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Conserved domains on  [gi|489936396|ref|WP_003839703|]
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MULTISPECIES: L-2-hydroxyglutarate oxidase [Citrobacter]

Protein Classification

L-2-hydroxyglutarate oxidase( domain architecture ID 11485473)

L-2-hydroxyglutarate oxidase oxidizes L-2-hydroxyglutarate, to recover alpha-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-393 0e+00

L-2-hydroxyglutarate oxidase;


:

Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 733.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   1 MYDFVIIGGGIIGMSTAMQLIDVYPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQN 80
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  81 GIRYDVCGKMLVATSPLEMERMRALWDRTAANGLEREWLNAQELREREPNITGLGGIFVPSSGIVSYREVTAAMANIFQA 160
Cdd:PRK11728  82 GIPYEECGKLLVATSELELERMEALYERARANGIEVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELIQA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 161 KGGEIIYNAEVSALKEHATGVIVHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGFIICPFRGEYFRLAPEHNQIVNHL 240
Cdd:PRK11728 162 RGGEIRLGAEVTALDEHANGVVVRTTQG-EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKNQLVNHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 241 IYPIPDPAMPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLSDTLEILGSSGIRRVLQNNLRSGLGEMKNSLCKS 320
Cdd:PRK11728 241 IYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMKNSLSKS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936396 321 GYLRLVQKYCPSLTLKDLQPWPAGVRAQAVSPDGKLIDDFLFVTTPRSIHTCNAPSPAATSAIPIGAHIVSKV 393
Cdd:PRK11728 321 GYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVETPRSLHVCNAPSPAATSSLPIGEHIVSKV 393
 
Name Accession Description Interval E-value
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-393 0e+00

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 733.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   1 MYDFVIIGGGIIGMSTAMQLIDVYPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQN 80
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  81 GIRYDVCGKMLVATSPLEMERMRALWDRTAANGLEREWLNAQELREREPNITGLGGIFVPSSGIVSYREVTAAMANIFQA 160
Cdd:PRK11728  82 GIPYEECGKLLVATSELELERMEALYERARANGIEVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELIQA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 161 KGGEIIYNAEVSALKEHATGVIVHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGFIICPFRGEYFRLAPEHNQIVNHL 240
Cdd:PRK11728 162 RGGEIRLGAEVTALDEHANGVVVRTTQG-EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKNQLVNHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 241 IYPIPDPAMPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLSDTLEILGSSGIRRVLQNNLRSGLGEMKNSLCKS 320
Cdd:PRK11728 241 IYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMKNSLSKS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936396 321 GYLRLVQKYCPSLTLKDLQPWPAGVRAQAVSPDGKLIDDFLFVTTPRSIHTCNAPSPAATSAIPIGAHIVSKV 393
Cdd:PRK11728 321 GYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVETPRSLHVCNAPSPAATSSLPIGEHIVSKV 393
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
15-405 2.99e-162

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 462.69  E-value: 2.99e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  15 STAMQLIDvYPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQNGIRYDVCGKMLVAT 94
Cdd:COG0579   18 ALARELSR-YEDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCRELGIPFKRCGKLVVAT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  95 SPLEMERMRALWDRTAANGLER-EWLNAQELREREPNIT--GLGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEV 171
Cdd:COG0579   97 GEEEVAFLEKLYERGKANGVPGlEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALAENAEANGVELLLNTEV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 172 SALKEHATGVIVHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGFIICPFRGEYFRLAPEHNqIVNHLIYPIPDPAMPF 251
Cdd:COG0579  177 TGIEREGDGWEVTTNGG-TIRARFVINAAGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPAE-LVNAKVYPVPDPGAPF 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 252 LGVHLTRMIDGSVTVGPNAVLAFKREGyrkrdfSLSDTLEILGSSGIRRVLQNNLRSGLGEMKNSLCKSGYLRLVQKYCP 331
Cdd:COG0579  255 LGVHLTRTIDGNLLFGPNAVFVPKKED------SLLDLFESLRFPNFWPMLAKNLLTKYLESVTSLSKEAFLEALRKYVP 328
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936396 332 SLTLKDLQPWPAGVRAQAVSPDGklidDFLFVTT--PRSIHTCNAPSPAATSAIPIGAHIVSKVHALLE-NQSNPGR 405
Cdd:COG0579  329 ELPDEDLIPAFAGIRAQIIKPDG----DFVIEEAddPGSIHVLGIESPGATSALAIAEHVAELLPEKLEeKDWQPKR 401
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
15-390 4.34e-47

