|
Name |
Accession |
Description |
Interval |
E-value |
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
3-449 |
4.64e-166 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 474.94 E-value: 4.64e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 3 KKILFLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLLSQAR 82
Cdd:COG0773 5 MHIHFIGIGGIGMSGLAEILLALGYKVSGSDLAESPMTERLEALGIPVFIGHDAENIDDADLVVVSSAIPRDNPELVAAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 83 TLGIQCLQRAMFLAVLMKDfSYSLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVVKHVDSNIQVNGTDKLVIEADES 162
Cdd:COG0773 85 ERGIPVLSRAEMLAELMRG-KRSIAVAGTHGKTTTTSMLAHILEEAGLDPTFLIGGILNNFGTNARLGDGDYFVAEADES 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 163 DASFLYLSPQVAIVTNIDLDHMATYKnSYQNLLENFANFISKesVKS---IYLCADDQGCRDLLAKytlTDKNITSYGFS 239
Cdd:COG0773 164 DGSFLHYSPDIAVVTNIEADHLDIYG-DLEAIKEAFHEFARN--VPFyglLVLCADDPGLRELLPR---CGRPVITYGFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 240 NDADVQIYDYHIADEITHFKIIYKGDEL-SFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIytk 318
Cdd:COG0773 238 EDADYRAENIRIDGGGSTFDVLRRGEELgEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFEL--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 319 IISGYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGEQVIKG 398
Cdd:COG0773 315 KGEVGGVTVIDDYAHHPTEIAATLAAAREKYPDRRLVAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYAAREKPIPG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1053731810 399 AESQDIAKGLSQY----LLADSFDHAIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:COG0773 395 VSSEDLAEAIRKRgkdvVYVPDLDELVEALAEIARPGDVVLTMGAGDIGGLGEKL 449
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
4-449 |
3.52e-125 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 370.87 E-value: 3.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 4 KILFLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLLSQART 83
Cdd:TIGR01082 1 KIHFVGIGGIGMSGIAEILLNRGYQVSGSDIAENATTKRLEALGIPIYIGHSAENLDDADVVVVSAAIKDDNPEIVEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 84 LGIQCLQRAMFLAVLMKdFSYSLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVVKHVDSNIQVNGTDKLVIEADESD 163
Cdd:TIGR01082 81 RGIPVIRRAEMLAELMR-FRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVVVGGLVKEAGTNARLGSGEYLVAEADESD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 164 ASFLYLSPQVAIVTNIDLDHMATYKNSYQNLLENFANFISK-ESVKSIYLCADDQGCRDLLAKytLTDKNITSYGFSNDA 242
Cdd:TIGR01082 160 ASFLHLQPNVAIVTNIEPDHLDTYGSSFERLKAAFEKFIHNlPFYGLAVICADDPVLRELVPK--ATEQVITYGGSGEDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 243 DVQIYDYHIADEITHFKIIYKGDE-LSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIYTKIis 321
Cdd:TIGR01082 238 DYRAENIQQSGAEGKFSVRGKGKLyLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEILGEF-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 322 gYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGEQVIKGAES 401
Cdd:TIGR01082 316 -GGVLLIDDYAHHPTEIKATLKAARQGYPDKRIVVVFQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAGEEPINGIDG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1053731810 402 QDIAKGLSQ------YLLADSFDHaIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:TIGR01082 395 KSLARKITQlgkiepYFVPDLAEL-VEFLAAVLQSGDLILTMGAGDIIKLAREL 447
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
1-449 |
4.53e-75 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 250.50 E-value: 4.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 1 MNKKIL--FLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLL 78
