|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
12-386 |
1.43e-167 |
|
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: 472.75 E-value: 1.43e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 12 AWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNE 91
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 92 SPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHF 171
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 172 ATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPRIQLVPAMS 251
Cdd:cd00430 162 ATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGLKPVMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 252 VRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVDVNDa 331
Cdd:cd00430 242 LKARVVQVKTVPAGEGVSYGRTYTAPRPT-RIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTM--VDVTD- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2553755746 332 rayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:cd00430 318 -----IPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
9-386 |
4.92e-162 |
|
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: 458.80 E-value: 4.92e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 9 TRAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLM 88
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 89 LNESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTF 168
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPRIQLVP 248
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 249 AMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTR-IATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIM--VDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553755746 329 NDarayrpVEPVERGDLVTVMGVDGdeeITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:COG0787 318 TD------IPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
10-386 |
1.77e-130 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 378.75 E-value: 1.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 10 RAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLML 89
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 NESPLQS-IDVLLEYDIMPSVYDMDFALAYgeRAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTF 168
Cdd:PRK00053 82 GGFFPAEdLPLIIAYNLTTAVHSLEQLEAL--EKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCglVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPR-IQLV 247
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKGKPL--RHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLdFGLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 248 PAMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVD 327
Cdd:PRK00053 238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTR-IAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLT--VD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553755746 328 VNDARAYRPvepverGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:PRK00053 315 LGPDPQDKV------GDEVTLWG----EALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
10-386 |
3.95e-111 |
|
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: 329.70 E-value: 3.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 10 RAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLML 89
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 NESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEF-RRMIDFHRGIECAGTF 168
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFvQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPAD--TTVPRIQL 246
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSAdmSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 247 VPAMSVRARVTRVARPAVGEGVGYGLTYrVPKPSIQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaV 326
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIM--V 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 327 DVNdarayrPVEPVERGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:TIGR00492 318 DLG------PDLQDKTGDEVILWG----EEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
16-236 |
1.24e-76 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 235.97 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNESPLQ 95
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 96 SIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHFATAD 175
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACAD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553755746 176 VVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPeLHNDMCRVGIGLYGLHP 236
Cdd:pfam01168 161 EPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-385 |
1.58e-45 |
|
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: 152.61 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 249 AMSVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNnMDVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDT-RIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLM--VDV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553755746 329 NDarayrpVEPVERGDLVTVMgvdGDEEITADEMARRRGTINYEVTCDFGMRLEKVF 385
Cdd:smart01005 77 TD------IPDVKVGDEVVLF---GPQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
12-386 |
1.43e-167 |
|
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: 472.75 E-value: 1.43e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 12 AWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNE 91
