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Conserved domains on  [gi|992392977|gb|AMH89274|]
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UDP-galactopyranose mutase [Streptococcus mitis]

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];
1-365 0e+00

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


:

Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 664.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAA-LKGKKVKVIEKRNHIAGNIHT-REEEGIQVHQYGAHIFHTSDKEIWDYVNQFAEFNRY 78
Cdd:COG0562    2 MYDYLIVGAGFFGAVFAERLAeELGKKVLVIDKRDHIGGNAYDeYDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  79 TNSPVANYKGEIYNLPFNMNTFNKLWGVV-TPAEAQAKIDEQRAvlNGKTPENLEEQAISLVGTDIYEKLIKDYTEKQWG 157
Cdd:COG0562   82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 158 KPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVDFFANKEQymKDFPKIVFTGMIDE 237
Cdd:COG0562  160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHPNIEVRLNTDFFEVRDE--IPADHVVYTGPIDE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 238 FFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTDADTPYTRIIEHKHFEFGSQAKTIITKEHSKTWEKGDEPYYPVNN 317
Cdd:COG0562  238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 992392977 318 DRNNHLYKSYKKLADEQGNVIFGGRLGHYRYYDMHQVIGAALQCVRNE 365
Cdd:COG0562  318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
 
Name Accession Description Interval E-value
Glf COG0562
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
1-365 0e+00

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


Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 664.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAA-LKGKKVKVIEKRNHIAGNIHT-REEEGIQVHQYGAHIFHTSDKEIWDYVNQFAEFNRY 78
Cdd:COG0562    2 MYDYLIVGAGFFGAVFAERLAeELGKKVLVIDKRDHIGGNAYDeYDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  79 TNSPVANYKGEIYNLPFNMNTFNKLWGVV-TPAEAQAKIDEQRAvlNGKTPENLEEQAISLVGTDIYEKLIKDYTEKQWG 157
Cdd:COG0562   82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 158 KPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVDFFANKEQymKDFPKIVFTGMIDE 237
Cdd:COG0562  160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHPNIEVRLNTDFFEVRDE--IPADHVVYTGPIDE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 238 FFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTDADTPYTRIIEHKHFEFGSQAKTIITKEHSKTWEKGDEPYYPVNN 317
Cdd:COG0562  238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 992392977 318 DRNNHLYKSYKKLADEQGNVIFGGRLGHYRYYDMHQVIGAALQCVRNE 365
Cdd:COG0562  318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
UDP-GALP_mutase TIGR00031
UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into ...
 1-366 1.33e-144

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: 414.18  E-value: 1.33e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977    1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVHQYGAHIFHTSDKEIWDYVNQFAEFNRYTN 80
Cdd:TIGR00031   1 MFDYIIVGAGLSGIVLANILAQLNKRVLVVEKRNHIGGNCYDEVDETILFHQYGPHIFHTNNQYVWDYISPFFELNNYQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   81 SPVANYKGEIYNLPFNMNTFNKLWGVVTPAEAQAKIDEQRAVLNGKTPENLEEQA---ISLVGTDIYEKLIKDYTEKQWG 157
Cdd:TIGR00031  81 RVLALYNNLDLTLPFNFNQFRKLLGVKDAQELQNFFNAQFKYGDHVPLEELQEIAdpdIQLLYQFLYQKVYKPYTVKQWG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  158 KPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVD-----------FFANKEQYmkdf 226
Cdd:TIGR00031 161 LPAEEIDPFVIGRVPVVLSEDSSYFPDRYQGLPKGGYTKLFEKMLDHPLIDVKLNCHinllkdkdsqlHFANKAIR---- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  227 PKIVFTGMIDEFFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTdADTPYTRIIEHKHFEFGSQAKTIITKEHSKTWE 306
Cdd:TIGR00031 237 KPVIYTGLIDQLFGYRFGALQYRSLKFEWERHEFKNFQGYAVVNFP-LNVPITRIVEYKHLTYVGSKQTIVSKEYPGEWK 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992392977  307 KGD-EPYYPVNNDRNNHLYKSYKKLADEQGNVIFGGRLGHYRYYDMHQVIGAALQCVRNEL 366
Cdd:TIGR00031 316 VGDpEPYYPVNDNKNMALFKKYLELASREDNLILLGRLAEYQYYDMDQAILAALYKAEQLL 376
GLF pfam03275
UDP-galactopyranose mutase;
146-348 5.93e-122

