|
Name |
Accession |
Description |
Interval |
E-value |
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
155-331 |
1.91e-20 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 88.98 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 155 VYITGLGKESVIWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNA-DGELLTIDSESNTIASRKKLQDDGKahfy 233
Cdd:COG3391 38 AAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSgSGRVSVIDLATGKVVATIPVGGGPR---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 234 lNLSLDTAGHRAFITDSKQPEVLVVDTRDGKVLEKIAAPESL-AVLFNPARNEAYVTHRKAGE----VSVIDGKSYKVVK 308
Cdd:COG3391 114 -GLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPhGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVA 192
|
170 180
....*....|....*....|...
gi 488996073 309 TFKTPTHPNSLALSEDGKTLYVS 331
Cdd:COG3391 193 TIPVGGGPVGVAVSPDGRRLYVA 215
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
38-219 |
3.16e-16 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 77.04 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 38 AVGKGAYEMAYSQQENALWVATSQSrsldkgGVVYRLDPTTLDVTQIIHNDLKPFGATINHATGTLWFGNTVDSTVTAID 117
Cdd:COG3391 65 AAVADADGADAGADGRRLYVANSGS------GRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 118 AKTGAVKGRLVLDErqrsetvrplQPRELAVNEQTNTVYITGLGKESV---IWVVDGATLKLKTTITgTGAMATGLAIDP 194
Cdd:COG3391 139 TATGKVVATIPVGA----------GPHGIAVDPDGKRLYVANSGSNTVsviVSVIDTATGKVVATIP-VGGGPVGVAVSP 207
|
170 180
....*....|....*....|....*
gi 488996073 195 QAKRLYTTNADGEllTIDSESNTIA 219
Cdd:COG3391 208 DGRRLYVANRGSN--TSNGGSNTVS 230
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
92-330 |
4.58e-11 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 63.14 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 92 FGATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERqrsetvrplqPRELAVNEQTNTVYITGlGKESVIWVVDG 171
Cdd:TIGR03866 2 LLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQR----------PRGITFSKDGKLLYVCA-SDSDTIQVIDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 172 ATLKLKTTITgTGAMATGLAIDPQAKRLYTTNADGELLT-IDsesntIASRKKLQD--------------DGK------- 229
Cdd:TIGR03866 71 ATGEVLHTLP-SGPDPEQFALHPNGKILYIANEDDALVTvID-----IETRKVLAQidvgvepegmavspDGKivvntse 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 230 ----AHFylnlsLDTAGHRafITDSkqpevLVVDTRdgkvlekiaaPESLAvlFNPARNEAYVTHRKAGEVSVIDGKSYK 305
Cdd:TIGR03866 145 ttnmAHW-----IDTATYE--IVDN-----TLVDAR----------PRFAE--FTADGKELWVSSEIGGTVTVIDVATRK 200
|
250 260 270
....*....|....*....|....*....|...
gi 488996073 306 VVK--TFKTP-THPNSL-----ALSEDGKTLYV 330
Cdd:TIGR03866 201 VIKkiTFAIPgVHPEKVqpvgiKLTKDGKTAFV 233
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
83-225 |
5.93e-06 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 47.34 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 83 QIIHN---DLKPFGATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERqrseTVRP--LQPRELAVNEQTNTVYI 157
Cdd:TIGR03866 158 EIVDNtlvDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIP----GVHPekVQPVGIKLTKDGKTAFV 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488996073 158 tGLGKESVIWVVDGATLKLKTTITgTGAMATGLAIDPQAKRLYTTNA-DGELLTIDsesntIASRKKLQ 225
Cdd:TIGR03866 234 -ALGPANRVAVVDAKTYEVLDYLL-VGQRVWQLAFTPDESRLLTTNGvSNDVSVID-----VAALKVIK 295
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
139-336 |
1.08e-05 |
|
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.
