|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
21-433 |
9.57e-145 |
|
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: 417.59 E-value: 9.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 21 TYPGQVIVDLKALRDNMRTLIERVSKDlqpgqksPAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACG 100
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPG-------AKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 101 IDSsrcRILTWLTSAPTSlFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLS 180
Cdd:COG0787 74 IDA---PILVLGGVPPED-LELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 181 eysSQGLIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIG 260
Cdd:COG0787 150 ---ALPGLEVEGIMSHFACADEPDHPF----TAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 261 LYGYEPDPvmGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhv 340
Cdd:COG0787 223 LYGLSPSP--EVAADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSN--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 341 dkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaEPTADDWAEAAGTISYEIMT 420
Cdd:COG0787 292 ---GGPVLI---NGKR-APIVGRVSMDQIMVDVTDIP---DVKVGDEVVLFGEQ------GITADELAEAAGTISYEILT 355
|
410
....*....|...
gi 490216569 421 GIGPRVPRLYKNA 433
Cdd:COG0787 356 RLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
23-431 |
1.86e-133 |
|
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: 388.78 E-value: 1.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLIERVSKDlqpgqksPAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPG-------TKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 ssrCRILTWLtSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEY 182
Cdd:cd00430 74 ---APILVLG-GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 183 SSqglIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIGLY 262
Cdd:cd00430 150 PG---LELEGVFTHFATADEPDKAY----TRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 263 GYEPDPVMGVPQtyDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhvdk 342
Cdd:cd00430 223 GLYPSPEVKSPL--GLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSN----------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 343 pGGPVRVetnNGARiLHVSGRVCMDQFIVDLkgsAKELGVKEGDTVRLFGPGRGieyAEPTADDWAEAAGTISYEIMTGI 422
Cdd:cd00430 290 -KGEVLI---RGKR-APIVGRVCMDQTMVDV---TDIPDVKVGDEVVLFGRQGD---EEITAEELAELAGTINYEILCRI 358
|
....*....
gi 490216569 423 GPRVPRLYK 431
Cdd:cd00430 359 SKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
23-431 |
1.47e-109 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 327.90 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLiervsKDLQPGQKspAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:PRK00053 3 PATAEIDLDALRHNLRQI-----RKHAPPKS--KLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 ssrCRILTWLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSvcTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEY 182
Cdd:PRK00053 76 ---APILILGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELG--KPLKVHLKIDTGMHRLGVRPEEAEAALERLLAC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 183 SSqglIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEpkIRHLANTAATLNRPEIRFELVRPGIGLY 262
Cdd:PRK00053 151 PN---VRLEGIFSHFATADEPDNSY----TEQQLNRFEAALAGLPGKGKP--LRHLANSAAILRWPDLHFDWVRPGIALY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 263 GYEPDPVmGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhvdk 342
Cdd:PRK00053 222 GLSPSGE-PLGLDFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPS----------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 343 pGGPVRVetnNGaRILHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaePTADDWAEAAGTISYEIMTGI 422
Cdd:PRK00053 290 -GTPVLV---NG-RRVPIVGRVSMDQLTVDLGPDP---QDKVGDEVTLWGEA-------LTAEDVAEIIGTINYELLCKL 354
|
....*....
gi 490216569 423 GPRVPRLYK 431
Cdd:PRK00053 355 SPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
23-430 |
6.88e-85 |
|
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: 264.60 E-value: 6.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLIERVSKDLQpgqkspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSK-------IMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 SSrcrILTwLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTP---AGFSDALEKL 179
Cdd:TIGR00492 75 AP---ILL-LGGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPdeaALFVQKLRQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 180 SeyssqGLIEVIGQWSHLAVADCPDVpefvASTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGI 259
Cdd:TIGR00492 151 K-----KFLELEGIFSHFATADEPKT----GTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 260 GLYGYEPDPVMGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrh 339
Cdd:TIGR00492 222 ILYGLYPSADMSDGAPFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSN-------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 340 vdkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAKelgVKEGDTVRLFGpgrgieyAEPTADDWAEAAGTISYEIM 419
Cdd:TIGR00492 294 ----GTPVLV---NGKR-VPIVGRVCMDMIMVDLGPDLQ---DKTGDEVILWG-------EEISIDEIAEMLGTIAYELI 355
|
410
....*....|.
