|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-368 |
3.91e-161 |
|
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: 456.57 E-value: 3.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 8 SAYMNVDLNAVASNFKVFST-LHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLG 86
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRlLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 87 VLPAKDIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKtYQEVIEIIQQYEQLVFEGVF 166
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQA-EALSAAAARLGKTLKVHLKIDTGMGRLGFRPEE-AEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 167 THFACADEPG-DMTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVqqKVKVHL 241
Cdd:cd00430 159 THFATADEPDkAYTRRQLERFLEALAELeeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEV--KSPLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 242 KPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIM-QGSFVNVIGHQCEVIGRVCMDQTIVKVP 320
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 613062023 321 D--QVKAGDSVILIDNHRESPQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:cd00430 317 DipDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-371 |
5.22e-161 |
|
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: 456.11 E-value: 5.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 6 YRSAYMNVDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILV 84
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 85 LGVLPAKDIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIkDTKTYQEVIEIIQQYEQLVFEG 164
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQL-EALAAAARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 165 VFTHFACADEPGD-MTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQkvKV 239
Cdd:COG0787 159 IMSHFACADEPDHpFTAEQLERFEEAVAALpaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAA--DL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 240 HLKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQ-GSFVNVIGHQCEVIGRVCMDQTIVK 318
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 613062023 319 VPD--QVKAGDSVILIDNHRespQSVEVAAEKQHTINYEVLCNLSRRLPRIYHDG 371
Cdd:COG0787 317 VTDipDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-368 |
3.64e-132 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 382.60 E-value: 3.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVFSTLHPNKT-VMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVL 85
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSkLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLP-AKDIDKAIQHRVALTVPSKQWLkEAIKNIsgEQEKKLWLHIKLDTGMGRLGIKDTKtYQEVIEIIQQYEQLVFEG 164
Cdd:PRK00053 82 GGFFpAEDLPLIIAYNLTTAVHSLEQL-EALEKA--ELGKPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNVRLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 165 VFTHFACADEP-GDMTTEQYHRFKDMVNEAIKP--EYIHCQNSAGSLLM-DCQFcNAIRPGISLYGYYPSEYVQQKvKVH 240
Cdd:PRK00053 158 IFSHFATADEPdNSYTEQQLNRFEAALAGLPGKgkPLRHLANSAAILRWpDLHF-DWVRPGIALYGLSPSGEPLGL-DFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 241 LKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQGSF-VNVIGHQCEVIGRVCMDQTIVKV 319
Cdd:PRK00053 236 LKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTpVLVNGRRVPIVGRVSMDQLTVDL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 613062023 320 PD--QVKAGDSVILIDNHrespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:PRK00053 316 GPdpQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-368 |
1.68e-114 |
|
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: 338.17 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVL 85
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIrNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLPAKDIDKAIQHRVALTVPSKQWLKeAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGV 165
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQ-ALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 166 FTHFACADEPGDMTTE-QYHRF----KDMVNEAIKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVH 240
Cdd:TIGR00492 160 FSHFATADEPKTGTTQkQIERFnsflEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 241 LKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLR-IMQGSFVNVIGHQCEVIGRVCMDQTIVKV 319
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRaLSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 613062023 320 P--DQVKAGDSVILIDNHrespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:TIGR00492 320 GpdLQDKTGDEVILWGEE----ISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-229 |
