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Conserved domains on  [gi|16129976|ref|NP_416540|]
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UDP-galactopyranose mutase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

UDP-galactopyranose mutase( domain architecture ID 11426203)

UDP-galactopyranose mutase converts uridine diphosphogalactopyranose (UDP-GalP) to uridine diphosphogalactofuranose (UDP-GalF)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glf COG0562
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
1-363 0e+00

UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 623.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANEL-KKLNKKVLVIEKRNHIGGNAYTE-DCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRF 78
Cdd:COG0562   2 MYDYLIVGAGFFGAVFAERLaEELGKKVLVIDKRDHIGGNAYDEyDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  79 TNSPLAIYKDKLFNLPFNMNTFHQMWGVK-DPQEAQNIINAQKKkyGDKVPENLEEQAISLVGEDLYQALIKGYTEKQWG 157
Cdd:COG0562  82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 158 RSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEG--VDVKLGIDFLKDKDslASKAHRIIYTGPIDQ 235
Cdd:COG0562 160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHpnIEVRLNTDFFEVRD--EIPADHVVYTGPIDE 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 236 YFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGDEPYYPVND 315
Cdd:COG0562 238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 16129976 316 NKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNI 363
Cdd:COG0562 318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
 
Name Accession Description Interval E-value
Glf COG0562
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
1-363 0e+00

UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 623.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANEL-KKLNKKVLVIEKRNHIGGNAYTE-DCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRF 78
Cdd:COG0562   2 MYDYLIVGAGFFGAVFAERLaEELGKKVLVIDKRDHIGGNAYDEyDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  79 TNSPLAIYKDKLFNLPFNMNTFHQMWGVK-DPQEAQNIINAQKKkyGDKVPENLEEQAISLVGEDLYQALIKGYTEKQWG 157
Cdd:COG0562  82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 158 RSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEG--VDVKLGIDFLKDKDslASKAHRIIYTGPIDQ 235
Cdd:COG0562 160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHpnIEVRLNTDFFEVRD--EIPADHVVYTGPIDE 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 236 YFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGDEPYYPVND 315
Cdd:COG0562 238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 16129976 316 NKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNI 363
Cdd:COG0562 318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
UDP-GALP_mutase TIGR00031
UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into ...
 1-365 0e+00

UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into UDP-GALF through a 2-keto intermediate. It contains FAD as a cofactor. The gene is known as glf, ceoA, and rfbD. It is known experimentally in E. coli, Mycobacterium tuberculosis, and Klebsiella pneumoniae. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 272864 [Multi-domain]  Cd Length: 377  Bit Score: 567.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976     1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRFTN 80
Cdd:TIGR00031   1 MFDYIIVGAGLSGIVLANILAQLNKRVLVVEKRNHIGGNCYDEVDETILFHQYGPHIFHTNNQYVWDYISPFFELNNYQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    81 SPLAIYKDKLFNLPFNMNTFHQMWGVKDPQEAQNIINAQkKKYGDKVP-ENLEEQA---ISLVGEDLYQALIKGYTEKQW 156
Cdd:TIGR00031  81 RVLALYNNLDLTLPFNFNQFRKLLGVKDAQELQNFFNAQ-FKYGDHVPlEELQEIAdpdIQLLYQFLYQKVYKPYTVKQW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   157 GRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEG--VDVKLG--IDFLKDKDS---LASKAHR--I 227
Cdd:TIGR00031 160 GLPAEEIDPFVIGRVPVVLSEDSSYFPDRYQGLPKGGYTKLFEKMLDHplIDVKLNchINLLKDKDSqlhFANKAIRkpV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   228 IYTGPIDQYFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTdANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGD 307
Cdd:TIGR00031 240 IYTGLIDQLFGYRFGALQYRSLKFEWERHEFKNFQGYAVVNFP-LNVPITRIVEYKHLTYVGSKQTIVSKEYPGEWKVGD 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129976   308 -EPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNIMS 365
Cdd:TIGR00031 319 pEPYYPVNDNKNMALFKKYLELASREDNLILLGRLAEYQYYDMDQAILAALYKAEQLLS 377
GLF pfam03275
UDP-galactopyranose mutase;
146-346 2.71e-117

UDP-galactopyranose mutase;