gi 490216569 420 TGIGPRVPRLY 430
Cdd:TIGR00492 356 CTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
28-266 |
2.26e-62 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 201.30 E-value: 2.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 28 VDLKALRDNMRTLIERvskdLQPGQKspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGIDssrCR 107
Cdd:pfam01168 1 IDLDALRHNLRRLRRR----AGPGAK---LMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGIT---AP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 108 ILTWLTSAPTSLfADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEYSSqgl 187
Cdd:pfam01168 71 ILVLGGFPPEEL-ALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPG--- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490216569 188 IEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEiRFELVRPGIGLYGYEP 266
Cdd:pfam01168 147 LRLEGLMTHFACADEPDDPY----TNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
281-430 |
3.43e-49 |
|
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: 163.78 E-value: 3.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 281 AMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASgfdmqgsrhvdkpGGPVRVetnNGARiLHV 360
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-------------NGPVLI---NGQR-VPV 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 361 SGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaEPTADDWAEAAGTISYEIMTGIGPRVPRLY 430
Cdd:smart01005 64 VGRVSMDQLMVDVTDIP---DVKVGDEVVLFGPQ------EITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
21-433 |
9.57e-145 |
|
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: 417.59 E-value: 9.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 21 TYPGQVIVDLKALRDNMRTLIERVSKDlqpgqksPAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACG 100
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPG-------AKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 101 IDSsrcRILTWLTSAPTSlFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLS 180
Cdd:COG0787 74 IDA---PILVLGGVPPED-LELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 181 eysSQGLIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIG 260
Cdd:COG0787 150 ---ALPGLEVEGIMSHFACADEPDHPF----TAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 261 LYGYEPDPvmGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhv 340
Cdd:COG0787 223 LYGLSPSP--EVAADLGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSN--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 341 dkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaEPTADDWAEAAGTISYEIMT 420
Cdd:COG0787 292 ---GGPVLI---NGKR-APIVGRVSMDQIMVDVTDIP---DVKVGDEVVLFGEQ------GITADELAEAAGTISYEILT 355
|
410
....*....|...
gi 490216569 421 GIGPRVPRLYKNA 433
Cdd:COG0787 356 RLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
23-431 |
1.86e-133 |
|
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: 388.78 E-value: 1.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLIERVSKDlqpgqksPAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPG-------TKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 ssrCRILTWLtSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEY 182
Cdd:cd00430 74 ---APILVLG-GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 183 SSqglIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIGLY 262
Cdd:cd00430 150 PG---LELEGVFTHFATADEPDKAY----TRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 263 GYEPDPVMGVPQtyDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhvdk 342
Cdd:cd00430 223 GLYPSPEVKSPL--GLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSN----------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 343 pGGPVRVetnNGARiLHVSGRVCMDQFIVDLkgsAKELGVKEGDTVRLFGPGRGieyAEPTADDWAEAAGTISYEIMTGI 422
Cdd:cd00430 290 -KGEVLI---RGKR-APIVGRVCMDQTMVDV---TDIPDVKVGDEVVLFGRQGD---EEITAEELAELAGTINYEILCRI 358
|
....*....
gi 490216569 423 GPRVPRLYK 431
Cdd:cd00430 359 SKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
23-431 |
1.47e-109 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 327.90 E-value: 1.47e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLiervsKDLQPGQKspAVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:PRK00053 3 PATAEIDLDALRHNLRQI-----RKHAPPKS--KLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 ssrCRILTWLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSvcTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEY 182
Cdd:PRK00053 76 ---APILILGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELG--KPLKVHLKIDTGMHRLGVRPEEAEAALERLLAC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 183 SSqglIEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEpkIRHLANTAATLNRPEIRFELVRPGIGLY 262
Cdd:PRK00053 151 PN---VRLEGIFSHFATADEPDNSY----TEQQLNRFEAALAGLPGKGKP--LRHLANSAAILRWPDLHFDWVRPGIALY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 263 GYEPDPVmGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhvdk 342
Cdd:PRK00053 222 GLSPSGE-PLGLDFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPS----------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 343 pGGPVRVetnNGaRILHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaePTADDWAEAAGTISYEIMTGI 422
Cdd:PRK00053 290 -GTPVLV---NG-RRVPIVGRVSMDQLTVDLGPDP---QDKVGDEVTLWGEA-------LTAEDVAEIIGTINYELLCKL 354
|
....*....
