|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-375 |
3.03e-169 |
|
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: 477.37 E-value: 3.03e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 8 RTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILG 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 88 HTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLEAE 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRP-----EEAEELLEALKALPGLELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 168 GIFTHFAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGAD---AK 244
Cdd:cd00430 156 GVFTHFAT---ADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSpevKS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 245 RLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMCM 324
Cdd:cd00430 233 PLGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 325 VDLTDLPDVKVGDTVEIFG----SRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:cd00430 313 VDVTDIPDVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-377 |
6.76e-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: 471.13 E-value: 6.76e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLEA 166
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRP-----EEAPALAARLAALPGLEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 167 EGIFTHFAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGV---GADA 243
Cdd:COG0787 157 EGIMSHFAC---ADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLspsPEVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 244 KRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMC 323
Cdd:COG0787 234 ADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQI 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 324 MVDLTDLPDVKVGDTVEIFGS-RQKVDDLAALLDTIPYELTCAVSRRVPRVYLED 377
Cdd:COG0787 314 MVDVTDIPDVKVGDEVVLFGEqGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-375 |
2.22e-140 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 403.79 E-value: 2.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAM-VPQLIEYRITQAVSALAKAREYSAvaAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLE 165
Cdd:PRK00053 82 GGFFPAEdLPLIIAYNLTTAVHSLEQLEALEK--AELGKPLKVHLKIDTGMHRLGVRP-----EEAEAALERLLACPNVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 166 AEGIFTHFAvsdEDDDDSEAYTREQFAVFTRVLDALaeRGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGV----GA 241
Cdd:PRK00053 155 LEGIFSHFA---TADEPDNSYTEQQLNRFEAALAGL--PGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLspsgEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 242 DAKRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMD 321
Cdd:PRK00053 230 LGLDFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1993152032 322 MCMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:PRK00053 310 QLTVDLGPDPQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-375 |
1.04e-123 |
|
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: 361.67 E-value: 1.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFlvrggHFDTGVDSIAAACALPG-LE 165
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGV-----KPDEAALFVQKLRQLKKfLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 166 AEGIFTHFAvsdEDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGADAKR 245
Cdd:TIGR00492 156 LEGIFSHFA---TADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 246 -----LDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICM 320
Cdd:TIGR00492 233 sdgapFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 321 DMCMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:TIGR00492 313 DMIMVDLGPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-239 |
5.22e-81 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 247.52 E-value: 5.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILGHTPPA 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 93 MVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFlvrggHFDTGVDSIAAACALPGLEAEGIFTH 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGF-----RPEEALALLARLAALPGLRLEGLMTH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993152032 173 FAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPeMYLDMVRPGIALYGV 239
Cdd:pfam01168 156 FAC---ADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGL 218
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
251-374 |
1.02e-46 |
|
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: 155.69 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 251 VMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRmSVVTDQGPAPQRGRICMDMCMVDLTDL 330
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1993152032 331 PDVKVGDTVEIFGS-RQKVDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:smart01005 80 PDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-375 |
3.03e-169 |
|
