|
Name |
Accession |
Description |
Interval |
E-value |
| alr |
PRK00053 |
alanine racemase; Reviewed |
35-403 |
1.63e-179 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 503.94 E-value: 1.63e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 35 LAEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAW- 112
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 113 LHPPGIDFGPALLADVQVAVSSLRQLDELLHAvrRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRG 192
Cdd:PRK00053 83 GFFPAEDLPLIIAYNLTTAVHSLEQLEALEKA--ELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLAC---PNVRLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 193 LMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVrfEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVP--ALGDMG 270
Cdd:PRK00053 158 IFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGK--PLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGepLGLDFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 271 LVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDL 350
Cdd:PRK00053 236 LKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489513204 351 GPGPlDVAEGDEAILFGPGIrgepTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:PRK00053 316 GPDP-QDKVGDEVTLWGEAL----TAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
36-405 |
3.96e-166 |
|
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: 470.36 E-value: 3.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAGpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRGLM 194
Cdd:COG0787 84 VPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAAL---PGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 195 SHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALG-DMGLVP 273
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAaDLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489513204 354 PlDVAEGDEAILFGPgirGEPTAQDWADLVGTIHYEVVTSPRGRITRTYREA 405
Cdd:COG0787 321 P-DVKVGDEVVLFGE---QGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
36-403 |
3.01e-161 |
|
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: 457.73 E-value: 3.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGpGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRGLM 194
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKAL---PGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 195 SHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPAL-GDMGLVP 273
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVkSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489513204 354 PlDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:cd00430 319 P-DVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
36-402 |
2.08e-110 |
|
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: 328.54 E-value: 2.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:TIGR00492 3 ATVEIDLAALKHNLSAIRNHIGpKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGP---AQFPAMLTALRQAMaedavRLR 191
Cdd:TIGR00492 83 FFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPdeaALFVQKLRQLKKFL-----ELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 192 GLMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALGD--- 268
Cdd:TIGR00492 158 GIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDgap 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 269 MGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMV 348
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489513204 349 DLGPGPlDVAEGDEAILFGPGIrgepTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:TIGR00492 318 DLGPDL-QDKTGDEVILWGEEI----SIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
40-262 |
4.89e-82 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 250.60 E-value: 4.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLREHAGH-AQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGI 118
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 119 DFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRqamAEDAVRLRGLMSHMV 198
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLA---ALPGLRLEGLMTHFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489513204 199 YADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLtFDLVRPGIAVYGLSP 262
Cdd:pfam01168 158 CADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPLH-FDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
274-402 |
4.98e-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: 185.35 E-value: 4.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRlEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489513204 354 PlDVAEGDEAILFGPgirGEPTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:smart01005 80 P-DVKVGDEVVLFGP---QEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| alr |
PRK00053 |
alanine racemase; Reviewed |
35-403 |
1.63e-179 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 503.94 E-value: 1.63e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 35 LAEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAW- 112
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 113 LHPPGIDFGPALLADVQVAVSSLRQLDELLHAvrRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRG 192