Pssm-ID: 467720 [Multi-domain] Cd Length: 380 Bit Score: 46.95 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 139 RPLQPRELAVNEQTNTVYITGLGKESViWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDSESNTI 218
Cdd:cd20718 14 RELPPVAYGIWDLENLMVVVERDAGSV-LVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYVISRDGWLTKIDLYTLRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 219 ASRKK---------LQDDGKahfYLNLSLDTAGHrAFITDSKQPEVL-VVDTRDGKVLEKIAAPESlAVLFNPARNEAYV 288
Cdd:cd20718 93 VASIRigvnsrgiaLSDDGK---YVIAGNYEPGH-VVILDADTLEPLkVIPTTGVNDDGIIESRVG-AILETPPGPYFLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488996073 289 THRKAGEVSVID---GKSYKVVKTFKTPTHPNSLALSEDGKTLYVSVkQAS 336
Cdd:cd20718 168 ALKDAGSVWVIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVAS-QGS 217
|
|
| Lactonase |
pfam10282 |
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ... |
142-337 |
5.35e-03 |
|
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.
Pssm-ID: 431196 [Multi-domain] Cd Length: 340 Bit Score: 38.36 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 142 QPRELAVNEQTNTVY-ITGLGKESVIWVV----DGATLKLKTTITGTGAMATGLAIDPQAKRLYTTN------------A 204
Cdd:pfam10282 38 NPSYLALSPDGRTLYaVNEEGDQGGVAAFridpDSGALTLLNQVPTGGASPCHLSVDPDGRFLFVANyhggsvsvfpldA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 205 DGELLTIDSESNTIAS--RKKLQDDGKAHFylnLSLDTAGHRAFITDSKQPEVLV--VDTRDGKvLEKIAA--------P 272
Cdd:pfam10282 118 DGSLGELSQVVQHEGSgpPPERQESPHPHS---VDLTPDGKFLVVPDLGTDRVRVykLDAGGGK-LTPPASvqtppgsgP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488996073 273 ESLAvlFNPARNEAYVTHRKAGEVSV--IDGKSYKVVKTFKTPTHP------NSLA---LSEDGKTLYVSVKQASS 337
Cdd:pfam10282 194 RHLA--FHPNGKYAYVVNELSSTVTVfeYDPATGTFEELQTVSTLPegftgtNGAAairVSPDGKFLYVSNRGHDS 267
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
155-331 |
1.91e-20 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 88.98 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 155 VYITGLGKESVIWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNA-DGELLTIDSESNTIASRKKLQDDGKahfy 233
Cdd:COG3391 38 AAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSgSGRVSVIDLATGKVVATIPVGGGPR---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 234 lNLSLDTAGHRAFITDSKQPEVLVVDTRDGKVLEKIAAPESL-AVLFNPARNEAYVTHRKAGE----VSVIDGKSYKVVK 308
Cdd:COG3391 114 -GLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPhGIAVDPDGKRLYVANSGSNTvsviVSVIDTATGKVVA 192
|
170 180
....*....|....*....|...
