|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-339 |
5.61e-116 |
|
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: 340.16 E-value: 5.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 2 SAPLRLRLDGDSLAANWKLL-ARLSGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDIS--VSV 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDapILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 79 LHGLRREDLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLM 147
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALaaaaRRLGKPLPVHLKVDTGMNRLGFRPEEAPalaarlaALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 148 SHLACADE-DVAMNARQRDAF----AALRGQTTAIRM-SLANSAGIALGAAYAFDLTRPGIALYGGR---QRSTHAGIAQ 218
Cdd:COG0787 161 SHFACADEpDHPFTAEQLERFeeavAALPAAGLDPPLrHLANSAAILRYPEAHFDMVRPGIALYGLSpspEVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 219 VVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGAT 298
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1567987624 299 PALNEGDWVSL----DYALPETAALSGLSQYELITGLGPRFDRVW 339
Cdd:COG0787 321 PDVKVGDEVVLfgeqGITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-338 |
5.55e-91 |
|
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: 276.30 E-value: 5.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLARLSGTAA-CGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVS--VLH 80
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTkIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPilVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 81 GLRREDLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLMSH 149
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPEEAEellealkALPGLELEGVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 150 LACADE-DVAMNARQRDAFAAL------RGQTTAIRmSLANSAGIALGAAYAFDLTRPGIALYG---GRQRSTHAGIAQV 219
Cdd:cd00430 161 FATADEpDKAYTRRQLERFLEAlaeleeAGIPPPLK-HLANSAAILRFPEAHFDMVRPGIALYGlypSPEVKSPLGLKPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 220 VTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATP 299
Cdd:cd00430 240 MSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1567987624 300 ALNEGDWVSL-----DYALP--ETAALSGLSQYELITGLGPRFDRV 338
Cdd:cd00430 320 DVKVGDEVVLfgrqgDEEITaeELAELAGTINYEILCRISKRVPRI 365
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
4-339 |
1.85e-87 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 267.04 E-value: 1.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLAR-LSGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVSVL--- 79
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILilg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 80 HGLRREDLASERPANVRPVLNSLAQIALWRAG--GGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLMSHL 150
Cdd:PRK00053 83 GFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAelGKPLKVHLKIDTGMHRLGVRPEEAEaalerllACPNVRLEGIFSHF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 151 ACADE-DVAMNARQRDAFAA----LRGQTTAIRmSLANSAGIALGAAYAFDLTRPGIALYG----GRQRSTHAGIAQVVT 221
Cdd:PRK00053 163 ATADEpDNSYTEQQLNRFEAalagLPGKGKPLR-HLANSAAILRWPDLHFDWVRPGIALYGlspsGEPLGLDFGLKPAMT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 222 PEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPAL 301
Cdd:PRK00053 242 LKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1567987624 302 NEGDWVSL-DYALPET--AALSGLSQYELITGLGPRFDRVW 339
Cdd:PRK00053 322 KVGDEVTLwGEALTAEdvAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
9-339 |
2.89e-55 |
|
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: 184.48 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 9 LDGDSLAANWKLLARLSGTAAC-GAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAI--ADLDISVSVLHGLRRE 85
Cdd:TIGR00492 7 IDLAALKHNLSAIRNHIGPKSKiMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLrkAGITAPILLLGGFFAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 86 DLASERPANVRPVLNSLAQI-ALWRA---GGGGAPCDVMIDTGMNRLGIAPSDAGSLEGLAID--------TLMSHLACA 153
