|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-331 |
2.08e-76 |
|
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: 239.62 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 2 TATWSVNKKIFLQNAITVKN----NQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 78 AV--YEFDLVREHQIHMTLPSLTYYYNHKNDLA----GIHVHLEFENLLHRSGFkDLNEIKEVLKDHHHNQNAKmiISGL 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAARrlgkPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLE--VEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 152 WTHFGYADEFDVSDYNVERSQWMEIVEALLSEGYQFDLIHAQNSASfyregqILL---PHHTHARVGIALYGSRPYSSL- 227
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAA------ILRypeAHFDMVRPGIALYGLSPSPEVa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 228 NQHDIVQSLTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPIR-ALMMSH 305
Cdd:COG0787 234 ADLGLKPVMTLKARIIQVKTVPAGETVGYGRTY-TAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQ 312
|
330 340
....*....|....*....|....*....
gi 1332406780 306 MFVEVDG--NVHAQDEVILY-NNDIRIDE 331
Cdd:COG0787 313 IMVDVTDipDVKVGDEVVLFgEQGITADE 341
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
19-331 |
8.54e-65 |
|
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: 209.66 E-value: 8.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 19 VKNNQPLMAVVKNNAY-HYDLEFAVTqFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY--EFDLVREHQIHMTLP 95
Cdd:cd00430 22 LGPGTKIMAVVKADAYgHGAVEVAKA-LEEAGADYFAVATLEEALELREAGITAPILVLGGTPpeEAEEAIEYDLTPTVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 96 SLTY--YYNHKNDLAG--IHVHLEFENLLHRSGFKDlNEIKEVLKDHHHNQNakMIISGLWTHFGYADEFDVSDYNVERS 171
Cdd:cd00430 101 SLEQaeALSAAAARLGktLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPG--LELEGVFTHFATADEPDKAYTRRQLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 172 QWMEIVEALLSEGYQFDLIHAQNSASFyregqILLP--HHTHARVGIALYGSRP-YSSLNQHDIVQSLTVKAHVIQVREV 248
Cdd:cd00430 178 RFLEALAELEEAGIPPPLKHLANSAAI-----LRFPeaHFDMVRPGIALYGLYPsPEVKSPLGLKPVMSLKARVVQVKTV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 249 QAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPIR-ALMMSHMFVEVDGNVHAQ--DEVILYN 324
Cdd:cd00430 253 PAGEGVSYGRTY-TAPRPTRIATLPVGYADGYPRALSnKGEVLIRGKRAPIVgRVCMDQTMVDVTDIPDVKvgDEVVLFG 331
|
330
....*....|.
gi 1332406780 325 ND----IRIDE 331
Cdd:cd00430 332 RQgdeeITAEE 342
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
25-331 |
1.09e-52 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 178.06 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 25 LMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY---EFDLVREHQIHMTLPSLTYY- 100
Cdd:PRK00053 30 LMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpaeDLPLIIAYNLTTAVHSLEQLe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 101 -YNHKNDLAGIHVHLEFENLLHRSGFkDLNEIKEVLKDHHHNQNAKMIisGLWTHFGYADEFDvSDYNVERSQ-WMEIVE 178
Cdd:PRK00053 110 aLEKAELGKPLKVHLKIDTGMHRLGV-RPEEAEAALERLLACPNVRLE--GIFSHFATADEPD-NSYTEQQLNrFEAALA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 179 ALLSEGyqFDLIHAQNSAsfyreGQILLP--HHTHARVGIALYGsrpYSSLNQHDIVQS-----LTVKAHVIQVREVQAG 251
Cdd:PRK00053 186 GLPGKG--KPLRHLANSA-----AILRWPdlHFDWVRPGIALYG---LSPSGEPLGLDFglkpaMTLKSSLIAVRELKAG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 252 DYCGYSFAFeVTKNNTKLAVVDIGYGDGILRT-RAKHEALINGKRYPI--RALMmsHMFVeVDGNVHAQ----DEVILYN 324
Cdd:PRK00053 256 EGVGYGGTF-TAERDTRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIvgRVSM--DQLT-VDLGPDPQdkvgDEVTLWG 331
|
....*..
