|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-374 |
8.19e-179 |
|
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: 501.64 E-value: 8.19e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 9 DTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLG 88
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 89 PSPPRDINVAAENDVALTVFQKEWVDEAIKLWD-GSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGVYT 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAArLGKTLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 168 HFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKle 247
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 248 PALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLPC 326
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVTD 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446312754 327 --KVPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:cd00430 318 ipDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-376 |
6.98e-173 |
|
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: 486.54 E-value: 6.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 7 YRDTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILV 86
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 87 LGPSPPRDINVAAENDVALTVFQKEWVDEAIK-LWDGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGV 165
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAaARRLGKPLPVHLKVDTGMNRLGFRP-EEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 166 YTHFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLK 245
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADLGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 246 lePALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQ-GFEVLVNGKRVPIVGRVTMDQFMI-- 322
Cdd:COG0787 240 --PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVdv 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446312754 323 -HLPcKVPLGTKVTLIGRQGdeyISATEVAEYSGTINYEIITTISFRVPRIFIRN 376
Cdd:COG0787 318 tDIP-DVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
10-374 |
1.96e-151 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 431.91 E-value: 1.96e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 10 TWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGP 89
Cdd:PRK00053 4 ATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 90 SPPR-DINVAAENDVALTVFQKEWVdEAIKLWDGSSTMKYHINFDSGMGRIGIRERkELKGFLKSLEGAPFLELEGVYTH 168
Cdd:PRK00053 84 FFPAeDLPLIIAYNLTTAVHSLEQL-EALEKAELGKPLKVHLKIDTGMHRLGVRPE-EAEAALERLLACPNVRLEGIFSH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 169 FATADEVETSYFDKQYNTFLEQLSWLKEFGVnPKFvHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEiRPFLPLKLEP 248
Cdd:PRK00053 162 FATADEPDNSYTEQQLNRFEAALAGLPGKGK-PLR-HLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 249 ALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLP-- 325
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLGpd 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446312754 326 CKVPLGTKVTLIGrqgdEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:PRK00053 319 PQDKVGDEVTLWG----EALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
8-374 |
2.35e-134 |
|
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: 388.64 E-value: 2.35e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 8 RDTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVL 87
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 88 GPSPPRDINVAAENDVALTVFQKEWVDEAIK-LWDGSSTMKYHINFDSGMGRIGIRERKELKGFLKSLEGAPFLELEGVY 166
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEaLLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 167 THFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKL 246
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 247 EPALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLP 325
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDLG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446312754 326 CKVPLGTKVTLIGRQgdEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:TIGR00492 321 PDLQDKTGDEVILWG--EEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
14-234 |
1.15e-87 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.47 E-value: 1.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 14 VDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGPSPPR 93
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 94 DINVAAENDVALTVFQKEWVDEAIKLW-DGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGVYTHFATA 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAArRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446312754 173 DEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGiTFNAVRIGIAMYGLSP 234
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-373 |
6.20e-58 |
|
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: 184.58 E-value: 6.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 249 ALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQGFEVLVNGKRVPIVGRVTMDQFMIHLP--C 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446312754 327 KVPLGTKVTLIGRQGdeyISATEVAEYSGTINYEIITTISFRVPRIF 373
Cdd:smart01005 81 DVKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-374 |
8.19e-179 |
|
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: 501.64 E-value: 8.19e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 9 DTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLG 88
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 89 PSPPRDINVAAENDVALTVFQKEWVDEAIKLWD-GSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGVYT 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAArLGKTLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 168 HFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKle 247
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 248 PALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLPC 326
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVTD 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446312754 327 --KVPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:cd00430 318 ipDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-376 |
