|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
19-356 |
3.54e-111 |
|
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: 328.61 E-value: 3.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 19 RLEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYV 97
Cdd:COG0787 5 WAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLGGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 98 NPENLK-VKNLPFSYVVYEIGQLNQILNY----QPDAKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSHFG 172
Cdd:COG0787 85 PPEDLElAIEYDLEPVVHSLEQLEALAAAarrlGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIMSHFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 173 ASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY--------------DS 238
Cdd:COG0787 165 CADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHF----DMVRPGIALYglspspevaadlglKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 818341335 319 KNVKVGDEVEIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:COG0787 321 PDVKVGDEVVLFGEQGITadelaeaaGTISYEILTRLGPRVPRVYV 366
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
18-356 |
2.76e-106 |
|
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: 315.98 E-value: 2.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 18 NRLEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGY 96
Cdd:cd00430 2 TWAEIDLDALRHNLRVIrRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 97 VNPENLK--VKNlPFSYVVYEIGQLNQI----LNYQPDAKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSH 170
Cdd:cd00430 82 TPPEEAEeaIEY-DLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 171 FGASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY-------------- 236
Cdd:cd00430 161 FATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHF----DMVRPGIALYglypspevksplgl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVS 316
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 818341335 317 KVKNVKVGDEVEII-----------FNPKINGRIPYEYMVHLNYEIKRVVV 356
Cdd:cd00430 317 DIPDVKVGDEVVLFgrqgdeeitaeELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
19-356 |
2.51e-79 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 247.01 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 19 RLEISQKKLIKNYKHLSA-IDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYV 97
Cdd:PRK00053 5 TAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 98 NPEN----LKVKNLpfSYVVYEIGQLNQILNYQPD--AKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSHF 171
Cdd:PRK00053 85 FPAEdlplIIAYNL--TTAVHSLEQLEALEKAELGkpLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFSHF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 172 GASEKPNAYETKDQAKKFKKAVSILNKYGIFPRwkHFANSDGLINSKvlglGSISNMARVGL---GLYDS---------- 238
Cdd:PRK00053 163 ATADEPDNSYTEQQLNRFEAALAGLPGKGKPLR--HLANSAAILRWP----DLHFDWVRPGIalyGLSPSgeplgldfgl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 --VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVS 316
Cdd:PRK00053 237 kpAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 818341335 317 KVKNVKVGDEVeIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:PRK00053 317 PDPQDKVGDEV-TLWGEALTaedvaeiiGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
21-356 |
6.29e-69 |
|
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: 220.30 E-value: 6.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 21 EISQKKLIKNykhLSAIDKKI----KVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGY 96
Cdd:TIGR00492 6 EIDLAALKHN---LSAIRNHIgpksKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 97 VNPENLK---VKNL-PFSYVVYEIGQLNQILNYQPDA-KIHIFVDTGMHREGILLKDLEEFLNDIPKRY-FGNIEGLSSH 170
Cdd:TIGR00492 83 FFAEDLKilaAWDLtTTVHSVEQLQALEEALLKEPKRlKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKkFLELEGIFSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 171 FGASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY-------------- 236
Cdd:TIGR00492 163 FATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHF----DMVRPGIILYglypsadmsdgapf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 --DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVD 314
Cdd:TIGR00492 239 glKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 818341335 315 VSKVKNVKVGDEVeIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:TIGR00492 319 LGPDLQDKTGDEV-ILWGEEISideiaemlGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
239-355 |
9.54e-45 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 149.82 E-value: 9.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 818341335 319 KNVKVGDEVEIIFNPKIN-----------GRIPYEYMVHLNYEIKRVV 355
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEeitadelaeaaGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
239-355 |
1.33e-41 |
|
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: 141.44 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNrGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 818341335 319 KNVKVGDEVEIIFNPKIN--------GRIPYEYMVHLNYEIKRVV 355
Cdd:smart01005 80 PDVKVGDEVVLFGPQEITadelaeaaGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
19-356 |
3.54e-111 |
|
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: 328.61 E-value: 3.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 19 RLEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYV 97
Cdd:COG0787 5 WAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLGGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 98 NPENLK-VKNLPFSYVVYEIGQLNQILNY----QPDAKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSHFG 172
Cdd:COG0787 85 PPEDLElAIEYDLEPVVHSLEQLEALAAAarrlGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIMSHFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 173 ASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY--------------DS 238