2.31e-83 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 253.30 E-value: 2.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 13 VDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLGVLPAK 91
Cdd:pfam01168 1 IDLDALRHNLRRLrRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 92 DIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDtKTYQEVIEIIQQYEQLVFEGVFTHFAC 171
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQL-EALAAAARRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613062023 172 ADEPGD-MTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFcNAIRPGISLYGYYP 229
Cdd:pfam01168 159 ADEPDDpYTNAQLARFREAAAALeaagLRPPVVHLANSAAILLHPLHF-DMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
245-368 |
4.68e-55 |
|
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: 177.26 E-value: 4.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 245 VQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQGSFVNVIGHQCEVIGRVCMDQTIVKVPD--Q 322
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDipD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 613062023 323 VKAGDSVILIDNHRespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:smart01005 82 VKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-368 |
3.91e-161 |
|
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: 456.57 E-value: 3.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 8 SAYMNVDLNAVASNFKVFST-LHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLG 86
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRlLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 87 VLPAKDIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKtYQEVIEIIQQYEQLVFEGVF 166
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQA-EALSAAAARLGKTLKVHLKIDTGMGRLGFRPEE-AEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 167 THFACADEPG-DMTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVqqKVKVHL 241
Cdd:cd00430 159 THFATADEPDkAYTRRQLERFLEALAELeeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEV--KSPLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 242 KPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIM-QGSFVNVIGHQCEVIGRVCMDQTIVKVP 320
Cdd:cd00430 237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 613062023 321 D--QVKAGDSVILIDNHRESPQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:cd00430 317 DipDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-371 |
5.22e-161 |
|
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: 456.11 E-value: 5.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 6 YRSAYMNVDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILV 84
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 85 LGVLPAKDIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIkDTKTYQEVIEIIQQYEQLVFEG 164
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQL-EALAAAARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 165 VFTHFACADEPGD-MTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQkvKV 239
Cdd:COG0787 159 IMSHFACADEPDHpFTAEQLERFEEAVAALpaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAA--DL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 240 HLKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQ-GSFVNVIGHQCEVIGRVCMDQTIVK 318
Cdd:COG0787 237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 613062023 319 VPD--QVKAGDSVILIDNHRespQSVEVAAEKQHTINYEVLCNLSRRLPRIYHDG 371
Cdd:COG0787 317 VTDipDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-368 |
3.64e-132 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 382.60 E-value: 3.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVFSTLHPNKT-VMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVL 85
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSkLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLP-AKDIDKAIQHRVALTVPSKQWLkEAIKNIsgEQEKKLWLHIKLDTGMGRLGIKDTKtYQEVIEIIQQYEQLVFEG 164
Cdd:PRK00053 82 GGFFpAEDLPLIIAYNLTTAVHSLEQL-EALEKA--ELGKPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNVRLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 165 VFTHFACADEP-GDMTTEQYHRFKDMVNEAIKP--EYIHCQNSAGSLLM-DCQFcNAIRPGISLYGYYPSEYVQQKvKVH 240
Cdd:PRK00053 158 IFSHFATADEPdNSYTEQQLNRFEAALAGLPGKgkPLRHLANSAAILRWpDLHF-DWVRPGIALYGLSPSGEPLGL-DFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 241 LKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQGSF-VNVIGHQCEVIGRVCMDQTIVKV 319
Cdd:PRK00053 236 LKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTpVLVNGRRVPIVGRVSMDQLTVDL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 613062023 320 PD--QVKAGDSVILIDNHrespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:PRK00053 316 GPdpQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-368 |
1.68e-114 |
|