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: 477.37 E-value: 3.03e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 8 RTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILG 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 88 HTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLEAE 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRP-----EEAEELLEALKALPGLELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 168 GIFTHFAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGAD---AK 244
Cdd:cd00430 156 GVFTHFAT---ADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSpevKS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 245 RLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMCM 324
Cdd:cd00430 233 PLGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 325 VDLTDLPDVKVGDTVEIFG----SRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:cd00430 313 VDVTDIPDVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-377 |
6.76e-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: 471.13 E-value: 6.76e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLEA 166
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRP-----EEAPALAARLAALPGLEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 167 EGIFTHFAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGV---GADA 243
Cdd:COG0787 157 EGIMSHFAC---ADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLspsPEVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 244 KRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMC 323
Cdd:COG0787 234 ADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQI 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 324 MVDLTDLPDVKVGDTVEIFGS-RQKVDDLAALLDTIPYELTCAVSRRVPRVYLED 377
Cdd:COG0787 314 MVDVTDIPDVKVGDEVVLFGEqGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-375 |
2.22e-140 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 403.79 E-value: 2.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAM-VPQLIEYRITQAVSALAKAREYSAvaAACGGTLKVHIKVDTGMSRLGFLVrgghfDTGVDSIAAACALPGLE 165
Cdd:PRK00053 82 GGFFPAEdLPLIIAYNLTTAVHSLEQLEALEK--AELGKPLKVHLKIDTGMHRLGVRP-----EEAEAALERLLACPNVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 166 AEGIFTHFAvsdEDDDDSEAYTREQFAVFTRVLDALaeRGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGV----GA 241
Cdd:PRK00053 155 LEGIFSHFA---TADEPDNSYTEQQLNRFEAALAGL--PGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLspsgEP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 242 DAKRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMD 321
Cdd:PRK00053 230 LGLDFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1993152032 322 MCMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:PRK00053 310 QLTVDLGPDPQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
8-374 |
4.33e-124 |
|
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: 362.83 E-value: 4.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 8 RTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILG 87
Cdd:cd06825 1 RAWLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 88 HTPPAMVPQLIEYRITQAVSALAKAREYSavaaACGGTLKVHIKVDTGMSRLGFlvrggHFDTgVDSIAAACALPGLEAE 167
Cdd:cd06825 81 YTPPVRAKELKKYSLTQTLISEAYAEELS----KYAVNIKVHLKVDTGMHRLGE-----SPED-IDSILAIYRLKNLKVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 168 GIFTHFAVSDEDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGAD----- 242
Cdd:cd06825 151 GIFSHLCVSDSLDEDDIAFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDpndpt 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 243 AKRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGP-APQRGRICMD 321
Cdd:cd06825 231 KLGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQKAYVLINGKrAPIIGNICMD 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1993152032 322 MCMVDLTDLPDVKVGDTVEIFG----SRQKVDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:cd06825 311 QLMVDVTDIPEVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-375 |
1.04e-123 |
|
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: 361.67 E-value: 1.04e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFlvrggHFDTGVDSIAAACALPG-LE 165
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGV-----KPDEAALFVQKLRQLKKfLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 166 AEGIFTHFAvsdEDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGADAKR 245
Cdd:TIGR00492 156 LEGIFSHFA---TADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 246 -----LDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICM 320
Cdd:TIGR00492 233 sdgapFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 321 DMCMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:TIGR00492 313 DMIMVDLGPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
11-374 |
1.16e-96 |
|
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: 292.09 E-value: 1.16e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 11 AEIDLDALAHNYQQARRRIgPHVKYLGVVKADAYGHGAIQIARKLEQlgADYLAVSSLDEAKELRHGGIQAPILIL-GHT 89
Cdd:cd06827 4 ATIDLAALRHNLRLVRELA-PNSKILAVVKANAYGHGLVRVAKALAD--ADGFAVACIEEALALREAGITKPILLLeGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 90 PPAMVPQLIEYRITQAV------SALAKAREYSavaaacggTLKVHIKVDTGMSRLGFlvRGGHFDtgvDSIAAACALPG 163