Cdd:TIGR00492 87 DLKILAAWDLTTTVHSVEQLqALEEAllkEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQlkkfleleGIFSHFATA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 154 DE-DVAMNARQRDAFAA----LRGQTTAIRM-SLANSAGIALGAAYAFDLTRPGIALYG-----GRQRSTHAGIAQVVTP 222
Cdd:TIGR00492 167 DEpKTGTTQKQIERFNSflegLKQQNIEPPFrHIANSAAILNWPESHFDMVRPGIILYGlypsaDMSDGAPFGLKPVLSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 223 EAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPALN 302
Cdd:TIGR00492 247 TSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPDLQDK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1567987624 303 EGDWVSL---DYALPETAALSGLSQYELITGLGPRFDRVW 339
Cdd:TIGR00492 327 TGDEVILwgeEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-208 |
2.64e-50 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 167.02 E-value: 2.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 9 LDGDSLAANWKLLARLSGTAA-CGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDIS--VSVLHGLRRE 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAkLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITapILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 86 DLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAGS-------LEGLAIDTLMSHLACAD 154
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFRPEEALAllarlaaLPGLRLEGLMTHFACAD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 155 E-DVAMNARQRDAF----AALRGQTTAIRM-SLANSAGIaLGAAYAFDLTRPGIALYGGR 208
Cdd:pfam01168 161 EpDDPYTNAQLARFreaaAALEAAGLRPPVvHLANSAAI-LLHPLHFDMVRPGIALYGLS 219
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
219-339 |
2.95e-38 |
|
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: 132.58 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 219 VVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGrGLARAGGAELPVIGRVSMDMVAVDVGAT 298
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1567987624 299 PALNEGDWVSL--DYALP--ETAALSGLSQYELITGLGPRFDRVW 339
Cdd:smart01005 80 PDVKVGDEVVLfgPQEITadELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
2-339 |
5.61e-116 |
|
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: 340.16 E-value: 5.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 2 SAPLRLRLDGDSLAANWKLL-ARLSGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDIS--VSV 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLrALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDapILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 79 LHGLRREDLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLM 147
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALaaaaRRLGKPLPVHLKVDTGMNRLGFRPEEAPalaarlaALPGLEVEGIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 148 SHLACADE-DVAMNARQRDAF----AALRGQTTAIRM-SLANSAGIALGAAYAFDLTRPGIALYGGR---QRSTHAGIAQ 218
Cdd:COG0787 161 SHFACADEpDHPFTAEQLERFeeavAALPAAGLDPPLrHLANSAAILRYPEAHFDMVRPGIALYGLSpspEVAADLGLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 219 VVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGAT 298
Cdd:COG0787 241 VMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTDI 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1567987624 299 PALNEGDWVSL----DYALPETAALSGLSQYELITGLGPRFDRVW 339
Cdd:COG0787 321 PDVKVGDEVVLfgeqGITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-338 |
5.55e-91 |
|
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: 276.30 E-value: 5.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLARLSGTAA-CGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVS--VLH 80
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTkIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPilVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 81 GLRREDLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLMSH 149
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALsaaaARLGKTLKVHLKIDTGMGRLGFRPEEAEellealkALPGLELEGVFTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 150 LACADE-DVAMNARQRDAFAAL------RGQTTAIRmSLANSAGIALGAAYAFDLTRPGIALYG---GRQRSTHAGIAQV 219