Cdd:PRK00053 83 GFFPAEDLPLIIAYNLTTAVHSLEQLEALEKA--ELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLAC---PNVRLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 193 LMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVrfEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVP--ALGDMG 270
Cdd:PRK00053 158 IFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGK--PLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGepLGLDFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 271 LVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDL 350
Cdd:PRK00053 236 LKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489513204 351 GPGPlDVAEGDEAILFGPGIrgepTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:PRK00053 316 GPDP-QDKVGDEVTLWGEAL----TAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
36-405 |
3.96e-166 |
|
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: 470.36 E-value: 3.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAGpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRGLM 194
Cdd:COG0787 84 VPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAAL---PGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 195 SHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALG-DMGLVP 273
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAaDLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489513204 354 PlDVAEGDEAILFGPgirGEPTAQDWADLVGTIHYEVVTSPRGRITRTYREA 405
Cdd:COG0787 321 P-DVKVGDEVVLFGE---QGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
36-403 |
3.01e-161 |
|
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: 457.73 E-value: 3.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGpGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAmaeDAVRLRGLM 194
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKAL---PGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 195 SHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPAL-GDMGLVP 273
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVkSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489513204 354 PlDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:cd00430 319 P-DVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
36-402 |
2.08e-110 |
|
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: 328.54 E-value: 2.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLH 114
Cdd:TIGR00492 3 ATVEIDLAALKHNLSAIRNHIGpKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 115 PPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGP---AQFPAMLTALRQAMaedavRLR 191
Cdd:TIGR00492 83 FFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPdeaALFVQKLRQLKKFL-----ELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 192 GLMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALGD--- 268
Cdd:TIGR00492 158 GIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDgap 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 269 MGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMV 348
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489513204 349 DLGPGPlDVAEGDEAILFGPGIrgepTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:TIGR00492 318 DLGPDL-QDKTGDEVILWGEEI----SIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
38-403 |
1.07e-88 |
|
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: 272.45 E-value: 1.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 38 AMVDLGAIEHNVRVLREHAGHAQLMAVVKADGYGHGATRVAQtALgAGAAELGVATVDEALALRADGITAPVLawlhppg 117
Cdd:cd06827 4 ATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAK-AL-ADADGFAVACIEEALALREAGITKPIL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 118 idfgpaLL--------------ADVQVAVSSLRQLDELLHAvrRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAM 183
Cdd:cd06827 75 ------LLegffsadelplaaeYNLWTVVHSEEQLEWLEQA--ALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 184 AEDAVrlrGLMSHMVYADKPDDSINDVQAQRFTAFLaqareQGVRFEVAhLSNSSATMARPDLTFDLVRPGIAVYGLSPV 263
Cdd:cd06827 147 NVASI---VLMTHFACADEPDSPGTAKQLAIFEQAT-----AGLPGPRS-LANSAAILAWPEAHGDWVRPGIMLYGASPF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 264 P--ALGDMGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRI 341
Cdd:cd06827 218 AdkSGADLGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489513204 342 CMDQFMVDLGPGPlDVAEGDEAILFGPGIrgepTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:cd06827 298 SMDMLTVDLTDLP-EAKVGDPVELWGKGL----PVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
40-262 |
4.89e-82 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 250.60 E-value: 4.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLREHAGH-AQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGI 118
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPgAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 119 DFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRqamAEDAVRLRGLMSHMV 198
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLA---ALPGLRLEGLMTHFA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489513204 199 YADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLtFDLVRPGIAVYGLSP 262
Cdd:pfam01168 158 CADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPLH-FDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
40-402 |
3.43e-76 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 252.19 E-value: 3.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLREHAG-HAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAwLHPPGI 118
Cdd:PRK11930 464 INLNAIVHNLNYYRSKLKpETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMV-MNPEPT 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 119 DFGPALLADVQVAVSSLRQLDELLHAVRRTGRTAT-VTVKVDTGLNRNGVGPAQFPAMLTALRQamaEDAVRLRGLMSHM 197
Cdd:PRK11930 543 SFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYpIHIKIDTGMHRLGFEPEDIPELARRLKK---QPALKVRSVFSHL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 198 VYADKPD-DSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPAlGDMGLVPAMT 276
Cdd:PRK11930 620 AGSDDPDhDDFTRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGA-GQQALRNVST 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 277 VKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLG-GRLEVLINGRRCPGVGRICMDQFMVDLgpGPL 355
Cdd:PRK11930 699 LKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGnGVGYVLVNGQKAPIVGNICMDMCMIDV--TDI 776
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489513204 356 DVAEGDEAILFGPgirgEPTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:PRK11930 777 DAKEGDEVIIFGE----ELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
40-403 |
1.16e-72 |
|
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: 231.86 E-value: 1.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLRE--HAGhAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAP--VLAWLHP 115
Cdd:cd06825 6 IDLSALEHNVKEIKRllPST-CKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEilILGYTPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 116 PGIDfgpaLL--ADVQVAVSSLR---QLDELLHAVRrtgrtatVTVKVDTGLNRNGVGPAQfpamLTALRQAMAEDAVRL 190
Cdd:cd06825 85 VRAK----ELkkYSLTQTLISEAyaeELSKYAVNIK-------VHLKVDTGMHRLGESPED----IDSILAIYRLKNLKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 191 RGLMSHMVYADKPD-DSINDVQAQ--RFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGL--SPVPA 265
Cdd:cd06825 150 SGIFSHLCVSDSLDeDDIAFTKHQiaCFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVlsDPNDP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 266 LG-DMGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLG-GRLEVLINGRRCPGVGRICM 343
Cdd:cd06825 230 TKlGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSnQKAYVLINGKRAPIIGNICM 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 344 DQFMVDLGPGPlDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTYR 403
Cdd:cd06825 310 DQLMVDVTDIP-EVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
40-392 |
2.24e-66 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 216.80 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLREHA-GHAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGI 118
Cdd:PRK13340 45 ISPGAFRHNIKTLRSLLaNKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRSASPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 119 DFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDT-GLNRNGVGPAQFPAMLTALRQAmAEDAVRLRGLMSHM 197
Cdd:PRK13340 125 EIEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEALRIA-TLPSLGIVGIMTHF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 198 VYADKpdDSInDVQAQRF---TAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGlSPVPAlgDMGLVPA 274
Cdd:PRK13340 204 PNEDE--DEV-RWKLAQFkeqTAWLIGEAGLKREKITLHVANSYATLNVPEAHLDMVRPGGILYG-DRHPA--NTEYKRI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 275 MTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPGP 354
Cdd:PRK13340 278 MTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLMVDVTDIP 357
|
330 340 350
....*....|....*....|....*....|....*...
gi 489513204 355 lDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVT 392
Cdd:PRK13340 358 -NVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYT 394
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
274-402 |
1.08e-62 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 197.59 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489513204 354 PlDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:pfam00842 81 P-EVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
36-402 |
2.86e-62 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 204.58 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 36 AEAMVDLGAIEHNVRVLREHAGHAQLMAVVKADGYGHGATRVAQtALGAgAAELGVATVDEALALRADGITAPVL---AW 112
Cdd:PRK03646 4 IQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWS-ALGA-TDGFAVLNLEEAITLRERGWKGPILmleGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 113 LHPPgiDFGPALLADVQVAVSSLRQLDELLHAvrRTGRTATVTVKVDTGLNRNGVGPAQFPamlTALRQAMAEDAVRLRG 192
Cdd:PRK03646 82 FHAQ--DLELYDQHRLTTCVHSNWQLKALQNA--RLKAPLDIYLKVNSGMNRLGFQPERVQ---TVWQQLRAMGNVGEMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 193 LMSHMVYADKPDDSinDVQAQRFtaflAQAReQGVRFEVAhLSNSSATMARPDLTFDLVRPGIAVYGLSP---VPALGDM 269