UDP-galactopyranose mutase;


Pssm-ID: 427229  Cd Length: 203  Bit Score: 349.92  E-value: 5.93e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  146 KLIKDYTEKQWGKPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVDFFANKEQYMKD 225
Cdd:pfam03275   1 KFFKGYTEKQWGLDPEELPASVIKRLPVRFNYDNRYFNDTYQGLPKDGYTKMFENMLDHPNIEVRLNTDFFDIRDNDVEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  226 FPKIVFTGMIDEFFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTDADTPYTRIIEHKHFEFGSQAKTIITKEHSKTW 305
Cdd:pfam03275  81 ADPVVYTGPIDEYFDYCFGELPYRSLDFETETLDQGDFQGNAVVNYPDDEVPYTRITEYKHFTPQKHDKTVITREYPRAW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 992392977  306 EKGDEPYYPVNNDRNNHLYKSYKKLADEQGNVIFGGRLGHYRY 348
Cdd:pfam03275 161 EEGDEPYYPINTEENRALYEKYRELAKKEPNVTFGGRLGTYRY 203
PRK07208 PRK07208
hypothetical protein; Provisional
 5-165 1.35e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 46.81  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   5 LIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVhQYGAHIFHTSDKEIWDYVNQ------FAEFNRY 78
Cdd:PRK07208   8 VIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGNRF-DIGGHRFFSKSPEVMDLWNEilpdddFLLRPRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  79 TnspVANYKGEIYNLPF-NMNTFNKLwGVVTPAEAQAKIDEQRaVLNGKTPENLEEQAISLVGTDIYEKLIKDYTEKQWG 157
Cdd:PRK07208  87 S---RIYYRGKFFDYPLkAFDALKNL-GLWRTAKCGASYLKAR-LRPRKEEDSFEDWVINRFGRRLYSTFFKGYTEKVWG 161


                 ....*...
gi 992392977 158 KPTTELPA 165
Cdd:PRK07208 162 VPCDEISA 169
 
Name Accession Description Interval E-value
Glf COG0562
UDP-galactopyranose mutase [Cell wall/membrane/envelope biogenesis];
1-365 0e+00

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


Pssm-ID: 440328 [Multi-domain]  Cd Length: 365  Bit Score: 664.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAA-LKGKKVKVIEKRNHIAGNIHT-REEEGIQVHQYGAHIFHTSDKEIWDYVNQFAEFNRY 78
Cdd:COG0562    2 MYDYLIVGAGFFGAVFAERLAeELGKKVLVIDKRDHIGGNAYDeYDETGILVHKYGPHIFHTNNKRVWDYLSRFTEFNPY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  79 TNSPVANYKGEIYNLPFNMNTFNKLWGVV-TPAEAQAKIDEQRAvlNGKTPENLEEQAISLVGTDIYEKLIKDYTEKQWG 157
Cdd:COG0562   82 QHRVLANVDGQLYPLPFNLNTINQLFGKKlTPDEARAFIAEQAE--PIKEPRNLEEQALSLVGRDLYEKFFKGYTEKQWG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 158 KPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVDFFANKEQymKDFPKIVFTGMIDE 237
Cdd:COG0562  160 RDPSELPASIIKRLPVRFNYDNRYFNDTYQGMPKGGYTAMFERMLDHPNIEVRLNTDFFEVRDE--IPADHVVYTGPIDE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 238 FFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTDADTPYTRIIEHKHFEFGSQAKTIITKEHSKTWEKGDEPYYPVNN 317
Cdd:COG0562  238 YFDYRFGRLPYRSLDFEFETLDVEDFQGVAVVNYPDADVPYTRITEFKHFTGQQHPKTVITREYPRAYEEGDEPYYPIND 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 992392977 318 DRNNHLYKSYKKLADEQGNVIFGGRLGHYRYYDMHQVIGAALQCVRNE 365
Cdd:COG0562  318 EENQALYKKYRALAEKEPNVIFGGRLATYRYYDMDQVIASALALFDKL 365
UDP-GALP_mutase TIGR00031
UDP-galactopyranose mutase; This enzyme is involved in the conversion of UDP-GALP into ...
 1-366 1.33e-144

