|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-368 |
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: 561.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 3 PSRALIDLDALRHNIRLLNSIAHNARCAAVIKADAYGHGAVEIARALKgEAPKLAVACYDEAVSLREAGVTTPLLVLEGF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALA-DADGFAVACIEEALALREAGITKPILLLEGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 83 YSSEELADSTRWcDIEWVVHDMEQLDMLSEVAPlrkagpdSTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVI 162
Cdd:cd06827 80 FSADELPLAAEY-NLWTVVHSEEQLEWLEQAAL-------SKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 163 GLMTHFACADELDSLLQQRQWRAFQagmQAAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMADKTGADFGLK 242
Cdd:cd06827 152 VLMTHFACADEPDSPGTAKQLAIFE---QATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 243 PVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLTVDISH 322
Cdd:cd06827 229 PVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 123534099 323 IPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:cd06827 309 LPEAKVGDPVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-369 |
2.75e-175 |
|
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: 491.93 E-value: 2.75e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIAH-NARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLV 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGpGAKLMAVVKADAYGHGAVEVARALLEAgADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 79 LEGFySSEELADSTRWcDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPG 158
Cdd:COG0787 81 LGGV-PPEDLELAIEY-DLEPVVHSLEQLEALAAAA--RRLG---KPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 159 LSVIGLMTHFACADELDSLLQQRQWRAFQAGMQAAGANGWSY---SSANSAALLQYPETHLDWVRPGIAMYGASPMADkT 235
Cdd:COG0787 154 LEVEGIMSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-V 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 236 GADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDM 315
Cdd:COG0787 233 AADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQ 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 123534099 316 LTVDISHIPEARIGSEVELWG-GTVSADEVAGYASTISYTLFTGMTSRVPRVYIN 369
Cdd:COG0787 313 IMVDVTDIPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-368 |
1.12e-165 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 467.35 E-value: 1.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIA-HNARCAAVIKADAYGHGAVEIARALK-GEAPKLAVACYDEAVSLREAGVTTPLLV 78
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHApPKSKLMAVVKANAYGHGAVEVAKTLLeAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 79 LEGFYSSEELADSTRWcDIEWVVHDMEQLDMLSEVAPLRKAgpdstrmQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPG 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAY-NLTTAVHSLEQLEALEKAELGKPL-------KVHLKIDTGMHRLGVRPEEAEAALERLLACPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 159 LSVIGLMTHFACADELDSLLQQRQWRAFQAGMQ-AAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMADKTGA 237
Cdd:PRK00053 153 VRLEGIFSHFATADEPDNSYTEQQLNRFEAALAgLPGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 238 DFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLT 317
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLT 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 123534099 318 VDISHIPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:PRK00053 313 VDLGPDPQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-368 |
4.39e-130 |
|
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: 377.46 E-value: 4.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 2 RPSRALIDLDALRHNIRLL-NSIAHNARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLVL 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIrNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAgADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 80 EGFySSEELADSTRWcDIEWVVHDMEQLDMLSEVAPlrkagPDSTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGL 159