gi 1332406780 325 NDIRIDE 331
Cdd:PRK00053 332 EALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-331 |
4.15e-40 |
|
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: 145.19 E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 3 ATWSVNKKIFLQNAITVKNNQP----LMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNA 78
Cdd:TIGR00492 3 ATVEIDLAALKHNLSAIRNHIGpkskIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 79 VYEFDL--VREHQIHMTLPSLTYYYNHKNDLA----GIHVHLEFENLLHRSGFK---DLNEIKEVLkdhhhnQNAKMI-I 148
Cdd:TIGR00492 83 FFAEDLkiLAAWDLTTTVHSVEQLQALEEALLkepkRLKVHLKIDTGMNRLGVKpdeAALFVQKLR------QLKKFLeL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 149 SGLWTHFGYADEFDVSDYNVERSQWMEIVEALLSEGYQFDLIHAQNSAsfyreGQILLP--HHTHARVGIALYGSRPYSS 226
Cdd:TIGR00492 157 EGIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSA-----AILNWPesHFDMVRPGIILYGLYPSAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 227 LNQHDIVQ---SLTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRT-RAKHEALINGKRYPIR-AL 301
Cdd:TIGR00492 232 MSDGAPFGlkpVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYPRAlSNGTPVLVNGKRVPIVgRV 310
|
330 340 350
....*....|....*....|....*....|..
gi 1332406780 302 MMSHMFVEVDGNVHAQ--DEVILYNNDIRIDE 331
Cdd:TIGR00492 311 CMDMIMVDLGPDLQDKtgDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
19-223 |
2.55e-38 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 136.20 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 19 VKNNQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY--EFDLVREHQIHMTLPS 96
Cdd:pfam01168 17 AGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpeELALAAEYDLTPTVDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 97 LTY--YYNH--KNDLAGIHVHLEFENLLHRSGFKDlNEIKEVLKDHHHNQNAKmiISGLWTHFGYADEFDVSDYNVERSQ 172
Cdd:pfam01168 97 LEQleALAAaaRRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLR--LEGLMTHFACADEPDDPYTNAQLAR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1332406780 173 WMEIVEALLSEGYQFDLIHAQNSASFYRegqiLLPHHTHARVGIALYGSRP 223
Cdd:pfam01168 174 FREAAAALEAAGLRPPVVHLANSAAILL----HPLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
236-356 |
4.83e-28 |
|
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: 106.00 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 236 LTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRAKHEALINGKRYPIRA-LMMSHMFVEVDG-- 312
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATF-TADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVTDip 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1332406780 313 NVHAQDEVILYNND-IRIDEYTFKGVGANSEQLSAMNHdSLKKEY 356
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP-RVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-331 |
2.08e-76 |
|
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: 239.62 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 2 TATWSVNKKIFLQNAITVKN----NQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 78 AV--YEFDLVREHQIHMTLPSLTYYYNHKNDLA----GIHVHLEFENLLHRSGFkDLNEIKEVLKDHHHNQNAKmiISGL 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAARrlgkPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLE--VEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 152 WTHFGYADEFDVSDYNVERSQWMEIVEALLSEGYQFDLIHAQNSASfyregqILL---PHHTHARVGIALYGSRPYSSL- 227
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAA------ILRypeAHFDMVRPGIALYGLSPSPEVa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 228 NQHDIVQSLTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPIR-ALMMSH 305
Cdd:COG0787 234 ADLGLKPVMTLKARIIQVKTVPAGETVGYGRTY-TAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQ 312
|
330 340
....*....|....*....|....*....