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 92 SPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHF 171
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 172 ATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPRIQLVPAMS 251
Cdd:cd00430 162 ATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPLGLKPVMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 252 VRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVDVNDa 331
Cdd:cd00430 242 LKARVVQVKTVPAGEGVSYGRTYTAPRPT-RIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTM--VDVTD- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2553755746 332 rayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:cd00430 318 -----IPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
9-386 |
4.92e-162 |
|
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: 458.80 E-value: 4.92e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 9 TRAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLM 88
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 89 LNESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTF 168
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPRIQLVP 248
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 249 AMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTR-IATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIM--VDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553755746 329 NDarayrpVEPVERGDLVTVMGVDGdeeITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:COG0787 318 TD------IPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYV 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
10-386 |
1.77e-130 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 378.75 E-value: 1.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 10 RAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLML 89
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 NESPLQS-IDVLLEYDIMPSVYDMDFALAYgeRAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTF 168
Cdd:PRK00053 82 GGFFPAEdLPLIIAYNLTTAVHSLEQLEAL--EKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCglVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPR-IQLV 247
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKGKPL--RHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLdFGLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 248 PAMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVD 327
Cdd:PRK00053 238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTR-IAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLT--VD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553755746 328 VNDARAYRPvepverGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:PRK00053 315 LGPDPQDKV------GDEVTLWG----EALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
10-386 |
3.95e-111 |
|
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: 329.70 E-value: 3.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 10 RAAWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLML 89
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 NESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEF-RRMIDFHRGIECAGTF 168
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFvQKLRQLKKFLELEGIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPAD--TTVPRIQL 246
Cdd:TIGR00492 161 SHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSAdmSDGAPFGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 247 VPAMSVRARVTRVARPAVGEGVGYGLTYrVPKPSIQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaV 326
Cdd:TIGR00492 241 KPVLSLTSKIIQVRTVKKGEPVSYGGTF-TAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIM--V 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 327 DVNdarayrPVEPVERGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:TIGR00492 318 DLG------PDLQDKTGDEVILWG----EEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
12-385 |
9.05e-110 |
|
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: 326.23 E-value: 9.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 12 AWVEVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNE 91
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 92 SPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALdkvgKYHLAIDTGMSRIGVMPEDAVEFRRMIDFhRGIECAGTFTHF 171
Cdd:cd06825 82 TPPVRAKELKKYSLTQTLISEAYAEELSKYAVNI----KVHLKVDTGMHRLGESPEDIDSILAIYRL-KNLKVSGIFSHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 172 ATADVVGDWDF---RQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGL--HPADTTVPRIQL 246
Cdd:cd06825 157 CVSDSLDEDDIaftKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVlsDPNDPTKLGLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 247 VPAMSVRARVTRVARPAVGEGVGYGLTYrVPKPSIQIATVPIGYADGLSRSLSN-NMDVLVRGQRARQVGRICMDQFMfa 325
Cdd:cd06825 237 RPVLSLKAKVILVRKVAKGEAVGYGRLF-VASRTTRIATVSIGYADGYPRSLSNqKAYVLINGKRAPIIGNICMDQLM-- 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 326 VDVNDarayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVF 385
Cdd:cd06825 314 VDVTD------IPEVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
15-385 |
6.99e-89 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 285.31 E-value: 6.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 15 EVDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNESPl 94
