|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
1-820 |
0e+00 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 1175.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 1 MNYTISEISKIIHAQLTLKENCEIRNLIIDSRNFVSSQDALFFAIRGERHDGHKYINDLYNKGVRNFVV--EQIPENSkd 78
Cdd:PRK11930 1 MSYTLESISGILGAEGLGDKDAIIDQILTDSRSLSFPENTLFFALKGERNDGHRYIQELYEKGVRNFVVseEKHPEES-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 79 YPNANFLVVRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKT 158
Cdd:PRK11930 79 YPDANFLKVKDPLKALQELAAYHRSQFDIPVIGITGSNGKTIVKEWLYQLLSPDYNIVRSPRSYNSQIGVPLSVWQLNEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 159 FNIAIFEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKHSEILVYCKDHVLIDKLISDApeL 238
Cdd:PRK11930 159 HELGIFEAGISQPGEMEALQKIIKPTIGILTNIGGAHQENFRSIKQKIMEKLKLFKDCDVIIYNGDNELISSCITKS--N 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 239 SQKKLFSWSVN-PGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLL 317
Cdd:PRK11930 237 LTLKLISWSRKdPEAPLYIPFVEKKEDHTVISYTYKGEDFHFEIPFIDDASIENLIHCIAVLLYLGYSADQIQERMARLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 318 PVAMRMELKKGMNGCSIINDSYNSDLNSLNIALNYLSQQNQHSKKVLILSDILQSGKSETVLYSEVASLIKKYQVDQIIG 397
Cdd:PRK11930 317 PVAMRLEVKEGINNCTLINDSYNSDLQSLDIALDFLNRRSQSKKKTLILSDILQSGQSPEELYRKVAQLISKRGIDRLIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 398 IGKSIVSQADVFDIP-KSFYSTTNEFLSDLSKKTFSDSSILLKGSRNFAFEKISALLEEKVHRTVLEINLNALVHNLNYF 476
Cdd:PRK11930 397 IGEEISSEASKFEGTeKEFFKTTEAFLKSFAFLKFRNELILVKGARKFEFEQITELLEQKVHETVLEINLNAIVHNLNYY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 477 KSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMNPEQNSFNLMIEYNLEPEI 556
Cdd:PRK11930 477 RSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEPTSFDTIIDYKLEPEI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 557 YSSLVLNQFQKTLENVGIPDYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAASDENIHDEFTDTQIK 636
Cdd:PRK11930 557 YSFRLLDAFIKAAQKKGITGYPIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKVRSVFSHLAGSDDPDHDDFTRQQIE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 637 LFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQEQ--LEIVSTLKSTVIQIKHVPKSETIG 714
Cdd:PRK11930 637 LFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQqaLRNVSTLKTTILQIKHVPKGETVG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 715 YGRKGKAINDMTIAIIPIGYADGLNRKLSNGKGKLFINGHIVPIVGNICMDMCMADITGCTIHEGDEVEVFGKEIPVNEI 794
Cdd:PRK11930 717 YGRKGVVTKPSRIATIPIGYADGLNRRLGNGVGYVLVNGQKAPIVGNICMDMCMIDVTDIDAKEGDEVIIFGEELPVTEL 796
|
810 820
....*....|....*....|....*.
gi 1082420391 795 ARTLETIPYEIFAGIPSRVKRVYYQE 820
Cdd:PRK11930 797 ADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
457-820 |
2.49e-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: 473.06 E-value: 2.49e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 457 VHRTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIV 536
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 537 MNP-EQNSFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASI 615
Cdd:COG0787 81 LGGvPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKP-LPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 616 FSHLAASDEnIHDEFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQE----QL 691
Cdd:COG0787 160 MSHFACADE-PDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVaadlGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 692 EIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMADI 771
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNG-GPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1082420391 772 TGC-TIHEGDEVEVFGKE-IPVNEIARTLETIPYEIFAGIPSRVKRVYYQE 820
Cdd:COG0787 318 TDIpDVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
459-817 |
1.19e-146 |
|
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: 435.39 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMN 538
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 539 PEQNS-FNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFS 617
Cdd:cd00430 81 GTPPEeAEEAIEYDLTPTVSSLEQAEALSAAAARLGKT-LKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 618 HLAASDENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGIS----SMQQEQLEI 693
Cdd:cd00430 160 HFATADEPDKA-YTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYpspeVKSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgKGKLFINGHIVPIVGNICMDMCMADITG 773
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSN-KGEVLIRGKRAPIVGRVCMDQTMVDVTD 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1082420391 774 C-TIHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:cd00430 318 IpDVKVGDEVVLFGRqgdeEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
459-817 |
1.02e-97 |
|