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: 164.49  E-value: 4.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   15 STAMQLIDvyPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQNGIRYDV--CGKMLV 92
Cdd:pfam01266  13 STAYELAR--RGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEELGIDCGFrrCGVLVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   93 ATSPlEMERMRALWDRTAANGLEREWLNAQELREREPNITGL-GGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEV 171
Cdd:pfam01266  91 ARDE-EEEALEKLLAALRRLGVPAELLDAEELRELEPLLPGLrGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  172 SALKEHATGVIVHTrqgqEYEGATLISCSGLMADrLVKMLGVEPgfIICPFRGEYFRLAPEHNqivNHLIYPIPDPAMPF 251
Cdd:pfam01266 170 TGIEEEGGVWGVVT----TGEADAVVNAAGAWAD-LLALPGLRL--PVRPVRGQVLVLEPLPE---ALLILPVPITVDPG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  252 LGVHLTRMIDGSVTVGPNAVLafkrEGYRKRDFSLSDTLEIlgssgirrvlqnnlrsglgemknslcksgyLRLVQKYCP 331
Cdd:pfam01266 240 RGVYLRPRADGRLLLGGTDEE----DGFDDPTPDPEEIEEL------------------------------LEAARRLFP 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489936396  332 SLTlKDLQPWpAGVRAqavSPDGKLIDDFLfvTTPRSIHTCNAPSPAATSAIPIGAHIV 390
Cdd:pfam01266 286 ALA-DIERAW-AGLRP---LPDGLPIIGRP--GSPGLYLATGHGGHGLTLAPGIGKLLA 337
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
82-242 1.40e-09

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 59.30  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   82 IRYDVCGKMLVATSPLEMERMRALWDRTAANGLEREWLNAQELREREPNITG--LGGIFVPSSGIVSYREVTAAMANIFQ 159
Cdd:TIGR02352  69 TGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRALRRLEPYLSGgiRGAVFYPDDAHVDPRALLKALEKALE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  160 AKGGEIIYNAEVSALK---EHATGVIvhTRQGQeYEGATLISCSGLMADRLVkmlgvepGFIICPFRGEYFRL----APE 232
Cdd:TIGR02352 149 KLGVEIIEHTEVQHIEirgEKVTAIV--TPSGD-VQADQVVLAAGAWAGELL-------PLPLRPVRGQPLRLeapaVPL 218
                         170
                  ....*....|
gi 489936396  233 HNQIVNHLIY 242
Cdd:TIGR02352 219 LNRPLRAVVY 228
 
Name Accession Description Interval E-value
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-393 0e+00

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 733.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   1 MYDFVIIGGGIIGMSTAMQLIDVYPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQN 80
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGHNSGVIHAGVYYTPGSLKARFCRRGNEATKAFCDQH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  81 GIRYDVCGKMLVATSPLEMERMRALWDRTAANGLEREWLNAQELREREPNITGLGGIFVPSSGIVSYREVTAAMANIFQA 160
Cdd:PRK11728  82 GIPYEECGKLLVATSELELERMEALYERARANGIEVERLDAEELREREPNIRGLGAIFVPSTGIVDYRAVAEAMAELIQA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 161 KGGEIIYNAEVSALKEHATGVIVHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGFIICPFRGEYFRLAPEHNQIVNHL 240
Cdd:PRK11728 162 RGGEIRLGAEVTALDEHANGVVVRTTQG-EYEARTLINCAGLMSDRLAKMAGLEPDFRIVPFRGEYYRLAPEKNQLVNHL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 241 IYPIPDPAMPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLSDTLEILGSSGIRRVLQNNLRSGLGEMKNSLCKS 320
Cdd:PRK11728 241 IYPVPDPAFPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSLRDLLEILTYPGFWKLAQKHWRSGLGEMKNSLSKS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936396 321 GYLRLVQKYCPSLTLKDLQPWPAGVRAQAVSPDGKLIDDFLFVTTPRSIHTCNAPSPAATSAIPIGAHIVSKV 393
Cdd:PRK11728 321 GYLRLVQKYCPSLTLSDLQPYPAGVRAQAVSRDGKLVDDFLFVETPRSLHVCNAPSPAATSSLPIGEHIVSKV 393
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
15-405 2.99e-162

