|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-332 |
1.24e-78 |
|
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: 245.40 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 2 TAIWSVDKEAFLQNAIKVKN----GNSIMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 78 AV--YDFEKVRHYQIQMTLPSLAYYYKYKNDLS----GIKVHLEFENLLHRSGFRTlEEIREVLNDHHinsNEDKMIISG 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAARrlgkPLPVHLKVDTGMNRLGFRP-EEAPALAARLA---ALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 152 LWTHFGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREgqkllPHHTHARVGIALYGSRPYSALN 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAilRYPE-----AHFDMVRPGIALYGLSPSPEVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 230 E-YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRA-KHEALIKGKRYPIR-ALMMSH 306
Cdd:COG0787 234 AdLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRD-TRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQ 312
|
330 340
....*....|....*....|....*....
gi 499595070 307 MFVEVDEEVDAQ--DEVILY-NNDIRIDE 332
Cdd:COG0787 313 IMVDVTDIPDVKvgDEVVLFgEQGITADE 341
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-332 |
2.55e-61 |
|
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: 200.80 E-value: 2.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQN--AIKVKNGNS--IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:cd00430 6 IDLDALRHNlrVIRRLLGPGtkIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGGTPpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 DFEKVRHYQIQMTLPSLAYYYKY----KNDLSGIKVHLEFENLLHRSGFRT---LEEIREVLNDHHInsnedkmIISGLW 153
Cdd:cd00430 86 EAEEAIEYDLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPeeaEELLEALKALPGL-------ELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 154 THFGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREgqkllPHHTHARVGIALYGSRP-YSALNE 230
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAilRFPE-----AHFDMVRPGIALYGLYPsPEVKSP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 231 YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGIlkSRA---KHEALIKGKRYPIR-ALMMSH 306
Cdd:cd00430 234 LGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRP-TRIATLPVGYADGY--PRAlsnKGEVLIRGKRAPIVgRVCMDQ 310
|
330 340 350
....*....|....*....|....*....|..
gi 499595070 307 MFVEVDEEVDAQ--DEVILYNND----IRIDE 332
Cdd:cd00430 311 TMVDVTDIPDVKvgDEVVLFGRQgdeeITAEE 342
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-332 |
7.06e-51 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 173.44 E-value: 7.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQN--AIKVKNGNS--IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:PRK00053 8 IDLDALRHNlrQIRKHAPPKskLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 -DFEKVRHYQIQMTLPSLAYYYKYKN-DLS-GIKVHLEFENLLHRSGFRtLEEIREVLND----HHINsnedkmiISGLW 153
Cdd:PRK00053 88 eDLPLIIAYNLTTAVHSLEQLEALEKaELGkPLKVHLKIDTGMHRLGVR-PEEAEAALERllacPNVR-------LEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 154 THFGYADEFDVPEYSIEREAWLNIVDTLLDEGyhFDLIHAQNSAsyyreGQKLLP--HHTHARVGIALYGSRP--YSALN 229
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKG--KPLRHLANSA-----AILRWPdlHFDWVRPGIALYGLSPsgEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 230 EYSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKS-RAKHEALIKGKRYPIR-ALMMSHM 307
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERD-TRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIVgRVSMDQL 311
|
330 340
....*....|....*....|....*..
gi 499595070 308 FVEV--DEEVDAQDEVILYNNDIRIDE 332
Cdd:PRK00053 312 TVDLgpDPQDKVGDEVTLWGEALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
6-332 |
9.81e-46 |
|
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: 159.83 E-value: 9.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 6 SVDKEAFLQN--AIKVKNG--NSIMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY- 80
Cdd:TIGR00492 6 EIDLAALKHNlsAIRNHIGpkSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGGFFa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 -DFEKVRHYQIQMTLPSLAYYYKYKNDL----SGIKVHLEFENLLHRSGFRTLEEIREVlndHHINSNEDKMIISGLWTH 155
Cdd:TIGR00492 86 eDLKILAAWDLTTTVHSVEQLQALEEALlkepKRLKVHLKIDTGMNRLGVKPDEAALFV---QKLRQLKKFLELEGIFSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 156 FGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREGqkllpHHTHARVGIALYGSRP---YSALNE 230
Cdd:TIGR00492 163 FATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAilNWPES-----HFDMVRPGIILYGLYPsadMSDGAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 231 YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGI---LKSRAkhEALIKGKRYPIR-ALMMSH 306
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEED-TRIGVVAIGYADGYpraLSNGT--PVLVNGKRVPIVgRVCMDM 314
|
330 340
....*....|....*....|....*...