gi 488996073 309 TFKTPTHPNSLALSEDGKTLYVS 331
Cdd:COG3391 193 TIPVGGGPVGVAVSPDGRRLYVA 215
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
62-303 |
5.78e-20 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 87.44 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 62 SRSLDKGGVVYRLDPTTLDVTQIIHNDLKPFGATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERqrsetvrpl 141
Cdd:COG3391 41 SGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGG--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 142 qPRELAVNEQTNTVYITGLGkESVIWVVDGATLKLKTTITgTGAMATGLAIDPQAKRLYTTNADgelltidseSNTIasr 221
Cdd:COG3391 112 -PRGLAVDPDGGRLYVADSG-NGRVSVIDTATGKVVATIP-VGAGPHGIAVDPDGKRLYVANSG---------SNTV--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 222 kklqddgkahfylnlsldtaghrAFItdskqpeVLVVDTRDGKVLEKIAAPES-LAVLFNPARNEAYVTHR-------KA 293
Cdd:COG3391 177 -----------------------SVI-------VSVIDTATGKVVATIPVGGGpVGVAVSPDGRRLYVANRgsntsngGS 226
|
250
....*....|
gi 488996073 294 GEVSVIDGKS 303
Cdd:COG3391 227 NTVSVIDLAT 236
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
38-219 |
3.16e-16 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 77.04 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 38 AVGKGAYEMAYSQQENALWVATSQSrsldkgGVVYRLDPTTLDVTQIIHNDLKPFGATINHATGTLWFGNTVDSTVTAID 117
Cdd:COG3391 65 AAVADADGADAGADGRRLYVANSGS------GRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 118 AKTGAVKGRLVLDErqrsetvrplQPRELAVNEQTNTVYITGLGKESV---IWVVDGATLKLKTTITgTGAMATGLAIDP 194
Cdd:COG3391 139 TATGKVVATIPVGA----------GPHGIAVDPDGKRLYVANSGSNTVsviVSVIDTATGKVVATIP-VGGGPVGVAVSP 207
|
170 180
....*....|....*....|....*
gi 488996073 195 QAKRLYTTNADGEllTIDSESNTIA 219
Cdd:COG3391 208 DGRRLYVANRGSN--TSNGGSNTVS 230
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
54-277 |
2.79e-12 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 66.20 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 54 ALWVAtsqsrsLDKGGVVYRLDPTTLDVTQIIHNDL-KPFGATINHAtGTLWFGNTVDSTVTAIDAKTGAVKgRLVLDER 132
Cdd:COG4257 29 AVWFT------DQGGGRIGRLDPATGEFTEYPLGGGsGPHGIAVDPD-GNLWFTDNGNNRIGRIDPKTGEIT-TFALPGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 133 QRsetvrplQPRELAVNEQTNtVYITGLGKeSVIWVVDGATLKLKT-TITGTGAMATGLAIDPQAKRLYTTNADGELLTI 211
Cdd:COG4257 101 GS-------NPHGIAFDPDGN-LWFTDQGG-NRIGRLDPATGEVTEfPLPTGGAGPYGIAVDPDGNLWVTDFGANAIGRI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488996073 212 DSESNTIaSRKKLQDDGKAHFYlnLSLDTAGhRAFITDSKQPEVLVVDTRDGKVLE-----KIAAPESLAV 277
Cdd:COG4257 172 DPDTGTL-TEYALPTPGAGPRG--LAVDPDG-NLWVADTGSGRIGRFDPKTGTVTEyplpgGGARPYGVAV 238
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
92-330 |
4.58e-11 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 63.14 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 92 FGATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERqrsetvrplqPRELAVNEQTNTVYITGlGKESVIWVVDG 171
Cdd:TIGR03866 2 LLAAGSAAAETAYVSNEKDNTISVIDTATLKVTRTFPVGQR----------PRGITFSKDGKLLYVCA-SDSDTIQVIDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 172 ATLKLKTTITgTGAMATGLAIDPQAKRLYTTNADGELLT-IDsesntIASRKKLQD--------------DGK------- 229
Cdd:TIGR03866 71 ATGEVLHTLP-SGPDPEQFALHPNGKILYIANEDDALVTvID-----IETRKVLAQidvgvepegmavspDGKivvntse 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 230 ----AHFylnlsLDTAGHRafITDSkqpevLVVDTRdgkvlekiaaPESLAvlFNPARNEAYVTHRKAGEVSVIDGKSYK 305
Cdd:TIGR03866 145 ttnmAHW-----IDTATYE--IVDN-----TLVDAR----------PRFAE--FTADGKELWVSSEIGGTVTVIDVATRK 200
|
250 260 270
....*....|....*....|....*....|...