gi 490216569 423 GPRVPRLYK 431
Cdd:PRK00053 355 SPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
23-430 |
6.88e-85 |
|
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: 264.60 E-value: 6.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLIERVSKDLQpgqkspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGID 102
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSK-------IMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 103 SSrcrILTwLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTP---AGFSDALEKL 179
Cdd:TIGR00492 75 AP---ILL-LGGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKRLKVHLKIDTGMNRLGVKPdeaALFVQKLRQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 180 SeyssqGLIEVIGQWSHLAVADCPDVpefvASTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGI 259
Cdd:TIGR00492 151 K-----KFLELEGIFSHFATADEPKT----GTTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 260 GLYGYEPDPVMGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrh 339
Cdd:TIGR00492 222 ILYGLYPSADMSDGAPFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSN-------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 340 vdkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAKelgVKEGDTVRLFGpgrgieyAEPTADDWAEAAGTISYEIM 419
Cdd:TIGR00492 294 ----GTPVLV---NGKR-VPIVGRVCMDMIMVDLGPDLQ---DKTGDEVILWG-------EEISIDEIAEMLGTIAYELI 355
|
410
....*....|.
gi 490216569 420 TGIGPRVPRLY 430
Cdd:TIGR00492 356 CTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
23-430 |
1.18e-72 |
|
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: 232.77 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 23 PGQVIVDLKALRDNMRTLiervsKDLQPGQKspaVMGVVKADAYGHGLIPSALAalaggatwLGTAQPY------EALRL 96
Cdd:cd06827 1 PARATIDLAALRHNLRLV-----RELAPNSK---ILAVVKANAYGHGLVRVAKA--------LADADGFavacieEALAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 97 RACGIDSsrcRILtwL---TSAPTSLfADLINADIDISVGSLDSIDAvaLAAKSVCTTARVHVKVDTGFGRNGFTPAGFS 173
Cdd:cd06827 65 REAGITK---PIL--LlegFFSADEL-PLAAEYNLWTVVHSEEQLEW--LEQAALSKPLNVWLKLDSGMHRLGFSPEEYA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 174 DALEKLSeysSQGLIEVIGQWSHLAVADCPDVPefvaSTDRQIEQFHDFTrrmreAGLEPKiRHLANTAATLNRPEIRFE 253
Cdd:cd06827 137 AAYQRLK---ASPNVASIVLMTHFACADEPDSP----GTAKQLAIFEQAT-----AGLPGP-RSLANSAAILAWPEAHGD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 254 LVRPGIGLYGYEPDPVmGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAAsgfd 333
Cdd:cd06827 204 WVRPGIMLYGASPFAD-KSGADLGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHA---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 334 mqgsrhvdkPGG-PVRVetnNGARILHVsGRVCMDQFIVDLKGSAKelgVKEGDTVRLFGPGrgieyaePTADDWAEAAG 412
Cdd:cd06827 279 ---------PSGtPVLV---NGQRTPLV-GRVSMDMLTVDLTDLPE---AKVGDPVELWGKG-------LPVDEVAAAAG 335
|
410
....*....|....*...
gi 490216569 413 TISYEIMTGIGPRVPRLY 430
Cdd:cd06827 336 TIGYELLCRLTPRVPRVY 353
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
28-431 |
8.44e-69 |
|
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: 223.00 E-value: 8.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 28 VDLKALRDNmrtlIERVSKDLQPGQKspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGIdSSRCR 107
Cdd:cd06825 6 IDLSALEHN----VKEIKRLLPSTCK---LMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGI-KGEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 108 ILTWltsAPTSLFADLINADIDISVGSLDSidAVALAAKSVCTtaRVHVKVDTGFGRNGFTPagfsDALEKLSEYSSQGL 187
Cdd:cd06825 78 ILGY---TPPVRAKELKKYSLTQTLISEAY--AEELSKYAVNI--KVHLKVDTGMHRLGESP----EDIDSILAIYRLKN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 188 IEVIGQWSHLAVADCPDvPEFVASTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIGLYGYEPD 267
Cdd:cd06825 147 LKVSGIFSHLCVSDSLD-EDDIAFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 268 PVMGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGIlraasgfdmqgSRHVDKPGGPV 347
Cdd:cd06825 226 PNDPTKLGLDLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGY-----------PRSLSNQKAYV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 348 RVetnNGARiLHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrGIEyaEPTADDWAEAAGTISYEIMTGIGPRVP 427
Cdd:cd06825 295 LI---NGKR-APIIGNICMDQLMVDVTDIP---EVKEGDTATLIGQD-GDE--ELSADEVARNAHTITNELLSRIGERVK 364
|
....