Cdd:cd06827 81 SADELPLAAEYNLWTVVhseeqlEWLEQAALSK--------PLNVWLKLDSGMHRLGF--SPEEYA---AAYQRLKASPN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 164 LEAEGIFTHFAvsdEDDDDSEAYTREQFAVFTRVLDALAergrtfaIRHC-ANSGALARYPEMYLDMVRPGIALYGV--- 239
Cdd:cd06827 148 VASIVLMTHFA---CADEPDSPGTAKQLAIFEQATAGLP-------GPRSlANSAAILAWPEAHGDWVRPGIMLYGAspf 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 240 -GADAKRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRI 318
Cdd:cd06827 218 aDKSGADLGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRV 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993152032 319 CMDMCMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:cd06827 298 SMDMLTVDLTDLPEAKVGDPVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
12-377 |
2.26e-94 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 299.95 E-value: 2.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 12 EIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILGHTPP 91
Cdd:PRK11930 463 EINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEPT 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 92 AmVPQLIEYRITQAVSALAKAREYSAVAAACGGT-LKVHIKVDTGMSRLGFLVRgghfdtGVDSIAAAC-ALPGLEAEGI 169
Cdd:PRK11930 543 S-FDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITgYPIHIKIDTGMHRLGFEPE------DIPELARRLkKQPALKVRSV 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 170 FTHFAvsDEDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGADAKRLD-L 248
Cdd:PRK11930 616 FSHLA--GSDDPDHDDFTRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQaL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 249 RPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGP-APQRGRICMDMCMVDL 327
Cdd:PRK11930 694 RNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVGYVLVNGQkAPIVGNICMDMCMIDV 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1993152032 328 TDLpDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYLED 377
Cdd:PRK11930 774 TDI-DAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
7-374 |
5.06e-82 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 256.47 E-value: 5.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 7 RRTWAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILIL 86
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTPPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDT-GMSRLGFLVrggHFDTGVDSIAAACALPGLE 165
Cdd:PRK13340 119 RSASPAEIEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLDM---STARGKWEALRIATLPSLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 166 AEGIFTHFAVSDEDdddseaYTREQFAVFTRVLDAL-AERG--RTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGAD 242
Cdd:PRK13340 196 IVGIMTHFPNEDED------EVRWKLAQFKEQTAWLiGEAGlkREKITLHVANSYATLNVPEAHLDMVRPGGILYGDRHP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 243 AkRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDM 322
Cdd:PRK13340 270 A-NTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNT 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1993152032 323 CMVDLTDLPDVKVGDTVEIFGSRQ----KVDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:PRK13340 349 LMVDVTDIPNVKPGDEVVLFGKQGnaeiTVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-239 |
5.22e-81 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 247.52 E-value: 5.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILGHTPPA 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 93 MVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFlvrggHFDTGVDSIAAACALPGLEAEGIFTH 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGF-----RPEEALALLARLAALPGLRLEGLMTH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993152032 173 FAVsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGALARYPeMYLDMVRPGIALYGV 239
Cdd:pfam01168 156 FAC---ADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGL 218
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
11-375 |
2.16e-68 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 219.60 E-value: 2.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 11 AEIDLDALAHNYQQARRrIGPHVKYLGVVKADAYGHGAIQIARKLEqlGADYLAVSSLDEAKELRHGGIQAPILIL-GHT 89
Cdd:PRK03646 6 ASLDLQALKQNLSIVRE-AAPGARVWSVVKANAYGHGIERIWSALG--ATDGFAVLNLEEAITLRERGWKGPILMLeGFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 90 PPAMVPQLIEYRITQAVSAL--AKAREYSAVAAAcggtLKVHIKVDTGMSRLGFlvrggHFDTGVDSIAAACALPGLEAE 167
Cdd:PRK03646 83 HAQDLELYDQHRLTTCVHSNwqLKALQNARLKAP----LDIYLKVNSGMNRLGF-----QPERVQTVWQQLRAMGNVGEM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 168 GIFTHFAVSDEDDDdseayTREQFAVFTRVLDALAERgrtfaiRHCANSGALARYPEMYLDMVRPGIALYG-----VGAD 242
Cdd:PRK03646 154 TLMSHFARADHPDG-----ISEAMARIEQAAEGLECE------RSLSNSAATLWHPQAHFDWVRPGIILYGaspsgQWRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 243 AKRLDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDM 322
Cdd:PRK03646 223 IANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDM 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1993152032 323 CMVDLTDLPDVKVGDTVEIFGSRQKVDDLAALLDTIPYELTCAVSRRVPRVYL 375
