|
Name |
Accession |
Description |
Interval |
E-value |
| HD_3 |
pfam13023 |
HD domain; HD domains are metal dependent phosphohydrolases. |
496-661 |
5.92e-67 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 432939 Cd Length: 163 Bit Score: 217.47 E-value: 5.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 496 IERLKTTKREGWRRFGIARGESIADHMYRMSLLSMLAPPALAPrLDLARCMKMCLIHDMAESLVGDITPVDGVAKPEKNR 575
Cdd:pfam13023 1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEYAGP-VDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 576 REAETMDYITKNLLGSVyggipGAEIREIWQEYEDSQTLNSHYVHDLDKMELLLQMMEYEKR--GQGKLDLGEFAYVATK 653
Cdd:pfam13023 80 REREAAERIFGLLPEDQ-----GEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDswAAFEADLSQFYGRNST 154
|
....*...
gi 2054124457 654 FTLPETKE 661
Cdd:pfam13023 155 ILAEGSPE 162
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
8-346 |
3.47e-59 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 201.69 E-value: 3.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 8 ISFAIIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-LAAELNVAHYTSVSDLLRSEHVpQAAIVCTPNHTHVAVSK 86
Cdd:COG0673 4 LRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEaFAEEYGVRVYTDYEELLADPDI-DAVVIATPNHLHAELAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 87 QLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGLWTTYKPgdyfE 166
Cdd:COG0673 83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRP----A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 167 APTEWRQGKD---GGVVLINAIHEIDLLHHLLG-PITRVHAEKTTSQRGH-EAEEGAALTIRFKSGVVGTFLISDNVPSP 241
Cdd:COG0673 159 GPADWRFDPElagGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDRvEVDDTAAATLRFANGAVATLEASWVAPGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 242 YNfeagtgenplipktgQNFYQIFGSDGSLsvpdlsiwsykgtnkswhsemareklavedgvpfelqlahFCRVIQGKES 321
Cdd:COG0673 239 ER---------------DERLEVYGTKGTL----------------------------------------FVDAIRGGEP 263
|
330 340
....*....|....*....|....*
gi 2054124457 322 PSCSPQAGLGALIVCQAIKDALEAN 346
Cdd:COG0673 264 PPVSLEDGLRALELAEAAYESARTG 288
|
|
| myo_inos_iolG |
TIGR04380 |
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ... |
10-346 |
9.13e-37 |
|
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]
Pssm-ID: 275173 [Multi-domain] Cd Length: 330 Bit Score: 140.82 E-value: 9.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 10 FAIIGTGLIGPRHARTVVES-PDAELVAVVDP-APAGAQLAAELNVAH-YTSVSDLLRSEHVpQAAIVCTPNHTHVAVSK 86
Cdd:TIGR04380 4 VGIIGAGRIGKVHAENLATHvPGARLKAIVDPfADAAAELAEKLGIEPvTQDPEAALADPEI-DAVLIASPTDTHADLII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 87 QLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGlwTTYKPG---- 162
Cdd:TIGR04380 83 EAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRI--TSRDPApppv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 163 DYFEAptewrqgkDGGVVLINAIHEIDLLHHLLG-PITRVHAekTTSQRGHEA--EEG----AALTIRFKSGVVGTflIS 235
Cdd:TIGR04380 161 AYVKV--------SGGLFLDMTIHDFDMARFLLGsEVEEVYA--QGSVLVDPAigEAGdvdtAVITLKFENGAIAV--ID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 236 DNVPSPYNFEAGTgenplipktgqnfyQIFGSDGSLSVPD-----LSIWSYKGT--NKSWHSEMAREKLAvedgvpFELQ 308
Cdd:TIGR04380 229 NSRRAAYGYDQRV--------------EVFGSKGMLRAENdtestVILYDAEGVrgDKPLNFFLERYRDA------YRAE 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 2054124457 309 LAHFCRVIQGKESPSCSPQAGLGALIVCQAIKDALEAN 346
Cdd:TIGR04380 289 IQAFVDAILEGRPPPVTGEDGLKALLLALAAKRSLEEG 326
|
|
| UDP-GlcNAcDh_Arch |
NF040723 |
UDP-N-acetylglucosamine 3-dehydrogenase; |
12-342 |
2.08e-32 |
|
UDP-N-acetylglucosamine 3-dehydrogenase;
Pssm-ID: 468687 [Multi-domain] Cd Length: 302 Bit Score: 127.39 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 12 IIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-LAAELNVAHYTSVSDLLRSEhvPQAAIVCTPNHTHVAVSKQLSS 90
Cdd:NF040723 5 VIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKeLAKQYNTKAFTDYKELLKED--LDAVSIVVPTKLHKQVALDAIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 91 GGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAInglwTTYKPGDYfeAPte 170
Cdd:NF040723 83 AGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLGKIVSI----SAKRVGPY--NP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 171 wrQGKDGGVVLINAIHEIDLLHHLLG-PITRVHAeKTTSQRgHEAEEGAALTIRFKSGVVGtfLISDNVPSPYnfeagtg 249
Cdd:NF040723 155 --RIRDVGVILDLGVHDIDVISYLYGsKVKEVYA-IAGSVI-HPFEDHASIMLRFEHNISG--LVETNWLTPH------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 250 enplipKTGQnfYQIFGSDGSLSVpdlsiwSYKGTNKSWHSEMAREKLAVEDGVPFELQLAHFCRVIQGKESPSCSPQAG 329
Cdd:NF040723 222 ------KTRK--LTVVGTEGIAYL------DYINQTLTIHDEEWVKEAKIEKEEPLKNELEHFIECVENGKEPLVSGEDG 287
|
330
....*....|....
gi 2054124457 330 LGALIVC-QAIKDA 342
Cdd:NF040723 288 LHALKVAlAAIESY 301
|
|
| YfbR |
COG1896 |
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ... |
490-638 |
1.19e-30 |
|
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only];
Pssm-ID: 441500 Cd Length: 162 Bit Score: 118.04 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 490 LPYFHLIERLKTTKREGWRRFGiaRGESIADHMYRMSLLSMLAPPALAPRLDLARCMKMCLIHDMAESLVGDITPVDGVA 569
Cdd:COG1896 2 LDFLAELDRLKLIKRWGLLRNS--RPENVAEHSWHVALIAHLLADIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2054124457 570 KPEKNRREAETMDYITKNLLGSVyggipGAEIREIWQEYEDSQTLNSHYVHDLDKMELLLQMMEYEKRG 638
Cdd:COG1896 80 NEAKKEIERAAAERLFGLLPEEL-----REEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAG 143
|
|
| GFO_IDH_MocA |
pfam01408 |
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ... |
8-126 |
1.33e-26 |
|
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 104.98 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 8 ISFAIIGTGLIGPRHARTVVES-PDAELVAVVDPAPAGAQLAAE-LNVAHYTSVSDLLRSEHvPQAAIVCTPNHTHVAVS 85
Cdd:pfam01408 1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERAEAVAEsFGVEVYSDLEELLNDPE-IDAVIVATPNGLHYDLA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2054124457 86 KQLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGH 126
Cdd:pfam01408 80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
|
|
| PRK10206 |
PRK10206 |
putative oxidoreductase; Provisional |
7-161 |
3.47e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182305 [Multi-domain] Cd Length: 344 Bit Score: 59.07 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 7 VISFAIIGTGLIGPR-HARTVVESPDAELVA-VVDPAPAGAQLAAELNVAHYTSVSDLLRSEHVPQAAIVCTPNHTHVAV 84
Cdd:PRK10206 1 VINCAFIGFGKSTTRyHLPYVLNRKDSWHVAhIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054124457 85 SKQLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGLWTTYKP 161
Cdd:PRK10206 81 AKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRP 157
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
11-96 |
3.16e-05 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 44.84 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 11 AIIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-------LAAELNVAHYTSVSDLLrSEHVPQAAIVCTPNHTHVA 83
Cdd:cd24146 4 VVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPAKVGkdlgelgGGAPLGVKVTDDLDAVL-AATKPDVVVHATTSFLADV 82
|
90
....*....|....*
gi 2054124457 84 VS--KQLSSGGVHVL 96
Cdd:cd24146 83 APqiERLLEAGLNVI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HD_3 |
pfam13023 |
HD domain; HD domains are metal dependent phosphohydrolases. |
496-661 |
5.92e-67 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 432939 Cd Length: 163 Bit Score: 217.47 E-value: 5.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 496 IERLKTTKREGWRRFGIARGESIADHMYRMSLLSMLAPPALAPrLDLARCMKMCLIHDMAESLVGDITPVDGVAKPEKNR 575
Cdd:pfam13023 1 ADKLKFVKRQGWLQDGRVRPESVAEHSWRMALMAMLLAEYAGP-VDIARVIKMALIHDLVEILAGDIIPYDGVAKEEKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 576 REAETMDYITKNLLGSVyggipGAEIREIWQEYEDSQTLNSHYVHDLDKMELLLQMMEYEKR--GQGKLDLGEFAYVATK 653
Cdd:pfam13023 80 REREAAERIFGLLPEDQ-----GEELLALWDEFEARETPEAKFAKDLDKLEPLLQNLEYEGDswAAFEADLSQFYGRNST 154
|
....*...