gi 499595070 307 MFVEVDEEVDAQ--DEVILYNNDIRIDE 332
Cdd:TIGR00492 315 IMVDLGPDLQDKtgDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
7-224 |
2.15e-40 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 141.59 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQNAIKVKN---GNS-IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:pfam01168 1 IDLDALRHNLRRLRRragPGAkLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 DFEKVRHYQIQMTLPSLAYYYKY----KNDLSGIKVHLEFENLLHRSGFRTlEEIREVLNDHHinsNEDKMIISGLWTHF 156
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLA---ALPGLRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595070 157 GYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSASYYRegqkLLPHHTHARVGIALYGSRP 224
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILL----HPLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
237-350 |
3.99e-25 |
|
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: 98.29 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 237 LTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRAKHEALIKGKRYPIRA-LMMSHMFVEV--DE 313
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRD-TRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVtdIP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 499595070 314 EVDAQDEVILYNND-IRIDEYTFKGVGANSEQLSAMNH 350
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP 118
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-332 |
1.24e-78 |
|
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: 245.40 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 2 TAIWSVDKEAFLQNAIKVKN----GNSIMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMN 77
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRAlagpGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 78 AV--YDFEKVRHYQIQMTLPSLAYYYKYKNDLS----GIKVHLEFENLLHRSGFRTlEEIREVLNDHHinsNEDKMIISG 151
Cdd:COG0787 83 GVppEDLELAIEYDLEPVVHSLEQLEALAAAARrlgkPLPVHLKVDTGMNRLGFRP-EEAPALAARLA---ALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 152 LWTHFGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREgqkllPHHTHARVGIALYGSRPYSALN 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAilRYPE-----AHFDMVRPGIALYGLSPSPEVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 230 E-YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRA-KHEALIKGKRYPIR-ALMMSH 306
Cdd:COG0787 234 AdLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRD-TRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVgRVSMDQ 312
|
330 340
....*....|....*....|....*....
gi 499595070 307 MFVEVDEEVDAQ--DEVILY-NNDIRIDE 332
Cdd:COG0787 313 IMVDVTDIPDVKvgDEVVLFgEQGITADE 341
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-332 |
2.55e-61 |
|
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: 200.80 E-value: 2.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQN--AIKVKNGNS--IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:cd00430 6 IDLDALRHNlrVIRRLLGPGtkIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGGTPpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 DFEKVRHYQIQMTLPSLAYYYKY----KNDLSGIKVHLEFENLLHRSGFRT---LEEIREVLNDHHInsnedkmIISGLW 153
Cdd:cd00430 86 EAEEAIEYDLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPeeaEELLEALKALPGL-------ELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 154 THFGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREgqkllPHHTHARVGIALYGSRP-YSALNE 230
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAilRFPE-----AHFDMVRPGIALYGLYPsPEVKSP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 231 YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGIlkSRA---KHEALIKGKRYPIR-ALMMSH 306
Cdd:cd00430 234 LGLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRP-TRIATLPVGYADGY--PRAlsnKGEVLIRGKRAPIVgRVCMDQ 310
|
330 340 350
....*....|....*....|....*....|..
gi 499595070 307 MFVEVDEEVDAQ--DEVILYNND----IRIDE 332
Cdd:cd00430 311 TMVDVTDIPDVKvgDEVVLFGRQgdeeITAEE 342
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-332 |
7.06e-51 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 173.44 E-value: 7.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQN--AIKVKNGNS--IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:PRK00053 8 IDLDALRHNlrQIRKHAPPKskLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGFFpa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 -DFEKVRHYQIQMTLPSLAYYYKYKN-DLS-GIKVHLEFENLLHRSGFRtLEEIREVLND----HHINsnedkmiISGLW 153
Cdd:PRK00053 88 eDLPLIIAYNLTTAVHSLEQLEALEKaELGkPLKVHLKIDTGMHRLGVR-PEEAEAALERllacPNVR-------LEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 154 THFGYADEFDVPEYSIEREAWLNIVDTLLDEGyhFDLIHAQNSAsyyreGQKLLP--HHTHARVGIALYGSRP--YSALN 229
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKG--KPLRHLANSA-----AILRWPdlHFDWVRPGIALYGLSPsgEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 230 EYSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKS-RAKHEALIKGKRYPIR-ALMMSHM 307
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERD-TRIAVVPIGYADGYPRNlPSGTPVLVNGRRVPIVgRVSMDQL 311
|
330 340
....*....|....*....|....*..