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 462.69  E-value: 2.99e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  15 STAMQLIDvYPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQNGIRYDVCGKMLVAT 94
Cdd:COG0579   18 ALARELSR-YEDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYTPGSLKARLCVEGNELFYELCRELGIPFKRCGKLVVAT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  95 SPLEMERMRALWDRTAANGLER-EWLNAQELREREPNIT--GLGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEV 171
Cdd:COG0579   97 GEEEVAFLEKLYERGKANGVPGlEILDREELRELEPLLSdeGVAALYSPSTGIVDPGALTRALAENAEANGVELLLNTEV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 172 SALKEHATGVIVHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGFIICPFRGEYFRLAPEHNqIVNHLIYPIPDPAMPF 251
Cdd:COG0579  177 TGIEREGDGWEVTTNGG-TIRARFVINAAGLYADRLAQMAGIGKDFGIFPVKGEYLVLDKPAE-LVNAKVYPVPDPGAPF 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 252 LGVHLTRMIDGSVTVGPNAVLAFKREGyrkrdfSLSDTLEILGSSGIRRVLQNNLRSGLGEMKNSLCKSGYLRLVQKYCP 331
Cdd:COG0579  255 LGVHLTRTIDGNLLFGPNAVFVPKKED------SLLDLFESLRFPNFWPMLAKNLLTKYLESVTSLSKEAFLEALRKYVP 328
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936396 332 SLTLKDLQPWPAGVRAQAVSPDGklidDFLFVTT--PRSIHTCNAPSPAATSAIPIGAHIVSKVHALLE-NQSNPGR 405
Cdd:COG0579  329 ELPDEDLIPAFAGIRAQIIKPDG----DFVIEEAddPGSIHVLGIESPGATSALAIAEHVAELLPEKLEeKDWQPKR 401
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
15-390 4.34e-47

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: 164.49  E-value: 4.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   15 STAMQLIDvyPDARIALLEKESGPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQNGIRYDV--CGKMLV 92
Cdd:pfam01266  13 STAYELAR--RGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALDLWEELEEELGIDCGFrrCGVLVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   93 ATSPlEMERMRALWDRTAANGLEREWLNAQELREREPNITGL-GGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEV 171
Cdd:pfam01266  91 ARDE-EEEALEKLLAALRRLGVPAELLDAEELRELEPLLPGLrGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  172 SALKEHATGVIVHTrqgqEYEGATLISCSGLMADrLVKMLGVEPgfIICPFRGEYFRLAPEHNqivNHLIYPIPDPAMPF 251
Cdd:pfam01266 170 TGIEEEGGVWGVVT----TGEADAVVNAAGAWAD-LLALPGLRL--PVRPVRGQVLVLEPLPE---ALLILPVPITVDPG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  252 LGVHLTRMIDGSVTVGPNAVLafkrEGYRKRDFSLSDTLEIlgssgirrvlqnnlrsglgemknslcksgyLRLVQKYCP 331
Cdd:pfam01266 240 RGVYLRPRADGRLLLGGTDEE----DGFDDPTPDPEEIEEL------------------------------LEAARRLFP 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489936396  332 SLTlKDLQPWpAGVRAqavSPDGKLIDDFLfvTTPRSIHTCNAPSPAATSAIPIGAHIV 390
Cdd:pfam01266 286 ALA-DIERAW-AGLRP---LPDGLPIIGRP--GSPGLYLATGHGGHGLTLAPGIGKLLA 337
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
27-267 9.49e-33

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 126.56  E-value: 9.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  27 ARIALLEKEsGPACHQTGHNSGVIHAGvYYTPGSLK-AQFCLAGNRATKAFCDQNGIRYDV--CGKMLVATSPLEMERMR 103
Cdd:COG0665   26 LDVTVLERG-RPGSGASGRNAGQLRPG-LAALADRAlVRLAREALDLWRELAAELGIDCDFrrTGVLYLARTEAELAALR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 104 ALWDRTAANGLEREWLNAQELREREPNITG---LGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEVSALKEHATG 180
Cdd:COG0665  104 AEAEALRALGLPVELLDAAELREREPGLGSpdyAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGR 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 181 VI-VHTRQGqEYEGATLISCSGLMADRLVKMLGVEPGfiICPFRGEYFRLAPEHNQIVNHLIYPipdpampfLGVHLTRM 259
Cdd:COG0665  184 VTgVRTERG-TVRADAVVLAAGAWSARLLPMLGLRLP--LRPVRGYVLVTEPLPDLPLRPVLDD--------TGVYLRPT 252