gi 2054124457 654 FTLPETKE 661
Cdd:pfam13023 155 ILAEGSPE 162
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
8-346 |
3.47e-59 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 201.69 E-value: 3.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 8 ISFAIIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-LAAELNVAHYTSVSDLLRSEHVpQAAIVCTPNHTHVAVSK 86
Cdd:COG0673 4 LRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEaFAEEYGVRVYTDYEELLADPDI-DAVVIATPNHLHAELAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 87 QLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGLWTTYKPgdyfE 166
Cdd:COG0673 83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRP----A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 167 APTEWRQGKD---GGVVLINAIHEIDLLHHLLG-PITRVHAEKTTSQRGH-EAEEGAALTIRFKSGVVGTFLISDNVPSP 241
Cdd:COG0673 159 GPADWRFDPElagGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDRvEVDDTAAATLRFANGAVATLEASWVAPGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 242 YNfeagtgenplipktgQNFYQIFGSDGSLsvpdlsiwsykgtnkswhsemareklavedgvpfelqlahFCRVIQGKES 321
Cdd:COG0673 239 ER---------------DERLEVYGTKGTL----------------------------------------FVDAIRGGEP 263
|
330 340
....*....|....*....|....*
gi 2054124457 322 PSCSPQAGLGALIVCQAIKDALEAN 346
Cdd:COG0673 264 PPVSLEDGLRALELAEAAYESARTG 288
|
|
| myo_inos_iolG |
TIGR04380 |
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ... |
10-346 |
9.13e-37 |
|
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]
Pssm-ID: 275173 [Multi-domain] Cd Length: 330 Bit Score: 140.82 E-value: 9.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 10 FAIIGTGLIGPRHARTVVES-PDAELVAVVDP-APAGAQLAAELNVAH-YTSVSDLLRSEHVpQAAIVCTPNHTHVAVSK 86
Cdd:TIGR04380 4 VGIIGAGRIGKVHAENLATHvPGARLKAIVDPfADAAAELAEKLGIEPvTQDPEAALADPEI-DAVLIASPTDTHADLII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 87 QLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGlwTTYKPG---- 162
Cdd:TIGR04380 83 EAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRI--TSRDPApppv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 163 DYFEAptewrqgkDGGVVLINAIHEIDLLHHLLG-PITRVHAekTTSQRGHEA--EEG----AALTIRFKSGVVGTflIS 235
Cdd:TIGR04380 161 AYVKV--------SGGLFLDMTIHDFDMARFLLGsEVEEVYA--QGSVLVDPAigEAGdvdtAVITLKFENGAIAV--ID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 236 DNVPSPYNFEAGTgenplipktgqnfyQIFGSDGSLSVPD-----LSIWSYKGT--NKSWHSEMAREKLAvedgvpFELQ 308
Cdd:TIGR04380 229 NSRRAAYGYDQRV--------------EVFGSKGMLRAENdtestVILYDAEGVrgDKPLNFFLERYRDA------YRAE 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 2054124457 309 LAHFCRVIQGKESPSCSPQAGLGALIVCQAIKDALEAN 346
Cdd:TIGR04380 289 IQAFVDAILEGRPPPVTGEDGLKALLLALAAKRSLEEG 326
|
|
| UDP-GlcNAcDh_Arch |
NF040723 |
UDP-N-acetylglucosamine 3-dehydrogenase; |
12-342 |
2.08e-32 |
|
UDP-N-acetylglucosamine 3-dehydrogenase;
Pssm-ID: 468687 [Multi-domain] Cd Length: 302 Bit Score: 127.39 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 12 IIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-LAAELNVAHYTSVSDLLRSEhvPQAAIVCTPNHTHVAVSKQLSS 90
Cdd:NF040723 5 VIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKeLAKQYNTKAFTDYKELLKED--LDAVSIVVPTKLHKQVALDAIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 91 GGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAInglwTTYKPGDYfeAPte 170
Cdd:NF040723 83 AGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLGKIVSI----SAKRVGPY--NP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 171 wrQGKDGGVVLINAIHEIDLLHHLLG-PITRVHAeKTTSQRgHEAEEGAALTIRFKSGVVGtfLISDNVPSPYnfeagtg 249
Cdd:NF040723 155 --RIRDVGVILDLGVHDIDVISYLYGsKVKEVYA-IAGSVI-HPFEDHASIMLRFEHNISG--LVETNWLTPH------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 250 enplipKTGQnfYQIFGSDGSLSVpdlsiwSYKGTNKSWHSEMAREKLAVEDGVPFELQLAHFCRVIQGKESPSCSPQAG 329
Cdd:NF040723 222 ------KTRK--LTVVGTEGIAYL------DYINQTLTIHDEEWVKEAKIEKEEPLKNELEHFIECVENGKEPLVSGEDG 287
|
330
....*....|....
gi 2054124457 330 LGALIVC-QAIKDA 342
Cdd:NF040723 288 LHALKVAlAAIESY 301
|
|
| YfbR |
COG1896 |
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and ... |
490-638 |
1.19e-30 |
|
5'-deoxynucleotidase YfbR and related HD superfamily hydrolases [Nucleotide transport and metabolism, General function prediction only];
Pssm-ID: 441500 Cd Length: 162 Bit Score: 118.04 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 490 LPYFHLIERLKTTKREGWRRFGiaRGESIADHMYRMSLLSMLAPPALAPRLDLARCMKMCLIHDMAESLVGDITPVDGVA 569
Cdd:COG1896 2 LDFLAELDRLKLIKRWGLLRNS--RPENVAEHSWHVALIAHLLADIANEGVDPERVAKMALLHDLVEIDTGDIPTPVKYA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2054124457 570 KPEKNRREAETMDYITKNLLGSVyggipGAEIREIWQEYEDSQTLNSHYVHDLDKMELLLQMMEYEKRG 638
Cdd:COG1896 80 NEAKKEIERAAAERLFGLLPEEL-----REEFRALWDEFEAGETPEARFVKAADKLEALLQALEEIGAG 143
|
|
| GFO_IDH_MocA |
pfam01408 |
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ... |
8-126 |
1.33e-26 |
|
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 104.98 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 8 ISFAIIGTGLIGPRHARTVVES-PDAELVAVVDPAPAGAQLAAE-LNVAHYTSVSDLLRSEHvPQAAIVCTPNHTHVAVS 85
Cdd:pfam01408 1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERAEAVAEsFGVEVYSDLEELLNDPE-IDAVIVATPNGLHYDLA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2054124457 86 KQLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGH 126
Cdd:pfam01408 80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
|
|
| GFO_IDH_MocA_C |
pfam02894 |
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ... |
138-339 |
1.45e-17 |
|
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 427044 Cd Length: 203 Bit Score: 81.70 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 138 KKVLESGVLGKIIAING-LWTTYKPGDYFEaptEWRQ--GKDGGVVLINAIHEIDLLHHLLGPITRVhaektTSQRGHea 214
Cdd:pfam02894 1 KELIENGVLGEVVMVTVhTRDPFRPPQEFK---RWRVdpEKSGGALYDLGIHTIDLLIYLFGEPPSV-----VAVYAS-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 215 EEGAALTIRFKSGVVGTFLISdnvpSPYNFEAGTGEnplipktgqnfYQIFGSDGSLSVPDLSIWSYKGT---NKSWHSE 291
Cdd:pfam02894 71 EDTAFATLEFKNGAVGTLETS----GGSIVEANGHR-----------ISIHGTKGSIELDGIDDGLLSVTvvgEPGWATD 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2054124457 292 MAREKLAVEDGVPFE--------LQLAHFCRVIQGKESPSCSPQAGLGALIVCQAI 339
Cdd:pfam02894 136 DPMVRKGGDEVPEFLgsfaggylLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAA 191
|
|
| PRK10206 |
PRK10206 |
putative oxidoreductase; Provisional |