gi 499595070 308 FVEV--DEEVDAQDEVILYNNDIRIDE 332
Cdd:PRK00053 312 TVDLgpDPQDKVGDEVTLWGEALTAED 338
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
6-332 |
9.81e-46 |
|
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: 159.83 E-value: 9.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 6 SVDKEAFLQN--AIKVKNG--NSIMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY- 80
Cdd:TIGR00492 6 EIDLAALKHNlsAIRNHIGpkSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGGFFa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 -DFEKVRHYQIQMTLPSLAYYYKYKNDL----SGIKVHLEFENLLHRSGFRTLEEIREVlndHHINSNEDKMIISGLWTH 155
Cdd:TIGR00492 86 eDLKILAAWDLTTTVHSVEQLQALEEALlkepKRLKVHLKIDTGMNRLGVKPDEAALFV---QKLRQLKKFLELEGIFSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 156 FGYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSAS--YYREGqkllpHHTHARVGIALYGSRP---YSALNE 230
Cdd:TIGR00492 163 FATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAilNWPES-----HFDMVRPGIILYGLYPsadMSDGAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 231 YSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGI---LKSRAkhEALIKGKRYPIR-ALMMSH 306
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEED-TRIGVVAIGYADGYpraLSNGT--PVLVNGKRVPIVgRVCMDM 314
|
330 340
....*....|....*....|....*...
gi 499595070 307 MFVEVDEEVDAQ--DEVILYNNDIRIDE 332
Cdd:TIGR00492 315 IMVDLGPDLQDKtgDEVILWGEEISIDE 342
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
7-224 |
2.15e-40 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 141.59 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQNAIKVKN---GNS-IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNAVY-- 80
Cdd:pfam01168 1 IDLDALRHNLRRLRRragPGAkLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 DFEKVRHYQIQMTLPSLAYYYKY----KNDLSGIKVHLEFENLLHRSGFRTlEEIREVLNDHHinsNEDKMIISGLWTHF 156
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLA---ALPGLRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499595070 157 GYADEFDVPEYSIEREAWLNIVDTLLDEGYHFDLIHAQNSASYYRegqkLLPHHTHARVGIALYGSRP 224
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILL----HPLHFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
7-327 |
1.03e-39 |
|
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: 144.03 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQNAIKVK----NGNSIMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVRE--IAPDATIFLMNAVY 80
Cdd:cd06825 6 IDLSALEHNVKEIKrllpSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREagIKGEILILGYTPPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 81 DFEKVRHYQIQMTLPSLAYYYKYKNDLSGIKVHLEFENLLHRSGF--RTLEEIREVLNDHHINsnedkmiISGLWTHFGY 158
Cdd:cd06825 86 RAKELKKYSLTQTLISEAYAEELSKYAVNIKVHLKVDTGMHRLGEspEDIDSILAIYRLKNLK-------VSGIFSHLCV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 159 ADEFDvpEYSIER-----EAWLNIVDTLLDEGYHFDLIHAQNsaSY----YREgqkllPHHTHARVGIALYG--SRPYSA 227
Cdd:cd06825 159 SDSLD--EDDIAFtkhqiACFDQVLADLKARGIEVGKIHIQS--SYgilnYPD-----LKYDYVRPGILLYGvlSDPNDP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 228 L-NEYSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRAKHEA--LIKGKRYPIRALM- 303
Cdd:cd06825 230 TkLGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRT-TRIATVSIGYADGYPRSLSNQKAyvLINGKRAPIIGNIc 308
|
330 340
....*....|....*....|....*.