Cdd:PRK03646 155 LMSHFARADHPDGI--SEAMARI----EQAA-EGLECERS-LSNSAATLWHPQAHFDWVRPGIILYGASPsgqWRDIANT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 270 GLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVD 349
Cdd:PRK03646 227 GLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVD 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489513204 350 LGPGPlDVAEGDEAILFGPGIRgeptAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:PRK03646 307 LTPCP-QAGIGTPVELWGKEIK----IDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
274-402 |
4.98e-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: 185.35 E-value: 4.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 274 AMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRlEVLINGRRCPGVGRICMDQFMVDLGPG 353
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNG-PVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489513204 354 PlDVAEGDEAILFGPgirGEPTAQDWADLVGTIHYEVVTSPRGRITRTY 402
Cdd:smart01005 80 P-DVKVGDEVVLFGP---QEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
40-392 |
1.20e-54 |
|
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: 184.85 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLREHA-GHAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGI 118
Cdd:cd06826 6 ISTGAFENNIKLLKKLLgGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTATPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 119 DFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDT-GLNRNGVGPAQFPAMLTALRqaMAED-AVRLRGLMSH 196
Cdd:cd06826 86 EIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLELSTAQGKEDAVA--IATLpNLKIVGIMTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 197 MVYADKPDDSINDVQAQRFTAFLAQA----REQgvrfEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPvpalGDMGLV 272
Cdd:cd06826 164 FPVEDEDDVRAKLARFNEDTAWLISNaklkREK----ITLHAANSFATLNVPEAHLDMVRPGGILYGDTP----PSPEYK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 273 PAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGP 352
Cdd:cd06826 236 RIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVTD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489513204 353 GPlDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVT 392
Cdd:cd06826 316 IP-GVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYT 354
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
45-255 |
5.18e-48 |
|
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: 162.87 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 45 IEHNVRVLREHAG-HAQLMAVVKAdgygHGATRVAQTALGAGAaELGVATVDEALALRADGI-TAPVLAWLHPP-GIDFG 121
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKA----NANPEVARTLAALGT-GFDVASLGEALLLRAAGIpPEPILFLGPCKqVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 122 PAL-LADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTG--LNRNGVGPAQFPAMLTALRQAmaeDAVRLRGLMSHMV 198
Cdd:cd06808 76 DAAeQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKEL---PHLRLVGLHTHFG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 199 YADKpDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMA---RPDLTFDLVRPGI 255
Cdd:cd06808 153 SADE-DYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILYlqeLPLGTFIIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
30-281 |
8.24e-16 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 78.25 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 30 QTPGLLaeamVDLGAIEHNVRVLREHAGHA--QLMAVVKAdgygHGATRVAQTALGAGAAELGVATVDEALALRADGITA 107
Cdd:COG3616 7 DTPALV----LDLDALERNIARMAARAAAHgvRLRPHGKT----HKSPELARRQLAAGAWGITVATLAEAEVLAAAGVDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 108 PVLAwlHPPgidFGPALLA----------DVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQfpAMLT 177
Cdd:COG3616 79 ILLA--YPL---VGPAKLArlaalaragaRLTVLVDSVEQAEALAAAAAAAGRPLRVLVELDVGGGRTGVRPPE--AALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 178 ALRQAMAEDAVRLRGLMSH--MVYADKPDDSINDVqAQRFTAFLAQARE--QGVRFEVAHLSN-SSATM--ARPDLTFDL 250
Cdd:COG3616 152 LARAIAASPGLRLAGLMTYegHIYGADDAEERRAA-AREELARLAAAAEalRAAGLPCPIVSGgGTPTFdfVADLPGVTE 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 489513204 251 VRPGIAVYGlspvPAL-----GDMGLVPAMTVKCAV 281
Cdd:COG3616 231 LRPGSYVFH----DAGyyrygVCFPFDPALSVLATV 262
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
44-283 |
8.10e-13 |
|
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: 69.03 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 44 AIEHNVRVLREHAGHAQ--LMAVVKAdgygHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAW--LHPPGID 119
Cdd:cd07376 1 ALEANISRMAARARASGvrLRPHVKT----HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYplVGPAAIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 120 FGPALLAD---VQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQfPAMLTALRQAMAEDAVRLRGLMSH 196
Cdd:cd07376 77 RLAGLLRQeaeFHVLVDSPEALAALAAFAAAHGVRLRVMLEVDVGGHRSGVRPEE-AAALALADAVQASPGLRLAGVMAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 197 MVYADKPDDSINDVQA-----QRFTAFLAQArEQGVRFEVAHLSNS-SATMARPDLTFDLVRPGIAVYGLSPVPALGDMG 270
Cdd:cd07376 156 EGHIYGAGGAREGAQArdqavAAVRAAAAAA-ERGLACPTVSGGGTpTYQLTAGDRAVTELRAGSYVFMDTGFDTLGACA 234
|
250
....*....|...
