|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
19-377 |
3.32e-145 |
|
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: 415.66 E-value: 3.32e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 19 ATGYLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFV 97
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPgAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREA-GIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 98 LNGLQPGNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIM 177
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 178 SHLASADDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGVLARPGIALYGGAPNAG--EKNPMEP 250
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLdpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEvaADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 251 VVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISAL 330
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517056602 331 PEGALtfGSLVEVLGRH-QTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:COG0787 321 PDVKV--GDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
22-377 |
3.37e-119 |
|
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: 349.87 E-value: 3.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 22 YLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFVLNG 100
Cdd:cd00430 3 WAEIDLDALRHNLRVIRRLLGPgTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREA-GITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 101 LQPGNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHL 180
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 181 ASADDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGVLARPGIALYGGAPNAGEKNPME--PVVS 253
Cdd:cd00430 162 ATADEPDKAYTRRQLERFLEALAELEEAGIppplkHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGlkPVMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 254 LDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEg 333
Cdd:cd00430 242 LKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIPD- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517056602 334 aLTFGSLVEVLGRH----QTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:cd00430 321 -VKVGDEVVLFGRQgdeeITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
24-377 |
8.67e-106 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 315.58 E-value: 8.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 24 TIDLAALGRNYRKLVSMLGPV-RAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRpALAQDAQVFVLNGLQ 102
Cdd:PRK00053 7 EIDLDALRHNLRQIRKHAPPKsKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELR-EAGITAPILILGGFF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 103 PGNEI-ACAEMGIVPVLNSLAQWRQWSAAAriLKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLA 181
Cdd:PRK00053 86 PAEDLpLIIAYNLTTAVHSLEQLEALEKAE--LGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFSHFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 182 SADDMDSEQNGEQFAEMSRIADEFPGFDI---SFANSGGVFLGEAYYGVLARPGIALYGGAP---NAGEKNPMEPVVSLD 255
Cdd:PRK00053 164 TADEPDNSYTEQQLNRFEAALAGLPGKGKplrHLANSAAILRWPDLHFDWVRPGIALYGLSPsgePLGLDFGLKPAMTLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 256 VAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEgaL 335
Cdd:PRK00053 244 SSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQ--D 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517056602 336 TFGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:PRK00053 322 KVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
25-376 |
6.83e-72 |
|
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: 228.78 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 25 IDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFVLNGLQP 103
Cdd:TIGR00492 7 IDLAALKHNLSAIRNHIGPkSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKA-GITAPILLLGGFFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNV-EILFIMSHLAS 182
Cdd:TIGR00492 86 EDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFlELEGIFSHFAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 183 ADDMDSEQNGEQFAEMSRIADEFPGFDISF-----ANSGGVFLGEAYYGVLARPGIALYGGAPNAG--EKNP--MEPVVS 253
Cdd:TIGR00492 166 ADEPKTGTTQKQIERFNSFLEGLKQQNIEPpfrhiANSAAILNWPESHFDMVRPGIILYGLYPSADmsDGAPfgLKPVLS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 254 LDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEG 333
Cdd:TIGR00492 246 LTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPDLQD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 517056602 334 ALtfGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:TIGR00492 326 KT--GDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
25-240 |
2.90e-61 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 196.29 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 25 IDLAALGRNYRKLVSMLGPV-RAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPALAqDAQVFVLNGLQP 103
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGaKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGI-TAPILVLGGFPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLASA 183