Cdd:TIGR00492 81 GGF-FAEDLKILAAW-DLTTTVHSVEQLQALEEALL-----KEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 160 SVI-GLMTHFACADELDS---LLQQRQWRAFQAGMQAAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMAD-K 234
Cdd:TIGR00492 154 LELeGIFSHFATADEPKTgttQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADmS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 235 TGADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMD 314
Cdd:TIGR00492 234 DGAPFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMD 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 123534099 315 MLTVDISHIPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:TIGR00492 314 MIMVDLGPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-230 |
2.85e-81 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 247.52 E-value: 2.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNSIA-HNARCAAVIKADAYGHGAVEIARAL-KGEAPKLAVACYDEAVSLREAGVTTPLLVLEGFySS 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALlEGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 EELADSTRWcDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVIGLM 165
Cdd:pfam01168 80 EELALAAEY-DLTPTVDSLEQLEALAAAA--RRLG---KPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123534099 166 THFACADELDSLLQQRQWRAFQAGMQAAGANGWS---YSSANSAALLQYPEtHLDWVRPGIAMYGASP 230
Cdd:pfam01168 154 THFACADEPDDPYTNAQLARFREAAAALEAAGLRppvVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
244-367 |
3.90e-61 |
|
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: 192.67 E-value: 3.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 244 VMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGaPVAVCGKRTKIIGRVSMDMLTVDISHI 323
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 123534099 324 PEARIGSEVELWG-GTVSADEVAGYASTISYTLFTGMTSRVPRVY 367
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-368 |
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: 561.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 3 PSRALIDLDALRHNIRLLNSIAHNARCAAVIKADAYGHGAVEIARALKgEAPKLAVACYDEAVSLREAGVTTPLLVLEGF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALA-DADGFAVACIEEALALREAGITKPILLLEGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 83 YSSEELADSTRWcDIEWVVHDMEQLDMLSEVAPlrkagpdSTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVI 162
Cdd:cd06827 80 FSADELPLAAEY-NLWTVVHSEEQLEWLEQAAL-------SKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 163 GLMTHFACADELDSLLQQRQWRAFQagmQAAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMADKTGADFGLK 242
Cdd:cd06827 152 VLMTHFACADEPDSPGTAKQLAIFE---QATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 243 PVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLTVDISH 322
Cdd:cd06827 229 PVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 123534099 323 IPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:cd06827 309 LPEAKVGDPVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-369 |
2.75e-175 |
|
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: 491.93 E-value: 2.75e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIAH-NARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLV 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGpGAKLMAVVKADAYGHGAVEVARALLEAgADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 79 LEGFySSEELADSTRWcDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPG 158
Cdd:COG0787 81 LGGV-PPEDLELAIEY-DLEPVVHSLEQLEALAAAA--RRLG---KPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 159 LSVIGLMTHFACADELDSLLQQRQWRAFQAGMQAAGANGWSY---SSANSAALLQYPETHLDWVRPGIAMYGASPMADkT 235
Cdd:COG0787 154 LEVEGIMSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-V 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 236 GADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDM 315
Cdd:COG0787 233 AADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQ 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 123534099 316 LTVDISHIPEARIGSEVELWG-GTVSADEVAGYASTISYTLFTGMTSRVPRVYIN 369
Cdd:COG0787 313 IMVDVTDIPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-368 |
