|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-371 |
0e+00 |
|
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: 524.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEkSVQEIIELNKLEYIDLEGMFT 166
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEE-AEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 167 HFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVfKDRLELRP 246
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEV-KSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 247 AMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNP-KVLIKGEVFDVVGRICMDQIMVRIDKD 325
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKgEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 326 IDIKVGDEVILFGE---GEVTAERIAKDLGTINYEVLCMISRRVDRVYM 371
Cdd:cd00430 319 PDVKVGDEVVLFGRqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-373 |
0e+00 |
|
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: 511.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLEGMF 165
Cdd:COG0787 83 GVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEE--APALAArLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 166 THFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDrLELR 245
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAAD-LGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 246 PAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRICMDQIMVRIDK 324
Cdd:COG0787 240 PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNgGPVLINGKRAPIVGRVSMDQIMVDVTD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 325 DIDIKVGDEVILFGEGEVTAERIAKDLGTINYEVLCMISRRVDRVYMEN 373
Cdd:COG0787 320 IPDVKVGDEVVLFGEQGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-370 |
1.93e-150 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 429.21 E-value: 1.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPD-EAFEDSIKNKITMTVYSLETAQKINEIakSLGEKACVHVKIDSGMTRIGFQPNEkSVQEIIELNKLEYIDLEGMF 165
Cdd:PRK00053 83 GFFPaEDLPLIIAYNLTTAVHSLEQLEALEKA--ELGKPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 166 THFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAikHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDRLELR 245
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKGKPLR--HLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 246 PAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTR-IQKNPKVLIKGEVFDVVGRICMDQIMVRIDK 324
Cdd:PRK00053 238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRnLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497589597 325 DIDIKVGDEVILFGEGeVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:PRK00053 318 DPQDKVGDEVTLWGEA-LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-371 |
5.39e-124 |
|
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: 362.44 E-value: 5.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEK--SVQEIIELNKLEyiDLEGM 164
Cdd:TIGR00492 82 GFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAalFVQKLRQLKKFL--ELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 165 FTHFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDV-FKDRLE 243
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMsDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 244 LRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRICMDQIMVRI 322
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNgTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 323 DKDIDIKVGDEVILFGEgEVTAERIAKDLGTINYEVLCMISRRVDRVYM 371
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGE-EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
12-233 |
3.27e-89 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 268.32 E-value: 3.27e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 12 INLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYTPDE 91
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 92 AFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLEGMFTHFAT 170
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEE--ALALLArLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497589597 171 ADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDlRLNMVRAGIILYGHYP 233
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
247-370 |
3.82e-60 |
|
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: 190.36 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 247 AMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNPKVLIKGEVFDVVGRICMDQIMVRIDKDI 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497589597 327 DIKVGDEVILFGEGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:smart01005 81 DVKVGDEVVLFGPQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
7-371 |
0e+00 |
|
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: 524.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEkSVQEIIELNKLEYIDLEGMFT 166
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEE-AEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 167 HFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVfKDRLELRP 246
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEV-KSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 247 AMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNP-KVLIKGEVFDVVGRICMDQIMVRIDKD 325
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKgEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 326 IDIKVGDEVILFGE---GEVTAERIAKDLGTINYEVLCMISRRVDRVYM 371