gi 489513204 271 LVPAMTVKCAVAL 283
Cdd:cd07376 235 QRPAAFRVTTVIS 247
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
72-259 |
5.48e-12 |
|
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: 66.57 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 72 HGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAW--LHPPGIDFGPALL--ADVQVAVSSLRQLDELLHAVRR 147
Cdd:cd06820 38 HKSPEIARLQLAAGAIGITVATVGEAEVMADAGLSDIFIAYpiVGRQKLERLRALAerVTLSVGVDSAEVARGLAEVAEG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 148 TGRTATVTVKVDTGLNRNGVG-PAQFPAMltaLRQAMAEDAVRLRGLMSHMVYADKPDDSINDV--QAQRFTAFLAQARE 224
Cdd:cd06820 118 AGRPLEVLVEVDSGMNRCGVQtPEDAVAL---ARAIASAPGLRFRGIFTYPGHSYAPGALEEAAadEAEALLAAAGILEE 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 489513204 225 QGVRFEVAHlSNSSATMARPDLTFDL--VRPGIAVYG 259
Cdd:cd06820 195 AGLEPPVVS-GGSTPTLWRSHEVPGIteIRPGTYIFN 230
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
30-194 |
1.83e-10 |
|
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: 61.85 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 30 QTPGLLaeamVDLGAIEHNVRVLREHAGHAQLMavVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGI---- 105
Cdd:cd06819 6 DTPALV----LDLDALERNIKRMAAFAKAHGVR--LRPHAKTHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIrdil 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 106 -TAPVLAwlhPPGIDFGPALL--ADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPaqFPAMLTALRQA 182
Cdd:cd06819 80 iTNEVVG---PAKIARLAALArrAPLIVCVDHPDNVRALAAAAVEAGVRLDVLVEIDVGQGRCGVPP--GEAALALARTI 154
|
170
....*....|..
gi 489513204 183 MAEDAVRLRGLM 194
Cdd:cd06819 155 AALPGLRFAGLQ 166
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
31-193 |
5.00e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143495 [Multi-domain] Cd Length: 361 Bit Score: 48.06 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 31 TPGLlaeaMVDLGAIEHNVRVLREHAGHAQ-LMAVVKAdgygHGATRVAQTALGAGAAELGVATVDEALALRADGITAPV 109
Cdd:cd06821 9 SPAL----AVYPDRIEENIRRMIRMAGDPQrLRPHVKT----HKMAEIVRLQLEAGITKFKCATIAEAEMLAEAGAPDVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 110 LAW-LHPPGIDFGPALLA-----DVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQfpAMLTALRQAM 183
Cdd:cd06821 81 LAYpLVGPNIERFLELAKkypgtRFSALVDDLEAAEALSAAAGSAGLTLSVLLDVNTGMNRTGIAPGE--DAEELYRAIA 158
|
170
....*....|
gi 489513204 184 AEDAVRLRGL 193
Cdd:cd06821 159 TLPGLVLAGL 168
|
|
| PLPDE_III_DSD_D-TA_like_1 |
cd06812 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
30-261 |
7.83e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143487 [Multi-domain] Cd Length: 374 Bit Score: 41.18 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 30 QTPGLLaeamVDLGAIEHNVRVLREHAghAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPV 109
Cdd:cd06812 5 DTPFLL----LDEARMDRNIARLRQRL--SRLGVRLRPHLKTAKSLEVARRLLAAGASPATVSTLKEAEAFAEAGYRDIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 110 LA-WLHPPGIDFGPALLA---DVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQfpAMLTALRQAMAE 185
Cdd:cd06812 79 YAvGIAPAKLPRVLALRRqgvNLTILLDSVEQAQAVAAFSRQHGVRFPVLIEIDCDGHRGGIAPDS--DALLEIARILHD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 186 DAVRLRGLMSHM--VYA-DKPDDSINDVQAQRFTAFLA--QAREQGVRFEVAHLSNSSATMARPDLT------------F 248
Cdd:cd06812 157 GGAELRGVLTHAgeSYAcRTPEALAAAAEQERAAAVRAaeRLRAAGLPCPVVSVGSTPTAHFAEDLTgvtevragvyvfF 236
|
250
....*....|...
