|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1-430 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 699.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 1 MEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSL 80
Cdd:cd01314 21 IEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 81 LAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQ 160
Cdd:cd01314 101 LEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMVDDEELLDVLKRAKELGALVM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 161 VHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYG 240
Cdd:cd01314 180 VHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 241 EPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTN 320
Cdd:cd01314 260 ETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGKDDFTKIPNGVP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 321 GTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEG 400
Cdd:cd01314 338 GVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEG 417
|
410 420 430
....*....|....*....|....*....|
gi 347543829 401 MECRGSPLVVISQGKIVLEDGTLHVTEGSG 430
Cdd:cd01314 418 MKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1-435 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 645.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 1 MEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSL 80
Cdd:TIGR02033 21 IEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 81 LAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQ 160
Cdd:TIGR02033 101 TEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMVDDEELFEILKRLKELGALLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 161 VHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYG 240
Cdd:TIGR02033 181 VHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 241 EPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQK-AVGKDNFTLIPEGT 319
Cdd:TIGR02033 261 ETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTFNFAQKkAIGKDDFTKIPNGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 320 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFE 399
Cdd:TIGR02033 339 PGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTTVISAETHHSNADYNPFE 418
|
410 420 430
....*....|....*....|....*....|....*.
gi 347543829 400 GMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 435
Cdd:TIGR02033 419 GFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
2-439 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 558.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLL 81
Cdd:PRK08323 24 EDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRAAACGGTTTIIDFALQPKGQSLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQV 161
Cdd:PRK08323 100 EALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALMLDDDELLRALQRAAELGALPMV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 162 HAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGE 241
Cdd:PRK08323 179 HAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 242 PITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKA-VGKDNFTLIPEGTN 320
Cdd:PRK08323 259 TCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCPFCFEQKKqLGRGDFTKIPNGTP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 321 GTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEG 400
Cdd:PRK08323 338 GVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEG 417
|
410 420 430
....*....|....*....|....*....|....*....
gi 347543829 401 MECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 439
Cdd:PRK08323 418 FEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-439 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 520.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGtSLL 81
Cdd:PLN02942 28 EDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQAAALAGGTTMHIDFVIPVNG-NLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADsKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQV 161
Cdd:PLN02942 107 AGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGSLMVTDELLLEGFKRCKSLGALAMV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 162 HAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGE 241
Cdd:PLN02942 186 HAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 242 PITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNG 321
Cdd:PLN02942 266 PVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDHCPFNSTQKAFGKDDFRKIPNGVNG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 322 TEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGM 401
Cdd:PLN02942 345 IEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGR 424
|
410 420 430
....*....|....*....|....*....|....*...
gi 347543829 402 ECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 439
Cdd:PLN02942 425 RGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
2-435 |
6.58e-115 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 347.08 E-value: 6.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLL 81
Cdd:COG0044 21 EDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQLTDCQIYEVLSVIRDIGAIAQ 160
Cdd:COG0044 99 EALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVLDDGLLRRALEYAAEFGALVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 161 VHAENGDIIAEeqqRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYG 240
Cdd:COG0044 178 VHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 241 E--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQVTGSAHCTFNTAQKAvgkDNF 312
Cdd:COG0044 255 EvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDVIATDHAPHTLEEKE---LPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 313 TLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSS 392
Cdd:COG0044 319 AEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEWTVTAEDLHSK 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 347543829 393 LEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 435
Cdd:COG0044 398 SKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-435 |
1.16e-114 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 347.84 E-value: 1.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 3 DGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLL 81
Cdd:PRK13404 28 GGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVSAAFGGTTTVIPFAAQHRGQSLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADSKSCCDYSLHVDISEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRFQLTDCQIYEVLSVIRDIGAIAQ 160
Cdd:PRK13404 106 EAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDLKLDDRQILDVLAVARRHGAMVM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 161 VHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYG 240