Cdd:PRK11930 463 EINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEP- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 95 QSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVG-KYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHFAT 173
Cdd:PRK11930 542 TSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGyPIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKVRSVFSHLAG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 174 ADvvgDWDF----RQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVPRIQLVpa 249
Cdd:PRK11930 622 SD---DPDHddftRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQALRNV-- 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 250 MSVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNM-DVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:PRK11930 697 STLKTTILQIKHVPKGETVGYGRKGVVTKPS-RIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDMCM--IDV 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553755746 329 NDArayrpvePVERGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVF 385
Cdd:PRK11930 774 TDI-------DAKEGDEVIIFG----EELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
16-236 |
1.24e-76 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 235.97 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRAFKALLRPGVQMMCAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNESPLQ 95
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 96 SIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHFATAD 175
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACAD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553755746 176 VVGDWDFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGTVLHPeLHNDMCRVGIGLYGLHP 236
Cdd:pfam01168 161 EPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
14-375 |
1.75e-76 |
|
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: 240.48 E-value: 1.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 14 VEVDLNAVRKNTRAFKALLrPGVQMMCAVKADAYGHGAVECARAMhaSGASQFAVATVDEGVELRKAGIEWPVLMLnESP 93
Cdd:cd06827 4 ATIDLAALRHNLRLVRELA-PNSKILAVVKANAYGHGLVRVAKAL--ADADGFAVACIEEALALREAGITKPILLL-EGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 94 LQSIDVLL--EYDIMPSVYDMDfALAYGERAvALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHF 171
Cdd:cd06827 80 FSADELPLaaEYNLWTVVHSEE-QLEWLEQA-ALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 172 ATADVVGDWDFRQQSTRFMDTVGALRdagldcGLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHP-ADTTVPRIQLVPAM 250
Cdd:cd06827 158 ACADEPDSPGTAKQLAIFEQATAGLP------GPRSLANSAAILAWPEAHGDWVRPGIMLYGASPfADKSGADLGLKPVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 251 SVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDqfMFAVDVND 330
Cdd:cd06827 232 TLSSEIIAVRELKAGESVGYGATWTAPRPM-RIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMD--MLTVDLTD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2553755746 331 arayrpVEPVERGDLVTVMGvdgdEEITADEMARRRGTINYEVTC 375
Cdd:cd06827 309 ------LPEAKVGDPVELWG----KGLPVDEVAAAAGTIGYELLC 343
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
7-386 |
1.44e-68 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 221.81 E-value: 1.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 7 PQTRAAWVEVDLNAVRKNTRAFKALLRPGVQMmCAV-KADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWP 85
Cdd:PRK13340 36 IQPRNAWLEISPGAFRHNIKTLRSLLANKSKV-CAVmKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 86 VLMLNESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDT-GMSRIGVMP------EDAVEfrrmIDF 158
Cdd:PRK13340 115 LLRVRSASPAEIEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLDMstargkWEALR----IAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 159 HRGIECAGTFTHFATADVVgdwDFRQQSTRF-MDTVGALRDAGLDCGLV--HCDNTPGTVLHPELHNDMCRVGIGLYG-L 234
Cdd:PRK13340 191 LPSLGIVGIMTHFPNEDED---EVRWKLAQFkEQTAWLIGEAGLKREKItlHVANSYATLNVPEAHLDMVRPGGILYGdR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 235 HPADTTVPRIqlvpaMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQV 314
Cdd:PRK13340 268 HPANTEYKRI-----MTFKSRIASVNTLPKGSTVGYDRTFTLKRDSR-LANLPVGYSDGYPRHASNKAPVLINGQRAPVV 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553755746 315 GRICMDQFMfaVDVNDarayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:PRK13340 342 GRVSMNTLM--VDVTD------IPNVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYV 405
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
12-386 |
2.05e-57 |
|
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: 191.40 E-value: 2.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 12 AWVEVDLNAVRKNTRAFKALLRPGVQMmCAV-KADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLN 90
Cdd:cd06826 2 AWLEISTGAFENNIKLLKKLLGGNTKL-CAVmKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 91 ESPLQSIDVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDT-GMSRIGV-MPEDA--VEFRRMIDFhRGIECAG 166
Cdd:cd06826 81 TATPSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLeLSTAQgkEDAVAIATL-PNLKIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 167 TFTHFATADV----VGDWDFRQQSTRFMDtVGALRDAGLdcgLVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTTVP 242
Cdd:cd06826 160 IMTHFPVEDEddvrAKLARFNEDTAWLIS-NAKLKREKI---TLHAANSFATLNVPEAHLDMVRPGGILYGDTPPSPEYK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 243 RIqlvpaMSVRARVTRVARPAVGEGVGYGLTYRVPKPSIqIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQF 322