Cdd:PRK14573 1 MMKSLFyhFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYSSSISKDNVEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 79 SQARTLGIQCLQRAMFLAVLMKDFSySLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVvkhvdSNIQVNG----TDK 154
Cdd:PRK14573 81 LSAKSRGNRLVHRAELLAELMQEQI-SILVSGSHGKTTVSSLITAIFQEAKKDPSYAIGGL-----NQEGLNGysgsSEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 155 LVIEADESDASFLYLSPQVAIVTNIDLDHMATYKNSYQNLLENFANFISKesVKSIYLCADDQGCRDLlaKYTLTDkniT 234
Cdd:PRK14573 155 FVAEADESDGSLKHYTPEFSVITNIDNEHLSNFEGDRELLLASIQDFARK--VQQINKCFYNGDCPRL--KGCLQG---H 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 235 SYGFSNDADVQIYDYHIADEITHFKIIYKG-DELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRF 313
Cdd:PRK14573 228 SYGFSSSCDLHILSYYQEGWRSYFSAKFLGvVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 314 DiyTKIISgYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGE 393
Cdd:PRK14573 308 E--RKNSS-ETFLFLEDYAHHPSEISCTLRAVRDAVGLRRIIAICQPHRFSRLRECLDSFPSAFQDADEVILTDVYSAGE 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053731810 394 QVIKGAESQDIAKGLSQ-------YLladSFDHAIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:PRK14573 385 EPEDSISYQKLAEAISQssivkctYV---PFHEIQRYLEQSIRVHDVCVSLGAGNIYTLGEAL 444
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
108-289 |
2.78e-22 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 93.91 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 108 VTGTHGKTTTSSILATLLCELDK-HSSFVVGGVVKHVDSN--IQVN---------GTDKLVIEADESDASFLYLS----P 171
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGvIGTIGTYIGKSGNTTNnaIGLPltlaemveaGAEYAVLEVSSHGLGEGRLSgllkP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 172 QVAIVTNIDLDHMATYKnSYQNLLENFANFISKESVKSIYLC-ADDQGCRDLLAKYTLTDKNITSYGFSNDADVQIYDYH 250
Cdd:pfam08245 81 DIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPEDGIAVInADDPYGAFLIAKLKKAGVRVITYGIEGEADLRAANIE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1053731810 251 IADEITHFKII-YKGDELSFKLQLPGRYNVQNATACIIAC 289
Cdd:pfam08245 160 LSSDGTSFDLFtVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
2-60 |
1.52e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.38 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053731810 2 NKKILFLGVGGIGVSAlAIAAKRLGADVAGYDSIPNKLtAKLQTLG--------------IAIFTSPSGVDVA 60
Cdd:cd05188 135 GDTVLVLGAGGVGLLA-AQLAKAAGARVIVTDRSDEKL-ELAKELGadhvidykeedleeELRLTGGGGADVV 205
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
4-72 |
2.65e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.26 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731810 4 KILFLGVGGIGVSALAIAaKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVD-----VANYDIVVysSAIL 72
Cdd:smart01002 22 KVVVIGAGVVGLGAAATA-KGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAElleeaVKEADLVI--GAVL 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
3-449 |
4.64e-166 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 474.94 E-value: 4.64e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 3 KKILFLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLLSQAR 82
Cdd:COG0773 5 MHIHFIGIGGIGMSGLAEILLALGYKVSGSDLAESPMTERLEALGIPVFIGHDAENIDDADLVVVSSAIPRDNPELVAAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 83 TLGIQCLQRAMFLAVLMKDfSYSLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVVKHVDSNIQVNGTDKLVIEADES 162
Cdd:COG0773 85 ERGIPVLSRAEMLAELMRG-KRSIAVAGTHGKTTTTSMLAHILEEAGLDPTFLIGGILNNFGTNARLGDGDYFVAEADES 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 163 DASFLYLSPQVAIVTNIDLDHMATYKnSYQNLLENFANFISKesVKS---IYLCADDQGCRDLLAKytlTDKNITSYGFS 239