Cdd:PRK03646 303 LAVDLTPCPQAGIGTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
10-374 |
4.97e-61 |
|
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: 201.03 E-value: 4.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 10 WAEIDLDALAHNYQQARRRIGPHVKYLGVVKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILGHT 89
Cdd:cd06826 3 WLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 90 PPAMVPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDT-GMSRLGFLVRGghfDTGVDSIAAACALPGLEAEG 168
Cdd:cd06826 83 TPSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLELST---AQGKEDAVAIATLPNLKIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 169 IFTHFAVSDEddddseAYTREQFAVFTRVLDALAERG---RTFAIRHCANSGALARYPEMYLDMVRPGIALYGVGADAkr 245
Cdd:cd06826 160 IMTHFPVEDE------DDVRAKLARFNEDTAWLISNAklkREKITLHAANSFATLNVPEAHLDMVRPGGILYGDTPPS-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 246 LDLRPVMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMCMV 325
Cdd:cd06826 232 PEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1993152032 326 DLTDLPDVKVGDTVEIFGSRQK----VDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:cd06826 312 DVTDIPGVKAGDEVVLFGKQGGaeitAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
251-374 |
3.67e-53 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 172.55 E-value: 3.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 251 VMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRMSVVTDQGPAPQRGRICMDMCMVDLTDL 330
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1993152032 331 PDVKVGDTVEIFGSRQK----VDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDeeitADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
251-374 |
1.02e-46 |
|
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: 155.69 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 251 VMRLKSSISTIKTFDPDTDISYGRTFRTTARTRIGVLPIGYADGFFRGLSNRmSVVTDQGPAPQRGRICMDMCMVDLTDL 330
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1993152032 331 PDVKVGDTVEIFGS-RQKVDDLAALLDTIPYELTCAVSRRVPRVY 374
Cdd:smart01005 80 PDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
18-234 |
3.38e-29 |
|
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: 112.41 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 18 LAHNYQQARRRIGPHVKYLGVVKADAyghgAIQIARKLEQLGaDYLAVSSLDEAKELRHGGI-QAPILILGHTP-PAMVP 95
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTLAALG-TGFDVASLGEALLLRAAGIpPEPILFLGPCKqVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 96 QLIEYRITQ-AVSALAKAREYSAVAAACGGTLKVHIKVDTG--MSRLGflVRGGHFDtgvDSIAAACALPGLEAEGIFTH 172
Cdd:cd06808 76 DAAEQGVIVvTVDSLEELEKLEEAALKAGPPARVLLRIDTGdeNGKFG--VRPEELK---ALLERAKELPHLRLVGLHTH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993152032 173 FAvsdeDDDDSEAYTREQFAVFTRVLDALAERGRTFAIRHCANSGA---LARYPEMYLDMVRPGI 234
Cdd:cd06808 151 FG----SADEDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAilyLQELPLGTFIIVEPGR 211
|
|
| YhfX |
COG3457 |
Predicted amino acid racemase [Amino acid transport and metabolism]; |
12-340 |
3.88e-16 |
|
Predicted amino acid racemase [Amino acid transport and metabolism];
Pssm-ID: 442680 [Multi-domain] Cd Length: 356 Bit Score: 78.70 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 12 EIDLDALAHNYQQARRRIGPH-VKYLGVVKAdayGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILgHTP 90
Cdd:COG3457 7 VIDLDKIRENARRLVELAAKHgIELYGVTKQ---FGGNPEIAKALLDGGIKGIVDSRIKNLKKLKRAGIPHPGHLL-RIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 91 PAMVPQLIEYR---ITqaVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLvrgghFDTGVDSIAAACALPGLEAE 167
Cdd:COG3457 83 MLSEVEEVVRYadiSL--NSELETARALSEAAKKQGKVHKVILMVDLGDLREGGF-----PEELVDTVEEILKLPGIELA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 168 GIFTHFAvsdeddddseAY-----TREQFAVFTRVLDALAER-GRTFAIRHCANSGALARYPEMYLD----MVRPGIALY 237
Cdd:COG3457 156 GLGTNLP----------CFggvlpTEENLGTLLELAELLEAKfGIKLPIVSGGNSTSLPLLAEGTLPkginHLRPGEALL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 238 -GVG-ADAKRLDL--RPVMRLKSSISTI--KTFDPDTDISYGRTFRTTARTRIGV-----LPIGYADGFFRGLSNRMSVV 306
Cdd:COG3457 226 lGTDpLNARPIPGleQDAFVLVAEIIELkeKPSVPIGEIGRDAFGNAPEFGDRGIrkraiLAIGRQDVDPEGLTPIDYGI 305
|
330 340 350
....*....|....*....|....*....|....*
gi 1993152032 307 TDQGpapqrgrICMDMCMVDLTDLP-DVKVGDTVE 340
Cdd:COG3457 306 EILG-------ASSDHLILDVTDSKeDYKVGDTVV 333
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
12-174 |
1.51e-10 |
|
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: 61.79 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 12 EIDLDALAHNYQQARRRIGPH-VKYLGVVKADAyghGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILghTP 90
Cdd:cd06815 5 EINLSKIRHNAKVLVELCKSRgIEVTGVTKVVC---GDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLL--RI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 91 PAM--VPQLIEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLvrgghFDTGVDSIAAACALPGLEAEG 168
Cdd:cd06815 80 PMLseVEDVVKYADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVL-----PEDLLDFVEEILKLPGIELVG 154
|
....*.