Cdd:cd00430 319 PDVKVGDEVVLFGRqgdEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-373 |
0e+00 |
|
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: 511.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:COG0787 3 PAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLEGMF 165
Cdd:COG0787 83 GVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEE--APALAArLAALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 166 THFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDrLELR 245
Cdd:COG0787 161 SHFACADEPDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAAD-LGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 246 PAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRICMDQIMVRIDK 324
Cdd:COG0787 240 PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNgGPVLINGKRAPIVGRVSMDQIMVDVTD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 325 DIDIKVGDEVILFGEGEVTAERIAKDLGTINYEVLCMISRRVDRVYMEN 373
Cdd:COG0787 320 IPDVKVGDEVVLFGEQGITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-370 |
1.93e-150 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 429.21 E-value: 1.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPD-EAFEDSIKNKITMTVYSLETAQKINEIakSLGEKACVHVKIDSGMTRIGFQPNEkSVQEIIELNKLEYIDLEGMF 165
Cdd:PRK00053 83 GFFPaEDLPLIIAYNLTTAVHSLEQLEALEKA--ELGKPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 166 THFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAikHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDRLELR 245
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGKGKPLR--HLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 246 PAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTR-IQKNPKVLIKGEVFDVVGRICMDQIMVRIDK 324
Cdd:PRK00053 238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRnLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497589597 325 DIDIKVGDEVILFGEGeVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:PRK00053 318 DPQDKVGDEVTLWGEA-LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-371 |
5.39e-124 |
|
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: 362.44 E-value: 5.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEK--SVQEIIELNKLEyiDLEGM 164
Cdd:TIGR00492 82 GFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAalFVQKLRQLKKFL--ELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 165 FTHFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDV-FKDRLE 243
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMsDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 244 LRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRICMDQIMVRI 322
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNgTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497589597 323 DKDIDIKVGDEVILFGEgEVTAERIAKDLGTINYEVLCMISRRVDRVYM 371
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGE-EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
7-370 |
2.48e-107 |
|
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: 319.68 E-value: 2.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:cd06825 1 RAWLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 YTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGekacVHVKIDSGMTRIGFQPNEksVQEIIELNKLEYIDLEGMFT 166
Cdd:cd06825 81 YTPPVRAKELKKYSLTQTLISEAYAEELSKYAVNIK----VHLKVDTGMHRLGESPED--IDSILAIYRLKNLKVSGIFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 167 HFATADEVSKE---YTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGhYPSD--DVFKDR 241
Cdd:cd06825 155 HLCVSDSLDEDdiaFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYG-VLSDpnDPTKLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 242 LELRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNPK--VLIKGEVFDVVGRICMDQIM 319
Cdd:cd06825 234 LDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQKayVLINGKRAPIIGNICMDQLM 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497589597 320 VRIDKDIDIKVGDEVILFG---EGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:cd06825 314 VDVTDIPEVKEGDTATLIGqdgDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
11-370 |
3.23e-101 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 317.67 E-value: 3.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 11 EINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYTPd 90
Cdd:PRK11930 463 EINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEP- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 91 EAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKAC-VHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLEGMFTHF 168
Cdd:PRK11930 542 TSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYpIHIKIDTGMHRLGFEPED--IPELARrLKKQPALKVRSVFSHL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 169 ATADE-VSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDdvfKDRLELRPA 247
Cdd:PRK11930 620 AGSDDpDHDDFTRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASG---AGQQALRNV 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 248 MKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN--PKVLIKGEVFDVVGRICMDQIMVRIdKD 325
Cdd:PRK11930 697 STLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNgvGYVLVNGQKAPIVGNICMDMCMIDV-TD 775