Cdd:cd06826 236 RI-----MSFKSRVASLNTYPKGSTVGYDRTFTLTRDSL-LANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTV 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553755746 323 MfaVDVNDarayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:cd06826 310 M--VDVTD------IPGVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
249-385 |
1.29e-55 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 178.71 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 249 AMSVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDT-RIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLM--VDV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553755746 329 NDarayrpVEPVERGDLVTVMGVDGDEEITADEMARRRGTINYEVTCDFGMRLEKVF 385
Cdd:pfam00842 78 TD------VPEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
9-386 |
6.65e-54 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 181.85 E-value: 6.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 9 TRAAWVEVDLNAVRKNTRAFKALlRPGVQMMCAVKADAYGHGAVECARAMhaSGASQFAVATVDEGVELRKAGIEWPVLM 88
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREA-APGARVWSVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRERGWKGPILM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 89 L----NESPLQSIDvllEYDIMPSVYDMdFALAYGERAvALDKVGKYHLAIDTGMSRIGVMPEDAVE-FRRMidfhRGIE 163
Cdd:PRK03646 78 LegffHAQDLELYD---QHRLTTCVHSN-WQLKALQNA-RLKAPLDIYLKVNSGMNRLGFQPERVQTvWQQL----RAMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 164 CAGTFT---HFATADVVGDWDfrQQSTRFmdtvgALRDAGLDCGlVHCDNTPGTVLHPELHNDMCRVGIGLYGLHPADTT 240
Cdd:PRK03646 149 NVGEMTlmsHFARADHPDGIS--EAMARI-----EQAAEGLECE-RSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 241 VPRIQ--LVPAMSVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNNMDVLVRGQRARQVGRIC 318
Cdd:PRK03646 221 RDIANtgLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQ-RIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVS 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553755746 319 MDqfMFAVDVNdarayrPVEPVERGDLVTVMGvdgdEEITADEMARRRGTINYEVTCDFGMRLEKVFV 386
Cdd:PRK03646 300 MD--MLAVDLT------PCPQAGIGTPVELWG----KEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-385 |
1.58e-45 |
|
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: 152.61 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 249 AMSVRARVTRVARPAVGEGVGYGLTYRVPKPSiQIATVPIGYADGLSRSLSNnMDVLVRGQRARQVGRICMDQFMfaVDV 328
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDT-RIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLM--VDV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553755746 329 NDarayrpVEPVERGDLVTVMgvdGDEEITADEMARRRGTINYEVTCDFGMRLEKVF 385
Cdd:smart01005 77 TD------IPDVKVGDEVVLF---GPQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
21-229 |
1.28e-25 |
|
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: 102.78 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 21 VRKNTRAFKALLRPGVQMMCAVKADAyghgAVECARAMhASGASQFAVATVDEGVELRKAGI-EWPVLMLNESPLQS--I 97
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTL-AALGTGFDVASLGEALLLRAAGIpPEPILFLGPCKQVSelE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 98 DVLLEYDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTG--MSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHFATAD 175
Cdd:cd06808 76 DAAEQGVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSAD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553755746 176 vvGDWD-FRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGT---VLHPELHNDMCRVGI 229
Cdd:cd06808 156 --EDYSpFVEALSRFVAALDQLGELGIDLEQLSIGGSFAIlylQELPLGTFIIVEPGR 211
|
|
| YhfX |
COG3457 |
Predicted amino acid racemase [Amino acid transport and metabolism]; |
14-172 |
1.79e-11 |
|
Predicted amino acid racemase [Amino acid transport and metabolism];
Pssm-ID: 442680 [Multi-domain] Cd Length: 356 Bit Score: 64.83 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 14 VEVDLNAVRKNTRAFKALLRP-GVQMMCAVKAdayGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLNES 92
Cdd:COG3457 6 LVIDLDKIRENARRLVELAAKhGIELYGVTKQ---FGGNPEIAKALLDGGIKGIVDSRIKNLKKLKRAGIPHPGHLLRIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 93 PLQSIDVLLEY-DIMpSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFTHF 171
Cdd:COG3457 83 MLSEVEEVVRYaDIS-LNSELETARALSEAAKKQGKVHKVILMVDLGDLREGGFPEELVDTVEEILKLPGIELAGLGTNL 161
|
.
gi 2553755746 172 A 172
Cdd:COG3457 162 P 162
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
16-262 |
3.54e-08 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 54.75 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRAFKALLRP-GVQMMCAVKAdaygHGAVECARAMHASGASQFAVATVDEGVELRKAGIEWpVLMLNESP- 93
Cdd:COG3616 13 LDLDALERNIARMAARAAAhGVRLRPHGKT----HKSPELARRQLAAGAWGITVATLAEAEVLAAAGVDD-ILLAYPLVg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 94 ---LQSIDVLLEYDIMPSVY--DMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMP-EDAVEFRRMIDFHRGIECAGT 167
Cdd:COG3616 88 pakLARLAALARAGARLTVLvdSVEQAEALAAAAAAAGRPLRVLVELDVGGGRTGVRPpEAALALARAIAASPGLRLAGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 168 FTHFATADVVGDWDFRQQS-----TRFMDTVGALRDAGLDCGLVHCDNTPG-TVLHPELHNDMCRVGIGLYGLHPADTTV 241
Cdd:COG3616 168 MTYEGHIYGADDAEERRAAareelARLAAAAEALRAAGLPCPIVSGGGTPTfDFVADLPGVTELRPGSYVFHDAGYYRYG 247
|
250 260
....*....|....*....|.