gi 488996073 306 VVK--TFKTP-THPNSL-----ALSEDGKTLYV 330
Cdd:TIGR03866 201 VIKkiTFAIPgVHPEKVqpvgiKLTKDGKTAFV 233
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
67-289 |
1.26e-08 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 55.28 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 67 KGGVVYRLDPTTLDVTQIIHNDLKPFGATInHATGTLWFGNTvDSTVTAIDAKTGAVkgRLVLDERQRSETvrplQPREL 146
Cdd:COG3386 27 PGGRIHRYDPDGGAVEVFAEPSGRPNGLAF-DPDGRLLVADH-GRGLVRFDPADGEV--TVLADEYGKPLN----RPNDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 147 AVNEQtNTVYITGLGKES---VIWVVDgATLKLKTTITGTgAMATGLAIDPQAKRLYTTN-ADGELLTID-SESNTIASR 221
Cdd:COG3386 99 VVDPD-GRLYFTDMGEYLptgALYRVD-PDGSLRVLADGL-TFPNGIAFSPDGRTLYVADtGAGRIYRFDlDADGTLGNR 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488996073 222 KKLQDDGKAHFYL-NLSLDTAGHrAFITDSKQPEVLVVDtRDGKVLEKIAAPESL--AVLFN-PARNEAYVT 289
Cdd:COG3386 176 RVFADLPDGPGGPdGLAVDADGN-LWVALWGGGGVVRFD-PDGELLGRIELPERRptNVAFGgPDLRTLYVT 245
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
91-331 |
1.77e-07 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 51.94 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 91 PFGATINhATGTLWFGNTVDSTVTAIDAKTGAVKgrlvlderqRSETVRPLQPRELAVNEQtNTVYITGLGkESVIWVVD 170
Cdd:COG4257 19 PRDVAVD-PDGAVWFTDQGGGRIGRLDPATGEFT---------EYPLGGGSGPHGIAVDPD-GNLWFTDNG-NNRIGRID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 171 GATLKLKTTITGTGAMA-TGLAIDPQAkRLYTTNADGELLT-IDSESNTIASRKKLQDDGKAHfylNLSLDTAGhRAFIT 248
Cdd:COG4257 87 PKTGEITTFALPGGGSNpHGIAFDPDG-NLWFTDQGGNRIGrLDPATGEVTEFPLPTGGAGPY---GIAVDPDG-NLWVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 249 DSKQPEVLVVDTRDGKVLE-----KIAAPESLAVLfnpARNEAYVTHRKAGEVSVIDGKSyKVVKTFKTPT---HPNSLA 320
Cdd:COG4257 162 DFGANAIGRIDPDTGTLTEyalptPGAGPRGLAVD---PDGNLWVADTGSGRIGRFDPKT-GTVTEYPLPGggaRPYGVA 237
|
250
....*....|.
gi 488996073 321 LSEDGKtLYVS 331
Cdd:COG4257 238 VDGDGR-VWFA 247
|
|
| Pgl |
COG2706 |
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism]; |
95-331 |
2.91e-07 |
|
6-phosphogluconolactonase, cycloisomerase 2 family [Carbohydrate transport and metabolism];
Pssm-ID: 442025 [Multi-domain] Cd Length: 352 Bit Score: 51.45 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 95 TINHATGTLWFGNTVDST-----VTAIDAKTGAvkgrlvLDERQRSETVRplQPRELAVNEQTNTVYITGLGKESVIWV- 168
Cdd:COG2706 2 KRLLLSTFVYVGTYTSGEsegiyVFRLDTATGE------LTLLGLVAALG--NPSFLALSPDGRFLYAVNEVDDGGVSAf 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 169 -VDGAT--LKLKTTITGTGAMATGLAIDPQAKRLYTTN------------ADGELLTI-----DSESNTIASRkklQDDG 228
Cdd:COG2706 74 rIDPADgtLTLLNTVSSGGASPCHLSVDPDGRFLFVANygggsvsvfpidADGSLGEPvqviqHEGSGPNPER---QEGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 229 KAHFylnLSLDTAGHRAFITDSKQPEVLV--VDTRDGK-------VLEKIAAPESLAvlFNPARNEAYVTHRKAGEVSV- 298
Cdd:COG2706 151 HAHS---VVFDPDGRFLYVPDLGTDRIYVyrLDPATGKlpeppevSLPPGSGPRHLA--FHPNGRFAYVINELDSTVSVy 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488996073 299 -IDGKSYKVVKTFKTPTHPNS---------LALSEDGKTLYVS 331
Cdd:COG2706 226 aYDAATGTLTLIQTVSTLPEDftgenwaadIHISPDGRFLYVS 268
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
146-331 |
6.63e-07 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 50.42 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 146 LAVNEQTNTVYITgLGKESVIWVVDGATLKLKTTITgTGAMATGLAIDPQAKRLYTTNADGELL-TIDSESNTIasRKKL 224