gi 490216569 428 RLYK 431
Cdd:cd06825 365 RIYK 368
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
28-266 |
2.26e-62 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 201.30 E-value: 2.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 28 VDLKALRDNMRTLIERvskdLQPGQKspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGIDssrCR 107
Cdd:pfam01168 1 IDLDALRHNLRRLRRR----AGPGAK---LMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGIT---AP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 108 ILTWLTSAPTSLfADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSDALEKLSEYSSqgl 187
Cdd:pfam01168 71 ILVLGGFPPEEL-ALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPG--- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490216569 188 IEVIGQWSHLAVADCPDVPEfvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEiRFELVRPGIGLYGYEP 266
Cdd:pfam01168 147 LRLEGLMTHFACADEPDDPY----TNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
25-430 |
1.37e-57 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 203.27 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 25 QVIVDLKALRDNM---RTLiervskdLQPGQKspaVMGVVKADAYGHGLIPSALAALAGGATWLGTAQPYEALRLRACGI 101
Cdd:PRK11930 461 VLEINLNAIVHNLnyyRSK-------LKPETK---IMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGI 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 102 DSSrcrILTwLTSAPTSlFADLINADIDISVGSLDSIDAVALAA-KSVCTTARVHVKVDTGFGRNGFTPagfSDALEKLS 180
Cdd:PRK11930 531 TLP---IMV-MNPEPTS-FDTIIDYKLEPEIYSFRLLDAFIKAAqKKGITGYPIHIKIDTGMHRLGFEP---EDIPELAR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 181 EYSSQGLIEVIGQWSHLAVADCPDVPEFvasTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATLNRPEIRFELVRPGIG 260
Cdd:PRK11930 603 RLKKQPALKVRSVFSHLAGSDDPDHDDF---TRQQIELFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIG 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 261 LYGYEPDpvmGVPQTYdLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGIlraasgfdmqgSRHV 340
Cdd:PRK11930 680 LYGVSAS---GAGQQA-LRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGL-----------NRRL 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 341 DKPGGPVRVetnNGARILHVsGRVCMDQFIVDLKGsakeLGVKEGDTVRLFGPgrgieyaEPTADDWAEAAGTISYEIMT 420
Cdd:PRK11930 745 GNGVGYVLV---NGQKAPIV-GNICMDMCMIDVTD----IDAKEGDEVIIFGE-------ELPVTELADALNTIPYEILT 809
|
410
....*....|
gi 490216569 421 GIGPRVPRLY 430
Cdd:PRK11930 810 SISPRVKRVY 819
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
28-432 |
1.94e-55 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 189.45 E-value: 1.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 28 VDLKALRDNmrtlIERVSKDLQPGQKSPAVMgvvKADAYGHG---LIPSALAALAGGatwLGTAQPYEALRLRACGIDSS 104
Cdd:PRK13340 45 ISPGAFRHN----IKTLRSLLANKSKVCAVM---KADAYGHGielLMPSIIKANVPC---IGIASNEEARRVRELGFTGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 105 rcriLTWLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDT-GFGRNGFTPAGFSDALEKLsEYS 183
Cdd:PRK13340 115 ----LLRVRSASPAEIEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEAL-RIA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 184 SQGLIEVIGQWSHLAVADCPDVpefvastDRQIEQFHDFTRR-MREAGLEPK--IRHLANTAATLNRPEIRFELVRPGIG 260
Cdd:PRK13340 190 TLPSLGIVGIMTHFPNEDEDEV-------RWKLAQFKEQTAWlIGEAGLKREkiTLHVANSYATLNVPEAHLDMVRPGGI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 261 LYGyepdpvMGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhv 340
Cdd:PRK13340 263 LYG------DRHPANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASN--------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 341 dkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGRGieyAEPTADDWAEAAGTISYEIMT 420
Cdd:PRK13340 328 ---KAPVLI---NGQR-APVVGRVSMNTLMVDVTDIP---NVKPGDEVVLFGKQGN---AEITVDEVEEASGTIFPELYT 394
|
410
....*....|..