1.12e-165 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 467.35 E-value: 1.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIA-HNARCAAVIKADAYGHGAVEIARALK-GEAPKLAVACYDEAVSLREAGVTTPLLV 78
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHApPKSKLMAVVKANAYGHGAVEVAKTLLeAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 79 LEGFYSSEELADSTRWcDIEWVVHDMEQLDMLSEVAPLRKAgpdstrmQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPG 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAY-NLTTAVHSLEQLEALEKAELGKPL-------KVHLKIDTGMHRLGVRPEEAEAALERLLACPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 159 LSVIGLMTHFACADELDSLLQQRQWRAFQAGMQ-AAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMADKTGA 237
Cdd:PRK00053 153 VRLEGIFSHFATADEPDNSYTEQQLNRFEAALAgLPGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 238 DFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLT 317
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLT 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 123534099 318 VDISHIPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:PRK00053 313 VDLGPDPQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
3-368 |
7.97e-152 |
|
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: 432.31 E-value: 7.97e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 3 PSRALIDLDALRHNIRLLNSIA-HNARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLVLE 80
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALEEAgADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 81 GFYSsEELADSTRWcDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLS 160
Cdd:cd00430 81 GTPP-EEAEEAIEY-DLTPTVSSLEQAEALSAAA--ARLG---KTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 161 VIGLMTHFACADELDSLLQQRQWRAFQAGMQAAGANGWS---YSSANSAALLQYPETHLDWVRPGIAMYGASPmADKTGA 237
Cdd:cd00430 154 LEGVFTHFATADEPDKAYTRRQLERFLEALAELEEAGIPpplKHLANSAAILRFPEAHFDMVRPGIALYGLYP-SPEVKS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 238 DFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLT 317
Cdd:cd00430 233 PLGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTM 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 123534099 318 VDISHIPEARIGSEVELWG----GTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:cd00430 313 VDVTDIPDVKVGDEVVLFGrqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-368 |
5.61e-131 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 379.07 E-value: 5.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIAHNARCAAVIKADAYGHGAVEIARALKGeAPKLAVACYDEAVSLREAGVTTPLLVLE 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGA-TDGFAVLNLEEAITLRERGWKGPILMLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 81 GFYSSEELA--DSTR-WCdiewVVHDMEQLDMLsEVAPLRKAgpdstrMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFP 157
Cdd:PRK03646 80 GFFHAQDLElyDQHRlTT----CVHSNWQLKAL-QNARLKAP------LDIYLKVNSGMNRLGFQPERVQTVWQQLRAMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 158 GLSVIGLMTHFACADELDSLLQQ-RQWRAFQAGMQAAgangwsYSSANSAALLQYPETHLDWVRPGIAMYGASPMA-DKT 235
Cdd:PRK03646 149 NVGEMTLMSHFARADHPDGISEAmARIEQAAEGLECE------RSLSNSAATLWHPQAHFDWVRPGIILYGASPSGqWRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 236 GADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDM 315
Cdd:PRK03646 223 IANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDM 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 123534099 316 LTVDISHIPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:PRK03646 303 LAVDLTPCPQAGIGTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-368 |
4.39e-130 |
|
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: 377.46 E-value: 4.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 2 RPSRALIDLDALRHNIRLL-NSIAHNARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLVL 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIrNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAgADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 80 EGFySSEELADSTRWcDIEWVVHDMEQLDMLSEVAPlrkagPDSTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGL 159