Cdd:TIGR03866 4 AAGSAAAETAYVS-NEKDNTISVIDTATLKVTRTFP-VGQRPRGITFSKDGKLLYVCASDSDTIqVIDPATGEV--LHTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 225 QDDGKAHFYlnlSLDTAGHRAFITDSKQPEVLVVDTRDGKVLEKI---AAPESLAVlfNPARNEAYVTHRKAGEVSVIDG 301
Cdd:TIGR03866 80 PSGPDPEQF---ALHPNGKILYIANEDDALVTVIDIETRKVLAQIdvgVEPEGMAV--SPDGKIVVNTSETTNMAHWIDT 154
|
170 180 190
....*....|....*....|....*....|
gi 488996073 302 KSYKVVKTFKTPTHPNSLALSEDGKTLYVS 331
Cdd:TIGR03866 155 ATYEIVDNTLVDARPRFAEFTADGKELWVS 184
|
|
| PQQ_ABC_repeats |
TIGR03866 |
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ... |
83-225 |
5.93e-06 |
|
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.
Pssm-ID: 274824 [Multi-domain] Cd Length: 310 Bit Score: 47.34 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 83 QIIHN---DLKPFGATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERqrseTVRP--LQPRELAVNEQTNTVYI 157
Cdd:TIGR03866 158 EIVDNtlvDARPRFAEFTADGKELWVSSEIGGTVTVIDVATRKVIKKITFAIP----GVHPekVQPVGIKLTKDGKTAFV 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488996073 158 tGLGKESVIWVVDGATLKLKTTITgTGAMATGLAIDPQAKRLYTTNA-DGELLTIDsesntIASRKKLQ 225
Cdd:TIGR03866 234 -ALGPANRVAVVDAKTYEVLDYLL-VGQRVWQLAFTPDESRLLTTNGvSNDVSVID-----VAALKVIK 295
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
139-336 |
1.08e-05 |
|
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.
Pssm-ID: 467720 [Multi-domain] Cd Length: 380 Bit Score: 46.95 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 139 RPLQPRELAVNEQTNTVYITGLGKESViWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDSESNTI 218
Cdd:cd20718 14 RELPPVAYGIWDLENLMVVVERDAGSV-LVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYVISRDGWLTKIDLYTLRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 219 ASRKK---------LQDDGKahfYLNLSLDTAGHrAFITDSKQPEVL-VVDTRDGKVLEKIAAPESlAVLFNPARNEAYV 288
Cdd:cd20718 93 VASIRigvnsrgiaLSDDGK---YVIAGNYEPGH-VVILDADTLEPLkVIPTTGVNDDGIIESRVG-AILETPPGPYFLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488996073 289 THRKAGEVSVID---GKSYKVVKTFKTPTHPNSLALSEDGKTLYVSVkQAS 336
Cdd:cd20718 168 ALKDAGSVWVIDysdPDGNKVTDIGNIGRPLHDAFLDPDGRYFIVAS-QGS 217
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
142-331 |
2.31e-05 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 45.40 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 142 QPRELAVNEQtNTVYITGLGKeSVIWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDSESNTIaSR 221
Cdd:COG4257 18 GPRDVAVDPD-GAVWFTDQGG-GRIGRLDPATGEFTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGEI-TT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 222 KKLQDDGKAHFYlnLSLDTAGhRAFITDSKQPEVLVVDTRDGKVLE-----KIAAPESLAVlfnPARNEAYVTHRKAGEV 296
Cdd:COG4257 95 FALPGGGSNPHG--IAFDPDG-NLWFTDQGGNRIGRLDPATGEVTEfplptGGAGPYGIAV---DPDGNLWVTDFGANAI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 488996073 297 SVIDGKSyKVVKTFKTPT---HPNSLALSEDGkTLYVS 331
Cdd:COG4257 169 GRIDPDT-GTLTEYALPTpgaGPRGLAVDPDG-NLWVA 204
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
40-124 |
5.88e-05 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 44.24 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 40 GKGAYEMAYSQQeNALWVATSQsrsldkGGVVYRLDPTTLDVTQI-IHNDLK-PFGATINHAtGTLWFGNTVDSTVTAID 117
Cdd:COG4257 144 GAGPYGIAVDPD-GNLWVTDFG------ANAIGRIDPDTGTLTEYaLPTPGAgPRGLAVDPD-GNLWVADTGSGRIGRFD 215
|
....*..