gi 1993152032 169 IFTHFA 174
Cdd:cd06815 155 IGTNLG 160
|
|
| PLPDE_III_yhfX_like |
cd06811 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ... |
13-348 |
2.22e-09 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the uncharacterized protein yhfX from Escherichia coli K-12 and similar bacterial proteins. These proteins are homologous 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: 143486 Cd Length: 382 Bit Score: 58.44 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHN----YQQARRRigpHVKYLGVVKAdaYGHGAIqIARKLEQLGADYLAVSSLDEAKELRHGGIqaPILILGH 88
Cdd:cd06811 33 IDLDQIEENarllAETAEKY---GIELYFMTKQ--FGRNPF-LARALLEAGIPGAVAVDFKEARALHEAGL--PLGHVGH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 89 ---TPPAMVPQLIEYR---ITqaVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVRGGHFDTGVDSIAAAC-AL 161
Cdd:cd06811 105 lvqIPRHQVPAVLAMRpevIT--VYSLEKAREISDAAVELGRVQDVLLRVYGDEDTLYPGQEGGFPLEELPAVLAAIkAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 162 PGLEAEGIfTHF-AVSDEDDDDSEAYTrEQFAVFTRVLDALAERGRtfAIRH--------CANSGALARYPEMYldmVRP 232
Cdd:cd06811 183 PGIRIAGL-TSFpCFLYDEEQGDIAPT-PNLFTLLKAKELLEKRGI--EILQlnapsatsCATLPLLAEYGVTH---GEP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 233 GIALYGVGADAKRLDL--RPVMRLKSSIStiKTFDPDtdiSYgrtfrttartrigvlpiGYADGFFR--GLSNRMsVVTD 308
Cdd:cd06811 256 GHALTGTTPLHAVGDQpeKPAMVYVSEVS--HTFGGH---SY-----------------CYGGGFYRrsHLKNAL-VGTD 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1993152032 309 QGPAPQRGRICMDMCMVDLT---DLPDVKVGDTV------EIFGSRQKV 348
Cdd:cd06811 313 PDDASAHRAELLDPENIDYYgtlDGPEFAVGDTVimafrtQIFVTRSDV 361
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
13-205 |
2.37e-09 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 58.22 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARRRIG-------PHVKylgvvkadayGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQaPILI 85
Cdd:COG3616 13 LDLDALERNIARMAARAAahgvrlrPHGK----------THKSPELARRQLAAGAWGITVATLAEAEVLAAAGVD-DILL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 86 ----LGhtPPAM--VPQLIEY--RITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGflVRGGhfDTGVDSIAA 157
Cdd:COG3616 82 ayplVG--PAKLarLAALARAgaRLTVLVDSVEQAEALAAAAAAAGRPLRVLVELDVGGGRTG--VRPP--EAALALARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1993152032 158 ACALPGLEAEGIFTHFAV--SDEDDDDSEAYTREQFAVFTRVLDALAERG 205
Cdd:COG3616 156 IAASPGLRLAGLMTYEGHiyGADDAEERRAAAREELARLAAAAEALRAAG 205
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
13-169 |
1.37e-08 |
|
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: 56.07 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYqqarRRIGPHVKYLGV-VKADAYGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQApILI----LG 87
Cdd:cd06819 12 LDLDALERNI----KRMAAFAKAHGVrLRPHAKTHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIRD-ILItnevVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 88 HTPPAMVPQLIEY-RITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGflVRGGhfDTGVDSIAAACALPGLEA 166
Cdd:cd06819 87 PAKIARLAALARRaPLIVCVDHPDNVRALAAAAVEAGVRLDVLVEIDVGQGRCG--VPPG--EAALALARTIAALPGLRF 162
|
...