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: 414.18  E-value: 1.33e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977    1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVHQYGAHIFHTSDKEIWDYVNQFAEFNRYTN 80
Cdd:TIGR00031   1 MFDYIIVGAGLSGIVLANILAQLNKRVLVVEKRNHIGGNCYDEVDETILFHQYGPHIFHTNNQYVWDYISPFFELNNYQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   81 SPVANYKGEIYNLPFNMNTFNKLWGVVTPAEAQAKIDEQRAVLNGKTPENLEEQA---ISLVGTDIYEKLIKDYTEKQWG 157
Cdd:TIGR00031  81 RVLALYNNLDLTLPFNFNQFRKLLGVKDAQELQNFFNAQFKYGDHVPLEELQEIAdpdIQLLYQFLYQKVYKPYTVKQWG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  158 KPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVD-----------FFANKEQYmkdf 226
Cdd:TIGR00031 161 LPAEEIDPFVIGRVPVVLSEDSSYFPDRYQGLPKGGYTKLFEKMLDHPLIDVKLNCHinllkdkdsqlHFANKAIR---- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  227 PKIVFTGMIDEFFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTdADTPYTRIIEHKHFEFGSQAKTIITKEHSKTWE 306
Cdd:TIGR00031 237 KPVIYTGLIDQLFGYRFGALQYRSLKFEWERHEFKNFQGYAVVNFP-LNVPITRIVEYKHLTYVGSKQTIVSKEYPGEWK 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992392977  307 KGD-EPYYPVNNDRNNHLYKSYKKLADEQGNVIFGGRLGHYRYYDMHQVIGAALQCVRNEL 366
Cdd:TIGR00031 316 VGDpEPYYPVNDNKNMALFKKYLELASREDNLILLGRLAEYQYYDMDQAILAALYKAEQLL 376
GLF pfam03275
UDP-galactopyranose mutase;
146-348 5.93e-122

UDP-galactopyranose mutase;


Pssm-ID: 427229  Cd Length: 203  Bit Score: 349.92  E-value: 5.93e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  146 KLIKDYTEKQWGKPTTELPAFIIRRLPVRLTYDNNYFNDTYQGIPIGGYTQIVEKMLDHENIDVETNVDFFANKEQYMKD 225
Cdd:pfam03275   1 KFFKGYTEKQWGLDPEELPASVIKRLPVRFNYDNRYFNDTYQGLPKDGYTKMFENMLDHPNIEVRLNTDFFDIRDNDVEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  226 FPKIVFTGMIDEFFDYKLGELEYRSLRFENETLDMENYQGNAVVNYTDADTPYTRIIEHKHFEFGSQAKTIITKEHSKTW 305
Cdd:pfam03275  81 ADPVVYTGPIDEYFDYCFGELPYRSLDFETETLDQGDFQGNAVVNYPDDEVPYTRITEYKHFTPQKHDKTVITREYPRAW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 992392977  306 EKGDEPYYPVNNDRNNHLYKSYKKLADEQGNVIFGGRLGHYRY 348
Cdd:pfam03275 161 EEGDEPYYPINTEENRALYEKYRELAKKEPNVTFGGRLGTYRY 203
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
6-72 3.29e-21

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 86.05  E-value: 3.29e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992392977    6 IVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIqVHQYGAHIFHTSDK-EIWDYVNQF 72
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGY-VFDYGAHIFHGSDEpNVRDLLDEL 67
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-287 1.71e-16