                 ....*...
gi 489936396 260 IDGSVTVG 267
Cdd:COG0665  253 ADGRLLVG 260
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
82-242 1.40e-09

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 59.30  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396   82 IRYDVCGKMLVATSPLEMERMRALWDRTAANGLEREWLNAQELREREPNITG--LGGIFVPSSGIVSYREVTAAMANIFQ 159
Cdd:TIGR02352  69 TGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRALRRLEPYLSGgiRGAVFYPDDAHVDPRALLKALEKALE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  160 AKGGEIIYNAEVSALK---EHATGVIvhTRQGQeYEGATLISCSGLMADRLVkmlgvepGFIICPFRGEYFRL----APE 232
Cdd:TIGR02352 149 KLGVEIIEHTEVQHIEirgEKVTAIV--TPSGD-VQADQVVLAAGAWAGELL-------PLPLRPVRGQPLRLeapaVPL 218
                         170
                  ....*....|
gi 489936396  233 HNQIVNHLIY 242
Cdd:TIGR02352 219 LNRPLRAVVY 228
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
13-208 3.92e-08

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 55.24  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  13 GMSTAMQLIdvypdAR---IALLEKESGPACHQTGHnsgviHAGVYYT----PGSLKAQFCLAGNRATKAFCDQN----- 80
Cdd:PRK01747 272 GAALALALA-----RRgwqVTLYEADEAPAQGASGN-----RQGALYPllskDDNALSRFFRAAFLFARRFYDALpaagv 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  81 GIRYDVCGKMLVATSPLEMERMRALWDRTAANGLEReWLNAQELREREPNITGLGGIFVPSSGIVSYREVTAAMANIFQA 160
Cdd:PRK01747 342 AFDHDWCGVLQLAWDEKSAEKIAKMLALGLPAELAR-ALDAEEAEELAGLPVPCGGIFYPQGGWLCPAELCRALLALAGQ 420
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489936396 161 kGGEIIYNAEVSALKEHATGVIVHTRQGQEYEGATLISCSGLMADRLV 208
Cdd:PRK01747 421 -QLTIHFGHEVARLEREDDGWQLDFAGGTLASAPVVVLANGHDAARFA 467
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
28-383 6.25e-08

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 54.74  E-value: 6.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  28 RIALLEKESGPA--CHQTGHNSGVIHAG---VYYTPGS---LKAQFCLAGNRATKAFCDQNGIRYDVCGKMLVATSPLEM 99
Cdd:PTZ00383  72 KIALIERRSDFAlvASHGKNNSQTIHCGdieTNYTLEKarkVKRQADMLRNYLTKLPPSERDSIIFKMQKMVLGVGEKEC 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 100 ERMRALWDRTAANGLEREWLNAQELREREPNIT----------GLGGIFVPSS-GIVSYREVT------AAMANIFQAKG 162
Cdd:PTZ00383 152 EFLEKRYPVFKELFPSMQLLDKKEIHRVEPRVVlknnhtlreePLAALYVPNElTTVDYQKLSesfvkhARRDALVPGKK 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 163 GEIIYNAEVSALKE-HATGVIVHTRQGQEYEGATLISCSG--LMadrLVKMLGVEPGFIICPFRGEYFrLAPEhnqIVNH 239
Cdd:PTZ00383 232 ISINLNTEVLNIERsNDSLYKIHTNRGEIRARFVVVSACGysLL---FAQKMGYGLEYSCLPVAGSFY-FSGN---ILNG 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 240 LIYPIPDPAMPFLGVHLTRMI--DGSVTVGPNAVLAFKREGYRKRdfSLSDTL--------------EILGSSGIRRVLq 303
Cdd:PTZ00383 305 KVYTVQNPALPFAAVHGDPDIiaKGKTRFGPTALPLPLLERYNMS--SLPDFLkvwnpdlnllavyfDLFKDSTMRKYV- 381
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 304 nnLRSGLGEMKnSLCKSGYLRLVQKYCPSLTLKDLQPWPA--GVRAQAVSPDG-KLIDDFLFVTTPRSIHTCNAPSPAAT 380
Cdd:PTZ00383 382 --LRNFLFEVP-LLNKYLFLKDARKIVPSLTRKDLRYCVGygGVRPQLIDKVSkKLLLGEGKIDPGKGIIFNITPSPGAT 458

                 ...
gi 489936396 381 SAI 383
Cdd:PTZ00383 459 TCL 461
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
110-212 1.65e-07