6.98e-173 |
|
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: 486.54 E-value: 6.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 7 YRDTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILV 86
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 87 LGPSPPRDINVAAENDVALTVFQKEWVDEAIK-LWDGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGV 165
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAaARRLGKPLPVHLKVDTGMNRLGFRP-EEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 166 YTHFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLK 245
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADLGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 246 lePALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQ-GFEVLVNGKRVPIVGRVTMDQFMI-- 322
Cdd:COG0787 240 --PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVdv 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446312754 323 -HLPcKVPLGTKVTLIGRQGdeyISATEVAEYSGTINYEIITTISFRVPRIFIRN 376
Cdd:COG0787 318 tDIP-DVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
10-374 |
1.96e-151 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 431.91 E-value: 1.96e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 10 TWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGP 89
Cdd:PRK00053 4 ATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 90 SPPR-DINVAAENDVALTVFQKEWVdEAIKLWDGSSTMKYHINFDSGMGRIGIRERkELKGFLKSLEGAPFLELEGVYTH 168
Cdd:PRK00053 84 FFPAeDLPLIIAYNLTTAVHSLEQL-EALEKAELGKPLKVHLKIDTGMHRLGVRPE-EAEAALERLLACPNVRLEGIFSH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 169 FATADEVETSYFDKQYNTFLEQLSWLKEFGVnPKFvHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEiRPFLPLKLEP 248
Cdd:PRK00053 162 FATADEPDNSYTEQQLNRFEAALAGLPGKGK-PLR-HLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 249 ALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLP-- 325
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLGpd 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446312754 326 CKVPLGTKVTLIGrqgdEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:PRK00053 319 PQDKVGDEVTLWG----EALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
8-374 |
2.35e-134 |
|
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: 388.64 E-value: 2.35e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 8 RDTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVL 87
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 88 GPSPPRDINVAAENDVALTVFQKEWVDEAIK-LWDGSSTMKYHINFDSGMGRIGIRERKELKGFLKSLEGAPFLELEGVY 166
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEaLLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 167 THFATADEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKL 246
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 247 EPALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHLP 325
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDLG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446312754 326 CKVPLGTKVTLIGRQgdEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:TIGR00492 321 PDLQDKTGDEVILWG--EEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
11-374 |
9.39e-91 |
|
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: 277.70 E-value: 9.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 11 WVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGPS 90
Cdd:cd06825 3 WLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 91 PPRDINVAAENDVALTVFQKEWvdeAIKLWDGSSTMKYHINFDSGMGRIGIreRKELKGFLKSLEGAPFLELEGVYTHFA 170
Cdd:cd06825 83 PPVRAKELKKYSLTQTLISEAY---AEELSKYAVNIKVHLKVDTGMHRLGE--SPEDIDSILAIYRLKNLKVSGIFSHLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 171 TADEVETS---YFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKLE 247
Cdd:cd06825 158 VSDSLDEDdiaFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPNDPTKLGLDLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 248 PALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL--QGFEVLVNGKRVPIVGRVTMDQFMI--- 322
Cdd:cd06825 238 PVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNICMDQLMVdvt 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446312754 323 HLPcKVPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:cd06825 318 DIP-EVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
14-234 |
1.15e-87 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.47 E-value: 1.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 14 VDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGPSPPR 93
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 94 DINVAAENDVALTVFQKEWVDEAIKLW-DGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGVYTHFATA 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAArRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446312754 173 DEVETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGiTFNAVRIGIAMYGLSP 234
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
9-376 |
6.29e-86 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 277.61 E-value: 6.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 9 DTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLG 88
Cdd:PRK11930 459 ETVLEINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 89 PSPPrDINVAAENDVALTVFQ----KEWVDEAIKlwDGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEG 164
Cdd:PRK11930 539 PEPT-SFDTIIDYKLEPEIYSfrllDAFIKAAQK--KGITGYPIHIKIDTGMHRLGFEP-EDIPELARRLKKQPALKVRS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 165 VYTHFATADE-VETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPflp 243
Cdd:PRK11930 615 VFSHLAGSDDpDHDDFTRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQ--- 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 244 lKLEPALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL--QGFEVLVNGKRVPIVGRVTMDQFM 321
Cdd:PRK11930 692 -ALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgnGVGYVLVNGQKAPIVGNICMDMCM 770
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446312754 322 I---HLPCKVplGTKVTLIGrqgdEYISATEVAEYSGTINYEIITTISFRVPRIFIRN 376