Cdd:PRK13404 184 VHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 241 EP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFN---TAQKAVGKD 310
Cdd:PRK13404 264 ETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFEVFSSDHAPFRfddTDGKLAAGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 311 N--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKT 388
Cdd:PRK13404 335 NpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNAD 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 347543829 389 HNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 435
Cdd:PRK13404 415 LHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
29-407 |
1.76e-61 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 205.32 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 29 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 108
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 109 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDCQIYEVLSVIRDIGAIAQVHAEngdiiaeeqqrildlgitgpeg 186
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 187 hvlsrpeeveaeavnRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 266
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 267 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 346
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347543829 347 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSP 407
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-433 |
1.64e-59 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 203.67 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 3 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDhvVP---EPGTS 79
Cdd:cd01315 24 GGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAAAAGGITTIID--MPlnsIPPTT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 80 LLAAFDQWREWADSKSccdyslHVDISEWH-------KGIQEEMEALVKdhGVNSFLVYMAFKDRFQLTDCQIYEVLSVI 152
Cdd:cd01315 100 TVENLEAKLEAAQGKL------HVDVGFWGglvpgnlDQLRPLDEAGVV--GFKCFLCPSGVDEFPAVDDEQLEEAMKEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 153 RDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQAR 232
Cdd:cd01315 172 AKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 233 KKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAH--CTfnTA 303
Cdd:cd01315 252 AEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGDIDMVVSDHspCT--PE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 304 QKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKT 383
Cdd:cd01315 318 LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 347543829 384 ISAkthnSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 433
Cdd:cd01315 398 VDA----EDLYYknkiSPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
2-436 |
4.74e-50 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 177.92 E-value: 4.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLL 81
Cdd:PRK02382 25 DGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADSKSCCDYSLHvdisewhKGIQEEMEALVK--DHGVNSF-LVYMA--------FKDRFQltdcqiyEVLS 150
Cdd:PRK02382 103 ESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMAdstggmgiDEELFE-------EALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 151 VIRDIGAIAQVHAENGDIIaEEQQRILDlGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVmskSSAEVIAQ 230
Cdd:PRK02382 169 EAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHI---STPEGVDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 231 ARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVG- 308
Cdd:PRK02382 244 ARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLND-GTIDVVASDHAPHTREEKDADi 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 309 KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKT 388
Cdd:PRK02382 316 WD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVLVDPDAAREIRGDD 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 347543829 389 HNSSLEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 436
Cdd:PRK02382 390 LHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
3-424 |
2.93e-46 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 167.96 E-value: 2.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 3 DGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDhvVP---EPGTS 79
Cdd:PRK06189 27 NGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAALAAGGCTTYFD--MPlnsIPPTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 80 LLAAFDQWREWADSKSCCDYSLhvdiseWHKGIQEEMEALVK--DHGVNSFLVYMAFK--DRFQLTD-CQIYEVLSVIRD 154
Cdd:PRK06189 102 TREALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgtDEFRSSDdLTLYEGMKEIAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 155 IGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKK 234
Cdd:PRK06189 176 LGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 235 GtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAH--CTFNTAQkavg 308
Cdd:PRK06189 256 G-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWRGLLAGEIDMISSDHspCPPELKE---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 309 KDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKT 388
Cdd:PRK06189 323 GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVLVDLDETYTLTKED 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 347543829 389 HNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 424
Cdd:PRK06189 402 LFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
2-420 |
8.28e-46 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 165.69 E-value: 8.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVPEPGTS 79
Cdd:TIGR00857 11 EGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKPPIDTP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 80 llAAFDQWREWADSKSCCDYSLHVDISEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDCQIYEVLSVI 152
Cdd:TIGR00857 88 --ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRRALEYA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 153 RDIGAIAQVHAENGDIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQAR 232
Cdd:TIGR00857 157 AIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 233 KkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKA 306
Cdd:TIGR00857 234 S-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEKT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 307 VgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISA 386
Cdd:TIGR00857 303 K---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINA 377
|
410 420 430
....*....|....*....|....*....|....