gi 2553755746 242 PRIQLVPAMSVRARVTRVARP 262
Cdd:COG3616 248 VCFPFDPALSVLATVVSRPEP 268
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
16-214 |
3.16e-07 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; Low specificity D-threonine aldolase (Low specificity D-TA, EC 4.3.1.18), encoded by dtaAS gene from Arthrobacter sp. strain DK-38, is the prototype of this subfamily. Low specificity D-TAs are fold type III PLP-dependent enzymes that catalyze the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Members of this subfamily show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143493 [Multi-domain] Cd Length: 358 Bit Score: 51.83 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRA-FKALLRPGVqmmcAVKADAYGHGAVECARAMHASGASQFAVATVDEGVELRKAGIEwPVLMLNE-SP 93
Cdd:cd06819 12 LDLDALERNIKRmAAFAKAHGV----RLRPHAKTHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIR-DILITNEvVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 94 LQSIDVLLE----YDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMP-EDAVEFRRMIDFH-----RGIE 163
Cdd:cd06819 87 PAKIARLAAlarrAPLIVCVDHPDNVRALAAAAVEAGVRLDVLVEIDVGQGRCGVPPgEAALALARTIAALpglrfAGLQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2553755746 164 C-AGTFTHFATADvvgdwDFRQQSTRFM----DTVGALRDAGLDCGLVHCDNTpGT 214
Cdd:cd06819 167 AyHGHLQHIRDYE-----ERRAAIAEAAealqATRDALEAAGLPCEIVTGGGT-GT 216
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
14-172 |
1.68e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 49.47 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 14 VEVDLNAVRKNTRAFKALLRP-GVQMMCAVKADAyghGAVECARAMHASGASQFAVATVDEGVELRKAGIEWPVLMLnES 92
Cdd:cd06815 4 LEINLSKIRHNAKVLVELCKSrGIEVTGVTKVVC---GDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLL-RI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 93 PLQS-IDVLLEY-DI-MPSvyDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMIDFHRGIECAGTFT 169
Cdd:cd06815 80 PMLSeVEDVVKYaDIsLNS--ELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIELVGIGT 157
|
...
gi 2553755746 170 HFA 172
Cdd:cd06815 158 NLG 160
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
16-214 |
2.19e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine Aldolase-like; This subfamily is composed of uncharacterized bacterial proteins with similarity to low specificity D-threonine aldolase (D-TA), which is a fold type III PLP-dependent enzyme that catalyzes the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Low specificity D-TAs show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143494 [Multi-domain] Cd Length: 353 Bit Score: 46.15 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRAFKALLRP-GVQMMCAVKAdaygHGAVECARAMHASGASQFAVATVDEGVELRKAGIE-----WPVLml 89
Cdd:cd06820 8 IDLDRLERNIARMQAYADAhGLSLRPHIKT----HKSPEIARLQLAAGAIGITVATVGEAEVMADAGLSdifiaYPIV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 NESPLQSIDVLLE-YDIMPSVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVM-PEDAVEFRRMIDFHRGIECAGT 167