Cdd:PRK11930 771 IdvtDIDAKE--GDEVIIFG----EELPVTELADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
2-375 |
3.54e-67 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 217.95 E-value: 3.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 2 EEAPFYRDTWVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGIT 81
Cdd:PRK13340 33 AEQIQPRNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 82 APILVLGPSPPRDINVAAENDVALTVFQKEWVDEAIKL-WDGSSTMKYHINFDS-GMGRIGIRERKElKGFLKSLE--GA 157
Cdd:PRK13340 113 GQLLRVRSASPAEIEQALRYDLEELIGDDEQAKLLAAIaKKNGKPIDIHLALNSgGMSRNGLDMSTA-RGKWEALRiaTL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 158 PFLELEGVYTHFATADEvetSYFDKQYNTFLEQLSWL-KEFGVNPKFV--HTANSAATLRFQGITFNAVRIGIAMYGlSP 234
Cdd:PRK13340 192 PSLGIVGIMTHFPNEDE---DEVRWKLAQFKEQTAWLiGEAGLKREKItlHVANSYATLNVPEAHLDMVRPGGILYG-DR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 235 SVEIRPFlplklEPALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQ-GFEVLVNGKRVPIVG 313
Cdd:PRK13340 268 HPANTEY-----KRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVVG 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446312754 314 RVTMDQFMIHL-PCK-VPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIFIR 375
Cdd:PRK13340 343 RVSMNTLMVDVtDIPnVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
249-373 |
5.35e-61 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 192.58 E-value: 5.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 249 ALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQG-FEVLVNGKRVPIVGRVTMDQFMIHLP-- 325
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNrGEVLINGKRAPIVGRVCMDQLMVDVTdv 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446312754 326 CKVPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIF 373
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-373 |
6.20e-58 |
|
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: 184.58 E-value: 6.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 249 ALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRLQGFEVLVNGKRVPIVGRVTMDQFMIHLP--C 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446312754 327 KVPLGTKVTLIGRQGdeyISATEVAEYSGTINYEIITTISFRVPRIF 373
Cdd:smart01005 81 DVKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
11-374 |
1.26e-55 |
|
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: 186.78 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 11 WVEVDLDAIYNNVTHIKEFIPSGVEIFAVVKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGPS 90
Cdd:cd06826 3 WLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 91 PPRDINVAAENDVAL---TVFQKEWVDEAIKLWDGssTMKYHINFDS-GMGRIGIrERKELKGFLKSLEGA--PFLELEG 164
Cdd:cd06826 83 TPSEIEDALAYNIEEligSLDQAEQIDSLAKRHGK--TLPVHLALNSgGMSRNGL-ELSTAQGKEDAVAIAtlPNLKIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 165 VYTHFATADEVETSYFDKQYNtflEQLSWL-KEFGVNPK--FVHTANSAATLRFQGITFNAVRIGIAMYG-LSPSVEIrp 240
Cdd:cd06826 160 IMTHFPVEDEDDVRAKLARFN---EDTAWLiSNAKLKREkiTLHAANSFATLNVPEAHLDMVRPGGILYGdTPPSPEY-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 241 flplklEPALSLHTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQ 319
Cdd:cd06826 235 ------KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFsNKAHVLINGQRVPVVGKVSMNT 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446312754 320 FMI---HLPcKVPLGTKVTLIGRQGDEYISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:cd06826 309 VMVdvtDIP-GVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
19-227 |
8.10e-54 |
|
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: 177.13 E-value: 8.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 19 IYNNVTHIKEFIPSGVEIFAVVKGNAYghdyVPVAKTALEAGaTRLAVAFLDEALVLRRAGI-TAPILVLGPSP-PRDIN 96
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANAN----PEVARTLAALG-TGFDVASLGEALLLRAAGIpPEPILFLGPCKqVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 97 VAAE-NDVALTVFQKEWVDEAIKLWD-GSSTMKYHINFDSG--MGRIGIRErKELKGFLKSLEGAPFLELEGVYTHFATA 172
Cdd:cd06808 76 DAAEqGVIVVTVDSLEELEKLEEAALkAGPPARVLLRIDTGdeNGKFGVRP-EELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446312754 173 DEvETSYFDKQYNTFLEQLSWLKEFGVNPKFVHTANSAATLRFQG---ITFNAVRIGI 227
Cdd:cd06808 155 DE-DYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQElplGTFIIVEPGR 211
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
14-374 |
1.89e-53 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 180.70 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 14 VDLDAIYNNVTHIKEFIPsGVEIFAVVKGNAYGHDYVPVAkTALEAgATRLAVAFLDEALVLRRAGITAPILVL-GPSPP 92
Cdd:PRK03646 8 LDLQALKQNLSIVREAAP-GARVWSVVKANAYGHGIERIW-SALGA-TDGFAVLNLEEAITLRERGWKGPILMLeGFFHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 93 RDINVAAENDVAlTVFQKEWVDEAIKLWDGSSTMKYHINFDSGMGRIGIRErKELKGFLKSLEGAPFLELEGVYTHFATA 172
Cdd:PRK03646 85 QDLELYDQHRLT-TCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQP-ERVQTVWQQLRAMGNVGEMTLMSHFARA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 173 DEVETSyfDKQYNTFlEQLSWlkefGVNPKfVHTANSAATLRFQGITFNAVRIGIAMYGLSPSVEIRPFLPLKLEPALSL 252
Cdd:PRK03646 163 DHPDGI--SEAMARI-EQAAE----GLECE-RSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 253 HTKVAHIKQVIKGDGISYNVTYRTKTEEWIATVAIGYADGWLRRL-QGFEVLVNGKRVPIVGRVTMDQFMIHL-PC-KVP 329
Cdd:PRK03646 235 SSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAVDLtPCpQAG 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446312754 330 LGTKVTLIGRQgdeyISATEVAEYSGTINYEIITTISFRVPRIFI 374
Cdd:PRK03646 315 IGTPVELWGKE----IKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
14-168 |
2.86e-07 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 52.06 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 14 VDLDAIYNNVTHIKEFIPS-GVEIFAVVKGnaygHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITaPILV----LG 88
Cdd:COG3616 13 LDLDALERNIARMAARAAAhGVRLRPHGKT----HKSPELARRQLAAGAWGITVATLAEAEVLAAAGVD-DILLayplVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 89 PSPPRDINVAAENDVALTVfqkeWVD--EAIKLWD-----GSSTMKYHINFDSGMGRIGIRERKELKGFLKSLEGAPFLE 161
Cdd:COG3616 88 PAKLARLAALARAGARLTV----LVDsvEQAEALAaaaaaAGRPLRVLVELDVGGGRTGVRPPEAALALARAIAASPGLR 163
|
....*..
