFEEAVAALPAagldppLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE--VAADL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 228 GLQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVD 307
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 495163301 308 LTPCPQAGIGSPVELWG-NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:COG0787 317 VTDIPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVP 362
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
3-353 |
4.78e-162 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 457.33 E-value: 4.78e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 3 RPIQASLDLQALRHNLEVVRR-AAPRSRVWSVVKANAYGHGLDRVWSAL---GAtDGFAMLNLEEAILLRERGWKGPILM 78
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLleaGA-DGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 79 LEGFFHADELPLFDKYRLTTSVHSNWQLKALAEAKLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMA 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 159 HFADADRPDG--IDAAMVRIEQAAEGIDAP----RSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQwRDIATSGLQPV 232
Cdd:PRK00053 161 HFATADEPDNsyTEQQLNRFEAALAGLPGKgkplRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 233 MTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCP 312
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 495163301 313 QAGIGSPVELWGNEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:PRK00053 320 QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPR 360
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-353 |
2.63e-161 |
|
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: 455.66 E-value: 2.63e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 3 RPIQASLDLQALRHNLEVVRR-AAPRSRVWSVVKANAYGHGLDRVWSALGA--TDGFAMLNLEEAILLRERGWKGPILML 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNhIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 80 EGFFhADELPLFDKYRLTTSVHSNWQLKALAEAKLNAP--LDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQIT-L 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEgI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 157 MAHFADADRP--DGIDAAMVRIEQAAEG-----IDAP-RSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRDIATSG 228
Cdd:TIGR00492 160 FSHFATADEPktGTTQKQIERFNSFLEGlkqqnIEPPfRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 229 LQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDL 308
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 495163301 309 TPCPQAGIGSPVELWGNEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPR 364
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-352 |
2.77e-127 |
|
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: 369.52 E-value: 2.77e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 7 ASLDLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL---GAtDGFAMLNLEEAILLRERGWKGPILMLeGF 82
Cdd:cd00430 4 AEIDLDALRHNLRVIRrLLGPGTKIMAVVKADAYGHGAVEVAKALeeaGA-DYFAVATLEEALELREAGITAPILVL-GG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 83 FHADELPLFDKYRLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHF 160
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 161 ADADRPDGIDAAM-------VRIEQAAEGIDAP-RSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQWRDIAtsGLQPV 232
Cdd:cd00430 162 ATADEPDKAYTRRqlerfleALAELEEAGIPPPlKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL--GLKPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 233 MTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPCP 312
Cdd:cd00430 240 MSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 495163301 313 QAGIGSPVELWG----NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:cd00430 320 DVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRVP 363
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
1-353 |
5.38e-122 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 357.40 E-value: 5.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 1 MSRPIQASLDLQALRHNLEVVRR-AAPRSRVWSVVKANAYGHGLDRVWSALGAT--DGFAMLNLEEAILLRERGWKGPIL 77
Cdd:PRK13340 37 QPRNAWLEISPGAFRHNIKTLRSlLANKSKVCAVMKADAYGHGIELLMPSIIKAnvPCIGIASNEEARRVRELGFTGQLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 78 MLEGffhAD--ELPLFDKYRLTTSVHSNWQLKALAE--AKLNAPLDVYLKINS-GMNRLGFVPERVHTIWQQLKA--IAN 150
Cdd:PRK13340 117 RVRS---ASpaEIEQALRYDLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEALRIatLPS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 151 VGQITLMAHFADADRpDGIDAAMVRIEQAAEGIDAPRSL---------ANSAAALWHPQAHFDWVRPGIVLYGAspsgqw 221
Cdd:PRK13340 194 LGIVGIMTHFPNEDE-DEVRWKLAQFKEQTAWLIGEAGLkrekitlhvANSYATLNVPEAHLDMVRPGGILYGD------ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 222 RDIATSGLQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSM 301
Cdd:PRK13340 267 RHPANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSM 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163301 302 DMLAVDLTPCPQAGIGSPVELWG----NEIKIDDVAAACGTIGYELMCALAPRVPV 353
Cdd:PRK13340 347 NTLMVDVTDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYTAWGRTNPR 402
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
9-356 |
2.05e-77 |
|
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: 242.26 E-value: 2.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 9 LDLQALRHNLEVVRRAAPR-SRVWSVVKANAYGHGLDRVWSALG--ATDGFAMLNLEEAILLRERGWKGPILMLeGFFHA 85
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPStCKLMAVVKANAYGHGDVEVARVLEqiGIDFFAVATIDEGIRLREAGIKGEILIL-GYTPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 86 DELPLFDKYRLTTSVHSNWQLKALAEAKLNapLDVYLKINSGMNRLGFVPERVHTIwqqlKAIANVGQIT---LMAHFAD 162
Cdd:cd06825 85 VRAKELKKYSLTQTLISEAYAEELSKYAVN--IKVHLKVDTGMHRLGESPEDIDSI----LAIYRLKNLKvsgIFSHLCV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 163 ADR--PDGIDAAMVRIEQ--------AAEGIDAPRS-LANSAAALWHPQAHFDWVRPGIVLYGaSPSGQWRDIATS-GLQ 230