gi 1332406780 306 MFVEVDG--NVHAQDEVILY-NNDIRIDE 331
Cdd:COG0787 313 IMVDVTDipDVKVGDEVVLFgEQGITADE 341
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
19-331 |
8.54e-65 |
|
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: 209.66 E-value: 8.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 19 VKNNQPLMAVVKNNAY-HYDLEFAVTqFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY--EFDLVREHQIHMTLP 95
Cdd:cd00430 22 LGPGTKIMAVVKADAYgHGAVEVAKA-LEEAGADYFAVATLEEALELREAGITAPILVLGGTPpeEAEEAIEYDLTPTVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 96 SLTY--YYNHKNDLAG--IHVHLEFENLLHRSGFKDlNEIKEVLKDHHHNQNakMIISGLWTHFGYADEFDVSDYNVERS 171
Cdd:cd00430 101 SLEQaeALSAAAARLGktLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPG--LELEGVFTHFATADEPDKAYTRRQLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 172 QWMEIVEALLSEGYQFDLIHAQNSASFyregqILLP--HHTHARVGIALYGSRP-YSSLNQHDIVQSLTVKAHVIQVREV 248
Cdd:cd00430 178 RFLEALAELEEAGIPPPLKHLANSAAI-----LRFPeaHFDMVRPGIALYGLYPsPEVKSPLGLKPVMSLKARVVQVKTV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 249 QAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPIR-ALMMSHMFVEVDGNVHAQ--DEVILYN 324
Cdd:cd00430 253 PAGEGVSYGRTY-TAPRPTRIATLPVGYADGYPRALSnKGEVLIRGKRAPIVgRVCMDQTMVDVTDIPDVKvgDEVVLFG 331
|
330
....*....|.
gi 1332406780 325 ND----IRIDE 331
Cdd:cd00430 332 RQgdeeITAEE 342
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
25-331 |
1.09e-52 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 178.06 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 25 LMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY---EFDLVREHQIHMTLPSLTYY- 100
Cdd:PRK00053 30 LMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpaeDLPLIIAYNLTTAVHSLEQLe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 101 -YNHKNDLAGIHVHLEFENLLHRSGFkDLNEIKEVLKDHHHNQNAKMIisGLWTHFGYADEFDvSDYNVERSQ-WMEIVE 178
Cdd:PRK00053 110 aLEKAELGKPLKVHLKIDTGMHRLGV-RPEEAEAALERLLACPNVRLE--GIFSHFATADEPD-NSYTEQQLNrFEAALA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 179 ALLSEGyqFDLIHAQNSAsfyreGQILLP--HHTHARVGIALYGsrpYSSLNQHDIVQS-----LTVKAHVIQVREVQAG 251
Cdd:PRK00053 186 GLPGKG--KPLRHLANSA-----AILRWPdlHFDWVRPGIALYG---LSPSGEPLGLDFglkpaMTLKSSLIAVRELKAG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 252 DYCGYSFAFeVTKNNTKLAVVDIGYGDGILRT-RAKHEALINGKRYPI--RALMmsHMFVeVDGNVHAQ----DEVILYN 324
Cdd:PRK00053 256 EGVGYGGTF-TAERDTRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIvgRVSM--DQLT-VDLGPDPQdkvgDEVTLWG 331
|
....*..
gi 1332406780 325 NDIRIDE 331
Cdd:PRK00053 332 EALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
3-331 |
4.15e-40 |
|
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: 145.19 E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 3 ATWSVNKKIFLQNAITVKNNQP----LMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNA 78
Cdd:TIGR00492 3 ATVEIDLAALKHNLSAIRNHIGpkskIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 79 VYEFDL--VREHQIHMTLPSLTYYYNHKNDLA----GIHVHLEFENLLHRSGFK---DLNEIKEVLkdhhhnQNAKMI-I 148
Cdd:TIGR00492 83 FFAEDLkiLAAWDLTTTVHSVEQLQALEEALLkepkRLKVHLKIDTGMNRLGVKpdeAALFVQKLR------QLKKFLeL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 149 SGLWTHFGYADEFDVSDYNVERSQWMEIVEALLSEGYQFDLIHAQNSAsfyreGQILLP--HHTHARVGIALYGSRPYSS 226
Cdd:TIGR00492 157 EGIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSA-----AILNWPesHFDMVRPGIILYGLYPSAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 227 LNQHDIVQ---SLTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRT-RAKHEALINGKRYPIR-AL 301
Cdd:TIGR00492 232 MSDGAPFGlkpVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYPRAlSNGTPVLVNGKRVPIVgRV 310
|
330 340 350
....*....|....*....|....*....|..