gi 488996073 118 AKTGAVK 124
Cdd:COG4257 216 PKTGTVT 222
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
234-330 |
1.42e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 42.96 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 234 LNLSLDTAGhRAFITDSKQPEVLVVDtRDGKVLEKIAA------PESLAVlfNPARNEAYVTHRKAGEVSVIDGKSyKVV 307
Cdd:cd14962 60 IGVAIDANG-NLYVSDAELGKVFVFD-RDGKFLRAIGAgalfkrPTGIAV--DPAGKRLYVVDTLAHKVKVFDLDG-RLL 134
|
90 100 110
....*....|....*....|....*....|
gi 488996073 308 KTFKTP-------THPNSLALSEDGKtLYV 330
Cdd:cd14962 135 FDIGKRgsgpgefNLPTDLAVDRDGN-LYV 163
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
156-314 |
2.32e-04 |
|
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.
Pssm-ID: 467720 [Multi-domain] Cd Length: 380 Bit Score: 42.71 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 156 YITGLGKESVIWVVDGATLKLKTTITgTGAM---ATGlAIDPQAKRLYTTNADGELLT-IDSESNTIAsrKKLQDDGKAH 231
Cdd:cd20718 210 FIVASQGSNTMWVLDLKTGKVVARIP-TGKTphpGPG-ATWGRKGVTATPHLGEGIVTvWDLDTWKPV--KYIPTPGPGR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 232 FYLN------LSLDTAGHrafitDSKQPEVLVVDTRDGKVLEKIA---APESLAVLFNPARNEAYVTHRKAGEVSVIDGK 302
Cdd:cd20718 286 FVRThpsspyVWADTVFG-----PENADEIYVIDKETLKVVKTLIpkpGKRALHPEFTRDGKYVYVSVWDGGEVVVYDAE 360
|
170
....*....|....
gi 488996073 303 SYKVVKTFK--TPT 314
Cdd:cd20718 361 TLELVKRIPaeTPT 374
|
|
| 8prop_heme_binding_protein |
cd20718 |
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ... |
168-318 |
2.53e-04 |
|
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.
Pssm-ID: 467720 [Multi-domain] Cd Length: 380 Bit Score: 42.71 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 168 VVDGATLKLKTTITGTGA---------MATGLAIDPQAKRLYTTNADGELLTID-SESNTiasrKKLQDDGKAHFYLNLS 237
Cdd:cd20718 126 ILDADTLEPLKVIPTTGVnddgiiesrVGAILETPPGPYFLVALKDAGSVWVIDySDPDG----NKVTDIGNIGRPLHDA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 238 LDTAGHRAFITDSKQPEVL-VVDTRDGKVLEKIAA-----PESLAVLFNpaRNEAYVTHRKAGEVSVIDGKSYKVVKTFK 311
Cdd:cd20718 202 FLDPDGRYFIVASQGSNTMwVLDLKTGKVVARIPTgktphPGPGATWGR--KGVTATPHLGEGIVTVWDLDTWKPVKYIP 279
|
170
....*....|....
gi 488996073 312 TP-------THPNS 318
Cdd:cd20718 280 TPgpgrfvrTHPSS 293
|
|
| 8prop_hemeD1_NirF |
cd20778 |
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ... |
241-332 |
3.62e-04 |
|
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.