Pssm-ID: 427229  Cd Length: 203  Bit Score: 338.36  E-value: 2.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   146 ALIKGYTEKQWGRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKML--EGVDVKLGIDFLKDKDSLASK 223
Cdd:pfam03275   1 KFFKGYTEKQWGLDPEELPASVIKRLPVRFNYDNRYFNDTYQGLPKDGYTKMFENMLdhPNIEVRLNTDFFDIRDNDVEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   224 AHRIIYTGPIDQYFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEW 303
Cdd:pfam03275  81 ADPVVYTGPIDEYFDYCFGELPYRSLDFETETLDQGDFQGNAVVNYPDDEVPYTRITEYKHFTPQKHDKTVITREYPRAW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 16129976   304 KVGDEPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKY 346
Cdd:pfam03275 161 EEGDEPYYPINTEENRALYEKYRELAKKEPNVTFGGRLGTYRY 203
PRK07233 PRK07233
hypothetical protein; Provisional
 6-325 1.41e-08

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 56.05  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    6 IVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKYGAHIFhTNDKYIWDYVNDL-----VEFNRFT- 79
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPIERFYHHIF-KSDEALLELLDELgledkLRWRETKt 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   80 -----------NSPLAIYKDKLFNL----PFNMNTFHQmwgvkdpqeaqniinaqkKKYGDKVP-ENL--EEQAISLVGE 141
Cdd:PRK07233  83 gyyvdgklyplGTPLELLRFPHLSLidkfRLGLLTLLA------------------RRIKDWRAlDKVpaEEWLRRWSGE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  142 DLYQALIKGYTEKQWGRSAKELPA-FIIKRIPVRFTFDNNYFSDRYqGIPVGGYTKLIEKMLE-----GVDVKLGI---D 212
Cdd:PRK07233 145 GVYEVFWEPLLESKFGDYADDVSAaWLWSRIKRRGNRRYSLFGEKL-GYLEGGFATLIDALAEaiearGGEIRLGTpvtS 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  213 FLKDKDSLAS--------KAHRIIYTGPIdQYFDYRFGALeyrsLKFETERHEFPNFQGNAV--------------INFT 270
Cdd:PRK07233 224 VVIDGGGVTGvevdgeeeDFDAVISTAPP-PILARLVPDL----PADVLARLRRIDYQGVVCmvlklrrpltdyywLNIN 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129976  271 DANVPYTRIIEHKHF---DYVETKHTV-VTKEYPlewkvGDEPYYPVNDNKNMELFKKY 325
Cdd:PRK07233 299 DPGAPFGGVIEHTNLvppERYGGEHLVyLPKYLP-----GDHPLWQMSDEELLDRFLSY 352
 
Name Accession Description Interval E-value
Glf COG0562
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
1-363 0e+00

UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 623.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANEL-KKLNKKVLVIEKRNHIGGNAYTE-DCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRF 78
Cdd:COG0562   2 MYDYLIVGAGFFGAVFAERLaEELGKKVLVIDKRDHIGGNAYDEyDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  79 TNSPLAIYKDKLFNLPFNMNTFHQMWGVK-DPQEAQNIINAQKKkyGDKVPENLEEQAISLVGEDLYQALIKGYTEKQWG 157
Cdd:COG0562  82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 158 RSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEG--VDVKLGIDFLKDKDslASKAHRIIYTGPIDQ 235
Cdd:COG0562 160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHpnIEVRLNTDFFEVRD--EIPADHVVYTGPIDE 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 236 YFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGDEPYYPVND 315
Cdd:COG0562 238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 16129976 316 NKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNI 363
Cdd:COG0562 318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
UDP-GALP_mutase TIGR00031
UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into ...
 1-365 0e+00

UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into UDP-GALF through a 2-keto intermediate. It contains FAD as a cofactor. The gene is known as glf, ceoA, and rfbD. It is known experimentally in E. coli, Mycobacterium tuberculosis, and Klebsiella pneumoniae. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 272864 [Multi-domain]  Cd Length: 377  Bit Score: 567.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976     1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRFTN 80
Cdd:TIGR00031   1 MFDYIIVGAGLSGIVLANILAQLNKRVLVVEKRNHIGGNCYDEVDETILFHQYGPHIFHTNNQYVWDYISPFFELNNYQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    81 SPLAIYKDKLFNLPFNMNTFHQMWGVKDPQEAQNIINAQkKKYGDKVP-ENLEEQA---ISLVGEDLYQALIKGYTEKQW 156
Cdd:TIGR00031  81 RVLALYNNLDLTLPFNFNQFRKLLGVKDAQELQNFFNAQ-FKYGDHVPlEELQEIAdpdIQLLYQFLYQKVYKPYTVKQW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   157 GRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEG--VDVKLG--IDFLKDKDS---LASKAHR--I 227
Cdd:TIGR00031 160 GLPAEEIDPFVIGRVPVVLSEDSSYFPDRYQGLPKGGYTKLFEKMLDHplIDVKLNchINLLKDKDSqlhFANKAIRkpV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   228 IYTGPIDQYFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTdANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGD 307
Cdd:TIGR00031 240 IYTGLIDQLFGYRFGALQYRSLKFEWERHEFKNFQGYAVVNFP-LNVPITRIVEYKHLTYVGSKQTIVSKEYPGEWKVGD 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129976   308 -EPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNIMS 365
Cdd:TIGR00031 319 pEPYYPVNDNKNMALFKKYLELASREDNLILLGRLAEYQYYDMDQAILAALYKAEQLLS 377
GLF pfam03275
UDP-galactopyranose mutase;
146-346 2.71e-117