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: 308.51 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMN 538
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 539 --PEQNSFNLmIEYNLEPEIYSSLVLNQFQKTLENVGiPDYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNI-KVASI 615
Cdd:TIGR00492 82 gfFAEDLKIL-AAWDLTTTVHSVEQLQALEEALLKEP-KRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFlELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 616 FSHLAASDENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGIS---SMQQE--- 689
Cdd:TIGR00492 160 FSHFATADEPKTG-TTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYpsaDMSDGapf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 690 QLEIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMA 769
Cdd:TIGR00492 239 GLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNG-TPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1082420391 770 DITGCT-IHEGDEVEVFGKEIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:TIGR00492 318 DLGPDLqDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
464-684 |
1.34e-66 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 220.56 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 464 INLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMNP-EQN 542
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGfPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 543 SFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAAS 622
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKP-LRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420391 623 DENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPyGQFDMVRLGIGLYGIS 684
Cdd:pfam01168 160 DEPDDP-YTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGLS 219
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
694-817 |
1.67e-52 |
|
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: 178.42 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgkGKLFINGHIVPIVGNICMDMCMADITG 773
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN--GPVLINGQRVPVVGRVSMDQLMVDVTD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1082420391 774 C-TIHEGDEVEVFGK-EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:smart01005 79 IpDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
1-820 |
0e+00 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 1175.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 1 MNYTISEISKIIHAQLTLKENCEIRNLIIDSRNFVSSQDALFFAIRGERHDGHKYINDLYNKGVRNFVV--EQIPENSkd 78
Cdd:PRK11930 1 MSYTLESISGILGAEGLGDKDAIIDQILTDSRSLSFPENTLFFALKGERNDGHRYIQELYEKGVRNFVVseEKHPEES-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 79 YPNANFLVVRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKT 158
Cdd:PRK11930 79 YPDANFLKVKDPLKALQELAAYHRSQFDIPVIGITGSNGKTIVKEWLYQLLSPDYNIVRSPRSYNSQIGVPLSVWQLNEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 159 FNIAIFEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKHSEILVYCKDHVLIDKLISDApeL 238
Cdd:PRK11930 159 HELGIFEAGISQPGEMEALQKIIKPTIGILTNIGGAHQENFRSIKQKIMEKLKLFKDCDVIIYNGDNELISSCITKS--N 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 239 SQKKLFSWSVN-PGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLL 317
Cdd:PRK11930 237 LTLKLISWSRKdPEAPLYIPFVEKKEDHTVISYTYKGEDFHFEIPFIDDASIENLIHCIAVLLYLGYSADQIQERMARLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 318 PVAMRMELKKGMNGCSIINDSYNSDLNSLNIALNYLSQQNQHSKKVLILSDILQSGKSETVLYSEVASLIKKYQVDQIIG 397
Cdd:PRK11930 317 PVAMRLEVKEGINNCTLINDSYNSDLQSLDIALDFLNRRSQSKKKTLILSDILQSGQSPEELYRKVAQLISKRGIDRLIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 398 IGKSIVSQADVFDIP-KSFYSTTNEFLSDLSKKTFSDSSILLKGSRNFAFEKISALLEEKVHRTVLEINLNALVHNLNYF 476
Cdd:PRK11930 397 IGEEISSEASKFEGTeKEFFKTTEAFLKSFAFLKFRNELILVKGARKFEFEQITELLEQKVHETVLEINLNAIVHNLNYY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 477 KSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMNPEQNSFNLMIEYNLEPEI 556
Cdd:PRK11930 477 RSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNPEPTSFDTIIDYKLEPEI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 557 YSSLVLNQFQKTLENVGIPDYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAASDENIHDEFTDTQIK 636
Cdd:PRK11930 557 YSFRLLDAFIKAAQKKGITGYPIHIKIDTGMHRLGFEPEDIPELARRLKKQPALKVRSVFSHLAGSDDPDHDDFTRQQIE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 637 LFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQEQ--LEIVSTLKSTVIQIKHVPKSETIG 714
Cdd:PRK11930 637 LFDEGSEELQEALGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQqaLRNVSTLKTTILQIKHVPKGETVG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 715 YGRKGKAINDMTIAIIPIGYADGLNRKLSNGKGKLFINGHIVPIVGNICMDMCMADITGCTIHEGDEVEVFGKEIPVNEI 794
Cdd:PRK11930 717 YGRKGVVTKPSRIATIPIGYADGLNRRLGNGVGYVLVNGQKAPIVGNICMDMCMIDVTDIDAKEGDEVIIFGEELPVTEL 796
|
810 820
....*....|....*....|....*.