Pssm-ID: 467722 [Multi-domain] Cd Length: 381 Bit Score: 41.89 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 241 AGHRAFITDSKQPEVLVVDTRDGKVLEKIA-APESLAVLFNPARNEAYVT--HRKAGEVSVIDGKSYKVVKTFKTP---T 314
Cdd:cd20778 249 AGDKAFVPAVGEHRVLVYDTNDWKFIKSIPlAGQPVFAVARPDGRYVWVNfsGPDNDTVQVIDTKTLKVVKTLEPGkrvL 328
|
90
....*....|....*...
gi 488996073 315 HpnsLALSEDGKTLYVSV 332
Cdd:cd20778 329 H---MEFTPRGEAVYISV 343
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
186-331 |
5.78e-04 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 41.03 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 186 MATGLAIDPqAKRLYTTN-ADGELLTIDSESNTIASRkkLQDDGKAHFylnLSLDTAGhRAFITDSKqPEVLVVDTRDGK 264
Cdd:COG3386 9 LGEGPVWDP-DGRLYWVDiPGGRIHRYDPDGGAVEVF--AEPSGRPNG---LAFDPDG-RLLVADHG-RGLVRFDPADGE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488996073 265 VlEKIAAPESLA------VLFNPARNeAYVT----HRKAGEVSVI--DGKSYKVVKTFktpTHPNSLALSEDGKTLYVS 331
Cdd:COG3386 81 V-TVLADEYGKPlnrpndGVVDPDGR-LYFTdmgeYLPTGALYRVdpDGSLRVLADGL---TFPNGIAFSPDGRTLYVA 154
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
166-331 |
1.85e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 39.89 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 166 IWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDSESNTIasRKKLQDDGKAHFYLNLSLDtaGHRa 245
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL--LRTLTGHSGSVRSVAFSPD--GRL- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 246 FITDSKQPEVLVVDTRDGKVLEKIAAPES--LAVLFNPaRNEAYVTHRKAGEVSVIDGKSYKVVKTFKTPTHP-NSLALS 322
Cdd:COG2319 261 LASGSADGTVRLWDLATGELLRTLTGHSGgvNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAvRSVAFS 339
|
....*....
gi 488996073 323 EDGKTLYVS 331
Cdd:COG2319 340 PDGKTLASG 348
|
|
| beta_rpt_yvtn |
TIGR02276 |
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in ... |
281-322 |
3.53e-03 |
|
40-residue YVTN family beta-propeller repeat; This repeat of about 40 amino acids is found in up to 14 copies per protein. Archaea Methanosarcina mazei and Methanosarcina acetivorans each have over 10 genes that encode tandem copies of this repeat, which is also found in other species. PSIPRED predicts with high confidence that each 40-residue repeats contains four beta strands. This model overlaps somewhat with the NHL repeat (pfam01436) and also shows sequence similarity to the WD domain, G-beta repeat (pfam00400).
Pssm-ID: 213697 [Multi-domain] Cd Length: 42 Bit Score: 34.96 E-value: 3.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488996073 281 PARNEAYVTHRKAGEVSVIDGKSYKVVKTFKTPTHPNSLALS 322
Cdd:TIGR02276 1 PDGTKLYVTNSGSNTVSVIDTATNKVIATIPVGGYPFGVAVS 42
|
|
| Lactonase |
pfam10282 |
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases ... |
142-337 |
5.35e-03 |
|
Lactonase, 7-bladed beta-propeller; This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyse 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.