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497589597 326 IDIKVGDEVILFGEgEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:PRK11930 776 IDAKEGDEVIIFGE-ELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
7-370 |
9.08e-99 |
|
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: 297.49 E-value: 9.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNNIKNLLEEDiKICGVIKADAYGHGAVEVAKLLEKekVDYLAVARTAEGIELRQNGITLPILNLG 86
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNS-KILAVVKANAYGHGLVRVAKALAD--ADGFAVACIEEALALREAGITKPILLLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 87 --YTPDEaFEDSIKNKITMTVYSletAQKINEIAKSLGEKAC-VHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLE 162
Cdd:cd06827 78 gfFSADE-LPLAAEYNLWTVVHS---EEQLEWLEQAALSKPLnVWLKLDSGMHRLGFSPEE--YAAAYQrLKASPNVASI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 163 GMFTHFATADEVSKEYTYKQAnnykfmsDKLDEAGVKIAIKH-VSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDR 241
Cdd:cd06827 152 VLMTHFACADEPDSPGTAKQL-------AIFEQATAGLPGPRsLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 242 LELRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN--PkVLIKGEVFDVVGRICMDQIM 319
Cdd:cd06827 225 LGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSgtP-VLVNGQRTPLVGRVSMDMLT 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 497589597 320 VRIDKDIDIKVGDEVILFGEGeVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:cd06827 304 VDLTDLPEAKVGDPVELWGKG-LPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
12-233 |
3.27e-89 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 268.32 E-value: 3.27e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 12 INLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYTPDE 91
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 92 AFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEksVQEIIE-LNKLEYIDLEGMFTHFAT 170
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEE--ALALLArLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497589597 171 ADEVSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIMDCPDlRLNMVRAGIILYGHYP 233
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
2-370 |
9.55e-79 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 248.00 E-value: 9.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 2 QKITVPTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLP 81
Cdd:PRK13340 35 QIQPRNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 82 ILNL-GYTPDEaFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDS-GMTRIGFQP-NEKSVQEIIELNKLEY 158
Cdd:PRK13340 115 LLRVrSASPAE-IEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLDMsTARGKWEALRIATLPS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 159 IDLEGMFTHFATADEvskEYTYKQANNYKFMSDKL-DEAGVKIA--IKHVSNSAAIMDCPDLRLNMVRAGIILYGhypsd 235
Cdd:PRK13340 194 LGIVGIMTHFPNEDE---DEVRWKLAQFKEQTAWLiGEAGLKREkiTLHVANSYATLNVPEAHLDMVRPGGILYG----- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 236 DVFKDRLELRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRIC 314
Cdd:PRK13340 266 DRHPANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNkAPVLINGQRAPVVGRVS 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 497589597 315 MDQIMVRIDKDIDIKVGDEVILFG---EGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:PRK13340 346 MNTLMVDVTDIPNVKPGDEVVLFGkqgNAEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
9-370 |
3.10e-64 |
|
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: 209.12 E-value: 3.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 9 WAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYT 88
Cdd:cd06826 3 WLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 89 PDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKIDS-GMTRIGFQPNE-KSVQEIIELNKLEYIDLEGMFT 166
Cdd:cd06826 83 TPSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLELSTaQGKEDAVAIATLPNLKIVGIMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 167 HFAT--ADEV-SKEYTYKQANNYKFMSDKLDEAGVKIaikHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDdvfkdrLE 243
Cdd:cd06826 163 HFPVedEDDVrAKLARFNEDTAWLISNAKLKREKITL---HAANSFATLNVPEAHLDMVRPGGILYGDTPPS------PE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 244 LRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGRICMDQIMVRI 322
Cdd:cd06826 234 YKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNkAHVLINGQRVPVVGKVSMNTVMVDV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 497589597 323 DKDIDIKVGDEVILFG---EGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:cd06826 314 TDIPGVKAGDEVVLFGkqgGAEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
247-370 |
3.82e-60 |
|
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: 190.36 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 247 AMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNPKVLIKGEVFDVVGRICMDQIMVRIDKDI 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 497589597 327 DIKVGDEVILFGEGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:smart01005 81 DVKVGDEVVLFGPQEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
247-370 |
8.95e-59 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 186.80 E-value: 8.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 247 AMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKNPK-VLIKGEVFDVVGRICMDQIMVRIDKD 325