gi 347543829 387 KTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 420
Cdd:TIGR00857 378 ETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
1-434 |
3.81e-44 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 162.17 E-value: 3.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 1 MEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDhvVP---EPG 77
Cdd:TIGR03178 22 VKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAAAAGGITTYID--MPlnsIPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 78 TSLLAAFDQWREWADSKsccdysLHVDISEWH-------KGIQEEMEALVkdHGVNSFLVYMAFKDRFQLTDCQIYEVLS 150
Cdd:TIGR03178 97 TTTRASLEAKFEAAKGK------LAVDVGFWGglvpynlDDLRELDEAGV--VGFKAFLSPSGDDEFPHVDDWQLYKGMR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 151 VIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQ 230
Cdd:TIGR03178 169 ELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 231 ARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKA 306
Cdd:TIGR03178 249 AKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNGLIDCVVSDHSPCTPDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 307 vgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISa 386
Cdd:TIGR03178 320 --AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDADFVFVDPDESYTLT- 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 347543829 387 kthNSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 434
Cdd:TIGR03178 396 ---PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
29-414 |
3.92e-37 |
|
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: 140.93 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 29 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 108
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 109 hkgiQEEMEALVKdHGVNSFLVYMA--FKDRFQltdcqIYEVLSVI-RDIGAIAQVHAENGDIIAEEQQRILDLGItgpe 185
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMGdsTGDLLD-----DEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 186 gHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 263
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 264 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 340
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 347543829 341 enQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQG 414
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
18-408 |
2.03e-33 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 130.82 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 18 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 97
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 98 DYSLH----VDISEWH------KGIQ----EEMEALvKDHGVNSFlvymaFKDRFQLTDCQI-YEVLSVIRDIGAIAQVH 162
Cdd:cd01317 66 ELLKNrakdVGIVRVLpigaltKGLKgeelTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 163 AENGDIIAEEQqrILDLGITGPEGhVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGtvvygEP 242
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 243 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 316
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 317 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYN 396
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 347543829 397 IFEGMECRGSPL 408
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
28-417 |
1.68e-31 |
|
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: 124.54 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 28 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 95
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 96 CC---DYSLHVDISEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDiiAEE 172
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 173 QQRILDLGITGPEGHVLSRPEEVeaeAVNRAITIANQTNCPLyitkvmSKSSAEVIAQARKKGTVVygepitasLGTDGS 252
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHL------SPTEANLLAEHLKGAGVA--------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 253 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 332
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 333 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSvktisakthnssleYNIFEGMECRGSPLVVIS 412
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 347543829 413 QGKIV 417
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
2-395 |
7.61e-27 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 113.03 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPE-PGTSL 80
Cdd:PRK08044 26 KGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAAAKGGITTMIEMPLNQlPATVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 81 LAAFDQWREWADSKsccdysLHVDISEWHKGIQEEMEAL--VKDHGVNSFLVYMAF-KDR-----FQ-LTDCQIYEVLSV 151
Cdd:PRK08044 102 RASIELKFDAAKGK------LTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcGDRgidndFRdVNDWQFYKGAQK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 152 IRDIGAIAQVHAENG---DIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVI 228
Cdd:PRK08044 176 LGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 229 AQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQ 304
Cdd:PRK08044 253 TRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLFN-GEIDCLVSDHSPCPPEM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 305 KAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSvkti 384
Cdd:PRK08044 324 KA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVFIQPNS---- 395
|
410
....*....|.
