|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
9-374 |
4.04e-169 |
|
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: 477.68 E-value: 4.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 9 RDTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 89 GATRPKDVKIAADLDISLTTFHKEWLVEAGNQLSE-GDRLNLHIKCDTGMGRIGVRsTGDLKGIEQYVQAHAQFNLEGIF 167
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRlGKPLPVHLKVDTGMNRLGFR-PEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPelPFPL 244
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAgldPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAA--DLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGgPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1733522655 324 GFLD--MGTRVTLIGKQGeeaITMDEIADKLDTINYEIPCMISTRVPRIYMRN 374
Cdd:COG0787 319 DIPDvkVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
10-372 |
1.87e-166 |
|
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: 470.83 E-value: 1.87e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 10 DTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLG 89
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 90 ATRPKDVKIAADLDISLTTFHKEWLvEAGNQLSE--GDRLNLHIKCDTGMGRIGVRSTgDLKGIEQYVQAHAQFNLEGIF 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQA-EALSAAAArlGKTLKVHLKIDTGMGRLGFRPE-EAEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPelPFPL 244
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKS--PLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKgEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1733522655 324 GFLDM--GTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIYM 372
Cdd:cd00430 317 DIPDVkvGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
11-371 |
1.73e-150 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 429.98 E-value: 1.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 11 TWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGA 90
Cdd:PRK00053 4 ATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 91 T-RPKDVKIAADLDISLTTFHKEWLvEAGNQLSEGDRLNLHIKCDTGMGRIGVRStgdlkgiEQYVQAHA------QFNL 163
Cdd:PRK00053 84 FfPAEDLPLIIAYNLTTAVHSLEQL-EALEKAELGKPLKVHLKIDTGMHRLGVRP-------EEAEAALErllacpNVRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 164 EGIFTHFATADELNDDYLDRQLARFEYMLNQLDSLPA-YIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEmKPELPF 242
Cdd:PRK00053 156 EGIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 243 PLKEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL-QGQDVIVNGERVPIVGRICMDQCMIR 321
Cdd:PRK00053 235 GLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 322 LPGFLDM--GTRVTLIGKqgeeAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:PRK00053 315 LGPDPQDkvGDEVTLWGE----ALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
9-372 |
5.96e-137 |
|
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: 395.95 E-value: 5.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 9 RDTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 89 GATRPKDVKIAADLDISLTTFHKEWLVEAGNQ-LSEGDRLNLHIKCDTGMGRIGVRSTGDLKGIEQYVQAHAQFNLEGIF 167
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEAlLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQL---DSLPAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPELPFPL 244
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLkqqNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL-QGQDVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDLG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1733522655 324 GFLD--MGTRVTLIGKQgeeaITMDEIADKLDTINYEIPCMISTRVPRIYM 372
Cdd:TIGR00492 321 PDLQdkTGDEVILWGEE----ISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
15-232 |
1.99e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 246.37 E-value: 1.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 15 INLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGATRPK 94
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 95 DVKIAADLDISLTTFHKEWLVEAGNQLSEGDR-LNLHIKCDTGMGRIGVRsTGDLKGIEQYVQAHAQFNLEGIFTHFATA 173
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKpLRVHLKIDTGMGRLGFR-PEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 174 DELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKtNTLFNAVRVGIAMYGLTP 232