Cdd:COG0773 164 DGSFLHYSPDIAVVTNIEADHLDIYG-DLEAIKEAFHEFARN--VPFyglLVLCADDPGLRELLPR---CGRPVITYGFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 240 NDADVQIYDYHIADEITHFKIIYKGDEL-SFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIytk 318
Cdd:COG0773 238 EDADYRAENIRIDGGGSTFDVLRRGEELgEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFEL--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 319 IISGYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGEQVIKG 398
Cdd:COG0773 315 KGEVGGVTVIDDYAHHPTEIAATLAAAREKYPDRRLVAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYAAREKPIPG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1053731810 399 AESQDIAKGLSQY----LLADSFDHAIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:COG0773 395 VSSEDLAEAIRKRgkdvVYVPDLDELVEALAEIARPGDVVLTMGAGDIGGLGEKL 449
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
4-449 |
3.52e-125 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 370.87 E-value: 3.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 4 KILFLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLLSQART 83
Cdd:TIGR01082 1 KIHFVGIGGIGMSGIAEILLNRGYQVSGSDIAENATTKRLEALGIPIYIGHSAENLDDADVVVVSAAIKDDNPEIVEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 84 LGIQCLQRAMFLAVLMKdFSYSLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVVKHVDSNIQVNGTDKLVIEADESD 163
Cdd:TIGR01082 81 RGIPVIRRAEMLAELMR-FRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVVVGGLVKEAGTNARLGSGEYLVAEADESD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 164 ASFLYLSPQVAIVTNIDLDHMATYKNSYQNLLENFANFISK-ESVKSIYLCADDQGCRDLLAKytLTDKNITSYGFSNDA 242
Cdd:TIGR01082 160 ASFLHLQPNVAIVTNIEPDHLDTYGSSFERLKAAFEKFIHNlPFYGLAVICADDPVLRELVPK--ATEQVITYGGSGEDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 243 DVQIYDYHIADEITHFKIIYKGDE-LSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIYTKIis 321
Cdd:TIGR01082 238 DYRAENIQQSGAEGKFSVRGKGKLyLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEILGEF-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 322 gYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGEQVIKGAES 401
Cdd:TIGR01082 316 -GGVLLIDDYAHHPTEIKATLKAARQGYPDKRIVVVFQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAGEEPINGIDG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1053731810 402 QDIAKGLSQ------YLLADSFDHaIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:TIGR01082 395 KSLARKITQlgkiepYFVPDLAEL-VEFLAAVLQSGDLILTMGAGDIIKLAREL 447
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
1-449 |
4.53e-75 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 250.50 E-value: 4.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 1 MNKKIL--FLGVGGIGVSALAIAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVDVANYDIVVYSSAILNNHPLL 78
Cdd:PRK14573 1 MMKSLFyhFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYSSSISKDNVEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 79 SQARTLGIQCLQRAMFLAVLMKDFSySLAVTGTHGKTTTSSILATLLCELDKHSSFVVGGVvkhvdSNIQVNG----TDK 154
Cdd:PRK14573 81 LSAKSRGNRLVHRAELLAELMQEQI-SILVSGSHGKTTVSSLITAIFQEAKKDPSYAIGGL-----NQEGLNGysgsSEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 155 LVIEADESDASFLYLSPQVAIVTNIDLDHMATYKNSYQNLLENFANFISKesVKSIYLCADDQGCRDLlaKYTLTDkniT 234
Cdd:PRK14573 155 FVAEADESDGSLKHYTPEFSVITNIDNEHLSNFEGDRELLLASIQDFARK--VQQINKCFYNGDCPRL--KGCLQG---H 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 235 SYGFSNDADVQIYDYHIADEITHFKIIYKG-DELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRF 313
Cdd:PRK14573 228 SYGFSSSCDLHILSYYQEGWRSYFSAKFLGvVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 314 DiyTKIISgYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIHVFQPHRYTRNRDLIKDWPKALALADQLILLPTYSAGE 393