Cdd:TIGR00492 81 GGF-FAEDLKILAAW-DLTTTVHSVEQLQALEEALL-----KEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 160 SVI-GLMTHFACADELDS---LLQQRQWRAFQAGMQAAGANGWSYSSANSAALLQYPETHLDWVRPGIAMYGASPMAD-K 234
Cdd:TIGR00492 154 LELeGIFSHFATADEPKTgttQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADmS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 235 TGADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMD 314
Cdd:TIGR00492 234 DGAPFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMD 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 123534099 315 MLTVDISHIPEARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:TIGR00492 314 MIMVDLGPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
2-369 |
2.54e-97 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 295.38 E-value: 2.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 2 RPSRALIDLDALRHNIRLLNS-IAHNARCAAVIKADAYGHGaveIARA----LKGEAPKLAVACYDEAVSLREAGVTTPL 76
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSlLANKSKVCAVMKADAYGHG---IELLmpsiIKANVPCIGIASNEEARRVRELGFTGQL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 77 LVLEGFySSEELADSTRWcDIEWVVHDMEQLDMLSEVAplrkAGPDST-RMQtwIKLNT-GMNRLGLPLNKLAHVAEKLQ 154
Cdd:PRK13340 116 LRVRSA-SPAEIEQALRY-DLEELIGDDEQAKLLAAIA----KKNGKPiDIH--LALNSgGMSRNGLDMSTARGKWEALR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 155 --QFPGLSVIGLMTHFACADE------LDSLLQQRQWRAFQAGMQAagaNGWSYSSANSAALLQYPETHLDWVRPGIAMY 226
Cdd:PRK13340 188 iaTLPSLGIVGIMTHFPNEDEdevrwkLAQFKEQTAWLIGEAGLKR---EKITLHVANSYATLNVPEAHLDMVRPGGILY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 227 GaspmaDKTGADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTK 306
Cdd:PRK13340 265 G-----DRHPANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAP 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123534099 307 IIGRVSMDMLTVDISHIPEARIGSEVELWG----GTVSADEVAGYASTISYTLFTGMTSRVPRVYIN 369
Cdd:PRK13340 340 VVGRVSMNTLMVDVTDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
8-368 |
1.49e-84 |
|
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: 261.13 E-value: 1.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNSIAH-NARCAAVIKADAYGHGAVEIARALKGEAPK-LAVACYDEAVSLREAGVTTPLLVLeGFYSS 85
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPsTCKLMAVVKANAYGHGDVEVARVLEQIGIDfFAVATIDEGIRLREAGIKGEILIL-GYTPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 EELADSTRWCDIEWVVhDMEQLDMLSEVAplrkagpdsTRMQTWIKLNTGMNRLGLPLNKLAHVaEKLQQFPGLSVIGLM 165
Cdd:cd06825 85 VRAKELKKYSLTQTLI-SEAYAEELSKYA---------VNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNLKVSGIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 166 THFACADELDS---LLQQRQWRAFQAGMQAAGANGWSYSSA---NSAALLQYPETHLDWVRPGIAMYGA-SPMADKTGAD 238
Cdd:cd06825 154 SHLCVSDSLDEddiAFTKHQIACFDQVLADLKARGIEVGKIhiqSSYGILNYPDLKYDYVRPGILLYGVlSDPNDPTKLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 239 FGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNG-APVAVCGKRTKIIGRVSMDMLT 317
Cdd:cd06825 234 LDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQkAYVLINGKRAPIIGNICMDQLM 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 123534099 318 VDISHIPEARIGSEVELWG----GTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:cd06825 314 VDVTDIPEVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-230 |
2.85e-81 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 247.52 E-value: 2.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNSIA-HNARCAAVIKADAYGHGAVEIARAL-KGEAPKLAVACYDEAVSLREAGVTTPLLVLEGFySS 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALlEGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 EELADSTRWcDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVIGLM 165
Cdd:pfam01168 80 EELALAAEY-DLTPTVDSLEQLEALAAAA--RRLG---KPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123534099 166 THFACADELDSLLQQRQWRAFQAGMQAAGANGWS---YSSANSAALLQYPEtHLDWVRPGIAMYGASP 230
Cdd:pfam01168 154 THFACADEPDDPYTNAQLARFREAAAALEAAGLRppvVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-368 |