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAglrPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
247-371 |
2.73e-59 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 188.43 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 247 VFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQDVIVNGERVPIVGRICMDQCMIRLPGFL 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1733522655 327 DM--GTRVTLIGKQGeeaITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:smart01005 81 DVkvGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
9-374 |
4.04e-169 |
|
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: 477.68 E-value: 4.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 9 RDTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 89 GATRPKDVKIAADLDISLTTFHKEWLVEAGNQLSE-GDRLNLHIKCDTGMGRIGVRsTGDLKGIEQYVQAHAQFNLEGIF 167
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRlGKPLPVHLKVDTGMNRLGFR-PEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPelPFPL 244
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAgldPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAA--DLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGgPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1733522655 324 GFLD--MGTRVTLIGKQGeeaITMDEIADKLDTINYEIPCMISTRVPRIYMRN 374
Cdd:COG0787 319 DIPDvkVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
10-372 |
1.87e-166 |
|
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: 470.83 E-value: 1.87e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 10 DTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLG 89
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 90 ATRPKDVKIAADLDISLTTFHKEWLvEAGNQLSE--GDRLNLHIKCDTGMGRIGVRSTgDLKGIEQYVQAHAQFNLEGIF 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQA-EALSAAAArlGKTLKVHLKIDTGMGRLGFRPE-EAEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPelPFPL 244
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKS--PLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKgEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1733522655 324 GFLDM--GTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIYM 372
Cdd:cd00430 317 DIPDVkvGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
11-371 |
1.73e-150 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 429.98 E-value: 1.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 11 TWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGA 90
Cdd:PRK00053 4 ATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 91 T-RPKDVKIAADLDISLTTFHKEWLvEAGNQLSEGDRLNLHIKCDTGMGRIGVRStgdlkgiEQYVQAHA------QFNL 163
Cdd:PRK00053 84 FfPAEDLPLIIAYNLTTAVHSLEQL-EALEKAELGKPLKVHLKIDTGMHRLGVRP-------EEAEAALErllacpNVRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 164 EGIFTHFATADELNDDYLDRQLARFEYMLNQLDSLPA-YIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEmKPELPF 242
Cdd:PRK00053 156 EGIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGE-PLGLDF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 243 PLKEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL-QGQDVIVNGERVPIVGRICMDQCMIR 321
Cdd:PRK00053 235 GLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 322 LPGFLDM--GTRVTLIGKqgeeAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:PRK00053 315 LGPDPQDkvGDEVTLWGE----ALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
9-372 |
5.96e-137 |
|
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: 395.95 E-value: 5.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 9 RDTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 89 GATRPKDVKIAADLDISLTTFHKEWLVEAGNQ-LSEGDRLNLHIKCDTGMGRIGVRSTGDLKGIEQYVQAHAQFNLEGIF 167
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEAlLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 168 THFATADELNDDYLDRQLARFEYMLNQL---DSLPAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPELPFPL 244
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLkqqNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 245 KEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL-QGQDVIVNGERVPIVGRICMDQCMIRLP 323
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDLG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1733522655 324 GFLD--MGTRVTLIGKQgeeaITMDEIADKLDTINYEIPCMISTRVPRIYM 372