gi 446312754 162 LEGVYTH 168
Cdd:COG3616 164 LAGLMTY 170
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
32-168 |
5.26e-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: 44.76 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 32 SGVEIFAVVKGnaygHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITaPILVLGPSPPRdINVAAENDVALTVFQKE 111
Cdd:cd07376 16 SGVRLRPHVKT----HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVK-DILMAYPLVGP-AAIARLAGLLRQEAEFH 89
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446312754 112 W-VD--EAIKLWDG-----SSTMKYHINFDSGMGRIGIR-ERKELKGFLKSLEGAPFLELEGVYTH 168
Cdd:cd07376 90 VlVDspEALAALAAfaaahGVRLRVMLEVDVGGHRSGVRpEEAAALALADAVQASPGLRLAGVMAY 155
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|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
47-168 |
7.90e-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: 44.23 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 47 HDYVPVAKTALEAGATRLAVAFLDEALVLRRAG-----ITAPILvlGPSPPRDIN-VAAENDVALTVFQKEWVDEAIKLW 120
Cdd:cd06820 38 HKSPEIARLQLAAGAIGITVATVGEAEVMADAGlsdifIAYPIV--GRQKLERLRaLAERVTLSVGVDSAEVARGLAEVA 115
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446312754 121 DG-SSTMKYHINFDSGMGRIGIRERKELKGFLKSLEGAPFLELEGVYTH 168
Cdd:cd06820 116 EGaGRPLEVLVEVDSGMNRCGVQTPEDAVALARAIASAPGLRFRGIFTY 164
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|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
12-230 |
1.11e-04 |
|
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: 43.69 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 12 VEVDLDAIYNNVTHIKE-FIPSGVEIFAVVKGNAyGHdyVPVAKTALEAGATRLAVAFLDEALVLRRAGITAPILVLGPS 90
Cdd:cd06815 4 LEINLSKIRHNAKVLVElCKSRGIEVTGVTKVVC-GD--PEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLLRIP 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 91 PPRDIN-VAAENDVAL-----TVfqKEWVDEAIKLwdgsstMKYH---INFDSGMGRIGIRErKELKGFLKSLEGAPFLE 161
Cdd:cd06815 81 MLSEVEdVVKYADISLnseleTI--KALSEEAKKQ------GKIHkiiLMVDLGDLREGVLP-EDLLDFVEEILKLPGIE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446312754 162 LEGVYTHFATADEVETSYFDkqyntfLEQLSWLKE-----FGVNPKFVHTANSAA-TLRFQGIT---FNAVRIGIAMY 230
Cdd:cd06815 152 LVGIGTNLGCYGGVLPTEEN------MGKLVELKEeiekeFGIKLPIISGGNSASlPLLLKGELpggINQLRIGEAIL 223
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
14-165 |
4.17e-04 |
|
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: 42.20 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 14 VDLDAIYNNVTHIKEFI-PSGVEIfavvKGNAYGHDYVPVAKTALEAGATRLAVAFLDEALVLRRAGITApIL----VLG 88
Cdd:cd06819 12 LDLDALERNIKRMAAFAkAHGVRL----RPHAKTHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIRD-ILitneVVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312754 89 PSPprdINVAAE--NDVALTVFqkewVDEAIKLWDGSSTMKYH-------INFDSGMGRIGIRERKELKGFLKSLEGAPF 159
Cdd:cd06819 87 PAK---IARLAAlaRRAPLIVC----VDHPDNVRALAAAAVEAgvrldvlVEIDVGQGRCGVPPGEAALALARTIAALPG 159
|
....*.
gi 446312754 160 LELEGV 165
Cdd:cd06819 160 LRFAGL 165
|
|
| PLPDE_III_yhfX_like |
cd06811 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ... |
9-80 |
5.61e-03 |
|
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: 38.41 E-value: 5.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446312754 9 DTWVeVDLDAIYNNVTHIKEFIPS-GVEIFAVVKG---NAYghdyvpVAKTALEAGATRLAVAFLDEALVLRRAGI 80
Cdd:cd06811 29 DTYV-IDLDQIEENARLLAETAEKyGIELYFMTKQfgrNPF------LARALLEAGIPGAVAVDFKEARALHEAGL 97
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