Cdd:PRK14573 308 E--RKNSS-ETFLFLEDYAHHPSEISCTLRAVRDAVGLRRIIAICQPHRFSRLRECLDSFPSAFQDADEVILTDVYSAGE 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053731810 394 QVIKGAESQDIAKGLSQ-------YLladSFDHAIYFLEELANDDTVVLVQGAGDITNLVEML 449
Cdd:PRK14573 385 EPEDSISYQKLAEAISQssivkctYV---PFHEIQRYLEQSIRVHDVCVSLGAGNIYTLGEAL 444
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
107-358 |
4.92e-30 |
|
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: 121.34 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 107 AVTGTHGKTTTSSILATLLCELDKHSSfVVGGVVKHVDSNIQV--------------------NGTDKLVIEAdESDA-- 164
Cdd:COG0769 84 GVTGTNGKTTTTYLLAQILRALGKKTG-LIGTVGNGIGGELIPsslttpealdlqrllaemvdAGVTHVVMEV-SSHAld 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 165 -------SFlylspQVAIVTNIDLDH------MATYKNSYQNLLENFANfiSKESVksiyLCADDQGCRDLLAKytlTDK 231
Cdd:COG0769 162 qgrvdgvRF-----DVAVFTNLTRDHldyhgtMEAYFAAKARLFDQLGP--GGAAV----INADDPYGRRLAAA---APA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 232 NITSYGFSNDADVQIYDYHIADEITHFKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVAR 311
Cdd:COG0769 228 RVITYGLKADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPG 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1053731810 312 RFDIytkIISGYQVTVIDDYGHHPVEVANSLSAVRDrYPNKKIIHVF 358
Cdd:COG0769 308 RMER---VDGGQGPTVIVDYAHTPDALENVLEALRP-HTKGRLIVVF 350
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
2-330 |
1.41e-28 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 117.10 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 2 NKKILFLGVGGIGVSAlAIAAKRLGADVAGYDS--IPNKLTAKLQTLGIAIFT-SPSGVDVANYDIVVYSSAILNNHPLL 78
Cdd:COG0771 4 GKKVLVLGLGKSGLAA-ARLLAKLGAEVTVSDDrpAPELAAAELEAPGVEVVLgEHPEELLDGADLVVKSPGIPPDHPLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 79 SQARTLGIQ---------CLQRAMFLAVlmkdfsyslavTGTHGKTTTSSILATLLCELDKHSsfVVGGvvkhvdsNI-- 147
Cdd:COG0771 83 KAARAAGIPvigeielayRLSPAPIIAI-----------TGTNGKTTTTTLIGHILKAAGLRV--AVGG-------NIgt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 148 -------QVNGTDKLVIEAdeSdaSF-L----YLSPQVAIVTNIDLDH------MATYKNSYQNLLENfanfiSKESVKS 209
Cdd:COG0771 143 plldlllEPEPPDVYVLEL--S--SFqLettpSLRPDVAVILNITPDHldrhgsMEAYAAAKARIFAN-----QTPDDYA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 210 IYlCADDQGCRDLLAKytlTDKNItsYGFSNDADVQiYDYHIADEithfKIIYKGDELSF----KLQLPGRYNVQNATAC 285
Cdd:COG0771 214 VL-NADDPLTRALAEE---AKARV--VPFSLKEPLE-GGAGLEDG----KLVDRASGEELlpvdDLRLPGRHNLENALAA 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1053731810 286 IIACLDLGFKYEDINNALITVAGVARRFDiYTKIISGyqVTVIDD 330
Cdd:COG0771 283 LAAARALGVPPEAIREALRSFKGLPHRLE-FVAEING--VRFIND 324
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
107-330 |
5.11e-24 |
|
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: 104.03 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 107 AVTGTHGKTTTSSILATLLceldkhSSFvvGGVVKHVDS-NIQV----------NGTDKLVIEA-----DESDasflYLS 170
Cdd:COG0770 104 AITGSNGKTTTKEMLAAVL------STK--GKVLATPGNfNNEIgvpltllrlpEDHEFAVLEMgmnhpGEIA----YLA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 171 ----PQVAIVTNIDLDHmatyknsyqnlLENFAnfiSKESV---KS-IY----------LCADDQGCRDLLAKytlTDKN 232
Cdd:COG0770 172 riarPDIAVITNIGPAH-----------LEGFG---SLEGIaraKGeIFeglppggvavLNADDPLLAALAER---AKAR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 233 ITSYGFSNDADVQIYDYHIADEITHFKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARR 312
Cdd:COG0770 235 VLTFGLSEDADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGR 314
|
250
....*....|....*...