Cdd:TIGR00492 321 PDLQdkTGDEVILWGEE----ISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
13-371 |
1.09e-98 |
|
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: 297.87 E-value: 1.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 13 AEINLDHLYENVKNIRNHIPgDVKVFAVVKANAYGHGDVQTAFtALsAGAHGLAVAFLDEAISLRRAGVTAPILVL-GAT 91
Cdd:cd06827 4 ATIDLAALRHNLRLVRELAP-NSKILAVVKANAYGHGLVRVAK-AL-ADADGFAVACIEEALALREAGITKPILLLeGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 92 RPKDVKIAADLDISlTTFHKEWLVEAGNQLSEGDRLNLHIKCDTGMGRIGVRStGDLKGIEQYVQAHAQFNLEGIFTHFA 171
Cdd:cd06827 81 SADELPLAAEYNLW-TVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSP-EEYAAAYQRLKASPNVASIVLMTHFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 172 TADELNDDYLDRQLARFEYMLNQLD---SLpayihsSNSAATLRKTNTLFNAVRVGIAMYGLTPSqEMKPELPFPLKEVF 248
Cdd:cd06827 159 CADEPDSPGTAKQLAIFEQATAGLPgprSL------ANSAAILAWPEAHGDWVRPGIMLYGASPF-ADKSGADLGLKPVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 249 SLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQ-GQDVIVNGERVPIVGRICMDQCMIRLPGFLD 327
Cdd:cd06827 232 TLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPsGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1733522655 328 --MGTRVTLIGKQgeeaITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:cd06827 312 akVGDPVELWGKG----LPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
12-371 |
8.52e-93 |
|
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: 283.48 E-value: 8.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 12 WAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGAT 91
Cdd:cd06825 3 WLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 92 RPKDVKIAADLDISLTTFHKEWlVEAGNQLSEgdRLNLHIKCDTGMGRIGVrSTGDLKGIEQyVQAHAQFNLEGIFTHFA 171
Cdd:cd06825 83 PPVRAKELKKYSLTQTLISEAY-AEELSKYAV--NIKVHLKVDTGMHRLGE-SPEDIDSILA-IYRLKNLKVSGIFSHLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 172 TADELNDDYLDR---QLARFEYMLNQLDS---LPAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPELPFPLK 245
Cdd:cd06825 158 VSDSLDEDDIAFtkhQIACFDQVLADLKArgiEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPNDPTKLGLDLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 246 EVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQD--VIVNGERVPIVGRICMDQCMIRLP 323
Cdd:cd06825 238 PVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQKayVLINGKRAPIIGNICMDQLMVDVT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1733522655 324 GF--LDMGTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:cd06825 318 DIpeVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
15-232 |
1.99e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 246.37 E-value: 1.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 15 INLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGATRPK 94
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 95 DVKIAADLDISLTTFHKEWLVEAGNQLSEGDR-LNLHIKCDTGMGRIGVRsTGDLKGIEQYVQAHAQFNLEGIFTHFATA 173
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKpLRVHLKIDTGMGRLGFR-PEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 174 DELNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKtNTLFNAVRVGIAMYGLTP 232
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAglrPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
10-374 |
7.68e-75 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 248.33 E-value: 7.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 10 DTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLG 89
Cdd:PRK11930 459 ETVLEINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 90 ATRPK-DVKIAADLDISLTTFHkewLVEAGNQLSEGDRLN---LHIKCDTGMGRIGVRSTgDLKGIEQYVQAHAQFNLEG 165
Cdd:PRK11930 539 PEPTSfDTIIDYKLEPEIYSFR---LLDAFIKAAQKKGITgypIHIKIDTGMHRLGFEPE-DIPELARRLKKQPALKVRS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 166 IFTHFATADELN-DDYLDRQLARFEYMLNQLDSLPAYI---HSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPElp 241
Cdd:PRK11930 615 VFSHLAGSDDPDhDDFTRQQIELFDEGSEELQEALGYKpirHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQA-- 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 242 fpLKEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL--QGQDVIVNGERVPIVGRICMDQCM 319