1.03e-74 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 247.18 E-value: 1.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNS-IAHNARCAAVIKADAYGHGAVEIARALKGE-APKLAVACYDEAVSLREAGVTTPLLVLE-GFYS 84
Cdd:PRK11930 464 INLNAIVHNLNYYRSkLKPETKIMCMVKAFAYGSGSYEIAKLLQEHrVDYLAVAYADEGVSLRKAGITLPIMVMNpEPTS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 85 SEELADstrWcDIEWVVHDMEQLDMLSEVAplRKAGPDSTRMQtwIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVIGL 164
Cdd:PRK11930 544 FDTIID---Y-KLEPEIYSFRLLDAFIKAA--QKKGITGYPIH--IKIDTGMHRLGFEPEDIPELARRLKKQPALKVRSV 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 165 MTHFACAD--ELDSLLQQrQWRAFQAGMQAAGANGwSYS----SANSAALLQYPETHLDWVRPGIAMYGASPmadkTGAD 238
Cdd:PRK11930 616 FSHLAGSDdpDHDDFTRQ-QIELFDEGSEELQEAL-GYKpirhILNSAGIERFPDYQYDMVRLGIGLYGVSA----SGAG 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 239 F-GLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNG-APVAVCGKRTKIIGRVSMDML 316
Cdd:PRK11930 690 QqALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGvGYVLVNGQKAPIVGNICMDMC 769
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 123534099 317 TVDISHIPeARIGSEVELWGGTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:PRK11930 770 MIDVTDID-AKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVYF 820
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
244-367 |
8.36e-63 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 196.82 E-value: 8.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 244 VMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDMLTVDISHI 323
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 123534099 324 PEARIGSEVELWG----GTVSADEVAGYASTISYTLFTGMTSRVPRVY 367
Cdd:pfam00842 81 PEVKVGDEVTLFGkqgdEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
244-367 |
3.90e-61 |
|
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: 192.67 E-value: 3.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 244 VMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGaPVAVCGKRTKIIGRVSMDMLTVDISHI 323
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 123534099 324 PEARIGSEVELWG-GTVSADEVAGYASTISYTLFTGMTSRVPRVY 367
Cdd:smart01005 80 PDVKVGDEVVLFGpQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-368 |
2.47e-60 |
|
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: 198.72 E-value: 2.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNS-IAHNARCAAVIKADAYGHGAVEIARA-LKGEAPKLAVACYDEAVSLREAGVTTPLLVLEGfYSS 85
Cdd:cd06826 6 ISTGAFENNIKLLKKlLGGNTKLCAVMKADAYGHGIALVMPSiIAQNIPCVGITSNEEARVVREAGFTGKILRVRT-ATP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 EELADSTRWcDIEWVVHDMEQLDMLSEVAPLRkagpdSTRMQTWIKLNT-GMNRLGLPLNKLAHVAEKLQ--QFPGLSVI 162
Cdd:cd06826 85 SEIEDALAY-NIEELIGSLDQAEQIDSLAKRH-----GKTLPVHLALNSgGMSRNGLELSTAQGKEDAVAiaTLPNLKIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 163 GLMTHFACADE------LDSLLQQRQWRAFQAGMQAAGANgwsYSSANSAALLQYPETHLDWVRPGIAMYGaspmadKTG 236
Cdd:cd06826 159 GIMTHFPVEDEddvrakLARFNEDTAWLISNAKLKREKIT---LHAANSFATLNVPEAHLDMVRPGGILYG------DTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 237 ADFGLKPVMTFESRLIATRELQAGDSIGYGAAWTADAPTRMGVVAVGYGDGYPRQMQNGAPVAVCGKRTKIIGRVSMDML 316
Cdd:cd06826 230 PSPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 123534099 317 TVDISHIPEARIGSEVELWG----GTVSADEVAGYASTISYTLFTGMTSRVPRVYI 368
Cdd:cd06826 310 MVDVTDIPGVKAGDEVVLFGkqggAEITAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-223 |
2.40e-30 |
|
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: 115.49 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 13 LRHNIRLL-NSIAHNARCAAVIKADAyghgAVEIARALKGEAPKLAVACYDEAVSLREAGVTT-PLLVLEGFYSSEELAD 90
Cdd:cd06808 1 IRHNYRRLrEAAPAGITLFAVVKANA----NPEVARTLAALGTGFDVASLGEALLLRAAGIPPePILFLGPCKQVSELED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 91 STRWCDIEWVVHDMEQLDMLSEVAplRKAGPdstRMQTWIKLNTG--MNRLGLPLNKLAHVAEKLQQFPGLSVIGLMTHF 168
Cdd:cd06808 77 AAEQGVIVVTVDSLEELEKLEEAA--LKAGP---PARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 169 ACADELDSLLQQ--RQWRAFQAGMQAAGANGWSYSSANSAALL---QYPETHLDWVRPGI 223