Cdd:COG0787 165 CADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHF----DMVRPGIALYglspspevaadlglKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 818341335 319 KNVKVGDEVEIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:COG0787 321 PDVKVGDEVVLFGEQGITadelaeaaGTISYEILTRLGPRVPRVYV 366
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
18-356 |
2.76e-106 |
|
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: 315.98 E-value: 2.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 18 NRLEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGY 96
Cdd:cd00430 2 TWAEIDLDALRHNLRVIrRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 97 VNPENLK--VKNlPFSYVVYEIGQLNQI----LNYQPDAKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSH 170
Cdd:cd00430 82 TPPEEAEeaIEY-DLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 171 FGASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY-------------- 236
Cdd:cd00430 161 FATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHF----DMVRPGIALYglypspevksplgl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVS 316
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 818341335 317 KVKNVKVGDEVEII-----------FNPKINGRIPYEYMVHLNYEIKRVVV 356
Cdd:cd00430 317 DIPDVKVGDEVVLFgrqgdeeitaeELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
19-356 |
2.51e-79 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 247.01 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 19 RLEISQKKLIKNYKHLSA-IDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYV 97
Cdd:PRK00053 5 TAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 98 NPEN----LKVKNLpfSYVVYEIGQLNQILNYQPD--AKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSHF 171
Cdd:PRK00053 85 FPAEdlplIIAYNL--TTAVHSLEQLEALEKAELGkpLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFSHF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 172 GASEKPNAYETKDQAKKFKKAVSILNKYGIFPRwkHFANSDGLINSKvlglGSISNMARVGL---GLYDS---------- 238
Cdd:PRK00053 163 ATADEPDNSYTEQQLNRFEAALAGLPGKGKPLR--HLANSAAILRWP----DLHFDWVRPGIalyGLSPSgeplgldfgl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 --VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVS 316
Cdd:PRK00053 237 kpAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLG 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 818341335 317 KVKNVKVGDEVeIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:PRK00053 317 PDPQDKVGDEV-TLWGEALTaedvaeiiGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
21-356 |
6.29e-69 |
|
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: 220.30 E-value: 6.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 21 EISQKKLIKNykhLSAIDKKI----KVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGY 96
Cdd:TIGR00492 6 EIDLAALKHN---LSAIRNHIgpksKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 97 VNPENLK---VKNL-PFSYVVYEIGQLNQILNYQPDA-KIHIFVDTGMHREGILLKDLEEFLNDIPKRY-FGNIEGLSSH 170
Cdd:TIGR00492 83 FFAEDLKilaAWDLtTTVHSVEQLQALEEALLKEPKRlKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKkFLELEGIFSH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 171 FGASEKPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLY-------------- 236
Cdd:TIGR00492 163 FATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHF----DMVRPGIILYglypsadmsdgapf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 --DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVD 314
Cdd:TIGR00492 239 glKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 818341335 315 VSKVKNVKVGDEVeIIFNPKIN--------GRIPYEYMVHLNYEIKRVVV 356
Cdd:TIGR00492 319 LGPDLQDKTGDEV-ILWGEEISideiaemlGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
20-330 |
1.23e-61 |
|
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: 201.43 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 20 LEISQKKLIKNYKHLS-AIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYVN 98
Cdd:cd06825 4 LEIDLSALEHNVKEIKrLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 99 PEN---LKVKNLPFSYVVYEIG-QLNQilnYQPDAKIHIFVDTGMHREGILLKDLEEFLNdIPKRYFGNIEGLSSHFGAS 174
Cdd:cd06825 84 PVRakeLKKYSLTQTLISEAYAeELSK---YAVNIKVHLKVDTGMHRLGESPEDIDSILA-IYRLKNLKVSGIFSHLCVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 175 E---KPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsisNMARVGLGLYDS------------- 238
Cdd:cd06825 160 DsldEDDIAFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKY----DYVRPGILLYGVlsdpndptklgld 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 ---VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSN-RGEVLIKRVRCPIIGRVSMNITTVD 314
Cdd:cd06825 236 lrpVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNqKAYVLINGKRAPIIGNICMDQLMVD 315
|
330
....*....|....*.
gi 818341335 315 VSKVKNVKVGDEVEII 330
Cdd:cd06825 316 VTDIPEVKEGDTATLI 331
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
19-328 |
1.90e-55 |
|
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: 185.01 E-value: 1.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 19 RLEISQKKLIKNYKHLSAIDKKIKVAPVLKSNAYGHGIAEVAKVLDrlNPPFFCVDSLYEAYKLYKAGIKSRILIM-GYV 97
Cdd:cd06827 3 RATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALA--DADGFAVACIEEALALREAGITKPILLLeGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 98 NPENLK-VKNLPFSYVVYEIGQLNQILNYQPDAKIHIF--VDTGMHREGILLKDLEEF---LNDIPKRyfGNIeGLSSHF 171
Cdd:cd06827 81 SADELPlAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWlkLDSGMHRLGFSPEEYAAAyqrLKASPNV--ASI-VLMTHF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 172 GASEKPNAYETKDQAKKFKKAVSILNkygifprWKH-FANSDGLINSKVlglgSISNMARVGLGLYDS------------ 238
Cdd:cd06827 158 ACADEPDSPGTAKQLAIFEQATAGLP-------GPRsLANSAAILAWPE----AHGDWVRPGIMLYGAspfadksgadlg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 ---VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDV 315
Cdd:cd06827 227 lkpVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDL 306
|
330
....*....|...