gi 1332406780 302 MMSHMFVEVDGNVHAQ--DEVILYNNDIRIDE 331
Cdd:TIGR00492 311 CMDMIMVDLGPDLQDKtgDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
19-223 |
2.55e-38 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 136.20 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 19 VKNNQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY--EFDLVREHQIHMTLPS 96
Cdd:pfam01168 17 AGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpeELALAAEYDLTPTVDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 97 LTY--YYNH--KNDLAGIHVHLEFENLLHRSGFKDlNEIKEVLKDHHHNQNAKmiISGLWTHFGYADEFDVSDYNVERSQ 172
Cdd:pfam01168 97 LEQleALAAaaRRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLR--LEGLMTHFACADEPDDPYTNAQLAR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1332406780 173 WMEIVEALLSEGYQFDLIHAQNSASFYRegqiLLPHHTHARVGIALYGSRP 223
Cdd:pfam01168 174 FREAAAALEAAGLRPPVVHLANSAAILL----HPLHFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
25-326 |
5.38e-37 |
|
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: 136.71 E-value: 5.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 25 LMAVVKNNAY-HYDLEFAvTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLM--NAVYEFDLVREHQIHMTLPSLTyyY 101
Cdd:cd06825 28 LMAVVKANAYgHGDVEVA-RVLEQIGIDFFAVATIDEGIRLREAGIKGEILILgyTPPVRAKELKKYSLTQTLISEA--Y 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 102 NHK-NDLAG-IHVHLEFENLLHRSGF--KDLNEIKEVLKDHHHNqnakmiISGLWTHFGYADEFDVSDYNVERSQ---WM 174
Cdd:cd06825 105 AEElSKYAVnIKVHLKVDTGMHRLGEspEDIDSILAIYRLKNLK------VSGIFSHLCVSDSLDEDDIAFTKHQiacFD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 175 EIVEALLSEGYQFDLIHAQNSASF--YREgqillPHHTHARVGIALYG--SRPYSSL-NQHDIVQSLTVKAHVIQVREVQ 249
Cdd:cd06825 179 QVLADLKARGIEVGKIHIQSSYGIlnYPD-----LKYDYVRPGILLYGvlSDPNDPTkLGLDLRPVLSLKAKVILVRKVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 250 AGDYCGYSFAFEVTKnNTKLAVVDIGYGDGILRTRAKHEA--LINGKRYPIRALM-MSHMFVEVDG--NVHAQDEVILYN 324
Cdd:cd06825 254 KGEAVGYGRLFVASR-TTRIATVSIGYADGYPRSLSNQKAyvLINGKRAPIIGNIcMDQLMVDVTDipEVKEGDTATLIG 332
|
..
gi 1332406780 325 ND 326
Cdd:cd06825 333 QD 334
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
14-331 |
8.89e-31 |
|
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: 119.91 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 14 QNAITVKNNQP---LMAVVKNNAYHYDLEfAVTQFIhAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVY---EFDLVRE 87
Cdd:cd06827 13 HNLRLVRELAPnskILAVVKANAYGHGLV-RVAKAL-ADADGFAVACIEEALALREAGITKPILLLEGFFsadELPLAAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 88 HQIHMTLPS---LTYYYNHKNDLAgIHVHLEFENLLHRSGFKdLNEIKEVLKDHHHNQNAKMIisGLWTHFGYADEFDvS 164
Cdd:cd06827 91 YNLWTVVHSeeqLEWLEQAALSKP-LNVWLKLDSGMHRLGFS-PEEYAAAYQRLKASPNVASI--VLMTHFACADEPD-S 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 165 DYNveRSQWmEIVEALLsEGYQFDLIHAqNSASfyregqILLPHHTHA---RVGIALYGSRPY--SSLNQHDIVQSLTVK 239
Cdd:cd06827 166 PGT--AKQL-AIFEQAT-AGLPGPRSLA-NSAA------ILAWPEAHGdwvRPGIMLYGASPFadKSGADLGLKPVMTLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 240 AHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTrAKHEA--LINGKRYPI--RALM-MshMFVEVDGNV 314
Cdd:cd06827 235 SEIIAVRELKAGESVGYGATW-TAPRPMRIGVVAIGYGDGYPRH-APSGTpvLVNGQRTPLvgRVSMdM--LTVDLTDLP 310
|
330
....*....|....*....