Cdd:cd06825 159 SDSldEDDIAFTKHQIACfdqvladlKARGIEVGKIhIQSSYGILNYPDLKYDYVRPGILLYG-VLSDPNDPTKLGlDLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 231 PVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDG-TPVLVDGVRTGIVGTVSMDMLAVDLT 309
Cdd:cd06825 238 PVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQkAYVLINGKRAPIIGNICMDQLMVDVT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 495163301 310 PCPQAGIGSPVELWG----NEIKIDDVAAACGTIGYELMCALAPRVPVSTR 356
Cdd:cd06825 318 DIPEVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-217 |
8.49e-75 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 230.19 E-value: 8.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 9 LDLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL--GATDGFAMLNLEEAILLRERGWKGPILMLEGFfHA 85
Cdd:pfam01168 1 IDLDALRHNLRRLRrRAGPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 86 DELPLFDKYRLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERVHTIWQQLKAIANVGQITLMAHFADA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163301 164 DRPD--GIDAAMVRIEQAAEGIDA------PRSLANSAAALWHPqAHFDWVRPGIVLYGASP 217
Cdd:pfam01168 160 DEPDdpYTNAQLARFREAAAALEAaglrppVVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
10-351 |
1.06e-65 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 222.14 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 10 DLQALRHNLEVVR-RAAPRSRVWSVVKANAYG------------HGLDRVWSAlgatdgFAmlnlEEAILLRERGWKGPI 76
Cdd:PRK11930 465 NLNAIVHNLNYYRsKLKPETKIMCMVKAFAYGsgsyeiakllqeHRVDYLAVA------YA----DEGVSLRKAGITLPI 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 77 LMLEGffhadELPLFDK---YRLTTSVHSNWQLKALAE-AKLNAPLD--VYLKINSGMNRLGFVPERVHTIWQQLKAIAN 150
Cdd:PRK11930 535 MVMNP-----EPTSFDTiidYKLEPEIYSFRLLDAFIKaAQKKGITGypIHIKIDTGMHRLGFEPEDIPELARRLKKQPA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 151 VGQITLMAHFADADRPDGIDAAMVRIEQ--------AAEGIDAP-RSLANSAAALWHPQAHFDWVRPGIVLYGASPSGQw 221
Cdd:PRK11930 610 LKVRSVFSHLAGSDDPDHDDFTRQQIELfdegseelQEALGYKPiRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGA- 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 222 rdiATSGLQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGT-PVLVDGVRTGIVGTVS 300
Cdd:PRK11930 689 ---GQQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNIC 765
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 495163301 301 MDMLAVDLTPCPqAGIGSPVELWGNEIKIDDVAAACGTIGYELMCALAPRV 351
Cdd:PRK11930 766 MDMCMIDVTDID-AKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRV 815
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
232-352 |
1.30e-59 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 187.96 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 232 VMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAVDLTPC 311
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 495163301 312 PQAGIGSPVELWG----NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:pfam00842 81 PEVKVGDEVTLFGkqgdEEITADELAEAAGTINYEILCSLGKRVP 125
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
232-352 |
8.90e-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: 185.73 E-value: 8.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 232 VMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPdGTPVLVDGVRTGIVGTVSMDMLAVDLTPC 311
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495163301 312 PQAGIGSPVELWG-NEIKIDDVAAACGTIGYELMCALAPRVP 352
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVP 121
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
10-343 |
1.86e-41 |
|
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: 148.64 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 10 DLQALRHNLEVVR-RAAPRSRVWSVVKANAYGHGLDRVWSAL--------GATDGfamlnlEEAILLRERGWKGPILMLE 80
Cdd:cd06826 7 STGAFENNIKLLKkLLGGNTKLCAVMKADAYGHGIALVMPSIiaqnipcvGITSN------EEARVVREAGFTGKILRVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 81 GFFHAdELPLFDKYRLTTSVHSNWQLKALAE--AKLNAPLDVYLKINS-GMNRLG--FVPERVHTIWQQLKAIANVGQIT 155
Cdd:cd06826 81 TATPS-EIEDALAYNIEELIGSLDQAEQIDSlaKRHGKTLPVHLALNSgGMSRNGleLSTAQGKEDAVAIATLPNLKIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 156 LMAHFADADRPDgIDAAMVRIEQAAEGIDAPRSL---------ANSAAALWHPQAHFDWVRPGIVLYGASPsgqwrdiAT 226
Cdd:cd06826 160 IMTHFPVEDEDD-VRAKLARFNEDTAWLISNAKLkrekitlhaANSFATLNVPEAHLDMVRPGGILYGDTP-------PS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 227 SGLQPVMTLKSEIIGVQTLKPGDTVGYGSRYRAAGEQRIGIVAGGYADGYPRHAPDGTPVLVDGVRTGIVGTVSMDMLAV 306
Cdd:cd06826 232 PEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 495163301 307 DLTPCPQAGIGSPVELWG----NEIKIDDVAAACGTIGYEL 343
Cdd:cd06826 312 DVTDIPGVKAGDEVVLFGkqggAEITAAEIEEGSGTILAEL 352
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
14-210 |
1.62e-22 |
|
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: 93.92 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 14 LRHNLEVVRRAAP-RSRVWSVVKANAYGHGLDrvwSALGATDGFAMLNLEEAILLRERGWKG-PILMLEGFFHADELPLF 91
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPEVAR---TLAALGTGFDVASLGEALLLRAAGIPPePILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163301 92 DKY-RLTTSVHSNWQLKALAEA--KLNAPLDVYLKINSG--MNRLGFVPERVHTIWQQLKAIANVGQITLMAHFADAD-R 165
Cdd:cd06808 78 AEQgVIVVTVDSLEELEKLEEAalKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSADeD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163301 166 PDGIDAAMVRIEQAAEGIDAP------RSLANSAAALWH---PQAHFDWVRPGI 210
Cdd:cd06808 158 YSPFVEALSRFVAALDQLGELgidleqLSIGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
105-150 |
7.09e-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: 38.04 E-value: 7.09e-03
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gi 495163301 105 QLKALAEA--KLNAPLDVYLKINSGMNRLGFVPERvhTIWQQLKAIAN 150
Cdd:cd06821 114 AAEALSAAagSAGLTLSVLLDVNTGMNRTGIAPGE--DAEELYRAIAT 159
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