gi 818341335 316 SKVKNVKVGDEVE 328
Cdd:cd06827 307 TDLPEAKVGDPVE 319
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
3-354 |
6.27e-55 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 192.48 E-value: 6.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 3 FDKLKKLIGRRYFPlNRLEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDrlnppFFCVDSLYEAY- 80
Cdd:PRK11930 446 FEQITELLEQKVHE-TVLEINLNAIVHNLNYYrSKLKPETKIMCMVKAFAYGSGSYEIAKLLQ-----EHRVDYLAVAYa 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 81 ----KLYKAGIKSRILIMgyvNPENLKVKNLpFSY----VVYEIGQLNQILNY-----QPDAKIHIFVDTGMHREGILLK 147
Cdd:PRK11930 520 degvSLRKAGITLPIMVM---NPEPTSFDTI-IDYklepEIYSFRLLDAFIKAaqkkgITGYPIHIKIDTGMHRLGFEPE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 148 DLEEFLNDIPKRYFGNIEGLSSHFGASEKPNAYE-TKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLINSKVLGLgsis 226
Cdd:PRK11930 596 DIPELARRLKKQPALKVRSVFSHLAGSDDPDHDDfTRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQY---- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 227 NMARVGLGLY------------DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNR-GEV 293
Cdd:PRK11930 672 DMVRLGIGLYgvsasgagqqalRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGvGYV 751
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818341335 294 LIKRVRCPIIGRVSMNITTVDVSKVkNVKVGDEVeIIFNPKIN--------GRIPYEYMVHLNYEIKRV 354
Cdd:PRK11930 752 LVNGQKAPIVGNICMDMCMIDVTDI-DAKEGDEV-IIFGEELPvteladalNTIPYEILTSISPRVKRV 818
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
20-356 |
2.49e-46 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 162.49 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 20 LEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYVN 98
Cdd:PRK13340 43 LEISPGAFRHNIKTLrSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRSAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 99 PENLKVKnlpFSYVVYE-IG---QLNQI--LNYQPDAKIHIFV---DTGMHREGI---LLKDLEEFLNdIPKRYFGNIEG 166
Cdd:PRK13340 123 PAEIEQA---LRYDLEElIGddeQAKLLaaIAKKNGKPIDIHLalnSGGMSRNGLdmsTARGKWEALR-IATLPSLGIVG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 167 LSSHFgASEkpNAYETKDQAKKFKKAVSILNKYGIFPRWK---HFANSDGLINSKVLGLgsisNMARVGLGLY------- 236
Cdd:PRK13340 199 IMTHF-PNE--DEDEVRWKLAQFKEQTAWLIGEAGLKREKitlHVANSYATLNVPEAHL----DMVRPGGILYgdrhpan 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 ---DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTV 313
Cdd:PRK13340 272 teyKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLMV 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 818341335 314 DVSKVKNVKVGDEVEIIFN-----------PKINGRIPYEYMVHLNYEIKRVVV 356
Cdd:PRK13340 352 DVTDIPNVKPGDEVVLFGKqgnaeitvdevEEASGTIFPELYTAWGRTNPRIYV 405
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
239-355 |
9.54e-45 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 149.82 E-value: 9.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 818341335 319 KNVKVGDEVEIIFNPKIN-----------GRIPYEYMVHLNYEIKRVV 355
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEeitadelaeaaGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
20-339 |
9.07e-44 |
|
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: 154.81 E-value: 9.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 20 LEISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYVN 98
Cdd:cd06826 4 LEISTGAFENNIKLLkKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 99 PENLKVKnlpFSYVVYE-IGQLNQIL-------NYQPDAKIHIFVDT-GMHREGILLKdLEEFLND---IPKRYFGNIEG 166
Cdd:cd06826 84 PSEIEDA---LAYNIEElIGSLDQAEqidslakRHGKTLPVHLALNSgGMSRNGLELS-TAQGKEDavaIATLPNLKIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 167 LSSHFgASEkpNAYETKDQAKKFKKAVSILNKYGIFPRWK---HFANSDGLINSKVLGLgsisNMARVGLGLY------- 236