gi 1993152032 167 EGI 169
Cdd:cd06819 163 AGL 165
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
13-238 |
2.79e-08 |
|
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: 55.01 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARR-------RIGPHVKylgvvkadayGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIqAPILI 85
Cdd:cd06820 8 IDLDRLERNIARMQAyadahglSLRPHIK----------THKSPEIARLQLAAGAIGITVATVGEAEVMADAGL-SDIFI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 86 lghTPPAMVPQLIE--------YRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRlgflvrgghfdTGVDSIAA 157
Cdd:cd06820 77 ---AYPIVGRQKLErlralaerVTLSVGVDSAEVARGLAEVAEGAGRPLEVLVEVDSGMNR-----------CGVQTPED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 158 ACAL-------PGLEAEGIFTHFAVSDEDDDDSEAYTREQfavftRVLDALAERGRTFAIRHCANSGALAryPEMY---- 226
Cdd:cd06820 143 AVALaraiasaPGLRFRGIFTYPGHSYAPGALEEAAADEA-----EALLAAAGILEEAGLEPPVVSGGST--PTLWrshe 215
|
250
....*....|....*
gi 1993152032 227 ---LDMVRPGIALYG 238
Cdd:cd06820 216 vpgITEIRPGTYIFN 230
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
13-169 |
3.92e-07 |
|
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: 51.53 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARRRIG------PHVKylgvvkadayGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGiqAPILIL 86
Cdd:cd06821 14 VYPDRIEENIRRMIRMAGdpqrlrPHVK----------THKMAEIVRLQLEAGITKFKCATIAEAEMLAEAG--APDVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 87 GHTP--PAMVpQLIEY-------RITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFLVRgghfDTGVDSIAA 157
Cdd:cd06821 82 AYPLvgPNIE-RFLELakkypgtRFSALVDDLEAAEALSAAAGSAGLTLSVLLDVNTGMNRTGIAPG----EDAEELYRA 156
|
170
....*....|..
gi 1993152032 158 ACALPGLEAEGI 169
Cdd:cd06821 157 IATLPGLVLAGL 168
|
|
| PLPDE_III_DSD_D-TA_like_3 |
cd06814 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
13-168 |
4.53e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 3; This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143489 [Multi-domain] Cd Length: 379 Bit Score: 41.94 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 13 IDLDALAHNYQQARRRIGPHVKYLGVVKADAyghgAIQIARKL-EQLGADYLAVSSLDEAKELRHGGIQAPILiLG---- 87
Cdd:cd06814 14 LDKDRLDHNIDLLREHLAGSLAYRIVAKSLP----SPPLLRHImKRAGTRRLMVFHQPFLNAVAKAFPDADIL-LGkpmp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 88 ----------HTPPAMVPqliEYRITQAVSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGFlVRGGHFDTGVDSIAa 157
Cdd:cd06814 89 vaaaarfyrqLTGSAFRP---ARQLQWLIDTPERLAQYRALARSLGLTLRINLELDVGLHRGGF-ADPQTLPKALTAID- 163
|
170
....*....|.
gi 1993152032 158 acALPGLEAEG 168
Cdd:cd06814 164 --APPRLRFSG 172
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
28-238 |
4.56e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 42.07 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 28 RIGPHVKylgvvkadayGHGAIQIARKLEQLGADYLAVSSLDEAKELRHGGIQAPILILGHTPPAMVPQLIEYRITQA-- 105
Cdd:cd07376 19 RLRPHVK----------THKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYPLVGPAAIARLAGLLRQEAef 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993152032 106 ---VSALAKAREYSAVAAACGGTLKVHIKVDTGMSRLGflVRGGHFDTGVdSIAAACALPGLEAEGIFTHFAVSDEDDDD 182
Cdd:cd07376 89 hvlVDSPEALAALAAFAAAHGVRLRVMLEVDVGGHRSG--VRPEEAAALA-LADAVQASPGLRLAGVMAYEGHIYGAGGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1993152032 183 SEAYTREQFAVfTRVLDALAERGRTFAIRHCANSG---ALARYPEMYLDMVRPGIALYG 238
Cdd:cd07376 166 REGAQARDQAV-AAVRAAAAAAERGLACPTVSGGGtptYQLTAGDRAVTELRAGSYVFM 223
|
|
| |