UDP-galactopyranose mutase;


Pssm-ID: 427229  Cd Length: 203  Bit Score: 338.36  E-value: 2.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   146 ALIKGYTEKQWGRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKML--EGVDVKLGIDFLKDKDSLASK 223
Cdd:pfam03275   1 KFFKGYTEKQWGLDPEELPASVIKRLPVRFNYDNRYFNDTYQGLPKDGYTKMFENMLdhPNIEVRLNTDFFDIRDNDVEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   224 AHRIIYTGPIDQYFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEW 303
Cdd:pfam03275  81 ADPVVYTGPIDEYFDYCFGELPYRSLDFETETLDQGDFQGNAVVNYPDDEVPYTRITEYKHFTPQKHDKTVITREYPRAW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 16129976   304 KVGDEPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKY 346
Cdd:pfam03275 161 EEGDEPYYPINTEENRALYEKYRELAKKEPNVTFGGRLGTYRY 203
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
6-72 3.96e-22

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 88.36  E-value: 3.96e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129976     6 IVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIqIHKYGAHIFHT-NDKYIWDYVNDL 72
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGY-VFDYGAHIFHGsDEPNVRDLLDEL 67
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-315 6.01e-17

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 81.80  E-value: 6.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIhKYGAHIFHTNDKYIWDYVNDLV---EFnR 77
Cdd:COG1232   1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRI-DRGPHSFLTRDPEVLELLRELGlgdEL-V 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  78 FTNSPLA-IYKD-KLFNLPFNMNTF--HQMWGVKDPQEA-QNIINAQKKKYGDkvpENLEEQAISLVGEDLYQALIKGYT 152
Cdd:COG1232  79 WPNTRKSyIYYGgKLHPLPQGPLALlrSPLLSLAGKLRAlLELLAPRRPPGED---ESLAEFVRRRFGREVYERLVEPLL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 153 EKQWGRSAKELPA-FIIKRIP------------VRFTFDNNYFSDRYQGiPVGGYTKLIEKM---LEGVDVKLG-----I 211
Cdd:COG1232 156 EGVYAGDPDELSAdWAFPRLKrlelehgslikgALALRKGAKAGEVFGY-LRGGLGTLVEALaeaLEAGEIRLGtrvtaI 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976 212 DFLKDKDSL------------------ASKAHRIIytGPIDQYFDYRFGALEYRS-----LKFetERHEFPNFQGNAVIN 268
Cdd:COG1232 235 EREGGGWRVttsdgetieadavvsatpAPALARLL--APLPPEVAAALAGIPYASvavvaLGF--DRPDLPPPDGFGWLV 310

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 16129976 269 FTDANVPYTRIIEHKH-FDYVETK-HTVVTKEYPlewKVGDEPYYPVND 315
Cdd:COG1232 311 PRDEGVPILAVTFSSNkWPHRAPDgKVLLRLEVG---GAGDPELWQLSD 356
PRK07233 PRK07233
hypothetical protein; Provisional
 6-325 1.41e-08