gi 1332406780 315 HAQ--DEVILYNNDIRIDE 331
Cdd:cd06827 311 EAKvgDPVELWGKGLPVDE 329
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
236-356 |
4.83e-28 |
|
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: 106.00 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 236 LTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRAKHEALINGKRYPIRA-LMMSHMFVEVDG-- 312
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATF-TADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVTDip 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1332406780 313 NVHAQDEVILYNND-IRIDEYTFKGVGANSEQLSAMNHdSLKKEY 356
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP-RVPRVY 124
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
25-331 |
2.28e-26 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 110.43 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 25 LMAVVKNNAYHYDlEFAVTQFI-HAGIDTFSTTSLREAIQIRQLAPDATIFLMN-AVYEFDLVREHQIHMTLPSLTYY-- 100
Cdd:PRK11930 486 IMCMVKAFAYGSG-SYEIAKLLqEHRVDYLAVAYADEGVSLRKAGITLPIMVMNpEPTSFDTIIDYKLEPEIYSFRLLda 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 101 ---YNHKNDLAGIHVHLEFENLLHRSGF--KDLNEIKEVLKDHHHnqnakMIISGLWTHFGYADEFDVSDYNVERSQ-WM 174
Cdd:PRK11930 565 fikAAQKKGITGYPIHIKIDTGMHRLGFepEDIPELARRLKKQPA-----LKVRSVFSHLAGSDDPDHDDFTRQQIElFD 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 175 EIVEALLSEGYQFDLIHAQNSASFYRegqILLPHHTHARVGIALYGSrpYSSLNQHDIVQS-LTVKAHVIQVREVQAGDY 253
Cdd:PRK11930 640 EGSEELQEALGYKPIRHILNSAGIER---FPDYQYDMVRLGIGLYGV--SASGAGQQALRNvSTLKTTILQIKHVPKGET 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 254 CGYSFAFEVTKnNTKLAVVDIGYGDGILR--TRAKHEALINGKRYPIRA-LMMSHMFVEVdGNVHAQ--DEVILYNNDIR 328
Cdd:PRK11930 715 VGYGRKGVVTK-PSRIATIPIGYADGLNRrlGNGVGYVLVNGQKAPIVGnICMDMCMIDV-TDIDAKegDEVIIFGEELP 792
|
...
gi 1332406780 329 IDE 331
Cdd:PRK11930 793 VTE 795
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
236-331 |
3.99e-21 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 87.81 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 236 LTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILR-TRAKHEALINGKRYPIRALM-MSHMFVEVDG- 312
Cdd:pfam00842 2 MTLKSRVIQVKTVPAGEGVGYGRTY-TAERDTRIATVPIGYADGYPRaLSNRGEVLINGKRAPIVGRVcMDQLMVDVTDv 80
|
90 100
....*....|....*....|....
gi 1332406780 313 -NVHAQDEVILY----NNDIRIDE 331
Cdd:pfam00842 81 pEVKVGDEVTLFgkqgDEEITADE 104
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
8-331 |
1.19e-15 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 77.36 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 8 NKKIFLQNAitvKNNQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIFLMNAVYEFDLVRE 87
Cdd:PRK13340 53 NIKTLRSLL---ANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRSASPAEIEQA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 88 HQIHMT-----------LPSLTYYYNHKndlagIHVHLEF------ENLLHRSGFKDLNEIKEVLKDHHHNqnakmiISG 150
Cdd:PRK13340 130 LRYDLEeligddeqaklLAAIAKKNGKP-----IDIHLALnsggmsRNGLDMSTARGKWEALRIATLPSLG------IVG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 151 LWTHFGYADEFDV----SDYNvERSQWMeIVEALLSEgyQFDLIHAQNSAsfyreGQILLP--HHTHARVGIALYGSRPY 224
Cdd:PRK13340 199 IMTHFPNEDEDEVrwklAQFK-EQTAWL-IGEAGLKR--EKITLHVANSY-----ATLNVPeaHLDMVRPGGILYGDRHP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 225 SSLnqhDIVQSLTVKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPI--RAL 301
Cdd:PRK13340 270 ANT---EYKRIMTFKSRIASVNTLPKGSTVGYDRTF-TLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVvgRVS 345
|
330 340 350
....*....|....*....|....*....|....*.