gi 1082420391 795 ARTLETIPYEIFAGIPSRVKRVYYQE 820
Cdd:PRK11930 797 ADALNTIPYEILTSISPRVKRVYFQE 822
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
457-820 |
2.49e-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: 473.06 E-value: 2.49e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 457 VHRTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIV 536
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 537 MNP-EQNSFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASI 615
Cdd:COG0787 81 LGGvPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKP-LPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 616 FSHLAASDEnIHDEFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQE----QL 691
Cdd:COG0787 160 MSHFACADE-PDHPFTAEQLERFEEAVAALPAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVaadlGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 692 EIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMADI 771
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNG-GPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1082420391 772 TGC-TIHEGDEVEVFGKE-IPVNEIARTLETIPYEIFAGIPSRVKRVYYQE 820
Cdd:COG0787 318 TDIpDVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYVGE 368
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
459-817 |
1.19e-146 |
|
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: 435.39 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMN 538
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 539 PEQNS-FNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFS 617
Cdd:cd00430 81 GTPPEeAEEAIEYDLTPTVSSLEQAEALSAAAARLGKT-LKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 618 HLAASDENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGIS----SMQQEQLEI 693
Cdd:cd00430 160 HFATADEPDKA-YTRRQLERFLEALAELEEAGIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYpspeVKSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgKGKLFINGHIVPIVGNICMDMCMADITG 773
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSN-KGEVLIRGKRAPIVGRVCMDQTMVDVTD 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1082420391 774 C-TIHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:cd00430 318 IpDVKVGDEVVLFGRqgdeEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
1-456 |
8.71e-146 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 436.46 E-value: 8.71e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 1 MNYTISEISKIIHAQLTLKENCEIRNLIIDSRNFvsSQDALFFAIRGERHDGHKYINDLYNKGVRNFVVEQIPEnskdyP 80
Cdd:COG0770 1 ILLTLAEIAEATGGRLIGDPDLVVTGVSTDSRKI--KPGDLFVALKGERFDGHDFVAQALAKGAAAALVSRPLP-----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 81 NANFLVVRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKTFN 160
Cdd:COG0770 74 DLPLIVVDDTLKALQQLAAAHRARFNIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFNNEIGVPLTLLRLPEDHE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 161 IAIFEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKH---SEILVYCKDHVLIDKLISDAPE 237
Cdd:COG0770 154 FAVLEMGMNHPGEIAYLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGlppGGVAVLNADDPLLAALAERAKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 238 lsqkKLFSWSVNPGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLL 317
Cdd:COG0770 234 ----RVLTFGLSEDADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 318 PVAMRMELKKGMNGCSIINDSYNSDLNSLNIALNYLSQQNQHSKKVLILSDILQSGKSETVLYSEVASLIKKYQVDQIIG 397
Cdd:COG0770 310 PVKGRLEVIEGAGGVTLIDDSYNANPDSMKAALDVLAQLPGGGRRIAVLGDMLELGEESEELHREVGELAAELGIDRLFT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 398 IGKSIVSQADVFDIPKS-FYSTTNEFLSDLSKKTFSDSSILLKGSRNFAFEKISALLEEK 456
Cdd:COG0770 390 VGELARAIAEAAGGERAeHFEDKEELLAALKALLRPGDVVLVKGSRGMGLERVVEALKEG 449
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
459-817 |
2.23e-117 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 359.88 E-value: 2.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMN 538
Cdd:PRK00053 3 PATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILILG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 539 --PEQNSFNLMIEYNLEPEIYSslvLNQFQKtLENVGIP-DYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASI 615
Cdd:PRK00053 83 gfFPAEDLPLIIAYNLTTAVHS---LEQLEA-LEKAELGkPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 616 FSHLAASDEnIHDEFTDTQIKLFDNLSSKIISKLNypVIRHVLNSSGIERFPYGQFDMVRLGIGLYGIS-SMQQEQLEI- 693
Cdd:PRK00053 159 FSHFATADE-PDNSYTEQQLNRFEAALAGLPGKGK--PLRHLANSAAILRWPDLHFDWVRPGIALYGLSpSGEPLGLDFg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 ---VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMAD 770
Cdd:PRK00053 236 lkpAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSG-TPVLVNGRRVPIVGRVSMDQLTVD 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1082420391 771 ITGC-TIHEGDEVEVFGKEIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:PRK00053 315 LGPDpQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
459-817 |
2.54e-99 |
|
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: 312.75 E-value: 2.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVM- 537
Cdd:cd06825 1 RAWLEIDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 538 --NPEQnsFNLMIEYNLEPEIYS---SLVLNQFQKTLEnvgipdypVHIKLDTGMHRLGFMPNEIDTlINNIVQSKNIKV 612
Cdd:cd06825 81 ytPPVR--AKELKKYSLTQTLISeayAEELSKYAVNIK--------VHLKVDTGMHRLGESPEDIDS-ILAIYRLKNLKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 613 ASIFSHLAASD----ENIhdEFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQ 688
Cdd:cd06825 150 SGIFSHLCVSDsldeDDI--AFTKHQIACFDQVLADLKARGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 689 EQ------LEIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGKGKLFINGHIVPIVGNI 762
Cdd:cd06825 228 DPtklgldLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSNQKAYVLINGKRAPIIGNI 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 763 CMDMCMADITGC-TIHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:cd06825 308 CMDQLMVDVTDIpEVKEGDTATLIGQdgdeELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
459-817 |
1.02e-97 |
|
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: 308.51 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 459 RTVLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMN 538