gi 1053731810 313 FDIyTKIISGyqVTVIDD 330
Cdd:COG0770 315 LEV-IEGAGG--VTLIDD 329
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
108-289 |
2.78e-22 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 93.91 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 108 VTGTHGKTTTSSILATLLCELDK-HSSFVVGGVVKHVDSN--IQVN---------GTDKLVIEADESDASFLYLS----P 171
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGvIGTIGTYIGKSGNTTNnaIGLPltlaemveaGAEYAVLEVSSHGLGEGRLSgllkP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 172 QVAIVTNIDLDHMATYKnSYQNLLENFANFISKESVKSIYLC-ADDQGCRDLLAKYTLTDKNITSYGFSNDADVQIYDYH 250
Cdd:pfam08245 81 DIAVFTNISPDHLDFHG-TMENYAKAKAELFEGLPEDGIAVInADDPYGAFLIAKLKKAGVRVITYGIEGEADLRAANIE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1053731810 251 IADEITHFKII-YKGDELSFKLQLPGRYNVQNATACIIAC 289
Cdd:pfam08245 160 LSSDGTSFDLFtVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
108-441 |
6.90e-21 |
|
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: 94.69 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 108 VTGTHGKTTTSSILATLLCELDKHSSFV------VGG--VVKHVDSN-----IQV---------NGTDKLVIEAdESDAS 165
Cdd:TIGR01085 90 VTGTNGKTTTTSLIAQLLRLLGKKTGLIgtigyrLGGndLIKNPAALttpeaLTLqstlaemveAGAQYAVMEV-SSHAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 166 FLY----LSPQVAIVTNIDLDHMaTYKNSYQNLLENFANFISKESVKSI-YLCADDQGCRDLLAKYTL--TDKNITSYGF 238
Cdd:TIGR01085 169 AQGrvrgVRFDAAVFTNLSRDHL-DFHGTMENYFAAKASLFTELGLKRFaVINLDDEYGAQFVKRLPKdiTVSAITQPAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 239 SNDADVQIYDYHIADEITHFKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLG-FKYEDINNALITVAGVARRFDIyt 317
Cdd:TIGR01085 248 GRAQDIKITDSGYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAALATLLHLGgIDLEDIVAALEKFRGVPGRMEL-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 318 kIISGYQVTVIDDYGHHPVEVANSLSAVRdRYPNKKIIHVFQPhryTRNRDLIKDWPKALA---LADQLILL---PTYSA 391
Cdd:TIGR01085 326 -VDGGQKFLVIVDYAHTPDALEKALRTLR-KHKDGRLIVVFGC---GGDRDRGKRPLMGAIaeqLADLVILTsdnPRGED 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1053731810 392 GEQVIKgaesqDIAKGLSQ----YLLADSFDhAIYFLEELANDDTVVLVQGAGD 441
Cdd:TIGR01085 401 PEQIIA-----DILAGISEkekvVIIADRRQ-AIRYAISNAKAGDVVLIAGKGH 448
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
2-319 |
3.34e-18 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 86.56 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 2 NKKILflgVGGIGVSALAIAA--KRLGADVAGYDS-IPNKLTAKLQTLGIA----IFTSPSGVDVANYDIVVYSSAILNN 74
Cdd:PRK14106 5 GKKVL---VVGAGVSGLALAKflKKLGAKVILTDEkEEDQLKEALEELGELgielVLGEYPEEFLEGVDLVVVSPGVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 75 HPLLSQARTLGIQCLQRAMFLAVLMKDFSYslAVTGTHGKTTTSsilaTLLCELDKHSSFVVggvvkHVDSNIQVNGTDK 154
Cdd:PRK14106 82 SPPVVQAHKKGIEVIGEVELAYRFSKAPIV--AITGTNGKTTTT----TLLGEIFKNAGRKT-----LVAGNIGYPLIDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 155 lVIEADESDA------SF-----LYLSPQVAIVTNIDLDHMATYKNsyqnlLENFAN-----FISKESVKSIYLCADDQG 218
Cdd:PRK14106 151 -VEEYGEDDIivaevsSFqletiKEFKPKVGCILNITPDHLDRHKT-----MENYIKakariFENQRPSDYTVLNYDDPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 219 CRDLLAK-----YTLTDKNIT--SYGFSNDADVQIYDYHIAdeithfKIIYKGDelsfkLQLPGRYNVQNATACIIACLD 291
Cdd:PRK14106 225 TRSLAKKakarvIFFSRKSLLeeGVFVKNGKIVISLGGKEE------EVIDIDE-----IFIPGEHNLENALAATAAAYL 293
|
330 340
....*....|....*....|....*...