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: 338.17 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVL 85
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIrNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLPAKDIDKAIQHRVALTVPSKQWLKeAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGV 165
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQ-ALEEALLKEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 166 FTHFACADEPGDMTTE-QYHRF----KDMVNEAIKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVH 240
Cdd:TIGR00492 160 FSHFATADEPKTGTTQkQIERFnsflEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 241 LKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLR-IMQGSFVNVIGHQCEVIGRVCMDQTIVKV 319
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRaLSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 613062023 320 P--DQVKAGDSVILIDNHrespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:TIGR00492 320 GpdLQDKTGDEVILWGEE----ISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
13-369 |
2.67e-94 |
|
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: 285.93 E-value: 2.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 13 VDLNAVASNFKVFSTLHPNKTVMAVVKANAYGLGSVKVARHLmeNGATFFAVATLDEAIELRMHGITAKILVL-GVLPAK 91
Cdd:cd06827 6 IDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKAL--ADADGFAVACIEEALALREAGITKPILLLeGFFSAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 92 DIDKAIQHRVALTVPSkQWLKEAIKNISGEqeKKLWLHIKLDTGMGRLGIKdTKTYQEVIEIIQQYEQLVFEGVFTHFAC 171
Cdd:cd06827 84 ELPLAAEYNLWTVVHS-EEQLEWLEQAALS--KPLNVWLKLDSGMHRLGFS-PEEYAAAYQRLKASPNVASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 172 ADEPGD-MTTEQYHRFKDMVNEAIKPEYIHcqNSAGSL-----LMDCqfcnaIRPGISLYGYYPSEyVQQKVKVHLKPSV 245
Cdd:cd06827 160 ADEPDSpGTAKQLAIFEQATAGLPGPRSLA--NSAAILawpeaHGDW-----VRPGIMLYGASPFA-DKSGADLGLKPVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 246 QLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQ-GSFVNVIGHQCEVIGRVCMDQTIVKVPD--Q 322
Cdd:cd06827 232 TLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPsGTPVLVNGQRTPLVGRVSMDMLTVDLTDlpE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 613062023 323 VKAGDSVILIDNHRespqSVEVAAEKQHTINYEVLCNLSRRLPRIYH 369
Cdd:cd06827 312 AKVGDPVELWGKGL----PVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
9-369 |
1.15e-90 |
|
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: 277.31 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 9 AYMNVDLNAVASNFKVFSTLHPNKT-VMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLGV 87
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPSTCkLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 88 LPAKDIDKAIQHRVALTVPSKQW------LKEAIKnisgeqekklwLHIKLDTGMGRLGIkdTKTYQEVIEIIQQYEQLV 161
Cdd:cd06825 82 TPPVRAKELKKYSLTQTLISEAYaeelskYAVNIK-----------VHLKVDTGMHRLGE--SPEDIDSILAIYRLKNLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 162 FEGVFTHFACAD--EPGDM--TTEQYHRFKDMVN----EAIKPEYIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYV 233
Cdd:cd06825 149 VSGIFSHLCVSDslDEDDIafTKHQIACFDQVLAdlkaRGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPND 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 234 QQKVKVHLKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIM--QGSFVNVIGHQCEVIGRVC 311
Cdd:cd06825 229 PTKLGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNIC 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 312 MDQTIVKVPD--QVKAGDSVILIDNHRESPQSVEVAAEKQHTINYEVLCNLSRRLPRIYH 369
Cdd:cd06825 309 MDQLMVDVTDipEVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-229 |
2.31e-83 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 253.30 E-value: 2.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 13 VDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLGVLPAK 91
Cdd:pfam01168 1 IDLDALRHNLRRLrRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 92 DIDKAIQHRVALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDtKTYQEVIEIIQQYEQLVFEGVFTHFAC 171
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQL-EALAAAARRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613062023 172 ADEPGD-MTTEQYHRFKDMVNEA----IKPEYIHCQNSAGSLLMDCQFcNAIRPGISLYGYYP 229
Cdd:pfam01168 159 ADEPDDpYTNAQLARFREAAAALeaagLRPPVVHLANSAAILLHPLHF-DMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
11-368 |
5.02e-80 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 261.43 E-value: 5.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 11 MNVDLNAVASNFKVF-STLHPNKTVMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLGvlP 89