Cdd:cd00430 161 FATADEpDKAYTRRQLERFLEAlaeleeAGIPPPLK-HLANSAAILRFPEAHFDMVRPGIALYGlypSPEVKSPLGLKPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 220 VTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATP 299
Cdd:cd00430 240 MSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1567987624 300 ALNEGDWVSL-----DYALP--ETAALSGLSQYELITGLGPRFDRV 338
Cdd:cd00430 320 DVKVGDEVVLfgrqgDEEITaeELAELAGTINYEILCRISKRVPRI 365
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
4-339 |
1.85e-87 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 267.04 E-value: 1.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLAR-LSGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVSVL--- 79
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILilg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 80 HGLRREDLASERPANVRPVLNSLAQIALWRAG--GGGAPCDVMIDTGMNRLGIAPSDAG-------SLEGLAIDTLMSHL 150
Cdd:PRK00053 83 GFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAelGKPLKVHLKIDTGMHRLGVRPEEAEaalerllACPNVRLEGIFSHF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 151 ACADE-DVAMNARQRDAFAA----LRGQTTAIRmSLANSAGIALGAAYAFDLTRPGIALYG----GRQRSTHAGIAQVVT 221
Cdd:PRK00053 163 ATADEpDNSYTEQQLNRFEAalagLPGKGKPLR-HLANSAAILRWPDLHFDWVRPGIALYGlspsGEPLGLDFGLKPAMT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 222 PEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPAL 301
Cdd:PRK00053 242 LKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1567987624 302 NEGDWVSL-DYALPET--AALSGLSQYELITGLGPRFDRVW 339
Cdd:PRK00053 322 KVGDEVTLwGEALTAEdvAEIIGTINYELLCKLSPRVPRVY 362
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-338 |
2.75e-64 |
|
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: 207.35 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLARLSGTAACGAAVKADGYGLGARGVVKRLADAGCrdFFVATWAEARAIADLDIS--VSVLHG 81
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADG--FAVACIEEALALREAGITkpILLLEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 82 LRRED---LASERpaNVRPVLNSLAQIALWRAGGGGAPCDV--MIDTGMNRLGIAPSDAG-------SLEGLAIDTLMSH 149
Cdd:cd06827 79 FFSADelpLAAEY--NLWTVVHSEEQLEWLEQAALSKPLNVwlKLDSGMHRLGFSPEEYAaayqrlkASPNVASIVLMTH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 150 LACADE-DVAMNARQRDAFAALRgQTTAIRMSLANSAGIaLGAAYA-FDLTRPGIALYG----GRQRSTHAGIAQVVTPE 223
Cdd:cd06827 157 FACADEpDSPGTAKQLAIFEQAT-AGLPGPRSLANSAAI-LAWPEAhGDWVRPGIMLYGaspfADKSGADLGLKPVMTLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 224 AQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCfsgrglARAG------GAELPVIGRVSMDMVAVDVGA 297
Cdd:cd06827 235 SEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRH------APSGtpvlvnGQRTPLVGRVSMDMLTVDLTD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1567987624 298 TPALNEGDWVSL-DYALP--ETAALSGLSQYELITGLGPRFDRV 338
Cdd:cd06827 309 LPEAKVGDPVELwGKGLPvdEVAAAAGTIGYELLCRLTPRVPRV 352
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
9-339 |
2.89e-55 |
|
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: 184.48 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 9 LDGDSLAANWKLLARLSGTAAC-GAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAI--ADLDISVSVLHGLRRE 85
Cdd:TIGR00492 7 IDLAALKHNLSAIRNHIGPKSKiMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLrkAGITAPILLLGGFFAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 86 DLASERPANVRPVLNSLAQI-ALWRA---GGGGAPCDVMIDTGMNRLGIAPSDAGSLEGLAID--------TLMSHLACA 153
Cdd:TIGR00492 87 DLKILAAWDLTTTVHSVEQLqALEEAllkEPKRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQlkkfleleGIFSHFATA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 154 DE-DVAMNARQRDAFAA----LRGQTTAIRM-SLANSAGIALGAAYAFDLTRPGIALYG-----GRQRSTHAGIAQVVTP 222
Cdd:TIGR00492 167 DEpKTGTTQKQIERFNSflegLKQQNIEPPFrHIANSAAILNWPESHFDMVRPGIILYGlypsaDMSDGAPFGLKPVLSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 223 EAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPALN 302
Cdd:TIGR00492 247 TSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDLGPDLQDK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1567987624 303 EGDWVSL---DYALPETAALSGLSQYELITGLGPRFDRVW 339