gi 1053731810 292 LGFKYEDINNALITVAGVARRFDIYTKI 319
Cdd:PRK14106 294 LGISPDVIANTLKTFKGVEHRIEFVAEI 321
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
106-440 |
4.00e-18 |
|
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: 87.45 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 106 LAVTGTHGKTTTSSILATLLCELDKhSSFVVGGV-VKHVDSNIQVN-------------------GTDKLVIEADES--D 163
Cdd:PRK11929 115 VAVTGTNGKTSCAQLLAQLLTRLGK-PCGSIGTLgARLDGRLIPGSlttpdaiilhrilarmraaGADAVAMEASSHglE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 164 ASFLY-LSPQVAIVTNIDLDH------MATYKNSYQNLLENFAnfiskeSVKSIYLCADDQGCRDLLAKYTLTDKnITSY 236
Cdd:PRK11929 194 QGRLDgLRIAVAGFTNLTRDHldyhgtMQDYEEAKAALFSKLP------GLGAAVINADDPAAARLLAALPRGLK-VGYS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 237 GFSNDADVQIYDYHIADEITHFKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIY 316
Cdd:PRK11929 267 PQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRMERV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 317 TKIISGYQVTVIDDYGHHPVEVANSLSAVRD--RYPNKKIIHVFQphrYTRNRDLIKDwPK----ALALADQLILL---P 387
Cdd:PRK11929 347 GPTAGAQGPLVVVDYAHTPDALAKALTALRPvaQARNGRLVCVFG---CGGDRDKGKR-PEmgriAAELADRVVVTsdnP 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 388 TYSAGEQVIkgaesQDIAKGL---SQYLL----ADSFDHAIYfleELANDDtVVLVQGAG 440
Cdd:PRK11929 423 RSEAPEAII-----DQILAGIpagARVFVisdrAEAIRQAIW---MAAPGD-VILIAGKG 473
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
107-358 |
8.49e-18 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 85.18 E-value: 8.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 107 AVTGTHGKTTTSSILATLLCELDKHS------SFVVGGvvKHVDSN------IQV---------NGTDKLVIEA------ 159
Cdd:PRK00139 99 GVTGTNGKTTTAYLLAQILRLLGEKTaligtlGNGIGG--ELIPSGlttpdaLDLqrllaelvdAGVTYAAMEVsshald 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 160 ----DESDasFlylspQVAIVTNIDLDHMatyknSYQNLLENFAN----FISKESVKSIyLCADDQGCRDLLAKytltdk 231
Cdd:PRK00139 177 qgrvDGLK--F-----DVAVFTNLSRDHL-----DYHGTMEDYLAakarLFSELGLAAV-INADDEVGRRLLAL------ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 232 nITSYGFS-NDADVQIYDYHIADEITHFKIIYKgdelsFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVA 310
Cdd:PRK00139 238 -PDAYAVSmAGADLRATDVEYTDSGQTFTLVTE-----VESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVP 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1053731810 311 RRFDIytkIISGYQVTVIDDYGHHPVEVANSLSAVRDrYPNKKIIHVF 358
Cdd:PRK00139 312 GRMER---VDAGQGPLVIVDYAHTPDALEKVLEALRP-HAKGRLICVF 355
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
4-330 |
2.41e-17 |
|
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: 83.93 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 4 KILFLGVGGIGVSALAIAAKRlGADVAGYDSIPN-KLTAKLQTL----GIAIFTSPSGVDVANYDIVVYSSAILNNHPLL 78
Cdd:TIGR01087 1 KILILGLGKTGRAVARFLHKK-GAEVTVTDLKPNeELEPSMGQLrlneGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 79 SQARTLGIQCLQRAMFLAVLMKDfsYSLAVTGTHGKTTTSSilatLLCELDKHSSF--VVGGvvkhvdsNIqvnGTDKL- 155
Cdd:TIGR01087 80 QAAAKRGIPVVGDIELFLRLVPL--PVVAITGTNGKTTTTS----LLYHLLKAAGLkaFLGG-------NI---GTPALe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 156 VIEADESDASFLYLS-----------PQVAIVTNIDLDHMATYKNsyqnlLENFanFISKEsvkSIYLCADdqgcRDLLA 224
Cdd:TIGR01087 144 VLDQEGAELYVLELSsfqletteslrPEIALILNISEDHLDWHGS-----FEDY--VAAKL---KIFARQT----EGDVA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 225 KYTLTDKNITSYGFSNDADVQIYDyhiADEITHFKIIYKGDELSFK-----LQLPGRYNVQNATACIIACLDLGFKYEDI 299
Cdd:TIGR01087 210 VLNADDPRFARLAQKSKAQVIWFS---VEKDAERGLCIRDGGLYLKpndleGSLLGLHNAENILAAIALAKSLGLNLEAI 286
|
330 340 350
....*....|....*....|....*....|.