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: 80.26  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVhQYGAHIFHTSDKEIWDYVNQF---AEFnR 77
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRI-DRGPHSFLTRDPEVLELLRELglgDEL-V 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  78 YTNSPVAN--YKGEIYNLPfnMNTFNKLWGVVTPAEAQAKI--DEQRAVLNGKTPENLEEQAISLVGTDIYEKLIKDYTE 153
Cdd:COG1232   79 WPNTRKSYiyYGGKLHPLP--QGPLALLRSPLLSLAGKLRAllELLAPRRPPGEDESLAEFVRRRFGREVYERLVEPLLE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 154 KQWGKPTTELPA-FIIRRLP------------VRLTYDNNYFNDTYQGiPIGGYTQIVEKMLDH-ENIDVETNVD----- 214
Cdd:COG1232  157 GVYAGDPDELSAdWAFPRLKrlelehgslikgALALRKGAKAGEVFGY-LRGGLGTLVEALAEAlEAGEIRLGTRvtaie 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 215 --------FFANKEQYmkDFPKIVFT-------GMIDEFFDY---KLGELEYRS-----LRFENETLDmeNYQGNAVVNY 271
Cdd:COG1232  236 regggwrvTTSDGETI--EADAVVSAtpapalaRLLAPLPPEvaaALAGIPYASvavvaLGFDRPDLP--PPDGFGWLVP 311

                        330
                 ....*....|....*.
gi 992392977 272 TDADTPYTRIIEHKHF 287
Cdd:COG1232  312 RDEGVPILAVTFSSNK 327
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-212 2.54e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 49.15  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGiqVHQY---GAHIFHTSDKEIWDYVNQF----A 73
Cdd:COG1231    7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGD--DGLYaelGAMRIPPSHTNLLALARELglplE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  74 EFNRYTNSPVANYKGEiynlPFNMNTFNKLWGVVtpAEAQAKIDEQ-RAVLNGKTPENLEEQAISL-------VGTDIYE 145
Cdd:COG1231   85 PFPNENGNALLYLGGK----RVRAGEIAADLRGV--AELLAKLLRAlAAALDPWAHPAAELDRESLaewlrrnGASPSAR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992392977 146 KLIKDYTEKQWGKPTTELPAFIIrrlpVRLTYDNNYFNDTYQgiPIGGYTQIVEKMLDHENIDVETN 212
Cdd:COG1231  159 RLLGLLGAGEYGADPDELSLLDL----LRYAASAGGGAQQFR--IVGGMDQLPRALAAELGDRIRLG 219
PRK07208 PRK07208
hypothetical protein; Provisional
 5-165 1.35e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 46.81  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   5 LIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVhQYGAHIFHTSDKEIWDYVNQ------FAEFNRY 78
Cdd:PRK07208   8 VIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGNRF-DIGGHRFFSKSPEVMDLWNEilpdddFLLRPRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  79 TnspVANYKGEIYNLPF-NMNTFNKLwGVVTPAEAQAKIDEQRaVLNGKTPENLEEQAISLVGTDIYEKLIKDYTEKQWG 157
Cdd:PRK07208  87 S---RIYYRGKFFDYPLkAFDALKNL-GLWRTAKCGASYLKAR-LRPRKEEDSFEDWVINRFGRRLYSTFFKGYTEKVWG 161


                 ....*...
gi 992392977 158 KPTTELPA 165
Cdd:PRK07208 162 VPCDEISA 169
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-58 4.11e-05

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 45.23  E-value: 4.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIqVHQYGAHIF 58
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGF-RFDVGPSVL 59
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-38 7.59e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.13  E-value: 7.59e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEkRNHIAG 38
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGS 38
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 23-100 8.11e-05

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: 44.40  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   23 KGKKVKVIEKRNHIAGNIHTREEEG--IQVhqyGAHIFHTSDKEIWDYVNQF-----------AEFNRYTNSPVANYKGE 89
Cdd:pfam01593  13 AGHDVTVLEARDRVGGRIRTVRDDGflIEL---GAMWFHGAQPPLLALLKELgledrlvlpdpAPFYTVLFAGGRRYPGD 89

                          90
                  ....*....|.
gi 992392977   90 IYNLPFNMNTF 100
Cdd:pfam01593  90 FRRVPAGWEGL 100
PLN02576 PLN02576
protoporphyrinogen oxidase
 2-65 1.43e-04

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 43.46  E-value: 1.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992392977   2 YDYLIVGAGLFGAVFAHEAALK-GKKVKVIEKRNHIAGNIHTREEEGIqVHQYGAHIFHTSDKEI 65
Cdd:PLN02576  13 KDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNITSVSEDGF-IWEEGPNSFQPSDPEL 76
PRK07233 PRK07233
hypothetical protein; Provisional
 6-287 1.70e-04