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056602 184 DDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGvLARPGIALYGGAP 240
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAGLrppvvHLANSAAILLHPLHFD-MVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
251-376 |
4.41e-49 |
|
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: 161.47 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 251 VVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDcGAVYFKGIRLPIVGRVSMDSATVDISAL 330
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 517056602 331 PEGALtfGSLVEVLGRH-QTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:smart01005 80 PDVKV--GDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
19-377 |
3.32e-145 |
|
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: 415.66 E-value: 3.32e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 19 ATGYLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFV 97
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPgAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREA-GIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 98 LNGLQPGNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIM 177
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 178 SHLASADDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGVLARPGIALYGGAPNAG--EKNPMEP 250
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLdpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEvaADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 251 VVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISAL 330
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517056602 331 PEGALtfGSLVEVLGRH-QTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:COG0787 321 PDVKV--GDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
22-377 |
3.37e-119 |
|
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: 349.87 E-value: 3.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 22 YLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFVLNG 100
Cdd:cd00430 3 WAEIDLDALRHNLRVIRRLLGPgTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREA-GITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 101 LQPGNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHL 180
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 181 ASADDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGVLARPGIALYGGAPNAGEKNPME--PVVS 253
Cdd:cd00430 162 ATADEPDKAYTRRQLERFLEALAELEEAGIppplkHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGlkPVMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 254 LDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEg 333
Cdd:cd00430 242 LKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIPD- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517056602 334 aLTFGSLVEVLGRH----QTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:cd00430 321 -VKVGDEVVLFGRQgdeeITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
24-377 |
8.67e-106 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 315.58 E-value: 8.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 24 TIDLAALGRNYRKLVSMLGPV-RAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRpALAQDAQVFVLNGLQ 102
Cdd:PRK00053 7 EIDLDALRHNLRQIRKHAPPKsKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELR-EAGITAPILILGGFF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 103 PGNEI-ACAEMGIVPVLNSLAQWRQWSAAAriLKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLA 181
Cdd:PRK00053 86 PAEDLpLIIAYNLTTAVHSLEQLEALEKAE--LGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFSHFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 182 SADDMDSEQNGEQFAEMSRIADEFPGFDI---SFANSGGVFLGEAYYGVLARPGIALYGGAP---NAGEKNPMEPVVSLD 255
Cdd:PRK00053 164 TADEPDNSYTEQQLNRFEAALAGLPGKGKplrHLANSAAILRWPDLHFDWVRPGIALYGLSPsgePLGLDFGLKPAMTLK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 256 VAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEgaL 335
Cdd:PRK00053 244 SSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQ--D 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517056602 336 TFGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:PRK00053 322 KVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
24-377 |
1.43e-81 |
|
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: 253.19 E-value: 1.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 24 TIDLAALGRNYRKLVSMLGPVRAGAVVKADAYGLGAERVARTLygEGCRHFFVAQFVEAVRLRpALAQDAQVFVLNGLQP 103
Cdd:cd06827 5 TIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKAL--ADADGFAVACIEEALALR-EAGITKPILLLEGFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIA-CAEMGIVPVLNSLAQWrQWSAAARiLKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLAS 182
Cdd:cd06827 82 ADELPlAAEYNLWTVVHSEEQL-EWLEQAA-LSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 183 ADDMDSEQNGEQFAEMSRIADEFPGfDISFANSGGVFLGEAYYGVLARPGIALYGGAP---NAGEKNPMEPVVSLDVAVV 259
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPG-PRSLANSAAILAWPEAHGDWVRPGIMLYGASPfadKSGADLGLKPVMTLSSEII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 260 QTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEGALtfGS 339