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGeVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 497589597 326 IDIKVGDEVILFG---EGEVTAERIAKDLGTINYEVLCMISRRVDRVY 370
Cdd:pfam00842 81 PEVKVGDEVTLFGkqgDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
7-371 |
3.65e-54 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 182.62 E-value: 3.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 7 PTWAEINLDNLRFNLNnIKNLLEEDIKICGVIKADAYGHGAVEVAKLLEKekVDYLAVARTAEGIELRQNGITLPILNL- 85
Cdd:PRK03646 3 PIQASLDLQALKQNLS-IVREAAPGARVWSVVKANAYGHGIERIWSALGA--TDGFAVLNLEEAITLRERGWKGPILMLe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 86 GYTPDEAFEDSIKNKITMTVYSLETAQKInEIAKsLGEKACVHVKIDSGMTRIGFQPNEKSV--QEIIELNKLEYIDLeg 163
Cdd:PRK03646 80 GFFHAQDLELYDQHRLTTCVHSNWQLKAL-QNAR-LKAPLDIYLKVNSGMNRLGFQPERVQTvwQQLRAMGNVGEMTL-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 164 mFTHFATADEVskeytykqannykfmsDKLDEAGVKI--------AIKHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSD 235
Cdd:PRK03646 156 -MSHFARADHP----------------DGISEAMARIeqaaegleCERSLSNSAATLWHPQAHFDWVRPGIILYGASPSG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 236 dVFKDRLE--LRPAMKLKSKIGHIKQVEPGVGISYGLKYTTTGKETIATVPIGYADGFTRIQKN-PKVLIKGEVFDVVGR 312
Cdd:PRK03646 219 -QWRDIANtgLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTgTPVLVDGVRTRTVGT 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 497589597 313 ICMDQIMVRIDKDIDIKVGDEVILFGEgEVTAERIAKDLGTINYEVLCMISRRVDRVYM 371
Cdd:PRK03646 298 VSMDMLAVDLTPCPQAGIGTPVELWGK-EIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
17-226 |
6.28e-31 |
|
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: 117.03 E-value: 6.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 17 LRFNLNNIKNLLEEDIKICGVIKADAyghgAVEVAKLLEKEkVDYLAVARTAEGIELRQNGI-TLPILNLGYTPDEA-FE 94
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTLAAL-GTGFDVASLGEALLLRAAGIpPEPILFLGPCKQVSeLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 95 DSIKNK-ITMTVYSLETAQKINEIAKSLGEKACVHVKIDSG--MTRIGFQPNEksVQEIIE-LNKLEYIDLEGMFTHFAT 170
Cdd:cd06808 76 DAAEQGvIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGdeNGKFGVRPEE--LKALLErAKELPHLRLVGLHTHFGS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497589597 171 ADEvSKEYTYKQANNYKFMSDKLDEAGVKIAIKHVSNSAAIM---DCPDLRLNMVRAGI 226
Cdd:cd06808 154 ADE-DYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILylqELPLGTFIIVEPGR 211
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
11-169 |
3.76e-08 |
|
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: 54.47 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 11 EINLDNLRFNLNNIKNLLEE-DIKICGVIKADAyghGAVEVAKLLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYTP 89
Cdd:cd06815 5 EINLSKIRHNAKVLVELCKSrGIEVTGVTKVVC---GDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLLRIPM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 90 DEAFEDSIKN-KITMtVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNE--KSVQEIIelnKLEYIDLEGMFT 166
Cdd:cd06815 82 LSEVEDVVKYaDISL-NSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDllDFVEEIL---KLPGIELVGIGT 157
|
...
gi 497589597 167 HFA 169
Cdd:cd06815 158 NLG 160
|
|
| PLPDE_III_yhfX_like |
cd06811 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ... |
49-200 |
1.16e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the uncharacterized protein yhfX from Escherichia coli K-12 and similar bacterial proteins. These proteins are homologous to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143486 Cd Length: 382 Bit Score: 49.97 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 49 EVAKLLEKEKVDYLAVARTAEGIELRQNGItlPILNLGY---TPDEAFEDSIKNKI-TMTVYSLETAQKINEIAKSLGEK 124
Cdd:cd06811 68 FLARALLEAGIPGAVAVDFKEARALHEAGL--PLGHVGHlvqIPRHQVPAVLAMRPeVITVYSLEKAREISDAAVELGRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 125 ACVHVKIDSGMTRI------GFqPNEKSVQEIIELNKLEYIDLEGMfTHFAT--ADEVSKEYTYkqANNYKFM---SDKL 193
Cdd:cd06811 146 QDVLLRVYGDEDTLypgqegGF-PLEELPAVLAAIKALPGIRIAGL-TSFPCflYDEEQGDIAP--TPNLFTLlkaKELL 221
|
....*..
gi 497589597 194 DEAGVKI 200
Cdd:cd06811 222 EKRGIEI 228
|
|
| PLPDE_III_MccE_like |
cd06841 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of ... |
82-170 |
2.53e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme MccE; This subfamily is composed of uncharacterized proteins with similarity to Escherichia coli MccE, a hypothetical protein that is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. ODC participates in the formation of putrescine by catalyzing the decarboxylation of ornithine, the first step in polyamine biosynthesis. DapDC participates in the last step of lysine biosynthesis, the conversion of meso-2,6-diaminoheptanedioate to L-lysine. Most members of this subfamily share the same domain architecture as ODC and DapDC. A few members, including Escherichia coli MccE, contain an additional acetyltransferase domain at the C-terminus.
Pssm-ID: 143508 [Multi-domain] Cd Length: 379 Bit Score: 39.55 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497589597 82 ILNLGYTPDEAFEDSIKNKITMTVYSLETAQKINEIAKSLGEKACVHVKI-----DSGMTRIGFQPNE--KSVQEIIELN 154
Cdd:cd06841 82 IFNGPYKSKEELEKALEEGALINIDSFDELERILEIAKELGRVAKVGIRLnmnygNNVWSRFGFDIEEngEALAALKKIQ 161
|
90
....*....|....*.
gi 497589597 155 KLEYIDLEGMFTHFAT 170
Cdd:cd06841 162 ESKNLSLVGLHCHVGS 177
|
|
| |