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 43.34  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   6 IVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGNIHTREEEGIQVHQYGAHIFhTSDKEIwdyVNQFAEFN-----RYTN 80
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPIERFYHHIF-KSDEAL---LELLDELGledklRWRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977  81 SPVA-NYKGEIYnlPFN----------MNTFNKL-WGVVTpaeAQAKIdeqraVLNGKTPENL--EEQAISLVGTDIYEK 146
Cdd:PRK07233  80 TKTGyYVDGKLY--PLGtplellrfphLSLIDKFrLGLLT---LLARR-----IKDWRALDKVpaEEWLRRWSGEGVYEV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 147 LIKDYTEKQWGKPTTELPA-FIIRRLPVRLTYDNNYFNDTYqGIPIGGYTQIVEKMLD-----HENIDVETNVDFFANKE 220
Cdd:PRK07233 150 FWEPLLESKFGDYADDVSAaWLWSRIKRRGNRRYSLFGEKL-GYLEGGFATLIDALAEaiearGGEIRLGTPVTSVVIDG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977 221 QYMK---------DFPKIVFTGMIDEffdykLGELEYRSLRFENETLDMENYQGNAVV--------------NYTDADTP 277
Cdd:PRK07233 229 GGVTgvevdgeeeDFDAVISTAPPPI-----LARLVPDLPADVLARLRRIDYQGVVCMvlklrrpltdyywlNINDPGAP 303

                        330
                 ....*....|
gi 992392977 278 YTRIIEHKHF 287
Cdd:PRK07233 304 FGGVIEHTNL 313
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 1-69 2.25e-04

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 42.90  E-value: 2.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992392977    1 MYDYLIVGAGLFGAVFAH----EAALKGKKVKVIEKRNHIAGNIHTREEEGIQVHQyGAHIFHTSDKEIWDYV 69
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAYylekEIPELPVELTLVEASDRVGGKIQTVKEDGYLIER-GPDSFLERKKSAPDLV 73
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-65 2.97e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 42.44  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992392977   1 MYDYLIVGAGLFGAVFAHE-AALKGKKVKVIEKRNHIA--------GNIHT------------------------REEEG 47
Cdd:COG0579    4 MYDVVIIGAGIVGLALARElSRYEDLKVLVLEKEDDVAqessgnnsGVIHAglyytpgslkarlcvegnelfyelCRELG 83

                         90
                 ....*....|....*...
gi 992392977  48 IQVHQYGAHIFHTSDKEI 65
Cdd:COG0579   84 IPFKRCGKLVVATGEEEV 101
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 3-38 4.39e-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: 41.61  E-value: 4.39e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 992392977    3 DYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAG 38
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 2-34 9.04e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 41.04  E-value: 9.04e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 992392977   2 YDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRN 34
Cdd:PRK12834   5 ADVIVVGAGLAGLVAAAELADAGKRVLLLDQEN 37
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-39 4.40e-03

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: 38.66  E-value: 4.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 992392977   1 MYDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGN 39
Cdd:COG1053    3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-39 5.11e-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: 38.45  E-value: 5.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 992392977    2 YDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGN 39
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYG 38
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-51 6.97e-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: 35.26  E-value: 6.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 992392977    5 LIVGAGLFGAVFAHEAALKGKKVKVIEKRNHI-------AGNIHTR--EEEGIQVH 51
Cdd:pfam00070   3 VVVGGGYIGLELAGALARLGSKVTVVERRDRLlpgfdpeIAKILQEklEKNGIEFL 58
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
2-42 8.33e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 37.83  E-value: 8.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 992392977   2 YDYLIVGAGLFGAVFAHEAALKGKKVKVIEKRNHIAGN-IHT 42
Cdd:PRK05249   6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGcTHT 47
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
2-31 8.57e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 37.85  E-value: 8.57e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 992392977   2 YDYLIVGAGLFGAVFAHEAALKGKKVKVIE 31
Cdd:COG3573    6 ADVIVVGAGLAGLVAAAELADAGRRVLLLD 35
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 3-32 9.69e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 37.65  E-value: 9.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 992392977    3 DYLIVGAGLFGAVFAHEAALKGKKVKVIEK 32
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEK 30
 
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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