Cdd:TIGR00492 2 PATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 539 --PEQNSFNLmIEYNLEPEIYSSLVLNQFQKTLENVGiPDYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNI-KVASI 615
Cdd:TIGR00492 82 gfFAEDLKIL-AAWDLTTTVHSVEQLQALEEALLKEP-KRLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFlELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 616 FSHLAASDENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGIS---SMQQE--- 689
Cdd:TIGR00492 160 FSHFATADEPKTG-TTQKQIERFNSFLEGLKQQNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYpsaDMSDGapf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 690 QLEIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMA 769
Cdd:TIGR00492 239 GLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNG-TPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1082420391 770 DITGCT-IHEGDEVEVFGKEIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:TIGR00492 318 DLGPDLqDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
460-817 |
2.78e-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: 299.03 E-value: 2.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 460 TVLEINLNALVHNLNYFKSRLnPKTRLMVMVKALSYGSGTYEIAGVLQyhGVDYLGVAFADEGVELREAGIKLPIIVM-- 537
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELA-PNSKILAVVKANAYGHGLVRVAKALA--DADGFAVACIEEALALREAGITKPILLLeg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 538 --NPEQnsFNLMIEYNLEPEIYsslvlNQFQ-KTLENVGIPD-YPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVA 613
Cdd:cd06827 79 ffSADE--LPLAAEYNLWTVVH-----SEEQlEWLEQAALSKpLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 614 SIFSHLAASDEnIHDEFTDTQIKLFDnlssKIISKLNYPviRHVLNSSGIERFPYGQFDMVRLGIGLYGIS-----SMQQ 688
Cdd:cd06827 152 VLMTHFACADE-PDSPGTAKQLAIFE----QATAGLPGP--RSLANSAAILAWPEAHGDWVRPGIMLYGASpfadkSGAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 689 EQLEIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGKgKLFINGHIVPIVGNICMDMCM 768
Cdd:cd06827 225 LGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGT-PVLVNGQRTPLVGRVSMDMLT 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1082420391 769 ADITGC-TIHEGDEVEVFGKEIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:cd06827 304 VDLTDLpEAKVGDPVELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
29-453 |
3.72e-73 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273468 [Multi-domain] Cd Length: 417 Bit Score: 245.25 E-value: 3.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 29 IDSRNFVssQDALFFAIRGERHDGHKYINDLYNKGVRNFVVEQIPENSkdyPNANFLVVRKALEALQNLAAHYRKQFNYP 108
Cdd:TIGR01143 1 TDSRAIK--PGDLFIALKGERFDGHDFVEQALAAGAVAVVVDREVGPD---NGLPQILVDDTLEALQALARAKRAKFSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 109 VIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKTFNIAIFEAGISLSGEMEKLEKMIQPTIGVI 188
Cdd:TIGR01143 76 VIGITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEIGLPLTLLRAPGDHDYAVLEMGASHPGEIAYLAEIAKPDIAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 189 TNIGESHQENFRDYKHKAIEKLKLF---KHSEILVYCKDHVLIDKLISdapELSQKKLFSWSVNpGAGLRL--VSNSKIN 263
Cdd:TIGR01143 156 TNIGPAHLEGFGSLEGIAEAKGEILqglKENGIAVINADDPAFADLAK---RLPNRNILSFGFE-GGDFVAkdISYSALG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 264 dKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLLPVAMRMELKKGmNGCSIINDSYNSDL 343
Cdd:TIGR01143 232 -STSFTLVAPGGEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQTK-NGLTLIDDTYNANP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 344 NSLNIALNYLSQQNqhSKKVLILSDILQSGKSETVLYSEVASLIKKYQVDQIIGIGKSIVSQADVFDIPKSFYSTTNEFL 423
Cdd:TIGR01143 310 DSMRAALDALARFP--GKKILVLGDMAELGEYSEELHAEVGRYANSLGIDLVFLVGEEAAVIYDSFGKQGKHFADKDELL 387
|
410 420 430
....*....|....*....|....*....|
gi 1082420391 424 SDLSKKTFSDSSILLKGSRNFAFEKISALL 453
Cdd:TIGR01143 388 AFLKTLVRKGDVVLVKGSRSVKLEKVVEAL 417
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
464-684 |
1.34e-66 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 220.56 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 464 INLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPIIVMNP-EQN 542
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGfPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 543 SFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAAS 622
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKP-LRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420391 623 DENIHDeFTDTQIKLFDNLSSKIISKLNYPVIRHVLNSSGIERFPyGQFDMVRLGIGLYGIS 684
Cdd:pfam01168 160 DEPDDP-YTNAQLARFREAAAALEAAGLRPPVVHLANSAAILLHP-LHFDMVRPGIALYGLS 219
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
461-817 |
2.10e-62 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 215.64 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 461 VLEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPII-VMNP 539
Cdd:PRK13340 42 WLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLrVRSA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 540 EQNSFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDT-GMHRLGFmpnEIDTL-----INNIVQSKNIKVA 613
Cdd:PRK13340 122 SPAEIEQALRYDLEELIGDDEQAKLLAAIAKKNGKP-IDIHLALNSgGMSRNGL---DMSTArgkweALRIATLPSLGIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 614 SIFSHLAASDEnihDEfTDTQIKLFDNLSSKIISKLN---YPVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQEQ 690
Cdd:PRK13340 198 GIMTHFPNEDE---DE-VRWKLAQFKEQTAWLIGEAGlkrEKITLHVANSYATLNVPEAHLDMVRPGGILYGDRHPANTE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 691 LEIVSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgKGKLFINGHIVPIVGNICMDMCMAD 770
Cdd:PRK13340 274 YKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASN-KAPVLINGQRAPVVGRVSMNTLMVD 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1082420391 771 ITGC-TIHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:PRK13340 353 VTDIpNVKPGDEVVLFGKqgnaEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
7-449 |
6.34e-61 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 222.66 E-value: 6.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 7 EISKIIHAQLTLKENCEIRNLIIDSRNFVSsqDALFFAIRGERHDGHKYINDLYNKGVRNFVVEQiPENSKDYPNanfLV 86