Cdd:TIGR00492 327 TGDEVILwgeEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
9-208 |
2.64e-50 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 167.02 E-value: 2.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 9 LDGDSLAANWKLLARLSGTAA-CGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDIS--VSVLHGLRRE 85
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAkLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITapILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 86 DLASERPANVRPVLNSLAQIALW----RAGGGGAPCDVMIDTGMNRLGIAPSDAGS-------LEGLAIDTLMSHLACAD 154
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALaaaaRRLGKPLRVHLKIDTGMGRLGFRPEEALAllarlaaLPGLRLEGLMTHFACAD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 155 E-DVAMNARQRDAF----AALRGQTTAIRM-SLANSAGIaLGAAYAFDLTRPGIALYGGR 208
Cdd:pfam01168 161 EpDDPYTNAQLARFreaaAALEAAGLRPPVvHLANSAAI-LLHPLHFDMVRPGIALYGLS 219
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
32-338 |
6.75e-42 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 155.12 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 32 AAVKADGYGLGARGVVKRLADAGCRDFFVATWAEA----RAIADLDISVsvlhglrredLASERPA-------NVRPVLN 100
Cdd:PRK11930 488 CMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGvslrKAGITLPIMV----------MNPEPTSfdtiidyKLEPEIY 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 101 SLAQIALW-----RAGGGGAPCDVMIDTGMNRLGIAPSDAGSL-------EGLAIDTLMSHLACADEDV--AMNARQRDA 166
Cdd:PRK11930 558 SFRLLDAFikaaqKKGITGYPIHIKIDTGMHRLGFEPEDIPELarrlkkqPALKVRSVFSHLAGSDDPDhdDFTRQQIEL 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 167 FAALRGQTTA------IRmSLANSAGIALGAAYAFDLTRPGIALYGGRQRSTHAGIAQ-VVTPEAQIIQRRHVPAGGVVG 239
Cdd:PRK11930 638 FDEGSEELQEalgykpIR-HILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQALRnVSTLKTTILQIKHVPKGETVG 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 240 YNATFTAPRDMEIAILNIGYADGYLRCFS-GRGLARAGGAELPVIGRVSMDMVAVDVGATPAlNEGDWVSL---DYALPE 315
Cdd:PRK11930 717 YGRKGVVTKPSRIATIPIGYADGLNRRLGnGVGYVLVNGQKAPIVGNICMDMCMIDVTDIDA-KEGDEVIIfgeELPVTE 795
|
330 340
....*....|....*....|...
gi 1567987624 316 TAALSGLSQYELITGLGPRFDRV 338
Cdd:PRK11930 796 LADALNTIPYEILTSISPRVKRV 818
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
219-339 |
4.33e-41 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 139.81 E-value: 4.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 219 VVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGAT 298
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1567987624 299 PALNEGDWVSL-----DYALP--ETAALSGLSQYELITGLGPRFDRVW 339
Cdd:pfam00842 81 PEVKVGDEVTLfgkqgDEEITadELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
1-338 |
3.93e-39 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 142.84 E-value: 3.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 1 MSAPLRLRLDGDSLAANWKLLARLSG--TAACgAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVSV 78
Cdd:PRK13340 37 QPRNAWLEISPGAFRHNIKTLRSLLAnkSKVC-AVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 79 L--HGLRREDLASERPANVRPVLNSLAQ---IALWrAGGGGAPCDV---MIDTGMNRLGIAPS---------DAGSLEGL 141
Cdd:PRK13340 116 LrvRSASPAEIEQALRYDLEELIGDDEQaklLAAI-AKKNGKPIDIhlaLNSGGMSRNGLDMStargkwealRIATLPSL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 142 AIDTLMSHLACADED-VAMNARQRDAFAA-LRGQTTAIRMSL----ANSAG-IALGAAYaFDLTRPGIALYGGRQrSTHA 214
Cdd:PRK13340 195 GIVGIMTHFPNEDEDeVRWKLAQFKEQTAwLIGEAGLKREKItlhvANSYAtLNVPEAH-LDMVRPGGILYGDRH-PANT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 215 GIAQVVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVD 294
Cdd:PRK13340 273 EYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLMVD 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1567987624 295 VGATPALNEGDWVSL-------DYALPETAALSGLSQYELITGLGPRFDRV 338
Cdd:PRK13340 353 VTDIPNVKPGDEVVLfgkqgnaEITVDEVEEASGTIFPELYTAWGRTNPRI 403
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
219-339 |
2.95e-38 |
|