gi 490216569 421 GIGPRVPRLYKN 432
Cdd:PRK13340 395 AWGRTNPRIYVP 406
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
281-430 |
1.16e-49 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 165.23 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 281 AMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgsrhvdkpGGPVRVetnNGARiLHV 360
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSN------------RGEVLI---NGKR-API 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 361 SGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGRGieyAEPTADDWAEAAGTISYEIMTGIGPRVPRLY 430
Cdd:pfam00842 65 VGRVCMDQLMVDVTDVP---EVKVGDEVTLFGKQGD---EEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
21-430 |
2.55e-49 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 171.84 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 21 TYPGQVIVDLKALRDNMRtlierVSKDLQPGQKspaVMGVVKADAYGHGLIpsalaalaGGATWLGTAQPY------EAL 94
Cdd:PRK03646 1 TRPIQASLDLQALKQNLS-----IVREAAPGAR---VWSVVKANAYGHGIE--------RIWSALGATDGFavlnleEAI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 95 RLRACGIdssrcriltwltSAPTSLFADLINAD----ID-----ISVGSLDSIDAVALAAKSVCTTarVHVKVDTGFGRN 165
Cdd:PRK03646 65 TLRERGW------------KGPILMLEGFFHAQdlelYDqhrltTCVHSNWQLKALQNARLKAPLD--IYLKVNSGMNRL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 166 GFTPAGFSDALEKLSEYSSQGLIEVIgqwSHLAVADCPDvpefvaSTDRQIEQFHDFTRrmreaGLEPKiRHLANTAATL 245
Cdd:PRK03646 131 GFQPERVQTVWQQLRAMGNVGEMTLM---SHFARADHPD------GISEAMARIEQAAE-----GLECE-RSLSNSAATL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 246 NRPEIRFELVRPGIGLYGYEPDPVMGVPQTYDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGI 325
Cdd:PRK03646 196 WHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 326 LRAASgfdmqgsrhvdkPGGPVRVEtnnGARILHVsGRVCMDQFIVDLKGsAKELGVkeGDTVRLFGPgrgieyaEPTAD 405
Cdd:PRK03646 276 PRHAP------------TGTPVLVD---GVRTRTV-GTVSMDMLAVDLTP-CPQAGI--GTPVELWGK-------EIKID 329
|
410 420
....*....|....*....|....*
gi 490216569 406 DWAEAAGTISYEIMTGIGPRVPRLY 430
Cdd:PRK03646 330 DVAAAAGTIGYELMCALALRVPVVT 354
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
281-430 |
3.43e-49 |
|
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: 163.78 E-value: 3.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 281 AMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASgfdmqgsrhvdkpGGPVRVetnNGARiLHV 360
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-------------NGPVLI---NGQR-VPV 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 361 SGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGrgieyaEPTADDWAEAAGTISYEIMTGIGPRVPRLY 430
Cdd:smart01005 64 VGRVSMDQLMVDVTDIP---DVKVGDEVVLFGPQ------EITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
28-431 |
9.55e-40 |
|
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: 146.33 E-value: 9.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 28 VDLKALRDNMRTLIervsKDLQPGQKSPAVMgvvKADAYGHG---LIPSALAALAGGatwLGTAQPYEALRLRACGIDSS 104
Cdd:cd06826 6 ISTGAFENNIKLLK----KLLGGNTKLCAVM---KADAYGHGialVMPSIIAQNIPC---VGITSNEEARVVREAGFTGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 105 RCRiltwLTSAPTSLFADLINADIDISVGSLDSIDAVALAAKSVCTTARVHVKVDT-GFGRNGF---TPAGFSDALEKLS 180
Cdd:cd06826 76 ILR----VRTATPSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSgGMSRNGLelsTAQGKEDAVAIAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 181 eyssQGLIEVIGQWSHLAVADCPDVPEFVAstdrqieQFH-DFTRRMREAGLEPK--IRHLANTAATLNRPEIRFELVRP 257
Cdd:cd06826 152 ----LPNLKIVGIMTHFPVEDEDDVRAKLA-------RFNeDTAWLISNAKLKREkiTLHAANSFATLNVPEAHLDMVRP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 258 GIGLYGYEPdpvmgvPQTyDLRPAMTLQAQLGTVKSVEAGHGISYGRTYLTPDNTSTAIVPLGYADGILRAASGfdmqgs 337
Cdd:cd06826 221 GGILYGDTP------PSP-EYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSN------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 338 rhvdkpGGPVRVetnNGARiLHVSGRVCMDQFIVDLKGSAkelGVKEGDTVRLFGPGRGieyAEPTADDWAEAAGTISYE 417
Cdd:cd06826 288 ------KAHVLI---NGQR-VPVVGKVSMNTVMVDVTDIP---GVKAGDEVVLFGKQGG---AEITAAEIEEGSGTILAE 351
|
410
....*....|....