Cdd:cd06808 152 GSADEDYSPFVEalSRFVAALDQLGELGIDLEQLSIGGSFAILylqELPLGTFIIVEPGR 211
|
|
| YhfX |
COG3457 |
Predicted amino acid racemase [Amino acid transport and metabolism]; |
1-333 |
1.38e-11 |
|
Predicted amino acid racemase [Amino acid transport and metabolism];
Pssm-ID: 442680 [Multi-domain] Cd Length: 356 Bit Score: 65.21 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 1 MRPSRALIDLDALRHNIRLLNSIA--HNARCAAVIKAdayGHGAVEIARAL-KGEAPKLAVACYDEAVSLREAGVTTPll 77
Cdd:COG3457 1 IPPPTLVIDLDKIRENARRLVELAakHGIELYGVTKQ---FGGNPEIAKALlDGGIKGIVDSRIKNLKKLKRAGIPHP-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 78 vleGFY----SSEELADSTRWCDIeWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKL 153
Cdd:COG3457 76 ---GHLlripMLSEVEEVVRYADI-SLNSELETARALSEAA--KKQG---KVHKVILMVDLGDLREGGFPEELVDTVEEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 154 QQFPGLSVIGLMTHFAC-------ADELDSLLQQRQWRAFQAGMQAAGANGwsySSANSAALL---QYPE--THLdwvRP 221
Cdd:COG3457 147 LKLPGIELAGLGTNLPCfggvlptEENLGTLLELAELLEAKFGIKLPIVSG---GNSTSLPLLaegTLPKgiNHL---RP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 222 GIAMY-GASPMADKTGaDFGLKPVMTFESRLIatrELQAGDSIGYGaawtadaptRMGVVAVG----YGD-GYPRQmqng 295
Cdd:COG3457 221 GEALLlGTDPLNARPI-PGLEQDAFVLVAEII---ELKEKPSVPIG---------EIGRDAFGnapeFGDrGIRKR---- 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 123534099 296 apvAVCG---------------KRTKIIGrVSMDMLTVDISHIPEA-RIGSEVE 333
Cdd:COG3457 284 ---AILAigrqdvdpegltpidYGIEILG-ASSDHLILDVTDSKEDyKVGDTVV 333
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
6-193 |
3.66e-10 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 60.53 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 6 ALIDLDALRHNIRLLNSIA--HNARCAAVIKAdaygHGAVEIARA-LKGEAPKLAVACYDEAVSLREAGVTtPLLVLEGF 82
Cdd:COG3616 11 LVLDLDALERNIARMAARAaaHGVRLRPHGKT----HKSPELARRqLAAGAWGITVATLAEAEVLAAAGVD-DILLAYPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 83 YSSEEL----ADSTRWCDIEWVVHDMEQLDMLSEVAplRKAGPdstRMQTWIKLNTGMNRLGL-PLNKLAHVAEKLQQFP 157
Cdd:COG3616 86 VGPAKLarlaALARAGARLTVLVDSVEQAEALAAAA--AAAGR---PLRVLVELDVGGGRTGVrPPEAALALARAIAASP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 123534099 158 GLSVIGLMTHFA-CADELDSLLQQRQWRAFQAGMQAA 193
Cdd:COG3616 161 GLRLAGLMTYEGhIYGADDAEERRAAAREELARLAAA 197
|
|
| PLPDE_III_yhfX_like |
cd06811 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ... |
7-245 |
4.09e-07 |
|
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: 51.51 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 7 LIDLDALRHNIRLLnsiahnarcaaVIKADAYG------------HGavEIARALKGEAPKLAVAC-YDEAVSLREAGVt 73
Cdd:cd06811 32 VIDLDQIEENARLL-----------AETAEKYGielyfmtkqfgrNP--FLARALLEAGIPGAVAVdFKEARALHEAGL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 74 tPL-----LVLegfYSSEELADSTRWCDIEWVVHDMEQLDMLSEVAplRKAGpdstRMQ-TWIKLNTGMNRL------GL 141
Cdd:cd06811 98 -PLghvghLVQ---IPRHQVPAVLAMRPEVITVYSLEKAREISDAA--VELG----RVQdVLLRVYGDEDTLypgqegGF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 142 PLNKLAHVAEKLQQFPGLSVIGLmTHFAC------------ADELDSLLQQRQWRAfQAGMQAAGANGWSYSSANSAALL 209
Cdd:cd06811 168 PLEELPAVLAAIKALPGIRIAGL-TSFPCflydeeqgdiapTPNLFTLLKAKELLE-KRGIEILQLNAPSATSCATLPLL 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 123534099 210 -QYPETHldwVRPGIAMYGASPM-ADKTGADfglKPVM 245
Cdd:cd06811 246 aEYGVTH---GEPGHALTGTTPLhAVGDQPE---KPAM 277
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
7-164 |
3.69e-06 |
|
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: 48.44 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 7 LIDLDALRHNIRLLNSIAHNA-RCAAVIKAdaygHGAVEIARALKGEA-PKLAVACYDEAVSLREAGVTTPLLV--LEGf 82
Cdd:cd06821 13 AVYPDRIEENIRRMIRMAGDPqRLRPHVKT----HKMAEIVRLQLEAGiTKFKCATIAEAEMLAEAGAPDVLLAypLVG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 83 ysseelADSTRWCDI--EW-------VVHDMEQLDMLSEVAplrkaGPDSTRMQTWIKLNTGMNRLGLPLNK-LAHVAEK 152
Cdd:cd06821 88 ------PNIERFLELakKYpgtrfsaLVDDLEAAEALSAAA-----GSAGLTLSVLLDVNTGMNRTGIAPGEdAEELYRA 156
|
170
....*....|..