gi 347543829 385 SAKTHNSSLEY 395
Cdd:PRK08044 396 SYVLKNEDLEY 406
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-420 |
3.10e-26 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 111.06 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTKAALAGGTTMiidhVVPEPGT--- 78
Cdd:PRK09357 25 DDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSRAAAAGGFTT----VVAMPNTkpv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 79 -SLLAAFDQWREWADSKSCCDysLHV--DISEWHKGIQE-EMEALvKDHGV-----------NSFLVYMAFK--DRFQLT 141
Cdd:PRK09357 98 iDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGVvafsddgipvqDARLMRRALEyaKALDLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 142 DCQIYEVLSVIRdiGAIAqvhaeNGDIIAEEqqrildLGITGpeghvlsRPEEVEAEAVNRAITIANQTNCPLYITKVMS 221
Cdd:PRK09357 175 IAQHCEDPSLTE--GGVM-----NEGEVSAR------LGLPG-------IPAVAEEVMIARDVLLAEATGARVHICHVST 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 222 KSSAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafvtsPPLSPDPTTPDFLNSLLScGD 289
Cdd:PRK09357 235 AGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN-----PPLRTEEDREALIEGLKD-GT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 290 LQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRIAVGS 369
Cdd:PRK09357 298 IDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGE 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 347543829 370 DADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 420
Cdd:PRK09357 373 PADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1-435 |
8.96e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.56 E-value: 8.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 1 MEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSL 80
Cdd:PRK01211 20 VEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 81 LAAFDQWREWADSKSCCDYSLHvdisewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVlSVIRDIG 156
Cdd:PRK01211 94 YNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 157 AIAQVHAENGDIIAEEQQRILDLgitgpEGHVLSRPEEVEAEAVNRAITIANQtncplyiTKVMS-KSSAEVIAQARKKG 235
Cdd:PRK01211 161 IPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGRFLREV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 236 T----VVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAvgkdN 311
Cdd:PRK01211 229 TphhlLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSDHAPHTEEDKQ----E 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 312 FTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRIAVGSDADLVIWDPDSVKTISAKTHNS 391
Cdd:PRK01211 287 FEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHS 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 347543829 392 SLEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 435
Cdd:PRK01211 364 KCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1-433 |
1.21e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 106.01 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 1 MEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSL 80
Cdd:PRK04250 19 IENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 81 LAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTdcqiYEVLSvirdigAIAQ 160
Cdd:PRK04250 95 EKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVD----YACAP------GIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 161 VHAENGDIIAEEqqrildlgitgPEghvlsRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYG 240
Cdd:PRK04250 163 VHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSFEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 241 EPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTAQKAVGKdnftlipEG 318
Cdd:PRK04250 227 TP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLEDKEAGA-------AG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 319 TNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIF 398
Cdd:PRK04250 288 IPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPY 364
|
410 420 430
....*....|....*....|....*....|....*
gi 347543829 399 EGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 433
Cdd:PRK04250 365 EGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PLN02795 |
PLN02795 |
allantoinase |
2-436 |
2.87e-24 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 106.01 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDhvVP---E 75
Cdd:PLN02795 67 EGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAAGGITTLVD--MPlnsF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 76 PGTSLLAAFDQWREWADSKsccdysLHVDISEWHKGIQE------EMEALVkDHGV---NSFLVYMAFKDRFQLTDCQIY 146
Cdd:PLN02795 143 PSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGAlglKSFMCPSGINDFPMTTATHIK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 147 EVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLgiTGPEGHVLSRPEEVEAEAVNRAITIANQTN-------CPLYITKV 219
Cdd:PLN02795 216 AALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQLLEVAKDTRpggvaegAHVHIVHL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 220 M-SKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA--------FVTSPPLSpDPTTPDFLNSLLSCGDL 290
Cdd:PLN02795 294 SdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIR-DAANRELLWKALLDGDI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 291 QVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSD 370
Cdd:PLN02795 361 DMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKD 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347543829 371 ADLVIWDP------DSVKTISAKTHNSSleynIFEGMECRGSPLVVISQGKIVLEDGtLHVTEGSGRYIPRK 436
Cdd:PLN02795 439 ADIVVWDPeaefvlDESYPIYHKHKSLS----PYLGTKLSGKVIATFVRGNLVFLEG-KHAKQACGSPILAK 505
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
2-421 |
6.30e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 104.37 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLL 81
Cdd:PRK07575 27 EDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 82 AAFDQWREWADSKSCCDYSLHVDISewhkgiQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQiyEVLSVI--RDIGAIA 159
Cdd:PRK07575 105 AALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSSHGPLLVDEE--AALERIfaEGTRLIA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 160 qVHAENGDIIAEEQQRILdlGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQArkKGTVVY 239
Cdd:PRK07575 177 -VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHILHLSTAIEAELLRQD--KPSWVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 240 GEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEG 318
Cdd:PRK07575 252 AEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPN---SPSG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 319 TNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIF 398
Cdd:PRK07575 323 MPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVLVDLNTYRPVRREELLTKCGWSPF 400
|
410 420
....*....|....*....|...