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: 132.58 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 219 VVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGrGLARAGGAELPVIGRVSMDMVAVDVGAT 298
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN-GPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1567987624 299 PALNEGDWVSL--DYALP--ETAALSGLSQYELITGLGPRFDRVW 339
Cdd:smart01005 80 PDVKVGDEVVLfgPQEITadELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
7-338 |
7.79e-37 |
|
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: 135.94 E-value: 7.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 7 LRLDGDSLAANWKLLARL-SGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVSVL------ 79
Cdd:cd06825 4 LEIDLSALEHNVKEIKRLlPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILilgytp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 80 ----HGLRREDL----ASERPANvrpvlnSLAQIAlwraggGGAPCDVMIDTGMNRLGIAPSD------AGSLEGLAIDT 145
Cdd:cd06825 84 pvraKELKKYSLtqtlISEAYAE------ELSKYA------VNIKVHLKVDTGMHRLGESPEDidsilaIYRLKNLKVSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 146 LMSHLACAD----EDVAMNARQRDAF----AALRGQTTAI-RMSLANSAGIALGAAYAFDLTRPGIALYG-----GRQRS 211
Cdd:cd06825 152 IFSHLCVSDsldeDDIAFTKHQIACFdqvlADLKARGIEVgKIHIQSSYGILNYPDLKYDYVRPGILLYGvlsdpNDPTK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 212 THAGIAQVVTPEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFS-GRGLARAGGAELPVIGRVSMDM 290
Cdd:cd06825 232 LGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSnQKAYVLINGKRAPIIGNICMDQ 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1567987624 291 VAVDVGATPALNEGDWVSL-------DYALPETAALSGLSQYELITGLGPRFDRV 338
Cdd:cd06825 312 LMVDVTDIPEVKEGDTATLigqdgdeELSADEVARNAHTITNELLSRIGERVKRI 366
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
4-339 |
8.54e-37 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 135.63 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 4 PLRLRLDGDSLAANWKLLARLSGTAACGAAVKADGYGLGARGVVKRLADAGcrDFFVATWAEARAIADLDIS--VSVLHG 81
Cdd:PRK03646 3 PIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATD--GFAVLNLEEAITLRERGWKgpILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 82 L-RREDLASERPANVRPVLNSLAQIALWRAGGGGAPCDVM--IDTGMNRLGIAPSDAGS-------LEGLAIDTLMSHLA 151
Cdd:PRK03646 81 FfHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYlkVNSGMNRLGFQPERVQTvwqqlraMGNVGEMTLMSHFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 152 CADEDVAMnARQRDAFAALRgQTTAIRMSLANSAGIALGAAYAFDLTRPGIALYG----GRQRSTHA-GIAQVVTPEAQI 226
Cdd:PRK03646 161 RADHPDGI-SEAMARIEQAA-EGLECERSLSNSAATLWHPQAHFDWVRPGIILYGaspsGQWRDIANtGLRPVMTLSSEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 227 IQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPALNEGDW 306
Cdd:PRK03646 239 IGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGTP 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 1567987624 307 VSL---DYALPETAALSGLSQYELITGLGPRFDRVW 339
Cdd:PRK03646 319 VELwgkEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
7-309 |
2.54e-29 |
|
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: 115.52 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 7 LRLDGDSLAANWK-LLARLSGTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARAIADLDISVSVLHgLR-- 83
Cdd:cd06826 4 LEISTGAFENNIKlLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILR-VRta 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 84 -REDLASERPANVRPVLNSLAQ----IALWRAGGGGAPCDVMIDT-GMNRLGIAPS-DAG--------SLEGLAIDTLMS 148
Cdd:cd06826 83 tPSEIEDALAYNIEELIGSLDQaeqiDSLAKRHGKTLPVHLALNSgGMSRNGLELStAQGkedavaiaTLPNLKIVGIMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 149 HLACADE-DVAMN-ARQRDAFAALRGQTTAIRMSL----ANS-AGIALGAAYaFDLTRPGIALYGgrQRSTHAGIAQVVT 221
Cdd:cd06826 163 HFPVEDEdDVRAKlARFNEDTAWLISNAKLKREKItlhaANSfATLNVPEAH-LDMVRPGGILYG--DTPPSPEYKRIMS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 222 PEAQIIQRRHVPAGGVVGYNATFTAPRDMEIAILNIGYADGYLRCFSGRGLARAGGAELPVIGRVSMDMVAVDVGATPAL 301
Cdd:cd06826 240 FKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVTDIPGV 319
|
....*...