7-161 |
3.47e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182305 [Multi-domain] Cd Length: 344 Bit Score: 59.07 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 7 VISFAIIGTGLIGPR-HARTVVESPDAELVA-VVDPAPAGAQLAAELNVAHYTSVSDLLRSEHVPQAAIVCTPNHTHVAV 84
Cdd:PRK10206 1 VINCAFIGFGKSTTRyHLPYVLNRKDSWHVAhIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054124457 85 SKQLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGLWTTYKP 161
Cdd:PRK10206 81 AKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRP 157
|
|
| PRK11579 |
PRK11579 |
putative oxidoreductase; Provisional |
13-197 |
3.42e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183212 [Multi-domain] Cd Length: 346 Bit Score: 49.72 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 13 IGTGLIG------PRHARTVVESPDAELvAVVDPAPAGAQLAAELNVAHYTSVSDLLRSEHVpQAAIVCTPNHTHVAVSK 86
Cdd:PRK11579 5 IRVGLIGygyaskTFHAPLIAGTPGLEL-AAVSSSDATKVKADWPTVTVVSEPQHLFNDPNI-DLIVIPTPNDTHFPLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 87 QLSSGGVHVLVEKPISSDIPSGTELLSHLQTTEVKTLVGHHRRFNPYIISTKKVLESGVLGKIIAINGLWTTYKPgdyfE 166
Cdd:PRK11579 83 AALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRP----Q 158
|
170 180 190
....*....|....*....|....*....|...
gi 2054124457 167 APTEWRQ--GKDGGVVLINAIHEIDLLHHLLGP 197
Cdd:PRK11579 159 VRQRWREqgGPGSGIWYDLAPHLLDQAIQLFGL 191
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
11-96 |
3.16e-05 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 44.84 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 11 AIIGTGLIGPRHARTVVESPDAELVAVVDPAPAGAQ-------LAAELNVAHYTSVSDLLrSEHVPQAAIVCTPNHTHVA 83
Cdd:cd24146 4 VVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPAKVGkdlgelgGGAPLGVKVTDDLDAVL-AATKPDVVVHATTSFLADV 82
|
90
....*....|....*
gi 2054124457 84 VS--KQLSSGGVHVL 96
Cdd:cd24146 83 APqiERLLEAGLNVI 97
|
|
| Peptidase_C6 |
pfam00851 |
Helper component proteinase; This protein is found in genome polyproteins of potyviruses. |
495-681 |
3.95e-03 |
|
Helper component proteinase; This protein is found in genome polyproteins of potyviruses.
Pssm-ID: 279223 Cd Length: 440 Bit Score: 40.36 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 495 LIERLKTTKREGWRRFGIARGESIADHMYRMSLLSMLAPPalaprldlarcmkmclihDMAESLVGDITPVDGVAKPEKN 574
Cdd:pfam00851 54 IVNALSKAKQRGMLEFGKERDRFIYDERVLIKLFELQAPP------------------PYKIATITEITTICCGSDDDPF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2054124457 575 RREAETMDYITKNLLGSVYGgipgaeireiWQEYEDSqtlnshyvhdldkmelLLQMMEYEKRGQGKLDLGEFAYVATKF 654
Cdd:pfam00851 116 AHIRIIMKVLAEPNLADVSG----------WQPASGS----------------LLLLARHLKNRHTSIQAGNSSMFHNSL 169
|
170 180
....*....|....*....|....*..
gi 2054124457 655 tlPETKEWADALLKEREHFWGTQQHVH 681
Cdd:pfam00851 170 --AGAQNWDNQIDRNQVRIWGQRNEEA 194
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
8-82 |
7.39e-03 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 37.55 E-value: 7.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2054124457 8 ISFAIIGTGLIGpRHARTVVE-SPDAELVAVVD-PAPAGAQLAAELNVAHytsVSDLLRSEHVPQAAIVCTPNHTHV 82
Cdd:cd02270 1 IRVAIVGYGNLG-RGVEEAIQaNPDMELVGVFRrRDPKSTKELTPVVVVS---VVEHISELDKVDVAILCGGSATDL 73
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