gi 347543829 399 EGMECRGSPLVVISQGKIVLEDG 421
Cdd:PRK07575 401 EGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-431 |
4.49e-20 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 92.68 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 3 DGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLA 82
Cdd:PRK09060 29 DGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 83 AFDQWREWADSKSCCDYSLHVDISewHKGIQE--EMEALVKDHGVNsflVYM--AFKDRFQLTDCQIYEVLSVIRDIGAi 158
Cdd:PRK09060 106 ALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGDLLVEDDEGLRRILRNGRRRAA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 159 aqVHAENGDIIAEEQqrilDLGITG-PEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTV 237
Cdd:PRK09060 180 --FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIHVLHVSTAEEIDFLADHKDVATV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 238 --------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAvgk 309
Cdd:PRK09060 254 evtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKA--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 310 DNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTH 389
Cdd:PRK09060 316 KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTIVDLKRRETITNEWI 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 347543829 390 NSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 431
Cdd:PRK09060 394 ASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
30-430 |
3.56e-09 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 58.62 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 30 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIS--E 107
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 108 WHKGIQeemealVKDHGVNS-FLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAqVHAENGDIIAeeqqrILDLgitgpeg 186
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 187 hvlsrpeeveAEAVNRAItianqtncplYITKVMSKSSAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 266
Cdd:cd01316 144 ----------ASLHNRSI----------HICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 267 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 346
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 347 VTSTNAAKVFNLYPrkgriavgsDADLVI-WDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 425
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 347543829 426 TEGSG 430
Cdd:cd01316 340 PPGFG 344
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
2-431 |
5.77e-09 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 58.08 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF----FQGTKAALAG------------GT 65
Cdd:cd01297 25 RDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrpssRQGVTTVVLGncgvspapanpdDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 66 TMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DISEWHKGI---------QEEMEALVKDH--- 123
Cdd:cd01297 101 ARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVMGLdareateeeLAKMRELLREAlea 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 124 ---GVNSFLVYMafkDRFQLTDCQIYEVLSVIRDIGAIAQVHaengdiIAEEQQRILdlgitgpeghvlsrpeeveaEAV 200
Cdd:cd01297 180 galGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTH------VRYEGDSIL--------------------EAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 201 NRAITIANQTNCPLYIT--KVMSKSSAEVIAQ-------ARKKGTVVYGE--PITASLGTDgshywsknwakAAAFVTSP 269
Cdd:cd01297 231 DELLRLGRETGRPVHIShlKSAGAPNWGKIDRllalieaARAEGLQVTADvyPYGAGSEDD-----------VRRIMAHP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 270 PLspdpttpdflnslLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEERMSVIWdkAVVTGKMDENQFVAVTS 349
Cdd:cd01297 300 VV-------------MGGSDGGALGKPHP-------------------RSYGDFTRVLGHY--VRERKLLSLEEAVRKMT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 350 TNAAKVFNLYPRkGRIAVGSDADLVIWDPDSVK---TISAKTHNSsleynifEGMEcrgspLVVISqGKIVLEDGtLHVT 426
Cdd:cd01297 346 GLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE-----AVLVN-GVPVVRDG-AFTG 410
|
....*
gi 347543829 427 EGSGR 431
Cdd:cd01297 411 ARPGR 415
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
2-102 |
2.27e-08 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 56.42 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTS 79
Cdd:PRK09236 25 ENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTT 100
|
90 100
....*....|....*....|...