Cdd:PRK11929 509 RAAKGGSNSLQINSLPHAGAVSTDSRSVGR--GELFVALRGENFDGHDYLPQAFAAGACAAVVER-QVADVDLPQ---IV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 87 VRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQIL---HSKINIIRSPKSFNSQVGVPLSVWLMNKTFNIAI 163
Cdd:PRK11929 583 VDDTRAALGRLATAWRARFSLPVVAITGSNGKTTTKEMIAAILaawQGEDRVLATEGNFNNEIGVPLTLLRLRAQHRAAV 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 164 FEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKH---SEILVYCKDhvliDKLISDAPELS- 239
Cdd:PRK11929 663 FELGMNHPGEIAYLAAIAAPTVALVTNAQREHQEFMHSVEAVARAKGEIIAAlpeDGVAVVNGD----DPYTAIWAKLAg 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 240 QKKLFSWSVNPGAGLRL---VSNSKINDKTSLKIAYES--EQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFE 314
Cdd:PRK11929 739 ARRVLRFGLQPGADVYAekiAKDISVGEAGGTRCQVVTpaGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLE 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 315 SLLPVAMRMELKKGMNGCSIINDSYNSDLNSLNIALNYLSQQnQHSKKVLILSDILQSGKSETVLYSEVASLIKKYQVDQ 394
Cdd:PRK11929 819 RFQPVAGRMQRRRLSCGTRIIDDTYNANPDSMRAAIDVLAEL-PNGPRALVLGDMLELGDNGPAMHREVGKYARQLGIDA 897
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420391 395 IIGIGKSIVSQADVFD--IPKSFYStTNEFLSDLSKKTFSDSSILLKGSRNFAFEKI 449
Cdd:PRK11929 898 LITLGEAARDAAAAFGagARGVCAS-VDEIIAALRGALPEGDSVLIKGSRFMRLERV 953
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
694-817 |
4.09e-58 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 194.12 E-value: 4.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGkGKLFINGHIVPIVGNICMDMCMADITG 773
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNR-GEVLINGKRAPIVGRVCMDQLMVDVTD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1082420391 774 C-TIHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:pfam00842 80 VpEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
464-817 |
2.65e-53 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 189.17 E-value: 2.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 464 INLNALVHNLNYFKsRLNPKTRLMVMVKALSYGSGTYEIAGVLQyhGVDYLGVAFADEGVELREAGIKLPIIVMNP--EQ 541
Cdd:PRK03646 8 LDLQALKQNLSIVR-EAAPGARVWSVVKANAYGHGIERIWSALG--ATDGFAVLNLEEAITLRERGWKGPILMLEGffHA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 542 NSFNLMIEYNLEPEIYSSLVLNQFQKTleNVGIPdYPVHIKLDTGMHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAA 621
Cdd:PRK03646 85 QDLELYDQHRLTTCVHSNWQLKALQNA--RLKAP-LDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHFAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 622 SDeniHDEFTDTQIKLFDNLSSKIISKlnypviRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQEQ------LEIVS 695
Cdd:PRK03646 162 AD---HPDGISEAMARIEQAAEGLECE------RSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRdiantgLRPVM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 696 TLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNGKgKLFINGHIVPIVGNICMDMCMADITGC- 774
Cdd:PRK03646 233 TLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGT-PVLVDGVRTRTVGTVSMDMLAVDLTPCp 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1082420391 775 --TIheGDEVEVFGKEIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:PRK03646 312 qaGI--GTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
694-817 |
1.67e-52 |
|
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: 178.42 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 694 VSTLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgkGKLFINGHIVPIVGNICMDMCMADITG 773
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSN--GPVLINGQRVPVVGRVSMDQLMVDVTD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1082420391 774 C-TIHEGDEVEVFGK-EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:smart01005 79 IpDVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
462-817 |
5.52e-44 |
|
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: 162.90 E-value: 5.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 462 LEINLNALVHNLNYFKSRLNPKTRLMVMVKALSYGSGTYEIAGVLQYHGVDYLGVAFADEGVELREAGIKLPII-VMNPE 540
Cdd:cd06826 4 LEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILrVRTAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 541 QNSFNLMIEYNLEPEIYSSLVLNQFQKTLENVGIPdYPVHIKLDT-GMHRLGFMPNEIDTLIN--NIVQSKNIKVASIFS 617
Cdd:cd06826 84 PSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKT-LPVHLALNSgGMSRNGLELSTAQGKEDavAIATLPNLKIVGIMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 618 HLAASDENihdeftDTQIKL--FDNLSSKIISKLNY---PVIRHVLNSSGIERFPYGQFDMVRLGIGLYGISSMQQEQLE 692
Cdd:cd06826 163 HFPVEDED------DVRAKLarFNEDTAWLISNAKLkreKITLHAANSFATLNVPEAHLDMVRPGGILYGDTPPSPEYKR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 693 IVStLKSTVIQIKHVPKSETIGYGRKGKAINDMTIAIIPIGYADGLNRKLSNgKGKLFINGHIVPIVGNICMDMCMADIT 772
Cdd:cd06826 237 IMS-FKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSN-KAHVLINGQRVPVVGKVSMNTVMVDVT 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1082420391 773 GCT-IHEGDEVEVFGK----EIPVNEIARTLETIPYEIFAGIPSRVKRVY 817
Cdd:cd06826 315 DIPgVKAGDEVVLFGKqggaEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
3-395 |
1.29e-34 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 138.37 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 3 YTISEISKIIHAQLTLKENCEIRNLIIDSRNFVSSqDAlFFAIRGERHDGHKYINDLYNKGVRNFVVEQiPENSKDYPNA 82
Cdd:PRK14093 7 WTSDAMAEAMGATRSGALPRDVTGISIDSRTLAPG-DA-YFAIKGDVHDGHAFVAAALKAGAALAVVER-AQRDKFAADA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 83 NFLVVRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKTFNIA 162
Cdd:PRK14093 84 PLLVVDDVLAALRDLGRAARARLEAKVIAVTGSVGKTSTKEALRGVLGAQGETHASVASFNNHWGVPLSLARCPADARFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 163 IFEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKHSE---ILVYCKDHVLIDKLISDAPELS 239
Cdd:PRK14093 164 VFEIGMNHAGEIEPLVKMVRPHVAIITTVEPVHLEFFSGIEAIADAKAEIFTGLEpggAAVLNRDNPQFDRLAASARAAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 240 QKKLFSWSVNPGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLLPV 319
Cdd:PRK14093 244 IARIVSFGADEKADARLLDVALHADCSAVHADILGHDVTYKLGMPGRHIAMNSLAVLAAAELAGADLALAALALSQVQPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 320 AMR-----MELKKGMngCSIINDSYNSDLNSLNIALNYLSQQ--NQHSKKVLILSDILQSGKSETVLYSEVASLIKKYQV 392
Cdd:PRK14093 324 AGRgvrhtLEVGGGE--ATLIDESYNANPASMAAALGVLGRApvGPQGRRIAVLGDMLELGPRGPELHRGLAEAIRANAI 401
|
...