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 56.05  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    6 IVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKYGAHIFhTNDKYIWDYVNDL-----VEFNRFT- 79
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPIERFYHHIF-KSDEALLELLDELgledkLRWRETKt 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   80 -----------NSPLAIYKDKLFNL----PFNMNTFHQmwgvkdpqeaqniinaqkKKYGDKVP-ENL--EEQAISLVGE 141
Cdd:PRK07233  83 gyyvdgklyplGTPLELLRFPHLSLidkfRLGLLTLLA------------------RRIKDWRAlDKVpaEEWLRRWSGE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  142 DLYQALIKGYTEKQWGRSAKELPA-FIIKRIPVRFTFDNNYFSDRYqGIPVGGYTKLIEKMLE-----GVDVKLGI---D 212
Cdd:PRK07233 145 GVYEVFWEPLLESKFGDYADDVSAaWLWSRIKRRGNRRYSLFGEKL-GYLEGGFATLIDALAEaiearGGEIRLGTpvtS 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  213 FLKDKDSLAS--------KAHRIIYTGPIdQYFDYRFGALeyrsLKFETERHEFPNFQGNAV--------------INFT 270
Cdd:PRK07233 224 VVIDGGGVTGvevdgeeeDFDAVISTAPP-PILARLVPDL----PADVLARLRRIDYQGVVCmvlklrrpltdyywLNIN 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129976  271 DANVPYTRIIEHKHF---DYVETKHTV-VTKEYPlewkvGDEPYYPVNDNKNMELFKKY 325
Cdd:PRK07233 299 DPGAPFGGVIEHTNLvppERYGGEHLVyLPKYLP-----GDHPLWQMSDEELLDRFLSY 352
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-58 1.83e-08

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 56.01  E-value: 1.83e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIqIHKYGAHIF 58
Cdd:COG1233   3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGF-RFDVGPSVL 59
PRK07208 PRK07208
hypothetical protein; Provisional
 5-165 1.86e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 55.67  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    5 IIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIhKYGAHIFHTNDKYIWDYVNDLV---EF------ 75
Cdd:PRK07208   8 VIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGNRF-DIGGHRFFSKSPEVMDLWNEILpddDFllrprl 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   76 ------NRFTNSPLAIYkDKLFNLPFNMNT---FHQMWgvkdpqeaqniinAQKKKYGDkvPENLEEQAISLVGEDLYQA 146
Cdd:PRK07208  87 sriyyrGKFFDYPLKAF-DALKNLGLWRTAkcgASYLK-------------ARLRPRKE--EDSFEDWVINRFGRRLYST 150

                        170
                 ....*....|....*....
gi 16129976  147 LIKGYTEKQWGRSAKELPA 165
Cdd:PRK07208 151 FFKGYTEKVWGVPCDEISA 169
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-210 3.11e-08

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 54.93  E-value: 3.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTE--DCEGIQIhKYGAHIFHTNDKYIWDYVN----DLVE 74
Cdd:COG1231   7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLrfGDDGLYA-ELGAMRIPPSHTNLLALARelglPLEP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976  75 FNRFTNSPLAIYKDKLFN---LPFNMNTFHQMWG--VKDPQEAQNIINAQKKKYgDKVP--ENLEEQAISLVGEDLYQAL 147
Cdd:COG1231  86 FPNENGNALLYLGGKRVRageIAADLRGVAELLAklLRALAAALDPWAHPAAEL-DRESlaEWLRRNGASPSARRLLGLL 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129976 148 IKGYTEKQWGR-SAKELpafiikripVRFTFDNNYFSDRYQgiPVGGYTKLIEKMLEGV--DVKLG 210
Cdd:COG1231 165 GAGEYGADPDElSLLDL---------LRYAASAGGGAQQFR--IVGGMDQLPRALAAELgdRIRLG 219
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 9-234 5.73e-08

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 54.03  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976     9 SGLfgaVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKyGAHIFHTNDKYIWDYVNDL-----------VEFNR 77
Cdd:pfam01593   2 AGL---AAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIEL-GAMWFHGAQPPLLALLKELgledrlvlpdpAPFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976    78 FTNSPLAIYKDKLFNLPFNMNTFHQMWGVKD-PQEAQNIINAQKKKYGDKVP---ENLEEQAISLVGEDLYQALIKGYTE 153
Cdd:pfam01593  78 VLFAGGRRYPGDFRRVPAGWEGLLEFGRLLSiPEKLRLGLAALASDALDEFDlddFSLAESLLFLGRRGPGDVEVWDRLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   154 KQWGRSAKELPAFIIKRIPVRFT-----FDNNYFSDRYQGI--PVGGYTKLIEKMLE---GVDVKLG-----IDFLKDKD 218
Cdd:pfam01593 158 DPELFAALPFASGAFAGDPSELSaglalPLLWALLGEGGSLllPRGGLGALPDALAAqllGGDVRLNtrvrsIDREGDGV 237

                         250       260
                  ....*....|....*....|..
gi 16129976   219 SLASK------AHRIIYTGPID 234
Cdd:pfam01593 238 TVTLTdgevieADAVIVTVPLG 259
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 2-41 2.58e-05