gi 499595070 304 MSHMFVEVD--EEVDAQDEVILYNND 327
Cdd:cd06825 309 MDQLMVDVTdiPEVKEGDTATLIGQD 334
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
237-350 |
3.99e-25 |
|
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: 98.29 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 237 LTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRAKHEALIKGKRYPIRA-LMMSHMFVEV--DE 313
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRD-TRIATVPIGYADGYPRALSNGPVLINGQRVPVVGrVSMDQLMVDVtdIP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 499595070 314 EVDAQDEVILYNND-IRIDEYTFKGVGANSEQLSAMNH 350
Cdd:smart01005 81 DVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGP 118
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
18-332 |
1.55e-24 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 105.04 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 18 KVKNGNSIMAVVKnnAYHYGL-EFAVTSFLKA-GINTFSTTSLKEAIKVREIAPDATIFLMNA-VYDFEKVRHYQIQ--- 91
Cdd:PRK11930 479 KLKPETKIMCMVK--AFAYGSgSYEIAKLLQEhRVDYLAVAYADEGVSLRKAGITLPIMVMNPePTSFDTIIDYKLEpei 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 92 ---MTLPSLAYYYKyKNDLSGIKVHLEFENLLHRSGFR--TLEEIREVLNDHhinsneDKMIISGLWTHFGYADEFDVPE 166
Cdd:PRK11930 557 ysfRLLDAFIKAAQ-KKGITGYPIHIKIDTGMHRLGFEpeDIPELARRLKKQ------PALKVRSVFSHLAGSDDPDHDD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 167 YSIEREAWLNIVDTLLDEGYHFDLI-HAQNSASYYREGQkllPHHTHARVGIALYGSrpYSALNEYSIKQS-LTVKGNVI 244
Cdd:PRK11930 630 FTRQQIELFDEGSEELQEALGYKPIrHILNSAGIERFPD---YQYDMVRLGIGLYGV--SASGAGQQALRNvSTLKTTIL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 245 QVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILK--SRAKHEALIKGKRYPIRA-LMMSHMFVEV-DEEVDAQDE 320
Cdd:PRK11930 705 QIKHVPKGETVGYGRKGVVTKP-SRIATIPIGYADGLNRrlGNGVGYVLVNGQKAPIVGnICMDMCMIDVtDIDAKEGDE 783
|
330
....*....|..
gi 499595070 321 VILYNNDIRIDE 332
Cdd:PRK11930 784 VIIFGEELPVTE 795
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
4-332 |
3.64e-19 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 87.76 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 4 IW-SVDKEAFLQNAIKVK---NGNS-IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIFLMNA 78
Cdd:PRK13340 41 AWlEISPGAFRHNIKTLRsllANKSkVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 79 V----------YDFEKVRHYQIQMT-LPSLAyyykYKNDlSGIKVHLEF------ENLLHRSGFRTLEEIREVLNDHHIN 141
Cdd:PRK13340 121 AspaeieqalrYDLEELIGDDEQAKlLAAIA----KKNG-KPIDIHLALnsggmsRNGLDMSTARGKWEALRIATLPSLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 142 snedkmiISGLWTHFGYADEFDVPEYSI---EREAWLNIVDTLLDEGYhfdLIHAQNSASYYRegqklLP--HHTHARVG 216
Cdd:PRK13340 196 -------IVGIMTHFPNEDEDEVRWKLAqfkEQTAWLIGEAGLKREKI---TLHVANSYATLN-----VPeaHLDMVRPG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 217 IALYGSRpYSALNEYsiKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRA-KHEALIKGK 295
Cdd:PRK13340 261 GILYGDR-HPANTEY--KRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRD-SRLANLPVGYSDGYPRHASnKAPVLINGQ 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499595070 296 RYPI--RALMMSHMfVEVDEEVDAQ--DEVILY----NNDIRIDE 332
Cdd:PRK13340 337 RAPVvgRVSMNTLM-VDVTDIPNVKpgDEVVLFgkqgNAEITVDE 380
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
237-332 |
1.74e-18 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 80.49 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 237 LTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGIlkSRA---KHEALIKGKRYPIRALM-MSHMFVEVD 312
Cdd:pfam00842 2 MTLKSRVIQVKTVPAGEGVGYGRTYTAERD-TRIATVPIGYADGY--PRAlsnRGEVLINGKRAPIVGRVcMDQLMVDVT 78
|
90 100
....*....|....*....|....*.