gi 1082420391 393 DQI 395
Cdd:PRK14093 402 DLV 404
|
|
| murF |
PRK10773 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed |
4-456 |
2.78e-27 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
Pssm-ID: 182718 [Multi-domain] Cd Length: 453 Bit Score: 115.90 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 4 TISEISKIIHAQLtLKENCEIRNLIIDSRNFVSSqdALFFAIRGERHDGHKYINDLYNKGVRNFVVeqipenSKDYP-NA 82
Cdd:PRK10773 5 TLSQLADILNGEL-QGADITIDAVTTDTRKVTPG--CLFVALKGERFDAHDFADDAKAAGAGALLV------SRPLDiDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 83 NFLVVRKALEALQNLAAHYRKQFNYPVIGITGSNGKTIVKEWIFQILHSKINIIRSPKSFNSQVGVPLSVWLMNKTFNIA 162
Cdd:PRK10773 76 PQLVVKDTRLAFGQLAAWVRQQVPARVVALTGSSGKTSVKEMTAAILRQCGNTLYTAGNLNNDIGVPLTLLRLTPEHDYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 163 IFEAGISLSGEMEKLEKMIQPTIGVITNIGESHQENFRDYKHKAIEKLKLFKHSEIlvycKDHVLIDKLISDAPE----L 238
Cdd:PRK10773 156 VIELGANHQGEIAYTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPE----NGIAIMNADSNDWLNwqsvI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 239 SQKKLFSWSVNPGAGLRL-VSNSKINDK-TSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESL 316
Cdd:PRK10773 232 GSKTVWRFSPNAANSVDFtATNIHVTSHgTEFTLHTPTGSVDVLLPLPGRHNIANALAAAALAMSVGATLDAVKAGLANL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 317 LPVAMRM---ELKKGMngcSIINDSYNSDLNSLNIALNYLSQQNQHskKVLILSDILQSGKSETVLYSEVASLIKKYQVD 393
Cdd:PRK10773 312 KAVPGRLfpiQLAEGQ---LLLDDSYNANVGSMTAAAQVLAEMPGY--RVMVVGDMAELGAESEACHRQVGEAAKAAGID 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420391 394 QIIGIGK--SIVSQA----DVFDIPKSFYSTTNEFLSDLSKKTfsdssILLKGSRNFAFEKISALLEEK 456
Cdd:PRK10773 387 KVLSVGKlsHAISEAsgvgEHFADKTALIARLKALLAEHQVIT-----ILVKGSRSAAMEEVVRALQEN 450
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
26-337 |
2.05e-22 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 101.31 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 26 NLIIDSRNfVSSQDaLFFAIRGERHDGHKYINDLYNKGVRNFVVEQipENSKDYPNANFLVVRKALEALQNLAAHYrkqF 105
Cdd:COG0769 1 GITYDSRK-VKPGD-LFVALPGARVDGHDFIAQAIARGAVAVVTEA--PGALLAAGVPVIVVPDPRAALALLAAAF---Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 106 NYP-----VIGITGSNGKTIVKEWIFQILH---------SKINIIRSPKSFNSQVGVPLSVwLMNKTFNIAIfEAGIS-- 169
Cdd:COG0769 74 GHPsqklkLIGVTGTNGKTTTTYLLAQILRalgkktgliGTVGNGIGGELIPSSLTTPEAL-DLQRLLAEMV-DAGVThv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 170 -------------LSGemeklekmIQPTIGVITNIGESHQenfrDYkHKAIE-----KLKLF---KHSEILVYCKDHVLI 228
Cdd:COG0769 152 vmevsshaldqgrVDG--------VRFDVAVFTNLTRDHL----DY-HGTMEayfaaKARLFdqlGPGGAAVINADDPYG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 229 DKLISDAPelsqKKLFSWSVNPGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSD 308
Cdd:COG0769 219 RRLAAAAP----ARVITYGLKADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEE 294
|
330 340
....*....|....*....|....*....