gi 347543829 80 LLAAFDQWREWADSKSCCDYSLH 102
Cdd:PRK09236 101 TLEALEAKYQIAAQRSLANYSFY 123
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-386 |
1.59e-07 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 53.43 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD---------QGMTSADDFFQGT----KAALAGGTT 66
Cdd:COG1228 34 EDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgravefeagGGITPTVDLVNPAdkrlRRALAAGVT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 67 MIIDHvvpePGTSL----------LAAFDQWREWAdskscCDYSLHVDISEWHKGIQEEMEAL--VKDHGVNSFLVYMAF 134
Cdd:COG1228 114 TVRDL----PGGPLglrdaiiageSKLLPGPRVLA-----AGPALSLTGGAHARGPEEARAALreLLAEGADYIKVFAEG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 135 KDRfQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIaeeqQRILDLGITGPEgHVLSRpeeveaeavnraitianqtncpl 214
Cdd:COG1228 185 GAP-DFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-HGTYL----------------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 215 yitkvmsksSAEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNWAKAAAFVtspplspDPTTPDFLNSLLSCGDLQVTG 294
Cdd:COG1228 236 ---------DDEVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV-------REAALANARRLHDAGVPVALG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 295 SAHctfntaqkavgkdNFTLIPEGTNGTEERMsviwdkaVVTGKMDENQ-FVAVTStNAAKVFNLYPRKGRIAVGSDADL 373
Cdd:COG1228 298 TDA-------------GVGVPPGRSLHRELAL-------AVEAGLTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADL 356
|
410
....*....|...
gi 347543829 374 VIWDPDSVKTISA 386
Cdd:COG1228 357 VLLDGDPLEDIAY 369
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
345-379 |
2.99e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.79 E-value: 2.99e-07
10 20 30
....*....|....*....|....*....|....*
gi 347543829 345 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 379
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
191-388 |
2.02e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 50.37 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 191 RPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKA 262
Cdd:PRK07369 207 DPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 263 aafvtsPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDEN 342
Cdd:PRK07369 281 ------PPL-GNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSAL 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 347543829 343 QFVAVTSTNAAKVFNLYPRkgRIAVGSDADLVIWDPDSVKTISAKT 388
Cdd:PRK07369 351 QLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
345-379 |
2.93e-06 |
|
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: 49.50 E-value: 2.93e-06
10 20 30
....*....|....*....|....*....|....*
gi 347543829 345 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 379
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
345-400 |
1.66e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 347543829 345 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEG 400
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
2-423 |
2.20e-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: 46.81 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM---------------------PDQGMTSADDFFQGTK 58
Cdd:cd01298 25 EDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplmewlkdliwPLERLLTEEDVYLGAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 59 AALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKsccdyslhvdisewhKGIQEEMEALVK 121
Cdd:cd01298 105 LALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEET---------------EEALAEAERLIR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 122 D-HGVNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-AENGDIIAEEQQR--------ILDLGITG 183
Cdd:cd01298 170 EwHGAADGRI------RVALAPHAPYTCsDELLREVAELAreygvplHIHlAETEDEVEESLEKygkrpveyLEELGLLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 184 PE---GH-VLSRPEEVEaeavnraitIANQTN-----CPlyiTKVMsKSSAEV--IAQARKKGtvvygepITASLGTDGS 252
Cdd:cd01298 244 PDvvlAHcVWLTDEEIE---------LLAETGtgvahNP---ASNM-KLASGIapVPEMLEAG-------VNVGLGTDGA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 253 hywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAVGKDNFTLIPEgtngteermsviwd 331
Cdd:cd01298 304 ---------------------------------ASNNnLDMFEEMRLAALL-QKLAHGDPTALPAE-------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 332 kavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNifegmeCRGSP--LV 409
Cdd:cd01298 336 -----------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS------ANGGDvdTV 397
|
490
....*....|....
gi 347543829 410 VISqGKIVLEDGTL 423
Cdd:cd01298 398 IVN-GRVVMEDGEL 410
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
360-438 |
1.05e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 45.07 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 360 PRKGRIAVGSDADLVIWDPDSVK---TISAKTHNSsleynifEGMEcrgsplVVISQGKIVLEDGTLHVTEGSGRYIpRK 436
Cdd:PRK09061 441 RRKGRLQAGADADIVVFDPETITdraTFEDPNRPS-------EGVR------HVLVNGVPVVSNGELVRDARPGRPV-RR 506
|
..