gi 490216569 418 IMTGIGPRVPRLYK 431
Cdd:cd06826 352 LYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
33-259 |
6.63e-22 |
|
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: 93.54 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 33 LRDNMRTLIERVSKDLQPgqkspavMGVVKADAYghgliPSALAALAGGATWLGTAQPYEALRLRACGIDSSRcrILTWL 112
Cdd:cd06808 1 IRHNYRRLREAAPAGITL-------FAVVKANAN-----PEVARTLAALGTGFDVASLGEALLLRAAGIPPEP--ILFLG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 113 TSAPTSLFADLINA-DIDISVGSLDSIDAVALAAKSVCTTARVHVKVDTGF--GRNGFTPAGFSDALEKLSEysSQGlIE 189
Cdd:cd06808 67 PCKQVSELEDAAEQgVIVVTVDSLEELEKLEEAALKAGPPARVLLRIDTGDenGKFGVRPEELKALLERAKE--LPH-LR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490216569 190 VIGQWSHLAVADcpdvpEFVASTDRQIEQFHDFTRRMREAGLEPKIRHLANTAATL---NRPEIRFELVRPGI 259
Cdd:cd06808 144 LVGLHTHFGSAD-----EDYSPFVEALSRFVAALDQLGELGIDLEQLSIGGSFAILylqELPLGTFIIVEPGR 211
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
132-396 |
2.45e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 39.75 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 132 VGSLDSIDAVALAAKSVCTTARVHVKVDTGFGRNGFTPAGFSdALEKLSEYSSQGLIEVIGQWSHLAV-ADCPDVPEFVA 210
Cdd:cd07376 92 VDSPEALAALAAFAAAHGVRLRVMLEVDVGGHRSGVRPEEAA-ALALADAVQASPGLRLAGVMAYEGHiYGAGGAREGAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 211 STDRQIEQFHDFTRRmREAGLEPKIRHLANTA-ATLNRPEIRFELVRPGIGLYGyepDPVMGVPQTYDLRPAMtlqaqlg 289
Cdd:cd07376 171 ARDQAVAAVRAAAAA-AERGLACPTVSGGGTPtYQLTAGDRAVTELRAGSYVFM---DTGFDTLGACAQRPAA------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 290 TVKSVEAGHGISYGRTYL----TPDNTSTAIVPLGYADG--ILRAASGFD--MQGSRHVDKPGGPVRVEtnnGARILHVS 361
Cdd:cd07376 240 FRVTTVISRPAPTGRAVLdagwKASSADTAFIGGGAVLGrpELRAVLLSEehEGRSEPLNTPDLDDLPI---GDRVFLVP 316
|
250 260 270
....*....|....*....|....*....|....*
gi 490216569 362 GRVCMDQFIVDlkgsakELGVKEGDTVRLFGPGRG 396
Cdd:cd07376 317 NHACETVALHD------ELYVVEGGRVAATWPVFG 345
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
124-263 |
3.85e-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: 39.22 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216569 124 INADIDISVGsLDSIDAVALAAKSVCTTAR---VHVKVDTGFGRNGFTPAGFSDALEKLSEySSQGLiEVIGQWSHLAVA 200
Cdd:cd06820 92 LAERVTLSVG-VDSAEVARGLAEVAEGAGRpleVLVEVDSGMNRCGVQTPEDAVALARAIA-SAPGL-RFRGIFTYPGHS 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490216569 201 DCPDVPEFVASTDRQIEQfhDFTRRMREAGLEPKIRHLANTaATLNRPEIRFEL--VRPGIGLYG 263
Cdd:cd06820 169 YAPGALEEAAADEAEALL--AAAGILEEAGLEPPVVSGGST-PTLWRSHEVPGIteIRPGTYIFN 230
|
|
| |