gi 1567987624 302 NEGDWVSL 309
Cdd:cd06826 320 KAGDEVVL 327
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
32-202 |
7.03e-09 |
|
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: 55.02 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 32 AAVKADGyglgARGVVKRLADAGCRdFFVATWAEARAIADLDIS---VSVLHGLRRED---LASERPANVRPV--LNSLA 103
Cdd:cd06808 20 AVVKANA----NPEVARTLAALGTG-FDVASLGEALLLRAAGIPpepILFLGPCKQVSeleDAAEQGVIVVTVdsLEELE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 104 QI-ALWRAGGGGAPCDVMIDTG--MNRLGIAPSD-------AGSLEGLAIDTLMSHLACADEDVAMNARQ----RDAFAA 169
Cdd:cd06808 95 KLeEAALKAGPPARVLLRIDTGdeNGKFGVRPEElkallerAKELPHLRLVGLHTHFGSADEDYSPFVEAlsrfVAALDQ 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1567987624 170 LRGQTTAIRM-SLANSAGI---ALGAAYAFDLTRPGI 202
Cdd:cd06808 175 LGELGIDLEQlSIGGSFAIlylQELPLGTFIIVEPGR 211
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
46-134 |
4.36e-05 |
|
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: 44.98 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 46 VVKRLADAGCRDFFVATWAEARAIADL---DISVSV-LHGLRRE---DLASERPANVRPVL-NSLAQIALWR--AGGGGA 115
Cdd:cd06821 48 IVRLQLEAGITKFKCATIAEAEMLAEAgapDVLLAYpLVGPNIErflELAKKYPGTRFSALvDDLEAAEALSaaAGSAGL 127
|
90 100
....*....|....*....|.
gi 1567987624 116 PCDVMID--TGMNRLGIAPSD 134
Cdd:cd06821 128 TLSVLLDvnTGMNRTGIAPGE 148
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|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
7-178 |
5.57e-03 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 38.19 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 7 LRLDGDSLAANWKLLARLsgTAACGAAVKADGYGLGARGVVKRLADAGCRDFFVATWAEARA-----IADLDISVSVL-- 79
Cdd:COG3616 11 LVLDLDALERNIARMAAR--AAAHGVRLRPHGKTHKSPELARRQLAAGAWGITVATLAEAEVlaaagVDDILLAYPLVgp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567987624 80 HGLRRedLAS--ERPANVRPVLNSLAQIALWR--AGGGGAPCDVMI--DTGMNRLGIAPSDAG--------SLEGLAIDT 145
Cdd:COG3616 89 AKLAR--LAAlaRAGARLTVLVDSVEQAEALAaaAAAAGRPLRVLVelDVGGGRTGVRPPEAAlalaraiaASPGLRLAG 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1567987624 146 LMS---HLACADEDVAMNARQRDAFAALRGQTTAIR 178
Cdd:COG3616 167 LMTyegHIYGADDAEERRAAAREELARLAAAAEALR 202
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