Pssm-ID: 431196 [Multi-domain] Cd Length: 340 Bit Score: 38.36 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 142 QPRELAVNEQTNTVY-ITGLGKESVIWVV----DGATLKLKTTITGTGAMATGLAIDPQAKRLYTTN------------A 204
Cdd:pfam10282 38 NPSYLALSPDGRTLYaVNEEGDQGGVAAFridpDSGALTLLNQVPTGGASPCHLSVDPDGRFLFVANyhggsvsvfpldA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 205 DGELLTIDSESNTIAS--RKKLQDDGKAHFylnLSLDTAGHRAFITDSKQPEVLV--VDTRDGKvLEKIAA--------P 272
Cdd:pfam10282 118 DGSLGELSQVVQHEGSgpPPERQESPHPHS---VDLTPDGKFLVVPDLGTDRVRVykLDAGGGK-LTPPASvqtppgsgP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488996073 273 ESLAvlFNPARNEAYVTHRKAGEVSV--IDGKSYKVVKTFKTPTHP------NSLA---LSEDGKTLYVSVKQASS 337
Cdd:pfam10282 194 RHLA--FHPNGKYAYVVNELSSTVTVfeYDPATGTFEELQTVSTLPegftgtNGAAairVSPDGKFLYVSNRGHDS 267
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
94-328 |
5.71e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 38.35 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 94 ATINHATGTLWFGNTVDSTVTAIDAKTGAVKGRLVLDERQRSETVRPLQPRELAVNEQTNTVYITGLGKESVIWVVDGAT 173
Cdd:COG2319 30 LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLAT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 174 LKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDsesntIASRKKLQD-DGKAHFYLNLSLDTAGHRaFITDSKQ 252
Cdd:COG2319 110 GLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWD-----LATGKLLRTlTGHSGAVTSVAFSPDGKL-LASGSDD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488996073 253 PEVLVVDTRDGKVLEKIAAPES--LAVLFNPaRNEAYVTHRKAGEVSVIDGKSYKVVKTFKTPTHP-NSLALSEDGKTL 328
Cdd:COG2319 184 GTVRLWDLATGKLLRTLTGHTGavRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSvRSVAFSPDGRLL 261
|
|
| COG5276 |
COG5276 |
Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function ... |
153-331 |
8.08e-03 |
|
Uncharacterized secreted protein, contains LVIVD repeats, choice-of-anchor domain [Function unknown];
Pssm-ID: 444087 [Multi-domain] Cd Length: 320 Bit Score: 37.61 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 153 NTVYITGLGKESVIW--VVDGATLKLKTTITGTGAMATGLAIDPqaKRLYTT-NADGELLTID---SESNTIASRKKLQD 226
Cdd:COG5276 73 DYLYVASEGSEGLQIfdISDPANPKLVGRYDTGGSGAHNIAVDG--NYAYVAgGSDNGLVIVDisdPTNPVLVGRYSLPG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 227 DGKAHfylnlSLDTAGHRAFITDsKQPEVLVVDTRDgkvlekIAAPESL------------AVLFNPARNEAYVTHRKAG 294
Cdd:COG5276 151 QAYLH-----DVQVVGDYAYVAD-WEDGLVIVDVSD------PSNPKLIgsydysppgythTAVPVEDGNYAYVGDELGG 218
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488996073 295 E-----VSVIDGKSYKVVKTFKTPTHPNSLALSEDGKTLYVS 331
Cdd:COG5276 219 PnglriLDVSDPANPVLIGTYPTPGADGAHNLYVSGNYLYVA 260
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
166-328 |
9.34e-03 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 37.58 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 166 IWVVDGATLKLKTTITGTGAMATGLAIDPQAKRLYTTNADGELLTIDSESNTIasRKKLQDDGKAHFYLNLSLDtaGHRa 245
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLTGHSGGVNSVAFSPD--GKL- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488996073 246 FITDSKQPEVLVVDTRDGKVLEKIAAPES--LAVLFNPARNEAYVTHRKaGEVSVIDGKSYKVVKTFKTPTHP-NSLALS 322
Cdd:COG2319 303 LASGSDDGTVRLWDLATGKLLRTLTGHTGavRSVAFSPDGKTLASGSDD-GTVRLWDLATGELLRTLTGHTGAvTSVAFS 381
|
....*.
gi 488996073 323 EDGKTL 328
Cdd:COG2319 382 PDGRTL 387
|
|
|