Cdd:PRK11930 693 --LRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgnGVGYVLVNGQKAPIVGNICMDMCM 770
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 320 IrlpgflDmgtrVTLI-GKQGEEAI------TMDEIADKLDTINYEIPCMISTRVPRIYMRN 374
Cdd:PRK11930 771 I------D----VTDIdAKEGDEVIifgeelPVTELADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
9-371 |
1.51e-72 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 232.59 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 9 RDTWAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 89 GATRPKDVKIAADLDIslttfhkEWLV---EAGNQLSE-----GDRLNLHIKCDT-GMGRIGVRSTGDlKGIEQYVQAHA 159
Cdd:PRK13340 119 RSASPAEIEQALRYDL-------EELIgddEQAKLLAAiakknGKPIDIHLALNSgGMSRNGLDMSTA-RGKWEALRIAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 160 QFNLE--GIFTHFATADElndDYLDRQLARFEymlNQLDSLPA---------YIHSSNSAATLRKTNTLFNAVRVGIAMY 228
Cdd:PRK13340 191 LPSLGivGIMTHFPNEDE---DEVRWKLAQFK---EQTAWLIGeaglkrekiTLHVANSYATLNVPEAHLDMVRPGGILY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 229 G-LTPSQemkpelpFPLKEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQ-GQDVIVNGER 306
Cdd:PRK13340 265 GdRHPAN-------TEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQR 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733522655 307 VPIVGRICMDQCMIRLPGFLDM--GTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:PRK13340 338 APVVGRVSMNTLMVDVTDIPNVkpGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
13-372 |
1.16e-69 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 223.45 E-value: 1.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 13 AEINLDHLYENVKNIRNHIPGdVKVFAVVKANAYGHGDVQTAfTALSAgAHGLAVAFLDEAISLRRAGVTAPILVL-GAT 91
Cdd:PRK03646 6 ASLDLQALKQNLSIVREAAPG-ARVWSVVKANAYGHGIERIW-SALGA-TDGFAVLNLEEAITLRERGWKGPILMLeGFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 92 RPKDVKIAADLDISlTTFHKEWLVEAGNQLSEGDRLNLHIKCDTGMGRIGVRStgdlkgiEQYVQAHAQFNLEG------ 165
Cdd:PRK03646 83 HAQDLELYDQHRLT-TCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQP-------ERVQTVWQQLRAMGnvgemt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 166 IFTHFATADELndDYLDRQLARFEYMLNQLDslpAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPSQEMKPELPFPLK 245
Cdd:PRK03646 155 LMSHFARADHP--DGISEAMARIEQAAEGLE---CERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 246 EVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKL-QGQDVIVNGERVPIVGRICMDQCMIRLPG 324
Cdd:PRK03646 230 PVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAVDLTP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1733522655 325 F--LDMGTRVTLIGKQgeeaITMDEIADKLDTINYEIPCMISTRVPRIYM 372
Cdd:PRK03646 310 CpqAGIGTPVELWGKE----IKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
247-371 |
3.49e-65 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 203.75 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 247 VFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRICMDQCMIRLPGF 325
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRgEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1733522655 326 LD--MGTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:pfam00842 81 PEvkVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
247-371 |
2.73e-59 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 188.43 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 247 VFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQDVIVNGERVPIVGRICMDQCMIRLPGFL 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1733522655 327 DM--GTRVTLIGKQGeeaITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:smart01005 81 DVkvGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
12-371 |
2.00e-50 |
|
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: 173.68 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 12 WAEINLDHLYENVKNIRNHIPGDVKVFAVVKANAYGHGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVLGAT 91
Cdd:cd06826 3 WLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 92 RPKDVKIAADLDI-----SLTTfhkewlVEAGNQLSE--GDRLNLHIKCDT-GMGRIGVRSTGDlKGIEQYVQAHAQFNL 163
Cdd:cd06826 83 TPSEIEDALAYNIeeligSLDQ------AEQIDSLAKrhGKTLPVHLALNSgGMSRNGLELSTA-QGKEDAVAIATLPNL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 164 E--GIFTHFATADElndDYLDRQLARFEYMLN------QLDSLPAYIHSSNSAATLRKTNTLFNAVRVGIAMYGLTPsqe 235