Cdd:cd06827 239 AVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKV--GD 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 517056602 340 LVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:cd06827 317 PVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
25-376 |
6.83e-72 |
|
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: 228.78 E-value: 6.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 25 IDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFVLNGLQP 103
Cdd:TIGR00492 7 IDLAALKHNLSAIRNHIGPkSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKA-GITAPILLLGGFFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNV-EILFIMSHLAS 182
Cdd:TIGR00492 86 EDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFlELEGIFSHFAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 183 ADDMDSEQNGEQFAEMSRIADEFPGFDISF-----ANSGGVFLGEAYYGVLARPGIALYGGAPNAG--EKNP--MEPVVS 253
Cdd:TIGR00492 166 ADEPKTGTTQKQIERFNSFLEGLKQQNIEPpfrhiANSAAILNWPESHFDMVRPGIILYGLYPSADmsDGAPfgLKPVLS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 254 LDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEG 333
Cdd:TIGR00492 246 LTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPDLQD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 517056602 334 ALtfGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:TIGR00492 326 KT--GDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
25-240 |
2.90e-61 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 196.29 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 25 IDLAALGRNYRKLVSMLGPV-RAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPALAqDAQVFVLNGLQP 103
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGaKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGI-TAPILVLGGFPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIACAEMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLASA 183
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056602 184 DDMDSEQNGEQFAEMSRIADEFPGFDI-----SFANSGGVFLGEAYYGvLARPGIALYGGAP 240
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEAAGLrppvvHLANSAAILLHPLHFD-MVRPGIALYGLSP 220
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
25-376 |
7.75e-59 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 194.56 E-value: 7.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 25 IDLAALGRNYRkLVSMLGP-VRAGAVVKADAYGLGAERVARTLygEGCRHFFVAQFVEAVRLRPAlAQDAQVFVLNGLQP 103
Cdd:PRK03646 8 LDLQALKQNLS-IVREAAPgARVWSVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRER-GWKGPILMLEGFFH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 104 GNEIAC-AEMGIVPVLNSLAQWRQWSAAAriLKRCLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEILFIMSHLAS 182
Cdd:PRK03646 84 AQDLELyDQHRLTTCVHSNWQLKALQNAR--LKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 183 ADDMDSeqNGEQfaeMSRIADEFPGFD--ISFANSGGVFLGEAYYGVLARPGIALYGGAPnAGEKNP-----MEPVVSLD 255
Cdd:PRK03646 162 ADHPDG--ISEA---MARIEQAAEGLEceRSLSNSAATLWHPQAHFDWVRPGIILYGASP-SGQWRDiantgLRPVMTLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 256 VAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISALPEGAL 335
Cdd:PRK03646 236 SEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 517056602 336 tfGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:PRK03646 316 --GTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
23-376 |
7.56e-57 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 198.64 E-value: 7.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 23 LTIDLAALGRN---YRklvSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPAlAQDAQVFVL 98
Cdd:PRK11930 462 LEINLNAIVHNlnyYR---SKLKPeTKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKA-GITLPIMVM 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 99 NGLQpgNEIACA-EMGIVPVLNSLAQWRQWSAAARilKR---CLPAVLQFDTGMSRLGFPREERAELAAALRDGTNVEIL 174
Cdd:PRK11930 538 NPEP--TSFDTIiDYKLEPEIYSFRLLDAFIKAAQ--KKgitGYPIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKVR 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 175 FIMSHLASADDMD----SEQNGEQFAEMS-RIADEFPGFDIS-FANSGGV--FLGEAYYGVlaRPGIALYGGAPNAGEKN 246
Cdd:PRK11930 614 SVFSHLAGSDDPDhddfTRQQIELFDEGSeELQEALGYKPIRhILNSAGIerFPDYQYDMV--RLGIGLYGVSASGAGQQ 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 247 PMEPVVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSD-CGAVYFKGIRLPIVGRVSMDSATV 325
Cdd:PRK11930 692 ALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNgVGYVLVNGQKAPIVGNICMDMCMI 771
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 517056602 326 DISALP--EgaltfGSLVEVLGRHQTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:PRK11930 772 DVTDIDakE-----GDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
22-377 |
5.28e-53 |
|
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: 179.86 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 22 YLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVRLRPALAQdAQVFVLNG 100
Cdd:cd06825 3 WLEIDLSALEHNVKEIKRLLPStCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIK-GEILILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 101 LQPGNEIACAEMGIVPVLNSLAQWRQWSAaariLKRCLPAVLQFDTGMSRLGFPREERAELAAALR-DGTNVEILFimSH 179
