|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
1-263 |
1.51e-116 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 345.16 E-value: 1.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVA-GGFAAAPPLAPDSP--LRHTVHVAPLAPEAF 77
Cdd:COG1001 292 MATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVEKVYADGKLVAeDGKLLVDLPKYPYPpwARNTVKLRPLTAEDF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 78 RLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNGWFVPC--DGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSH 154
Cdd:COG1001 372 AIPAPGGVKvRVIGVIPGQIITEHLEAELPVEDGEVVPDpeRDILKIAVVERHGGTGNIGLGFVKGFGLKRGAIASTVAH 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 155 DSHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPEGiEPF 234
Cdd:COG1001 452 DSHNLIVVGTNDEDMALAANRLIEIGGGIVVVKDGKVLAELPLPIAGLMSDEPAEEVAEKLEALRAAARELGCTLE-EPF 530
|
250 260
....*....|....*....|....*....
gi 2663956077 235 ITLSFLALPVIPAVRLTPRGLFDVEKFAF 263
Cdd:COG1001 531 MTLSFLALPVIPELKLTDRGLVDVTTFEF 559
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
96-261 |
4.67e-73 |
|
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine deaminase enzyme.
Pssm-ID: 463864 [Multi-domain] Cd Length: 168 Bit Score: 220.78 E-value: 4.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 96 LATEHLTRKLPAQNGWFVPC--DGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHDSHNLLVAGDNDADMLAAV 173
Cdd:pfam13382 1 LITKELEVELPVKDGVVVPDpeRDILKIAVVERHGGTGNIGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 174 AELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPeGIEPFITLSFLALPVIPAVRLTPR 253
Cdd:pfam13382 81 NRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALRELGCE-LDDPFMTLSFLALPVIPELKITDK 159
|
....*...
gi 2663956077 254 GLFDVEKF 261
Cdd:pfam13382 160 GLVDVKKF 167
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
1-257 |
1.58e-67 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 215.17 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGkdvaggfaaapplapdsplrhtvhvaplapeafrlk 80
Cdd:cd01295 243 MATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG------------------------------------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 81 ameggqdvigliagqlatehltrklpaqngwfvpcdgfnkLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHDSHNLL 160
Cdd:cd01295 287 ----------------------------------------IAVVERHGKTGNIGVGFVKGFGLKEGAIASSVAHDSHNII 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 161 VAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGvPEGIEPFITLSFL 240
Cdd:cd01295 327 VIGTNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELG-YALDDPFMTLSFL 405
|
250
....*....|....*..
gi 2663956077 241 ALPVIPAVRLTPRGLFD 257
Cdd:cd01295 406 SLPVIPELKITDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
1-264 |
1.77e-67 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 218.49 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVAG------GFAAAPPLAPdsPLRHTVHVAPLAP 74
Cdd:TIGR01178 284 MASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKVNKTYVKGKLLDLnevfndEISRIPLINE--IPINVKARSPKSI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 75 EAFRLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNGWFVPCDgFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVS 153
Cdd:TIGR01178 362 SDFGIQFKTGNRiRVIKVISNQLITHKTSNSVAEEFGSDIEED-ILKIAVIERHKDNGKIGKGLIKGFGLKEGAIASTVA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 154 HDSHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGvPEGIEP 233
Cdd:TIGR01178 441 HDSHNIIAVGSNDEDLALAVNKLIQIGGGLCAAKNGEVTIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG-GSRDNP 519
|
250 260 270
....*....|....*....|....*....|.
gi 2663956077 234 FITLSFLALPVIPAVRLTPRGLFDVEKFAFI 264
Cdd:TIGR01178 520 FLTLSFLSLPVIPHLKITDKGLFDVESFCFV 550
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
1-267 |
1.36e-56 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 190.81 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVAG----GFAAAPPLAPDSPLRHTVHVAPLAPEA 76
Cdd:PRK10027 318 VASWSTARHFGLNHLGLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAqtlqAEESARLAQSAPPYGNTIARQPVSASD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 77 FRLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNgwfVPCDGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHD 155
Cdd:PRK10027 398 FALQFTPGKRyRVIDVIHNELITHSRSSVYSENG---FDRDDVCFIAVLERYGQRLAPACGLLGGFGLNEGALAATVSHD 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 156 SHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPEGiEPFI 235
Cdd:PRK10027 475 SHNIVVIGRSAEEMALAVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPD-EPFI 553
|
250 260 270
....*....|....*....|....*....|..
gi 2663956077 236 TLSFLALPVIPAVRLTPRGLFDVEKFAFIAAQ 267
Cdd:PRK10027 554 QMAFLSLPVIPALKLTSQGLFDGEKFAFTTLE 585
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
1-263 |
1.51e-116 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 345.16 E-value: 1.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVA-GGFAAAPPLAPDSP--LRHTVHVAPLAPEAF 77
Cdd:COG1001 292 MATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVEKVYADGKLVAeDGKLLVDLPKYPYPpwARNTVKLRPLTAEDF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 78 RLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNGWFVPC--DGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSH 154
Cdd:COG1001 372 AIPAPGGVKvRVIGVIPGQIITEHLEAELPVEDGEVVPDpeRDILKIAVVERHGGTGNIGLGFVKGFGLKRGAIASTVAH 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 155 DSHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPEGiEPF 234
Cdd:COG1001 452 DSHNLIVVGTNDEDMALAANRLIEIGGGIVVVKDGKVLAELPLPIAGLMSDEPAEEVAEKLEALRAAARELGCTLE-EPF 530
|
250 260
....*....|....*....|....*....
gi 2663956077 235 ITLSFLALPVIPAVRLTPRGLFDVEKFAF 263
Cdd:COG1001 531 MTLSFLALPVIPELKLTDRGLVDVTTFEF 559
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
96-261 |
4.67e-73 |
|
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine deaminase enzyme.