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 53.10  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 110 AANGLEREWLNAQELREREPNITG--LGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEVSALKEHATGVIVHTRQ 187
Cdd:PRK12409 157 AEGGLERRAVTPEEMRAIEPTLTGeyYGGYYTPSDSTGDIHKFTTGLAAACARLGVQFRYGQEVTSIKTDGGGVVLTVQP 236
                         90       100       110
                 ....*....|....*....|....*....|
gi 489936396 188 GQEY-----EGATLISCSGLMADRLVKMLG 212
Cdd:PRK12409 237 SAEHpsrtlEFDGVVVCAGVGSRALAAMLG 266
solA PRK11259
N-methyl-L-tryptophan oxidase;
113-212 6.36e-07

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 50.99  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 113 GLEREWLNAQELREREPNIT---GLGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEVSALKEHATGVIVHTRQGq 189
Cdd:PRK11259 111 GLPHEVLDAAEIRRRFPQFRlpdGYIALFEPDGGFLRPELAIKAHLRLAREAGAELLFNEPVTAIEADGDGVTVTTADG- 189
                         90       100
                 ....*....|....*....|...
gi 489936396 190 EYEGATLISCSGLMADRLVKMLG 212
Cdd:PRK11259 190 TYEAKKLVVSAGAWVKDLLPPLE 212
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
99-265 7.76e-06

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 47.63  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  99 MERMRAL--WDRTAANGLE------REWLNAQELREREPNITGLGGIFvpssgIVSYREVTAAMANIFQAKGGEIIYNAE 170
Cdd:COG0654   52 LELLRRLglWDRLLARGAPirgirvRDGSDGRVLARFDAAETGLPAGL-----VVPRADLERALLEAARALGVELRFGTE 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396 171 VSALKEHATGVIVHTRQGQEYEGATLISCSGL------MADRLVKMLGVEPGFIICPFRGEYFRLAPEHNQIVNHLIYPI 244
Cdd:COG0654  127 VTGLEQDADGVTVTLADGRTLRADLVVGADGArsavrrLLGIGFTGRDYPQRALWAGVRTELRARLAAAGPRLGELLELS 206
                        170       180
                 ....*....|....*....|.
gi 489936396 245 PDPAMPFLGVHLTRMIDGSVT 265
Cdd:COG0654  207 PRSAFPLRRRRAERWRRGRVV 227
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
113-214 3.60e-05

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 45.59  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936396  113 GLEREWLNAQELREREPNIT---GLGGIFVPSSGIVSYREVTAAMANIFQAKGGEIIYNAEVSALKEHAtGVIVHTRQGQ 189
Cdd:TIGR01377 107 GLEHELLSSKQLKQRFPNIRvprNEVGLLDPNGGVLYAEKALRALQELAEAHGATVRDGTKVVEIEPTE-LLVTVKTTKG 185
                          90       100
                  ....*....|....*....|....*
gi 489936396  190 EYEGATLISCSGLMADRLVKMLGVE 214
Cdd:TIGR01377 186 SYQANKLVVTAGAWTSKLLSPLGIE 210
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
148-198 1.28e-03

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 40.77  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489936396 148 REVTAAMANIFQAKGGEIIYNAEVSALKEHATGVIVHTRQGQEYEGATLIS 198
Cdd:PRK08010 199 RDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIA 249
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
135-198 1.56e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 40.60  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489936396 135 GGIFVPSSGIvsyREVTAAMANIFQAKGGEIIYNAEVSAL---KEHATGviVHTRQGQEYEGATLIS 198
Cdd:COG1233  212 GGVWYPKGGM---GALADALARLAEELGGEIRTGAEVERIlveGGRATG--VRLADGEEIRADAVVS 273
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
135-202 4.76e-03

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: 39.01  E-value: 4.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489936396  135 GGIFVPSSGivsYREVTAAMANifQAKGGEIIYNAEVSALKEHATGVIVHTRQGQEYEGATLISCSGL 202
Cdd:pfam01593 196 GSLLLPRGG---LGALPDALAA--QLLGGDVRLNTRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPL 258
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
144-216 9.86e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 37.64  E-value: 9.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489936396 144 IVSYREVTAAMANIFQAKGGEIIYNAEVSALKEHATGVIVHTRQGQEYEGATLISCSGlMADRLVKMLGVEPG 216
Cdd:COG0644   82 VVDRARFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADG-ARSLLARKLGLKRR 153
 
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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