gi 1332406780 302 MMSHMfVEVDG--NVHAQDEVILY----NNDIRIDE 331
Cdd:PRK13340 346 MNTLM-VDVTDipNVKPGDEVVLFgkqgNAEITVDE 380
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
26-282 |
7.83e-12 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 65.52 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 26 MAVVKNNAYHYDLEfAVTQFIHAGiDTFSTTSLREAIQIRQLAPDATIFLMNAVYEFD---LVREHQIHMTLPSLTYYYN 102
Cdd:PRK03646 30 WSVVKANAYGHGIE-RIWSALGAT-DGFAVLNLEEAITLRERGWKGPILMLEGFFHAQdleLYDQHRLTTCVHSNWQLKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 103 HKNDL--AGIHVHLEFENLLHRSGF--KDLNEIKEVLKdhHHNQNAKMIisgLWTHFGYADEFDVSDynversQWMEIVE 178
Cdd:PRK03646 108 LQNARlkAPLDIYLKVNSGMNRLGFqpERVQTVWQQLR--AMGNVGEMT---LMSHFARADHPDGIS------EAMARIE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 179 ALlSEGYQFDlIHAQNSASFYREGQIllpHHTHARVGIALYGSRPYSslNQHDIVQS-----LTVKAHVIQVREVQAGDY 253
Cdd:PRK03646 177 QA-AEGLECE-RSLSNSAATLWHPQA---HFDWVRPGIILYGASPSG--QWRDIANTglrpvMTLSSEIIGVQTLKAGER 249
|
250 260
....*....|....*....|....*....
gi 1332406780 254 CGYSFAFeVTKNNTKLAVVDIGYGDGILR 282
Cdd:PRK03646 250 VGYGGRY-TARREQRIGIVAAGYADGYPR 277
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
25-216 |
1.50e-11 |
|
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: 63.11 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 25 LMAVVKNNAYhydleFAVTQFIHAGIDTFSTTSLREAIQIRQL--APDATIFLMN--AVYEFDLVREH-QIHMTLPSLTY 99
Cdd:cd06808 18 LFAVVKANAN-----PEVARTLAALGTGFDVASLGEALLLRAAgiPPEPILFLGPckQVSELEDAAEQgVIVVTVDSLEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 100 --YYNHKNDLAG----IHVHLEFENLLHRSGF--KDLNEIKEVLKDHHHNQnakmiISGLWTHFGYADEfDVSDYNVERS 171
Cdd:cd06808 93 leKLEEAALKAGpparVLLRIDTGDENGKFGVrpEELKALLERAKELPHLR-----LVGLHTHFGSADE-DYSPFVEALS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1332406780 172 QWMEIVEALLSEGYQFDLIHAQNSASFYREGQILLPHHTHARVGI 216
Cdd:cd06808 167 RFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFIIVEPGR 211
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
19-323 |
1.21e-08 |
|
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: 55.81 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 19 VKNNQPLMAVVKNNAYHYDLEFAVTQFIHAGIDTFSTTSLREAIQIRQLAPDATIF---------LMNAV-YEF-DLVRE 87
Cdd:cd06826 22 LGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILrvrtatpseIEDALaYNIeELIGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 88 HQIHMTLPSLTYYYNHKndlagIHVHLEFEnllhrSGFKDLNEIkEVLKDHHHNQNAKMI------ISGLWTHFGYADEF 161
Cdd:cd06826 102 LDQAEQIDSLAKRHGKT-----LPVHLALN-----SGGMSRNGL-ELSTAQGKEDAVAIAtlpnlkIVGIMTHFPVEDED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 162 DVSD----YNVErSQWMEIVEALLSEGYqfdLIHAQNSasfYREGQILLPHHTHARVGIALYGSRPYSSlnqhDIVQSLT 237
Cdd:cd06826 171 DVRAklarFNED-TAWLISNAKLKREKI---TLHAANS---FATLNVPEAHLDMVRPGGILYGDTPPSP----EYKRIMS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332406780 238 VKAHVIQVREVQAGDYCGYSFAFeVTKNNTKLAVVDIGYGDGILRTRA-KHEALINGKRYPI--RALMMSHMfVEVDG-- 312
Cdd:cd06826 240 FKSRVASLNTYPKGSTVGYDRTF-TLTRDSLLANIPVGYSDGYRRSFSnKAHVLINGQRVPVvgKVSMNTVM-VDVTDip 317
|
330
....*....|.
gi 1332406780 313 NVHAQDEVILY 323
Cdd:cd06826 318 GVKAGDEVVLF 328
|
|
| |