Pssm-ID: 463864 [Multi-domain] Cd Length: 168 Bit Score: 220.78 E-value: 4.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 96 LATEHLTRKLPAQNGWFVPC--DGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHDSHNLLVAGDNDADMLAAV 173
Cdd:pfam13382 1 LITKELEVELPVKDGVVVPDpeRDILKIAVVERHGGTGNIGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 174 AELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPeGIEPFITLSFLALPVIPAVRLTPR 253
Cdd:pfam13382 81 NRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALRELGCE-LDDPFMTLSFLALPVIPELKITDK 159
|
....*...
gi 2663956077 254 GLFDVEKF 261
Cdd:pfam13382 160 GLVDVKKF 167
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
1-257 |
1.58e-67 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 215.17 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGkdvaggfaaapplapdsplrhtvhvaplapeafrlk 80
Cdd:cd01295 243 MATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG------------------------------------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 81 ameggqdvigliagqlatehltrklpaqngwfvpcdgfnkLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHDSHNLL 160
Cdd:cd01295 287 ----------------------------------------IAVVERHGKTGNIGVGFVKGFGLKEGAIASSVAHDSHNII 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 161 VAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGvPEGIEPFITLSFL 240
Cdd:cd01295 327 VIGTNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELG-YALDDPFMTLSFL 405
|
250
....*....|....*..
gi 2663956077 241 ALPVIPAVRLTPRGLFD 257
Cdd:cd01295 406 SLPVIPELKITDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
1-264 |
1.77e-67 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 218.49 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVAG------GFAAAPPLAPdsPLRHTVHVAPLAP 74
Cdd:TIGR01178 284 MASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKVNKTYVKGKLLDLnevfndEISRIPLINE--IPINVKARSPKSI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 75 EAFRLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNGWFVPCDgFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVS 153
Cdd:TIGR01178 362 SDFGIQFKTGNRiRVIKVISNQLITHKTSNSVAEEFGSDIEED-ILKIAVIERHKDNGKIGKGLIKGFGLKEGAIASTVA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 154 HDSHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGvPEGIEP 233
Cdd:TIGR01178 441 HDSHNIIAVGSNDEDLALAVNKLIQIGGGLCAAKNGEVTIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG-GSRDNP 519
|
250 260 270
....*....|....*....|....*....|.
gi 2663956077 234 FITLSFLALPVIPAVRLTPRGLFDVEKFAFI 264
Cdd:TIGR01178 520 FLTLSFLSLPVIPHLKITDKGLFDVESFCFV 550
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
1-267 |
1.36e-56 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 190.81 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAAVYHKGKDVAG----GFAAAPPLAPDSPLRHTVHVAPLAPEA 76
Cdd:PRK10027 318 VASWSTARHFGLNHLGLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAqtlqAEESARLAQSAPPYGNTIARQPVSASD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 77 FRLKAMEGGQ-DVIGLIAGQLATEHLTRKLPAQNgwfVPCDGFNKLAVVERHHATGAVGVAPIMGYGLRGGAIATTVSHD 155
Cdd:PRK10027 398 FALQFTPGKRyRVIDVIHNELITHSRSSVYSENG---FDRDDVCFIAVLERYGQRLAPACGLLGGFGLNEGALAATVSHD 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2663956077 156 SHNLLVAGDNDADMLAAVAELARVGGGYTIVSHGEPLATLPLSVLGLVSDRPYEEVEQKLHHMISLARKMGVPEGiEPFI 235
Cdd:PRK10027 475 SHNIVVIGRSAEEMALAVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPD-EPFI 553
|
250 260 270
....*....|....*....|....*....|..
gi 2663956077 236 TLSFLALPVIPAVRLTPRGLFDVEKFAFIAAQ 267
Cdd:PRK10027 554 QMAFLSLPVIPALKLTSQGLFDGEKFAFTTLE 585
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-42 |
1.67e-05 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 45.66 E-value: 1.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLrDLRRVDIAAVYH 42
Cdd:cd01298 340 MATIGGAKALGLDEIGSLEVGKKADLILI-DLDGPHLLPVHD 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1-29 |
1.01e-04 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 42.87 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|
gi 2663956077 1 MASINTAQCYGLRH-LGAIAPGYQADFVVL 29
Cdd:pfam01979 278 MATINPAKALGLDDkVGSIEVGKDADLVVV 307
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
1-45 |
4.00e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 41.24 E-value: 4.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2663956077 1 MASINTAQCYGLRH-LGAIAPGYQADFVVL-RDLRrvdIAAVYHKGK 45
Cdd:COG1820 330 MASLNPARALGLDDrKGSIAPGKDADLVVLdDDLN---VRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
1-44 |
1.16e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 39.87 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2663956077 1 MASINTAQCYGLRH-LGAIAPGYQADFVVL-RDLrrvDIAAVYHKG 44
Cdd:cd00854 332 MASLNPAKLLGLDDrKGSLKPGKDADLVVLdDDL---NVKATWING 374
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1-39 |
1.16e-03 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 39.62 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2663956077 1 MASINTAQCYGLRHLGAIAPGYQADFVVLRDLRRVDIAA 39
Cdd:cd01318 295 LTSHNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRA 333
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1-42 |
1.78e-03 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 39.42 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2663956077 1 MASINTAQCYGLRH-LGAIAPGYQADFVVLrDLRRVDIAAVYH 42
Cdd:COG0402 348 MATLGGARALGLDDeIGSLEPGKRADLVVL-DLDAPHLAPLHD 389
|
|
| |