gi 489513204 249 DLVRPGIAVYGLS 261
Cdd:cd06812 237 DLVMAGIGVCGLD 249
|
|
| PLPDE_III_yhfX_like |
cd06811 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ... |
30-275 |
9.27e-04 |
|
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: 41.11 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 30 QTPGLLAEA--------------MVDLGAIEHNVRVLREHAG--HAQLMAVVKADGyghgatR---VAQTALGAGAAelG 90
Cdd:cd06811 9 RNPALIEAAltlhqsgaippdtyVIDLDQIEENARLLAETAEkyGIELYFMTKQFG------RnpfLARALLEAGIP--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 91 VATVD--EALALRADGITAPVLAWLHPPGIDFGPALLA---DVqVAVSSLRQLDELLHAVRRTGRTATVTVKVDTglNRN 165
Cdd:cd06811 81 AVAVDfkEARALHEAGLPLGHVGHLVQIPRHQVPAVLAmrpEV-ITVYSLEKAREISDAAVELGRVQDVLLRVYG--DED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 166 GVGPAQ---FP-AMLTALRQA-MAEDAVRLRGLMSH--MVYadkpDDSINDVQAQRFTAFLAQAREQ----GVrfEVAHL 234
Cdd:cd06811 158 TLYPGQeggFPlEELPAVLAAiKALPGIRIAGLTSFpcFLY----DEEQGDIAPTPNLFTLLKAKELlekrGI--EILQL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489513204 235 SNSSATMARpdlTFDLVR--------PGIAVYGLSPVPALGDMGLVPAM 275
Cdd:cd06811 232 NAPSATSCA---TLPLLAeygvthgePGHALTGTTPLHAVGDQPEKPAM 277
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
40-193 |
1.48e-03 |
|
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: 40.22 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 40 VDLGAIEHNVRVLRE--HAGHAQLMAVVKAdgyGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLaWLHPPG 117
Cdd:cd06815 6 INLSKIRHNAKVLVElcKSRGIEVTGVTKV---VCGDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKM-LLRIPM 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513204 118 IDFGPAL--LADVQVaVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFpamLTALRQAMAEDAVRLRGL 193
Cdd:cd06815 82 LSEVEDVvkYADISL-NSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDL---LDFVEEILKLPGIELVGI 155
|
|
| PLPDE_III_DSD_D-TA_like_3 |
cd06814 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
135-228 |
1.92e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 3; This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. DSD and D-TA are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on their similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143489 [Multi-domain] Cd Length: 379 Bit Score: 40.01 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513204 135 LRQLDELLHAVRRTGRTAtvtVKVDTGLNRNGVG-PAQFPAMLTALRqamAEDAVRLRGLM------SHMVYADKPDDSI 207
Cdd:cd06814 120 LAQYRALARSLGLTLRIN---LELDVGLHRGGFAdPQTLPKALTAID---APPRLRFSGLMgyephvAKLPGLISPAKAR 193
|
90 100
....*....|....*....|.
gi 489513204 208 NDVQAqRFTAFLAQAREQGVR 228
Cdd:cd06814 194 AAAMA-RYQAFVALARAHLGA 213
|
|
| |