gi 1053731810 300 NNALITVAGVARRFDiYTKIISGyqVTVIDD 330
Cdd:TIGR01087 287 LEALRSFKGLPHRLE-YVGQKNG--VHFYND 314
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
309-394 |
2.75e-10 |
|
Mur ligase family, glutamate ligase 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: 460731 [Multi-domain] Cd Length: 87 Bit Score: 56.58 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 309 VARRFDIYTkiiSGYQVTVIDDYGHHPVEVANSLSAVRDRYPNKKIIhVFQPHRyTRNRDLIKDWPKALA-LADQLILLP 387
Cdd:pfam02875 1 VPGRLEVVG---ENNGVLVIDDYAHNPDAMEAALRALRNLFPGRLIL-VFGGMG-DRDAEFHALLGRLAAaLADVVILTG 75
|
....*..
gi 1053731810 388 TYSAGEQ 394
Cdd:pfam02875 76 DYPRAED 82
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
106-331 |
4.43e-08 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 55.73 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 106 LAVTGTHGKTTTSSILATLLceldkHSSFVVGGVVKHVDSNI-------QVNGTDKLVI-EA-----DESDASFLYLSPQ 172
Cdd:PRK11930 110 IGITGSNGKTIVKEWLYQLL-----SPDYNIVRSPRSYNSQIgvplsvwQLNEEHELGIfEAgisqpGEMEALQKIIKPT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 173 VAIVTNIDLDHMATYKNSYQNLLENFANFISKEsvKSIYlCADdqgCRDLLAKYTLTDKNITSYGFS---NDADVQIYDY 249
Cdd:PRK11930 185 IGILTNIGGAHQENFRSIKQKIMEKLKLFKDCD--VIIY-NGD---NELISSCITKSNLTLKLISWSrkdPEAPLYIPFV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 250 HIADEITHFKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIYTKIIsgyQVTVID 329
Cdd:PRK11930 259 EKKEDHTVISYTYKGEDFHFEIPFIDDASIENLIHCIAVLLYLGYSADQIQERMARLEPVAMRLEVKEGIN---NCTLIN 335
|
..
gi 1053731810 330 DY 331
Cdd:PRK11930 336 DS 337
|
|
| Mur_ligase |
pfam01225 |
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ... |
4-102 |
8.10e-08 |
|
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: 49.54 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 4 KILFLGVGGIGVSALAIAAKRLGADVAGYDSIPNkltakLQTLGIAIFTSPSGVDvanydivvyssAILNNHPLLSQART 83
Cdd:pfam01225 1 EIHFVGIDGRGMSPGALFLALKGYRVDGSDFIES-----LIALGAAAVVGHDAAN-----------NISPDNPELEAAKV 64
|
90
....*....|....*....
gi 1053731810 84 LGIQCLQRAMFLAVLMKDF 102
Cdd:pfam01225 65 PGIPVIDRREALAELAAAF 83
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
106-435 |
5.15e-07 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 51.96 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 106 LAVTGTHGKTTTSSILATLLCELDKHS------SFVVGGVV--------------KHVDSNIQvNGTDKLVIEAdESDAS 165
Cdd:PRK14022 113 LAFTGTKGKTTAAYFAYHILKQLHKPAmlstmnTTLDGETFfksalttpesldlfKMMAEAVD-NGMTHLIMEV-SSQAY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 166 FLY----LSPQVAIVTNIDLDH--------MATYKNSYQNLLENfanfiskesVKSIYLCADDQGCRDLLAkyTLTDKNI 233
Cdd:PRK14022 191 LVGrvygLTFDVGVFLNITPDHigpiehptFEDYFYHKRLLMEN---------SKAVVVNSDMDHFSELLE--QVTPQEH 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 234 TSYGFSNDADVqiydyhiaDEITHFKIIYKGD-ELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNAlITVAGVARR 312
Cdd:PRK14022 260 DFYGIDSENQI--------MASNAFSFEATGKlAGTYDIQLIGKFNQENAMAAGLACLRLGASLEDIQKG-IAQTPVPGR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 313 FDIYTKIIsgyQVTVIDDYGHHPVEVANSLSAVRDrYPNKKIIHVFQPhryTRNRDLIK--DWPKALALADQL--ILLPT 388
Cdd:PRK14022 331 MEVLTQSN---GAKVFIDYAHNGDSLNKLIDVVEE-HQKGKLILLLGA---AGNKGESRrpDFGRVANRHPYLqvILTAD 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1053731810 389 YSAGE--QVIkgaeSQDIAKGLSQYL-----LADSFDHAIyfleELAN--DDTVVL 435
Cdd:PRK14022 404 DPNNEdpKMI----TQEIASHITHPVeiiddRAEAIKHAM----SITEgpGDAVII 451
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
106-438 |
1.79e-05 |
|