gi 499595070 313 EEVDAQ--DEVILY----NNDIRIDE 332
Cdd:pfam00842 79 DVPEVKvgDEVTLFgkqgDEEITADE 104
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
7-324 |
1.89e-14 |
|
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: 73.53 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 7 VDKEAFLQN---AIKVKNGNS-IMAVVKNNAYHYGLEFAVTSFLKAGINTFSTTSLKEAIKVREIAPDATIF-------- 74
Cdd:cd06826 6 ISTGAFENNiklLKKLLGGNTkLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILrvrtatps 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 75 -LMNAV-YDFEKVRHYQIQMT-LPSLAYYYKYKndlsgIKVHLEF------ENLLHRSGFRTLEEIREVLNDHHINsned 145
Cdd:cd06826 86 eIEDALaYNIEELIGSLDQAEqIDSLAKRHGKT-----LPVHLALnsggmsRNGLELSTAQGKEDAVAIATLPNLK---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 146 kmiISGLWTHFGYADEFDVPEYSI---EREAWLnIVDTLLDEGyhfDL-IHAQNSasyYREGQKLLPHHTHARVGIALYG 221
Cdd:cd06826 157 ---IVGIMTHFPVEDEDDVRAKLArfnEDTAWL-ISNAKLKRE---KItLHAANS---FATLNVPEAHLDMVRPGGILYG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 222 SRPYSAlnEYsiKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDGILKSRA-KHEALIKGKRYPI- 299
Cdd:cd06826 227 DTPPSP--EY--KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRD-SLLANIPVGYSDGYRRSFSnKAHVLINGQRVPVv 301
|
330 340
....*....|....*....|....*...
gi 499595070 300 -RALMMSHMfVEVDE--EVDAQDEVILY 324
Cdd:cd06826 302 gKVSMNTVM-VDVTDipGVKAGDEVVLF 328
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
6-280 |
1.26e-12 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 68.22 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 6 SVDKEAFLQN---AIKVKNGNSIMAVVKNNAYHYGLEfAVTSFLKAGiNTFSTTSLKEAIKVREIAPDATIFLMN----- 77
Cdd:PRK03646 7 SLDLQALKQNlsiVREAAPGARVWSVVKANAYGHGIE-RIWSALGAT-DGFAVLNLEEAITLRERGWKGPILMLEgffha 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 78 ------AVYDFEKVRHYQIQMTLPSLAYYYKykndlsGIKVHLEFENLLHRSGFRTlEEIREVLNDHHINSNEDKMIisg 151
Cdd:PRK03646 85 qdlelyDQHRLTTCVHSNWQLKALQNARLKA------PLDIYLKVNSGMNRLGFQP-ERVQTVWQQLRAMGNVGEMT--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 152 LWTHFGYADEFDVPEYSIEREAwlnivdtLLDEGYHFDlIHAQNSASYYREGQKllpHHTHARVGIALYGSRP---YSAL 228
Cdd:PRK03646 155 LMSHFARADHPDGISEAMARIE-------QAAEGLECE-RSLSNSAATLWHPQA---HFDWVRPGIILYGASPsgqWRDI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499595070 229 NEYSIKQSLTVKGNVIQVREVNAGDNCGYSFAFEATRDhTRLAVVDVGYGDG 280
Cdd:PRK03646 224 ANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARRE-QRIGIVAAGYADG 274
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
25-217 |
7.21e-08 |
|
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: 52.32 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 25 IMAVVKNNAYhygleFAVTSFLKAGINTFSTTSLKEAIKVRE--IAPDATIFLMN--AVYDFEK-VRHYQIQMTLPSL-- 97
Cdd:cd06808 18 LFAVVKANAN-----PEVARTLAALGTGFDVASLGEALLLRAagIPPEPILFLGPckQVSELEDaAEQGVIVVTVDSLee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595070 98 -----AYYYKYKNDLSgIKVHLEFENLLHRSGFR---TLEEIREVLNDHHINsnedkmiISGLWTHFGYADEfDVPEYSI 169
Cdd:cd06808 93 lekleEAALKAGPPAR-VLLRIDTGDENGKFGVRpeeLKALLERAKELPHLR-------LVGLHTHFGSADE-DYSPFVE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499595070 170 EREAWLNIVDTLLDEGYHFDLIHAQNSASYYREGQKLLPHHTHARVGI 217
Cdd:cd06808 164 ALSRFVAALDQLGELGIDLEQLSIGGSFAILYLQELPLGTFIIVEPGR 211
|
|
| |