gi 1082420391 309 FKSQFESLLPVAMRMELKKGMNGCSIIND 337
Cdd:COG0769 295 ILAALEKLKGVPGRMERVDGGQGPTVIVD 323
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
469-678 |
3.30e-18 |
|
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: 83.91 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 469 LVHNLNYFKSRLNPKTRLMVMVKALsygsGTYEIAGVLqYHGVDYLGVAFADEGVELREAGIKL-PIIVMNP--EQNSFN 545
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKAN----ANPEVARTL-AALGTGFDVASLGEALLLRAAGIPPePILFLGPckQVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 546 LMIEYNLEPEIYSSLV-LNQFQKTLENVGIPdYPVHIKLDTG--MHRLGFMPNEIDTLINNIVQSKNIKVASIFSHLAAS 622
Cdd:cd06808 76 DAAEQGVIVVTVDSLEeLEKLEEAALKAGPP-ARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420391 623 DENIH--DEFTDTQIKLFDNLSSKIISklnyPVIRHVLNSSGIERFPY---GQFDMVRLGI 678
Cdd:cd06808 155 DEDYSpfVEALSRFVAALDQLGELGID----LEQLSIGGSFAILYLQElplGTFIIVEPGR 211
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
23-337 |
8.81e-17 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 84.03 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 23 EIRNLIIDSRNfvSSQDALFFAIRGERHDGHKYINDLYNKGVRNFVVEQIPEnskDYPNANFLVVRKALEALQNLAAHYr 102
Cdd:PRK00139 14 EITGLTYDSRK--VKPGDLFVALPGHKVDGRDFIAQAIANGAAAVVAEADGE---AGTGVPVIIVPDLRKALALLAAAF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 103 kqFNYP-----VIGITGSNGKTIVKEWIFQILH---------SKINIIRSPKSFNSQVGVPLSVWLmNKTFNIAIfEAGI 168
Cdd:PRK00139 88 --YGHPsdklkLIGVTGTNGKTTTAYLLAQILRllgektaliGTLGNGIGGELIPSGLTTPDALDL-QRLLAELV-DAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 169 SLsGEME--------------KLEkmiqptIGVITNIGESHQenfrDYkHKAIE-----KLKLFK-HSEILVYCKDHVLI 228
Cdd:PRK00139 164 TY-AAMEvsshaldqgrvdglKFD------VAVFTNLSRDHL----DY-HGTMEdylaaKARLFSeLGLAAVINADDEVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 229 DKLISDAPELSQKKlfswsvnPGAGLRLVSNSKINDKTSLKIAYEseqVELTIP--FtdNASveDAMHVIACLCVLGFKL 306
Cdd:PRK00139 232 RRLLALPDAYAVSM-------AGADLRATDVEYTDSGQTFTLVTE---VESPLIgrF--NVS--NLLAALAALLALGVPL 297
|
330 340 350
....*....|....*....|....*....|.
gi 1082420391 307 SDFKSQFESLLPVAMRMELKKGMNGCSIIND 337
Cdd:PRK00139 298 EDALAALAKLQGVPGRMERVDAGQGPLVIVD 328
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
112-299 |
9.96e-17 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 79.27 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 112 ITGSNGKTIVKEWIFQILHSKINII--------RSPKSFNSQVGVPLSVWLM-NKTFNIAIFEAGISLSGEmEKLEKMIQ 182
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVIgtigtyigKSGNTTNNAIGLPLTLAEMvEAGAEYAVLEVSSHGLGE-GRLSGLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 183 PTIGVITNIGESHQENFRDYKHKAIEKLKLFKHSE---ILVYCKDHVLIDKLISDAPELSQKKLfSWSVNPGAGLRLVSN 259
Cdd:pfam08245 80 PDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPedgIAVINADDPYGAFLIAKLKKAGVRVI-TYGIEGEADLRAANI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1082420391 260 SKINDKTSLKI-AYESEQVELTIPFTDNASVEDAMHVIACL 299
Cdd:pfam08245 159 ELSSDGTSFDLfTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
21-337 |
1.47e-14 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 76.97 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 21 NCEIRNLIIDSRNfVSSQDaLFFAIRGERHDGHKYINDLYNKGVRNFVVEqiPENSKDYPNANFLVVRKALEALQNLAAH 100
Cdd:TIGR01085 1 DLEVTGLTLDSRE-VKPGD-LFVAIKGTHVDGHDFIHDAIANGAVAVVVE--RDVDFYVAPVPVIIVPDLRHALSSLAAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 101 YrkqFNYP-----VIGITGSNGKTIVKEWIFQILHSK----------------INIIRSPKSFNSqvGVPLSVWLMNKTF 159
Cdd:TIGR01085 77 F---YGHPskklkVIGVTGTNGKTTTTSLIAQLLRLLgkktgligtigyrlggNDLIKNPAALTT--PEALTLQSTLAEM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 160 N-----IAIFEA---GISLsGEMEKLEKmiqpTIGVITNIGESHQenfrDYkHKAIE-----KLKLFKHseilVYCKDH- 225
Cdd:TIGR01085 152 VeagaqYAVMEVsshALAQ-GRVRGVRF----DAAVFTNLSRDHL----DF-HGTMEnyfaaKASLFTE----LGLKRFa 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 226 -VLIDKLISD--APELSQKKLFSWSVNPGAG----LRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIAC 298
Cdd:TIGR01085 218 vINLDDEYGAqfVKRLPKDITVSAITQPADGraqdIKITDSGYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAALAT 297
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1082420391 299 LC-VLGFKLSDFKSQFESLLPVAMRMELKKGMNGCSIIND 337
Cdd:TIGR01085 298 LLhLGGIDLEDIVAALEKFRGVPGRMELVDGGQKFLVIVD 337
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
24-324 |
3.11e-13 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 73.58 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 24 IRNLIIDSRNfVSSQDaLFFAIRGERHDGHKYINDLYNKGVRNFVVEQIPENSKDYPNANFLVVRKALEALQNLAAHYRK 103
Cdd:PRK11929 29 TADLRLDSRE-VQPGD-LFVACRGAASDGRAFIDQALARGAAAVLVEAEGEDQVAAADALVLPVADLRKALGELAARWYG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 104 QFNYP--VIGITGSNGKTIVKEWIFQILHS---KINIIRSPKSFNSQVGVPLS-----VWLMNKTFNiAIFEAGI----- 168
Cdd:PRK11929 107 RPSEQlsLVAVTGTNGKTSCAQLLAQLLTRlgkPCGSIGTLGARLDGRLIPGSlttpdAIILHRILA-RMRAAGAdavam 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 169 ---SLSGEMEKLEKmIQPTIGVITNIGESHQenfrDYkHKAIE-----KLKLF---KHSEILVYCKDHVLIDKLISDAPE 237
Cdd:PRK11929 186 easSHGLEQGRLDG-LRIAVAGFTNLTRDHL----DY-HGTMQdyeeaKAALFsklPGLGAAVINADDPAAARLLAALPR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 238 LSQKKLfsWSVNPGAGLRLVSNSKINDKTSLKIAYESEQVELTIPFTDNASVEDAMHVIACLCVLGFKLSDFKSQFESLL 317
Cdd:PRK11929 260 GLKVGY--SPQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVS 337
|
....*..