Cdd:cd06826 160 IMTHF-PVE--DEDDVRAKLARFNEDTAWLISNAKLKREKitlHAANSFATLNVPEAHL----DMVRPGGILYgdtppsp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 237 --DSVLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVD 314
Cdd:cd06826 233 eyKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVD 312
|
330 340
....*....|....*....|....*
gi 818341335 315 VSKVKNVKVGDEVeIIFNPKINGRI 339
Cdd:cd06826 313 VTDIPGVKAGDEV-VLFGKQGGAEI 336
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
239-355 |
1.33e-41 |
|
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: 141.44 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 239 VLRFITHINQIKELKKGDKVGYDFTYTAKKDMTMAVLPVGYNDGVDRILSNrGEVLIKRVRCPIIGRVSMNITTVDVSKV 318
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 818341335 319 KNVKVGDEVEIIFNPKIN--------GRIPYEYMVHLNYEIKRVV 355
Cdd:smart01005 80 PDVKVGDEVVLFGPQEITadelaeaaGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
22-236 |
1.29e-40 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 142.36 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 22 ISQKKLIKNYKHL-SAIDKKIKVAPVLKSNAYGHGIAEVAKVLDRLNPPFFCVDSLYEAYKLYKAGIKSRILIMGYVNPE 100
Cdd:pfam01168 1 IDLDALRHNLRRLrRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 101 NLK-VKNLPFSYVVYEIGQLNQILNY----QPDAKIHIFVDTGMHREGILLKDLEEFLNDIPKRYFGNIEGLSSHFGASE 175
Cdd:pfam01168 81 ELAlAAEYDLTPTVDSLEQLEALAAAarrlGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACAD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818341335 176 KPNAYETKDQAKKFKKAVSILNKYGIFPRWKHFANSDGLinskvLGLGSISNMARVGLGLY 236
Cdd:pfam01168 161 EPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAI-----LLHPLHFDMVRPGIALY 216
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
42-356 |
8.88e-29 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 114.44 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 42 KVAPVLKSNAYGHGIAEVAKVLDRLNPpfFCVDSLYEAYKLYKAGIKSRILIM-GYVNPENLKV-KNLPFSYVVYEIGQL 119
Cdd:PRK03646 28 RVWSVVKANAYGHGIERIWSALGATDG--FAVLNLEEAITLRERGWKGPILMLeGFFHAQDLELyDQHRLTTCVHSNWQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 120 NQILNYQPDAKIHIF--VDTGMHREGILLKDLEEFLNDIpkRYFGNIEG--LSSHFGASEKPNAyeTKDQAKKFKKAvsi 195
Cdd:PRK03646 106 KALQNARLKAPLDIYlkVNSGMNRLGFQPERVQTVWQQL--RAMGNVGEmtLMSHFARADHPDG--ISEAMARIEQA--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 196 lnKYGIFPRwKHFANSDGlinskVLGLGSI-SNMARVGLGLYDS----------------VLRFITHINQIKELKKGDKV 258
Cdd:PRK03646 179 --AEGLECE-RSLSNSAA-----TLWHPQAhFDWVRPGIILYGAspsgqwrdiantglrpVMTLSSEIIGVQTLKAGERV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 259 GYDFTYTAKKDMTMAVLPVGYNDGVDRILSNRGEVLIKRVRCPIIGRVSMNITTVDVSKVKNVKVGDEVEIIFNP-KIN- 336
Cdd:PRK03646 251 GYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTPVELWGKEiKIDd 330
|
330 340
....*....|....*....|....*
gi 818341335 337 -----GRIPYEYMVHLNYEIKRVVV 356
Cdd:PRK03646 331 vaaaaGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
27-233 |
8.10e-13 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 66.57 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 27 LIKNYKHL-SAIDKKIKVAPVLKSNAYghgiAEVAKVLDRLNPPFFCVdSLYEAYKLYKAGIKS-RILIMG---YVNPEN 101
Cdd:cd06808 1 IRHNYRRLrEAAPAGITLFAVVKANAN----PEVARTLAALGTGFDVA-SLGEALLLRAAGIPPePILFLGpckQVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818341335 102 LKVKNLPFSYVVY---EIGQLNQI-LNYQPDAKIHIFVDTG--MHREGILLKDLEEFLNDIPKRYFGNIEGLSSHFG-AS 174
Cdd:cd06808 76 DAAEQGVIVVTVDsleELEKLEEAaLKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGsAD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 818341335 175 EKPNAYEtkDQAKKFKKAVSILNKYGIFPRWKHFANSDGlINSKVLGLGSISNMARVGL 233
Cdd:cd06808 156 EDYSPFV--EALSRFVAALDQLGELGIDLEQLSIGGSFA-ILYLQELPLGTFIIVEPGR 211
|
|
| |