Cdd:PRK11930 462 LEINLNAIVHNLNYYrSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMN--P 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 90 AK-DIDKAIQHRVALTVPSKQWLKEAIKNISGEQEKKLWLHIKLDTGMGRLGIkDTKTYQEVIEIIQQYEQLVFEGVFTH 168
Cdd:PRK11930 540 EPtSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYPIHIKIDTGMHRLGF-EPEDIPELARRLKKQPALKVRSVFSH 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 169 FACADEP--GDMTTEQYHRFkDMVNEAIKPEYI-----HCQNSAG-SLLMDCQFcNAIRPGISLYGYYPSEYVQQKvkvh 240
Cdd:PRK11930 619 LAGSDDPdhDDFTRQQIELF-DEGSEELQEALGykpirHILNSAGiERFPDYQY-DMVRLGIGLYGVSASGAGQQA---- 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 241 LKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRiMQGS---FVNVIGHQCEVIGRVCMDQTIV 317
Cdd:PRK11930 693 LRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNR-RLGNgvgYVLVNGQKAPIVGNICMDMCMI 771
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 613062023 318 KVPD-QVKAGDSVILIDNHrespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:PRK11930 772 DVTDiDAKEGDEVIIFGEE----LPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
7-368 |
1.51e-63 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 206.89 E-value: 1.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVFSTLHPNKTVMAVVKANAYGLGSVKVARHLmeNGATFFAVATLDEAIELRMHGITAKILVL- 85
Cdd:PRK03646 2 RPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRERGWKGPILMLe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLPAKDIDKAIQHRVALTVPSkQWLKEAIKNISGEQEKKLWLhiKLDTGMGRLGIKdTKTYQEVieiiqqYEQLVFEG- 164
Cdd:PRK03646 80 GFFHAQDLELYDQHRLTTCVHS-NWQLKALQNARLKAPLDIYL--KVNSGMNRLGFQ-PERVQTV------WQQLRAMGn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 165 -----VFTHFACADEPgDMTTEQYHRFkDMVNEAIKPEyIHCQNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKV 239
Cdd:PRK03646 150 vgemtLMSHFARADHP-DGISEAMARI-EQAAEGLECE-RSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 240 HLKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIM-QGSFVNVIGHQCEVIGRVCMDQTIVK 318
Cdd:PRK03646 227 GLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAVD 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 613062023 319 VPD--QVKAGDSVILIDNHresPQSVEVAAEKQhTINYEVLCNLSRRLPRIY 368
Cdd:PRK03646 307 LTPcpQAGIGTPVELWGKE---IKIDDVAAAAG-TIGYELMCALALRVPVVT 354
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
7-368 |
4.36e-57 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 191.76 E-value: 4.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 7 RSAYMNVDLNAVASNFKVFSTLHPNKT-VMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVL 85
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSLLANKSkVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 86 GVLPAKDIDKAIQHRVALTVPSKQWLKeAIKNISGEQEKKLWLHIKLDT-GMGRLGIkDTKTYQ---EVIEIIQQyEQLV 161
Cdd:PRK13340 119 RSASPAEIEQALRYDLEELIGDDEQAK-LLAAIAKKNGKPIDIHLALNSgGMSRNGL-DMSTARgkwEALRIATL-PSLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 162 FEGVFTHFACADEpgDMTTEQYHRFKD----MVNEA-IKPEYI--HCQNSAGSL-LMDCQFcNAIRPGISLYGYYPSEYV 233
Cdd:PRK13340 196 IVGIMTHFPNEDE--DEVRWKLAQFKEqtawLIGEAgLKREKItlHVANSYATLnVPEAHL-DMVRPGGILYGDRHPANT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 234 QqkvkvhLKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQ-GSFVNVIGHQCEVIGRVCM 312
Cdd:PRK13340 273 E------YKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVVGRVSM 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 613062023 313 DQTIVKVPD--QVKAGDSVILIDNHRESPQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:PRK13340 347 NTLMVDVTDipNVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
245-368 |
4.68e-55 |
|
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: 177.26 E-value: 4.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 245 VQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQGSFVNVIGHQCEVIGRVCMDQTIVKVPD--Q 322
Cdd:smart01005 2 MTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDipD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 613062023 323 VKAGDSVILIDNHRespQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:smart01005 82 VKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
245-368 |
9.45e-55 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 176.40 E-value: 9.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 245 VQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIMQGS-FVNVIGHQCEVIGRVCMDQTIVKVPD-- 321
Cdd:pfam00842 2 MTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRgEVLINGKRAPIVGRVCMDQLMVDVTDvp 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 613062023 322 QVKAGDSVILIDNHRESPQSVEVAAEKQHTINYEVLCNLSRRLPRIY 368
Cdd:pfam00842 82 EVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-368 |
1.37e-41 |
|