gi 123534099 153 LQQFPGLSVIGL 164
Cdd:cd06821 157 IATLPGLVLAGL 168
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
7-165 |
3.79e-06 |
|
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: 48.37 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 7 LIDLDALRHNIRLLNSIAHNARCAavIKADAYGHGAVEIARA-LKGEAPKLAVACYDEAVSLREAGVTTPLLvlegfySS 85
Cdd:cd06819 11 VLDLDALERNIKRMAAFAKAHGVR--LRPHAKTHKCPAIARRqIAAGAVGVCCQKLSEAEVMAAAGIRDILI------TN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 E--------ELADSTRWCDIEWVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLA-HVAEKLQQF 156
Cdd:cd06819 83 EvvgpakiaRLAALARRAPLIVCVDHPDNVRALAAAA--VEAG---VRLDVLVEIDVGQGRCGVPPGEAAlALARTIAAL 157
|
....*....
gi 123534099 157 PGLSVIGLM 165
Cdd:cd06819 158 PGLRFAGLQ 166
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
8-170 |
4.65e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 47.92 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 8 IDLDALRHNIRLLNSIA--HNARCAAVIKADAyghGAVEIARAL-KGEAPKLAVACYDEAVSLREAGVTTPLLVLEgFYS 84
Cdd:cd06815 6 INLSKIRHNAKVLVELCksRGIEVTGVTKVVC---GDPEIAEALlEGGITHLADSRIENLKKLKDLGISGPKMLLR-IPM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 85 SEELADSTRWCDIEwVVHDMEQLDMLSEVAplRKAGpdsTRMQTWIKLNTGMNRLGLPLNKLAHVAEKLQQFPGLSVIGL 164
Cdd:cd06815 82 LSEVEDVVKYADIS-LNSELETIKALSEEA--KKQG---KIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIELVGI 155
|
....*.
gi 123534099 165 MTHFAC 170
Cdd:cd06815 156 GTNLGC 161
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
6-167 |
1.00e-05 |
|
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: 46.92 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 6 ALIDLDALRHNIRLLNSIA--HNARCAAVIKAdaygHGAVEIAR-ALKGEAPKLAVACYDEAVSLREAG-----VTTPLL 77
Cdd:cd06820 6 LLIDLDRLERNIARMQAYAdaHGLSLRPHIKT----HKSPEIARlQLAAGAIGITVATVGEAEVMADAGlsdifIAYPIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 78 VLEGFyssEELADSTRWCDIEWVVHDMEQLDMLSEVAplrkAGPDSTrMQTWIKLNTGMNRLGLPLNKLA-HVAEKLQQF 156
Cdd:cd06820 82 GRQKL---ERLRALAERVTLSVGVDSAEVARGLAEVA----EGAGRP-LEVLVEVDSGMNRCGVQTPEDAvALARAIASA 153
|
170
....*....|.
gi 123534099 157 PGLSVIGLMTH 167
Cdd:cd06820 154 PGLRFRGIFTY 164
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
12-289 |
3.27e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 45.53 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 12 ALRHNIRLLNS--IAHNARCAAVIKAdaygHGAVEIA-RALKGEAPKLAVACYDEAVSLREAGVTTPLL---VLEGFYSS 85
Cdd:cd07376 1 ALEANISRMAAraRASGVRLRPHVKT----HKSPELAqRQLAAGARGVTVATLAEAETFAEAGVKDILMaypLVGPAAIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 86 EELADSTRWCDIEWVVHDMEQLDMLSEVAplRKAGPdstRMQTWIKLNTGMNRLGL---PLNKLAHVAEKLQQfPGLSVI 162
Cdd:cd07376 77 RLAGLLRQEAEFHVLVDSPEALAALAAFA--AAHGV---RLRVMLEVDVGGHRSGVrpeEAAALALADAVQAS-PGLRLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123534099 163 GLMTHFACADELDsLLQQRQWRAFQAgMQA---------AGANGWSYSSANSA-ALLQYPETHLDWVRPGIAMYGASPMA 232
Cdd:cd07376 151 GVMAYEGHIYGAG-GAREGAQARDQA-VAAvraaaaaaeRGLACPTVSGGGTPtYQLTAGDRAVTELRAGSYVFMDTGFD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 123534099 233 DKTGADFglKPVMTFESRLIatRELQAGDSIGYGAAWTADAPTRmGVVAVGYGDGYP 289
Cdd:cd07376 229 TLGACAQ--RPAAFRVTTVI--SRPAPTGRAVLDAGWKASSADT-AFIGGGAVLGRP 280
|
|
| |