gi 1082420391 318 PVAMRME 324
Cdd:PRK11929 338 PVPGRME 344
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
105-338 |
2.50e-11 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 66.60 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 105 FNYPVIGITGSNGKTIVKEWIFQILhsKINIIRSPKSFNsqVGVPLSVWLMNKTFNIAIFEagISlSGEMEKLEKMIqPT 184
Cdd:TIGR01087 100 VPLPVVAITGTNGKTTTTSLLYHLL--KAAGLKAFLGGN--IGTPALEVLDQEGAELYVLE--LS-SFQLETTESLR-PE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 185 IGVITNIGESHQE---NFRDYkHKAieKLKLFKH---SEILVYCKDHVLIDKLISDAPelSQKKLFSWSVNPGAGLRLVs 258
Cdd:TIGR01087 172 IALILNISEDHLDwhgSFEDY-VAA--KLKIFARqteGDVAVLNADDPRFARLAQKSK--AQVIWFSVEKDAERGLCIR- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 259 nskiNDKTSLKIAYEseqvELTIPFTDNAsvEDAMHVIACLCVLGFKLSDFKSQFESLLPVAMRMELKKGMNGCSIINDS 338
Cdd:TIGR01087 246 ----DGGLYLKPNDL----EGSLLGLHNA--ENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDS 315
|
|
| Mur_ligase |
pfam01225 |
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ... |
23-102 |
1.02e-10 |
|
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460121 [Multi-domain] Cd Length: 84 Bit Score: 58.40 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 23 EIRNLIIDSRnFVSSqDALFFAIRGERHDGHKYINDLYNKGVRNFVVE--------QIPENskDYPNANFLVVRKALEAL 94
Cdd:pfam01225 1 EIHFVGIDGR-GMSP-GALFLALKGYRVDGSDFIESLIALGAAAVVGHdaannispDNPEL--EAAKVPGIPVIDRREAL 76
|
....*...
gi 1082420391 95 QNLAAHYR 102
Cdd:pfam01225 77 AELAAAFY 84
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
108-338 |
3.10e-06 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 50.35 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 108 PVIGITGSNGKTIVKEWIFQILhsKINIIRSPKSFNsqVGVPLSVWLMNKTFNiAIFEAGISlSGEMEKLeKMIQPTIGV 187
Cdd:PRK14106 109 PIVAITGTNGKTTTTTLLGEIF--KNAGRKTLVAGN--IGYPLIDAVEEYGED-DIIVAEVS-SFQLETI-KEFKPKVGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 188 ITNIGESHQEnfrdyKHKAIE-----KLKLFKH---SEILVYCKDHVLIDKLISDAPE----LSQKKLFSWSVnpgaglr 255
Cdd:PRK14106 182 ILNITPDHLD-----RHKTMEnyikaKARIFENqrpSDYTVLNYDDPRTRSLAKKAKArvifFSRKSLLEEGV------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 256 LVSNSKI----NDKTSLKIAYEseqvELTIPFTDNasVEDAMHVIACLCVLGFKLSDFKSQFESLLPVAMRMELKKGMNG 331
Cdd:PRK14106 250 FVKNGKIvislGGKEEEVIDID----EIFIPGEHN--LENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAEING 323
|
....*..
gi 1082420391 332 CSIINDS 338
Cdd:PRK14106 324 VKFINDS 330
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
5-129 |
1.90e-04 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 44.64 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420391 5 ISEISKIIHAQLTLkENCEIRNLIIDSRNfvSSQDALFFAIRGerHDGHKYINDLYNKGVRNFVVEqipensKDYP-NAN 83
Cdd:PRK14022 16 FREIIDQDHYHYNY-SGVQFDDISYDSRT--ADEGTLFFAKGA--YFKHKFLQNAITQGLKLYVSE------KDYEvGIP 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1082420391 84 FLVVRKALEALQNLAAHYrkqFNYP-----VIGITGSNGKTIVKEWIFQIL 129
Cdd:PRK14022 85 QVIVPDIKKAMSLIAMEF---YDNPqhklkLLAFTGTKGKTTAAYFAYHIL 132
|
|
| |