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: 149.80 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 8 SAYMNVDLNAVASNFKVFSTLHPNKT-VMAVVKANAYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLG 86
Cdd:cd06826 1 NAWLEISTGAFENNIKLLKKLLGGNTkLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 87 VLPAKDIDKAIQHRVALTVPSKQwLKEAIKNISGEQEKKLWLHIKLDT-GMGRLGIkDTKTYQ---EVIEIIQQyEQLVF 162
Cdd:cd06826 81 TATPSEIEDALAYNIEELIGSLD-QAEQIDSLAKRHGKTLPVHLALNSgGMSRNGL-ELSTAQgkeDAVAIATL-PNLKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 163 EGVFTHFACADEpgDMTTEQYHRFKD-----MVNEAIKPEYI--HCQNSAGSL-LMDCQFcNAIRPGISLYGYYPS--EY 232
Cdd:cd06826 158 VGIMTHFPVEDE--DDVRAKLARFNEdtawlISNAKLKREKItlHAANSFATLnVPEAHL-DMVRPGGILYGDTPPspEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 233 vqqkvkvhlKPSVQLIANVVQTKTLQAGESVSYGATYTATDPTTIALLPIGYADGYLRIM-QGSFVNVIGHQCEVIGRVC 311
Cdd:cd06826 235 ---------KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFsNKAHVLINGQRVPVVGKVS 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613062023 312 MDQTIVKVPD--QVKAGDSVILIDnhRESPQSVEVAA--EKQHTINYEVLCNLSRRLPRIY 368
Cdd:cd06826 306 MNTVMVDVTDipGVKAGDEVVLFG--KQGGAEITAAEieEGSGTILAELYTLWGQTNPRVY 364
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
30-222 |
3.25e-32 |
|
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: 120.50 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 30 PNKTVMAVVKANAYglgsVKVARhLMENGATFFAVATLDEAIELRMHGI-TAKILVLGVLP-AKDIDKAIQHRV-ALTVP 106
Cdd:cd06808 14 AGITLFAVVKANAN----PEVAR-TLAALGTGFDVASLGEALLLRAAGIpPEPILFLGPCKqVSELEDAAEQGViVVTVD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 107 SKQWLKEAIKnISGEQEKKLWLHIKLDTG--MGRLGIKDtKTYQEVIEIIQQYEQLVFEGVFTHFACADEPGDMTTEQYH 184
Cdd:cd06808 89 SLEELEKLEE-AALKAGPPARVLLRIDTGdeNGKFGVRP-EELKALLERAKELPHLRLVGLHTHFGSADEDYSPFVEALS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613062023 185 RFKDMVNEA----IKPEYIHCQNSAG----SLLMDCQFcNAIRPGI 222
Cdd:cd06808 167 RFVAALDQLgelgIDLEQLSIGGSFAilylQELPLGTF-IIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
32-168 |
1.72e-08 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 55.52 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 32 KTVMavvkanayglgSVKVARHLMENGATFFAVATLDEAIELRMHGIT-----------AKILVLGVLPAKDIdkaiqhR 100
Cdd:COG3616 41 KTHK-----------SPELARRQLAAGAWGITVATLAEAEVLAAAGVDdillayplvgpAKLARLAALARAGA------R 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613062023 101 VALTVPSKQWLkEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGVFTH 168
Cdd:COG3616 104 LTVLVDSVEQA-EALAAAAAAAGRPLRVLVELDVGGGRTGVRPPEAALALARAIAASPGLRLAGLMTY 170
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
12-211 |
9.75e-05 |
|
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: 44.07 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 12 NVDLNAVASNFKVFSTLHPNK--TVMAVVKANaygLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAKILVLGvLP 89
Cdd:cd06815 5 EINLSKIRHNAKVLVELCKSRgiEVTGVTKVV---CGDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLLR-IP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 90 AK-DIDKAIQHrVALTVPSKQWLKEAIKNISGEQEKKLWLHIKLDTGMGRLGIKDTKTYqEVIEIIQQYEQLVFEGVFTH 168
Cdd:cd06815 81 MLsEVEDVVKY-ADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLL-DFVEEILKLPGIELVGIGTN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 613062023 169 FAC--ADEPGDMTTEQYHRFKDMVNEA--IKPEYIHCQNSAG-SLLMD 211
Cdd:cd06815 159 LGCygGVLPTEENMGKLVELKEEIEKEfgIKLPIISGGNSASlPLLLK 206
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
49-164 |
3.45e-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: 39.20 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 49 KVARHLMENGATFFAVATLDEAIELRMHGItAKILVLGVLPAKDIDKAI-------QHRVALTVPSKQWLkEAIKNISGE 121
Cdd:cd06821 47 EIVRLQLEAGITKFKCATIAEAEMLAEAGA-PDVLLAYPLVGPNIERFLelakkypGTRFSALVDDLEAA-EALSAAAGS 124
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 613062023 122 QEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEG 164
Cdd:cd06821 125 AGLTLSVLLDVNTGMNRTGIAPGEDAEELYRAIATLPGLVLAG 167
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
47-168 |
5.95e-03 |
|
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: 38.45 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613062023 47 SVKVARHLMENGATFFAVATLDEAIELRMHGIT-----------AKILVLGVLPAkdidkaiQHRVALTVPSKQWLkEAI 115
Cdd:cd06820 40 SPEIARLQLAAGAIGITVATVGEAEVMADAGLSdifiaypivgrQKLERLRALAE-------RVTLSVGVDSAEVA-RGL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 613062023 116 KNISGEQEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGVFTH 168
Cdd:cd06820 112 AEVAEGAGRPLEVLVEVDSGMNRCGVQTPEDAVALARAIASAPGLRFRGIFTY 164
|
|
| |