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 46.04  E-value: 2.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 16129976    2 YDYIIVGSGLFGAVCANELKKLNKKVLVI--EKRNHIGGNAY 41
Cdd:PRK12834   5 ADVIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGGQAF 46
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-40 3.21e-05

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 45.28  E-value: 3.21e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEkRNHIGGNA 40
Cdd:COG0665   2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSGA 40
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-37 4.46e-05

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 45.14  E-value: 4.46e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKL-NKKVLVIEKRNHIG 37
Cdd:COG0579   4 MYDVVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-45 9.15e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 44.01  E-value: 9.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16129976    1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHiGGNAYTEDC 45
Cdd:PRK06292   3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPL-GGTCLNVGC 46
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
2-39 1.12e-04

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 43.99  E-value: 1.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 16129976    2 YDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGN 39
Cdd:PRK05249   6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGG 43
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-39 1.18e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 43.67  E-value: 1.18e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGN 39
Cdd:COG1053   3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 3-40 2.17e-04

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 42.77  E-value: 2.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 16129976     3 DYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNA 40
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-68 2.23e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 42.89  E-value: 2.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976   1 MYDYIIVGSGLFGAVCANEL-KKLNKKVLVIEKrnhiGGNAYTEdcegiQIHKYGAHIF-HTNDKYIWDY 68
Cdd:COG2303   4 EYDYVIVGAGSAGCVLANRLsEDAGLRVLLLEA----GGRDDDP-----LIRMPAGYAKlLGNPRYDWRY 64
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
2-41 2.32e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 42.86  E-value: 2.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16129976   2 YDYIIVGSGLFGAVCANELKKLNKKVLVI--EKRNHIGGNAY 41
Cdd:COG3573   6 ADVIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGGQAF 47
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-38 2.58e-04

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 42.77  E-value: 2.58e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 16129976   1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRnHIGG 38
Cdd:COG1249   3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGG 39
PLN03000 PLN03000
amine oxidase
 5-47 1.14e-03

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 41.16  E-value: 1.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 16129976    5 IIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEG 47
Cdd:PLN03000 188 VIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEA 230
PLN02529 PLN02529
lysine-specific histone demethylase 1
 5-43 1.47e-03

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 40.64  E-value: 1.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 16129976    5 IIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTE 43
Cdd:PLN02529 164 IIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQ 202
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-58 1.56e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.99  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129976     2 YDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHI--GGNAYTEDCEGIQIHKYGAHIF 58
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpyGGCVLSKALLGAAEAPEIASLW 59
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 2-72 1.64e-03

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 40.22  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129976     2 YDYIIVGSGLFGAVCANELKKLNKKVLVIE--------KRNHIGGNAYTEDCEGIQIHKYGAH---IFHTNDKYIWDYVN 70
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgTRWGIGGTCVNVGCIPKKLMHQAALlgqALKDSRNYGWKVEE 82


                  ..
gi 16129976    71 DL 72
Cdd:TIGR01438  83 TV 84
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 3-40 2.66e-03

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 39.51  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16129976     3 DYIIVGSGLFG---AVCAnelKKLNKKVLVIEKRNHIGGNA 40
Cdd:pfam12831   1 DVVVVGGGPAGvaaAIAA---ARAGAKVLLVERRGFLGGML 38
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 2-32 2.88e-03

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 39.45  E-value: 2.88e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 16129976    2 YDYIIVGSGLFGAVCANELKKLNKKVLVIEK 32
Cdd:PTZ00367  34 YDVIIVGGSIAGPVLAKALSKQGRKVLMLER 64
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-36 3.09e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 36.03  E-value: 3.09e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 16129976     5 IIVGSGLFGAVCANELKKLNKKVLVIEKRNHI 36
Cdd:pfam00070   3 VVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 1-42 5.42e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 38.74  E-value: 5.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 16129976    1 MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYT 42
Cdd:PRK10157   5 IFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVT 46
PRK06370 PRK06370
FAD-containing oxidoreductase;
2-38 5.64e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 38.64  E-value: 5.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16129976    2 YDYIIVGSGLFGAVCANELKKLNKKVLVIEkRNHIGG 38
Cdd:PRK06370   6 YDAIVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
PRK02106 PRK02106
choline dehydrogenase; Validated
 1-31 5.72e-03

choline dehydrogenase; Validated


Pssm-ID: 235000 [Multi-domain]  Cd Length: 560  Bit Score: 38.66  E-value: 5.72e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 16129976    1 MYDYIIVGSGLFGAVCANEL-KKLNKKVLVIE 31
Cdd:PRK02106   5 EYDYIIIGAGSAGCVLANRLsEDPDVSVLLLE 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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