gi 347543829 437 PF 438
Cdd:PRK09061 507 PV 508
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
320-380 |
1.61e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.17 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347543829 320 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDS 380
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
294-393 |
4.01e-04 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 42.70 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 294 GSAHCTFNTAQKAVGKDnftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKG 363
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIG 300
|
90 100 110
....*....|....*....|....*....|
gi 347543829 364 RIAVGSDADLVIWDPDSVKTISAKTHNSSL 393
Cdd:cd01307 301 TLAVGYDADLTVFDLKDGRVELVDSEGDTL 330
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
352-437 |
4.03e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 42.85 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 352 AAKVFNLYPRkGRIAVGSDADLVIWDPDSVKtiSAKTHNSSLEYNifEGMECrgsplVVISqGKIVLEDGTlHVTEGSGR 431
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-----VIVN-GVVVVEDGK-PTGARPGR 520
|
....*.
gi 347543829 432 YIPRKP 437
Cdd:COG3653 521 VLRGGG 526
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-184 |
5.19e-04 |
|
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: 42.51 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 2 EDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSADDFFQ--------------------GT 57
Cdd:COG0402 27 EDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDLPLLDwleeyiwplearldpedvyaGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 58 KAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDYSLHVDISEWHKGIQEEMEALVKD-HG 124
Cdd:COG0402 107 LLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDRGFPDGLREDADEGLADSERLIERwHG 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347543829 125 VNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-----AENGDIIAEEQQRILD----LGITGP 184
Cdd:COG0402 182 AADGRI------RVALAPHAPYTVsPELLRAAAALArelglplHTHlaetrDEVEWVLELYGKRPVEyldeLGLLGP 252
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
347-387 |
8.87e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 41.61 E-value: 8.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 347543829 347 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPD-SVKTISAK 387
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
3-379 |
8.90e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 3 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 61
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 62 AGGTTMIidHVVPEP-----GTSLLAAFDQW-------REWADSKSCCDYslHVDISEWHKGI---------QEEMEALV 120
Cdd:cd01309 81 AGGVTTV--QVLPGSanligGQGVVIKTDGGtiedmfiKAPAGLKMALGE--NPKRVYGGKGKepatrmgvaALLRDAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 121 K-DHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRdiGAI-AQVHAengdiiaeeqqrildlgitgpeghvlSRPEEVEAe 198
Cdd:cd01309 157 KaQEYGRKYDLGKNAKKDPPERDLKLEALLPVLK--GEIpVRIHA--------------------------HRADDILT- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 199 avnrAITIANQTNCPLYITKVM-SKSSAEVIAQARKKgtVVYGEPITASLGTDGSHYwskNWAKAAAFVTSPPLSPDPTT 277
Cdd:cd01309 208 ----AIRIAKEFGIKITIEHGAeGYKLADELAKHGIP--VIYGPTLTLPKKVEEVND---AIDTNAYLLKKGGVAFAISS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 278 pdflnsllscgDLQVTGSAHCTFNTAqkavgkdnftlipegtngteermsviwdKAVVTGKMDENQFVAVTStNAAKVFN 357
Cdd:cd01309 279 -----------DHPVLNIRNLNLEAA----------------------------KAVKYGLSYEEALKAITI-NPAKILG 318
|
410 420
....*....|....*....|..
gi 347543829 358 LYPRKGRIAVGSDADLVIWDPD 379
Cdd:cd01309 319 IEDRVGSLEPGKDADLVVWNGD 340
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
347-431 |
2.93e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 40.47 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347543829 347 VTSTNAAKVFNLyPRKGRIAVGSDADLVIW--DPDSVKTisakthnssLEYNIFEGMECRgsPLVVISQGKIVLEDGTLh 424
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDP---------SDYEKVEKAFSR--AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 347543829 425 VTEGSGR 431
Cdd:cd01304 502 VAEPWGR 508
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
330-377 |
4.02e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 39.45 E-value: 4.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 347543829 330 WDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWD 377
Cdd:PRK09237 282 YSLATVMSKflalgMPLEEVIAAVTKNAADALRL-PELGRLQVGSDADLTLFT 333
|
|
| |