Cdd:cd06826 156 KivGIMTHFPVEDE---DDVRAKLARFNEDTAwlisnaKLKREKITLHAANSFATLNVPEAHLDMVRPGGILYGDTP--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 236 mkPELPFplKEVFSLHSRLIHTKELSAGEKVSYGATYETGEAEWIGTIPIGYADGWLRKLQGQ-DVIVNGERVPIVGRIC 314
Cdd:cd06826 230 --PSPEY--KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKaHVLINGQRVPVVGKVS 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 315 MDQCMI---RLPGfLDMGTRVTLIGKQGEEAITMDEIADKLDTINYEIPCMISTRVPRIY 371
Cdd:cd06826 306 MNTVMVdvtDIPG-VKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
20-225 |
2.47e-35 |
|
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: 129.36 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 20 LYENVKNIRNHIPGDVKVFAVVKANAyghgDVQTAFTALSAGAhGLAVAFLDEAISLRRAGV-TAPILVLGAT-RPKDVK 97
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTLAALGT-GFDVASLGEALLLRAAGIpPEPILFLGPCkQVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 98 IAADLDISLTTFHKEWLVEAGNQLS--EGDRLNLHIKCDTG--MGRIGVRStGDLKGIEQYVQAHAQFNLEGIFTHFATA 173
Cdd:cd06808 76 DAAEQGVIVVTVDSLEELEKLEEAAlkAGPPARVLLRIDTGdeNGKFGVRP-EELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733522655 174 DElNDDYLDRQLARFEYMLNQLDSL---PAYIHSSNSAATLRKTN---TLFNAVRVGI 225
Cdd:cd06808 155 DE-DYSPFVEALSRFVAALDQLGELgidLEQLSIGGSFAILYLQElplGTFIIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
58-187 |
2.99e-06 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 48.98 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 58 LSAGAHGLAVAFLDEAISLRRAGVTaPILV------------LGATRPKDVKIAADLDiSLTtfHKEWLVEAGnqLSEGD 125
Cdd:COG3616 53 LAAGAWGITVATLAEAEVLAAAGVD-DILLayplvgpaklarLAALARAGARLTVLVD-SVE--QAEALAAAA--AAAGR 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733522655 126 RLNLHIKCDTGMGRIGVRSTGDLKGIEQYVQAHAQFNLEGIFTHFATADELNDDYLDRQLAR 187
Cdd:COG3616 127 PLRVLVELDVGGGRTGVRPPEAALALARAIAASPGLRLAGLMTYEGHIYGADDAEERRAAAR 188
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
48-169 |
2.67e-04 |
|
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: 42.69 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 48 HGDVQTAFTALSAGAHGLAVAFLDEAISLRRAG-----VTAPILvlgaTRPKDVKIAA---DLDISLTTFHKEWLVEAGN 119
Cdd:cd06820 38 HKSPEIARLQLAAGAIGITVATVGEAEVMADAGlsdifIAYPIV----GRQKLERLRAlaeRVTLSVGVDSAEVARGLAE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1733522655 120 QLSEGDR-LNLHIKCDTGMGRIGVRSTGDLKGIEQYVQAHAQFNLEGIFTH 169
Cdd:cd06820 114 VAEGAGRpLEVLVEVDSGMNRCGVQTPEDAVALARAIASAPGLRFRGIFTY 164
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
57-169 |
3.40e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 42.45 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 57 ALSAGAHGLAVAFLDEAISLRRAGVTApiLVLGATRPKDVKIAADLDISLTTFHKEWLVE--------AGNQLSEGDRLN 128
Cdd:cd07376 36 QLAAGARGVTVATLAEAETFAEAGVKD--ILMAYPLVGPAAIARLAGLLRQEAEFHVLVDspealaalAAFAAAHGVRLR 113
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1733522655 129 LHIKCDTGMGRIGVR-STGDLKGIEQYVQAHAQFNLEGIFTH 169
Cdd:cd07376 114 VMLEVDVGGHRSGVRpEEAAALALADAVQASPGLRLAGVMAY 155
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
16-136 |
4.41e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 42.27 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 16 NLDHLYENVKNIRNHIPGDVKVFAVVKANAYGhgdvqTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPiLVLGATRPKD 95
Cdd:cd06843 8 DLAALRAHARALRASLPPGCELFYAIKANSDP-----PILRALAPHVDGFEVASGGEIAHVRAAVPDAP-LIFGGPGKTD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1733522655 96 VKIAADLDISLTTFHkewlVEAGNQLSegdRLNlHIKCDTG 136
Cdd:cd06843 82 SELAQALAQGVERIH----VESELELR---RLN-AVARRAG 114
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
14-108 |
7.99e-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: 41.38 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733522655 14 EINLDHLYENVKNI-----RNHIpgdvKVFAVVKANAyghGDVQTAFTALSAGAHGLAVAFLDEAISLRRAGVTAPILVL 88
Cdd:cd06815 5 EINLSKIRHNAKVLvelckSRGI----EVTGVTKVVC---GDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLL 77
|
90 100
....*....|....*....|....*..
gi 1733522655 89 gatRP-------KDVKIAadlDISLTT 108
Cdd:cd06815 78 ---RIpmlseveDVVKYA---DISLNS 98
|
|
| |