Cdd:cd06825 82 TPPVRAKELKKYSLTQTLISEAYAEELSK----YAVNIKVHLKVDTGMHRLGESPEDIDSILAIYRlKNLKVSGIF--SH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 180 LASADDMDSEQNG---EQFAEMSRIADEFPGFDISFansgGVFLGEAYYGVL---------ARPGIALYG--GAPNAGEK 245
Cdd:cd06825 156 LCVSDSLDEDDIAftkHQIACFDQVLADLKARGIEV----GKIHIQSSYGILnypdlkydyVRPGILLYGvlSDPNDPTK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 246 NPM--EPVVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGA-VYFKGIRLPIVGRVSMDS 322
Cdd:cd06825 232 LGLdlRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQKAyVLINGKRAPIIGNICMDQ 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 517056602 323 ATVDISALPEgaLTFGSLVEVLGRHQ----TLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:cd06825 312 LMVDVTDIPE--VKEGDTATLIGQDGdeelSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
251-376 |
1.06e-50 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 166.00 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 251 VVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVSMDSATVDISAL 330
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 517056602 331 PEGALtfGSLVEVLGR----HQTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:pfam00842 81 PEVKV--GDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
251-376 |
4.41e-49 |
|
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: 161.47 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 251 VVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDcGAVYFKGIRLPIVGRVSMDSATVDISAL 330
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 517056602 331 PEGALtfGSLVEVLGRH-QTLEDIARDAGTISYEILTGLGDRYHRQY 376
Cdd:smart01005 80 PDVKV--GDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
6-377 |
1.38e-43 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 155.94 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 6 LASRTRIATTAQGATGYLTIDLAALGRNYRKLVSML-GPVRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEAVR 84
Cdd:PRK13340 26 LSDNSANAEQIQPRNAWLEISPGAFRHNIKTLRSLLaNKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 85 LRpALAQDAQVFVLNGLQPGnEIACA-EMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDT-GMSRLGF-PREER-AE 160
Cdd:PRK13340 106 VR-ELGFTGQLLRVRSASPA-EIEQAlRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLdMSTARgKW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 161 LAAALRDGTNVEILFIMSHLASADDMDSEQNGEQFAEMSRIADEFPGFD-----ISFANSGGVF-LGEAYYGvLARPGIA 234
Cdd:PRK13340 184 EALRIATLPSLGIVGIMTHFPNEDEDEVRWKLAQFKEQTAWLIGEAGLKrekitLHVANSYATLnVPEAHLD-MVRPGGI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 235 LYGGAPNAgeKNPMEPVVSLD--VAVVQTrsVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRL 312
Cdd:PRK13340 263 LYGDRHPA--NTEYKRIMTFKsrIASVNT--LPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRA 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517056602 313 PIVGRVSMDSATVDISALPEGALtfGSLVEVLGRHQ----TLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:PRK13340 339 PVVGRVSMNTLMVDVTDIPNVKP--GDEVVLFGKQGnaeiTVDEVEEASGTIFPELYTAWGRTNPRIYV 405
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
20-377 |
1.01e-33 |
|
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: 128.23 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 20 TGYLTIDLAALGRNYRKLVSMLGP-VRAGAVVKADAYGLGAERVARTLYGEGCRHFFVAQFVEA--VR--------LRPA 88
Cdd:cd06826 1 NAWLEISTGAFENNIKLLKKLLGGnTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEArvVReagftgkiLRVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 89 LAQDAQVfvLNGLQpgneiacaeMGIVPVLNSLAQWRQWSAAARILKRCLPAVLQFDT-GMSRLGFPREERAELAAALR- 166
Cdd:cd06826 81 TATPSEI--EDALA---------YNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLELSTAQGKEDAVAi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 167 -DGTNVEILFIMSHLASADDMDSEQNGEQFAEMSRIADEFPGFD-----ISFANS-GGVFLGEAYYGvLARPGIALYGGA 239
Cdd:cd06826 150 aTLPNLKIVGIMTHFPVEDEDDVRAKLARFNEDTAWLISNAKLKrekitLHAANSfATLNVPEAHLD-MVRPGGILYGDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 240 PNAGEknpMEPVVSLDVAVVQTRSVPAGAKVGYGGAHVTQRETRLATIAAGYADGLPRSLSDCGAVYFKGIRLPIVGRVS 319
Cdd:cd06826 229 PPSPE---YKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVS 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056602 320 MDSATVDISALPEGALtfGSLVEVLGRHQ----TLEDIARDAGTISYEILTGLGDRYHRQYR 377
Cdd:cd06826 306 MNTVMVDVTDIPGVKA--GDEVVLFGKQGgaeiTAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
32-233 |
1.00e-13 |
|
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: 69.66 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 32 RNYRKLVSMLGP-VRAGAVVKADAyglgAERVARTLYGEGCRhFFVAQFVEAVRLRPALAQDAQVFVLNGLQPGNEIA-C 109
Cdd:cd06808 3 HNYRRLREAAPAgITLFAVVKANA----NPEVARTLAALGTG-FDVASLGEALLLRAAGIPPEPILFLGPCKQVSELEdA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056602 110 AEMGIVPV-LNSLAQWRQWSAAARILKRCLPAVLQFDTG--MSRLGFPREERAELAAALRDGTNVEILFIMSHLASADDM 186
Cdd:cd06808 78 AEQGVIVVtVDSLEELEKLEEAALKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSADED 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517056602 187 DSEQNgEQFAEMSRIADEFP--GFDISFANSGGVFLGEAYYG------VLARPGI 233
Cdd:cd06808 158 YSPFV-EALSRFVAALDQLGelGIDLEQLSIGGSFAILYLQElplgtfIIVEPGR 211
|
|
| |