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: 47.39 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 106 LAVTGTHGKTTTSSILATLLCELdkHSSFVVGGVVKHVDSNIQV--------NGTDKLVIEAD-ESDASFLYLS----PQ 172
Cdd:PRK11929 606 VAITGSNGKTTTKEMIAAILAAW--QGEDRVLATEGNFNNEIGVpltllrlrAQHRAAVFELGmNHPGEIAYLAaiaaPT 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 173 VAIVTNIDLDHMATYKNSYQNLLENFAnFISKESVKSI-YLCADDQGCRDLLAKYTLTDKNITSYGFSNDADVQIYDYHI 251
Cdd:PRK11929 684 VALVTNAQREHQEFMHSVEAVARAKGE-IIAALPEDGVaVVNGDDPYTAIWAKLAGARRVLRFGLQPGADVYAEKIAKDI 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 252 ADEITH---FKIIYKGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIytKIISGyQVTVI 328
Cdd:PRK11929 763 SVGEAGgtrCQVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQR--RRLSC-GTRII 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 329 DD-YGhhpvevANSLSAvrdrypnKKIIHVFqphrytrnrDLIKDWPKALALADQLIL----------LPTYsAGEQVIK 397
Cdd:PRK11929 840 DDtYN------ANPDSM-------RAAIDVL---------AELPNGPRALVLGDMLELgdngpamhreVGKY-ARQLGID 896
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1053731810 398 -----GAESQDIAKGLSQYLLAD--SFDHAIYFLEELANDDTVVLVQG 438
Cdd:PRK11929 897 alitlGEAARDAAAAFGAGARGVcaSVDEIIAALRGALPEGDSVLIKG 944
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
171-343 |
8.39e-04 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 41.68 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 171 PQVAIVTNIDLDHMATYKNsyqnlLENFAN-----FISKESVKSIYLCADD-QGCRDLLAKYTLTDKNITSYGFSNDADV 244
Cdd:PRK14093 184 PHVAIITTVEPVHLEFFSG-----IEAIADakaeiFTGLEPGGAAVLNRDNpQFDRLAASARAAGIARIVSFGADEKADA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731810 245 QIYD--YHIADEITHFKIIykGDELSFKLQLPGRYNVQNATACIIACLDLGFKYEDINNALITVAGVARRFDIYTKIISG 322
Cdd:PRK14093 259 RLLDvaLHADCSAVHADIL--GHDVTYKLGMPGRHIAMNSLAVLAAAELAGADLALAALALSQVQPAAGRGVRHTLEVGG 336
|
170 180
....*....|....*....|..
gi 1053731810 323 YQVTVIDD-YGHHPVEVANSLS 343
Cdd:PRK14093 337 GEATLIDEsYNANPASMAAALG 358
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
2-60 |
1.52e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 40.38 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1053731810 2 NKKILFLGVGGIGVSAlAIAAKRLGADVAGYDSIPNKLtAKLQTLG--------------IAIFTSPSGVDVA 60
Cdd:cd05188 135 GDTVLVLGAGGVGLLA-AQLAKAAGARVIVTDRSDEKL-ELAKELGadhvidykeedleeELRLTGGGGADVV 205
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-66 |
1.91e-03 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 40.05 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053731810 1 MNKKILFLGVGGIGvSALA---IAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVdVANYDIVV 66
Cdd:COG0345 1 MSMKIGFIGAGNMG-SAIIkglLKSGVPPEDIIVSDRSPERLEALAERYGVRVTTDNAEA-AAQADVVV 67
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
4-72 |
2.65e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.26 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053731810 4 KILFLGVGGIGVSALAIAaKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVD-----VANYDIVVysSAIL 72
Cdd:smart01002 22 KVVVIGAGVVGLGAAATA-KGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAElleeaVKEADLVI--GAVL 92
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-66 |
6.26e-03 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 38.20 E-value: 6.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1053731810 1 MNKKILFLGVGGIGvSALA---IAAKRLGADVAGYDSIPNKLTAKLQTLGIAIFTSPSGVdVANYDIVV 66
Cdd:PRK11880 1 MMKKIGFIGGGNMA-SAIIgglLASGVPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEA-AQEADVVV 67
|
|
| |