Cdd:cd06820 82 GRQKLERLRALAErVTLSVGVDSAEVARGLAEVAEGAGRPLEVLVEVDSGMNRCGVQtPEDAVALARAIASAPGLRFRGI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553755746 168 FTHFATADVVGDW--DFRQQSTRFMDTVGALRDAGLDCGLVHCDNTPGT 214
Cdd:cd06820 162 FTYPGHSYAPGALeeAAADEAEALLAAAGILEEAGLEPPVVSGGSTPTL 210
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
20-266 |
3.91e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 38.98 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 20 AVRKNTRAFKALLRP-GVQMMCAVKAdaygHGAVECARAMHASGASQFAVATVDEGVELRKAGIEwPVLMLNESPLQ-SI 97
Cdd:cd07376 1 ALEANISRMAARARAsGVRLRPHVKT----HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVK-DILMAYPLVGPaAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 98 DVLL-------EYDIMpsVYDMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMPEDAVEFRRMI--DFHRGIECAGTF 168
Cdd:cd07376 76 ARLAgllrqeaEFHVL--VDSPEALAALAAFAAAHGVRLRVMLEVDVGGHRSGVRPEEAAALALADavQASPGLRLAGVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 169 THFATADVVGDWDFRQQSTRfmDTVGALRDA------GLDCGLVHCDNTPGTVLH-PELHNDMCRVGIGLYGLHPADTTV 241
Cdd:cd07376 154 AYEGHIYGAGGAREGAQARD--QAVAAVRAAaaaaerGLACPTVSGGGTPTYQLTaGDRAVTELRAGSYVFMDTGFDTLG 231
|
250 260
....*....|....*....|....*.
gi 2553755746 242 PRIQLVPAMsvraRVTRVA-RPAVGE 266
Cdd:cd07376 232 ACAQRPAAF----RVTTVIsRPAPTG 253
|
|
| PLPDE_III_DapDC |
cd06828 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ... |
17-202 |
4.96e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143501 [Multi-domain] Cd Length: 373 Bit Score: 38.62 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 17 DLNAVRKNTRAFK-ALLRPGVQMMCAVKA----------DAYGHGAV-----ECARAMHASGASQ---F-AVATVDEgvE 76
Cdd:cd06828 9 DEATIRENYRRLKeAFSGPGFKICYAVKAnsnlailkllAEEGLGADvvsggELYRALKAGFPPErivFtGNGKSDE--E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 77 LRKAgIEWPVLMLNesplqsIDVLLEYDIMPSVydmdfALAYGERA-VAL----DKVGKYHLAIDTGM--SRIGVMPEDA 149
Cdd:cd06828 87 LELA-LELGILRIN------VDSLSELERLGEI-----APELGKGApVALrvnpGVDAGTHPYISTGGkdSKFGIPLEQA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553755746 150 VEFRRMIDFHRGIECAGtfTHFATADVVGDWD-FRQQSTRFMDTVGALRDAGLD 202
Cdd:cd06828 155 LEAYRRAKELPGLKLVG--LHCHIGSQILDLEpFVEAAEKLLDLAAELRELGID 206
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
16-212 |
5.35e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143495 [Multi-domain] Cd Length: 361 Bit Score: 38.43 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 16 VDLNAVRKNTRAFKAL------LRPGVQMmcavkadaygHGAVECARAMHASGASQFAVATVDEGVELRKAGIEwpvlml 89
Cdd:cd06821 14 VYPDRIEENIRRMIRMagdpqrLRPHVKT----------HKMAEIVRLQLEAGITKFKCATIAEAEMLAEAGAP------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553755746 90 nesplqsiDVLLEY-----------DIM---PSVY------DMDFALAYGERAVALDKVGKYHLAIDTGMSRIGVMP-ED 148
Cdd:cd06821 78 --------DVLLAYplvgpnierflELAkkyPGTRfsalvdDLEAAEALSAAAGSAGLTLSVLLDVNTGMNRTGIAPgED 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553755746 149 AVEFRRMIDFHRGIECAGTFT---HFATADVvgdwDFRQQST-----RFMDTVGALRDAGLDCGLVHCDNTP 212
Cdd:cd06821 150 AEELYRAIATLPGLVLAGLHAydgHHRNTDL----AEREAAAdaaykPVLALREALEAAGLPVPELVAGGTP 217
|
|
| |
