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Conserved domains on  [gi|6754156|ref|NP_034533|]
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hydroxyacid oxidase 1 [Mus musculus]

Protein Classification

alpha-hydroxy-acid oxidizing protein (domain architecture ID 12014085)

FMN-dependent alpha-hydroxyacid oxidizing protein such as bacterial L-lactate dehydrogenase or eukaryotic 2-hydroxy-acid oxidase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FMN_dh pfam01070
FMN-dependent dehydrogenase;
16-362 0e+00

FMN-dependent dehydrogenase;


:

Pssm-ID: 395850  Cd Length: 350  Bit Score: 512.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     16 RSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATV 95
Cdd:pfam01070   2 RKRLPRFAFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQTLSLPFGIAPVGMQGLAHPDGELALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     96 RACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRF 175
Cdd:pfam01070  82 RAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    176 KLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKH 250
Cdd:pfam01070 161 TLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    251 GVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQ 330
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 6754156    331 DVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 319 HALEILRDELERTMALLGCTSIADLTPSLLRR 350
 
Name Accession Description Interval E-value
FMN_dh pfam01070
FMN-dependent dehydrogenase;
16-362 0e+00

FMN-dependent dehydrogenase;


Pssm-ID: 395850  Cd Length: 350  Bit Score: 512.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     16 RSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATV 95
Cdd:pfam01070   2 RKRLPRFAFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQTLSLPFGIAPVGMQGLAHPDGELALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     96 RACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRF 175
Cdd:pfam01070  82 RAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    176 KLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKH 250
Cdd:pfam01070 161 TLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    251 GVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQ 330
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 6754156    331 DVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 319 HALEILRDELERTMALLGCTSIADLTPSLLRR 350
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
9-357 2.23e-169

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203  Cd Length: 299  Bit Score: 474.24  E-value: 2.23e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02809   1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRi 168
Cdd:cd02809  81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  169 ddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqaidpsLSWDDITWLRRLTSLPIVVKGILRGDDAKEAV 248
Cdd:cd02809 159 ------------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  249 KHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
                       330       340
                ....*....|....*....|....*....
gi 6754156  329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
8-357 4.51e-140

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134  Cd Length: 367  Bit Score: 402.57  E-value: 4.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     8 ISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:PLN02493   6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493  86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   168 IDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   248 VKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
                        330       340       350
                 ....*....|....*....|....*....|
gi 6754156   328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
8-361 3.20e-124

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only];


Pssm-ID: 224223  Cd Length: 360  Bit Score: 361.99  E-value: 3.20e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    8 ISDYEQHVRSVLQKsVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:COG1304   1 VADLRRAAQRRLPK-AFHYIDGGAEDEVTLRRNREAFEDIALRPRVLPEVDDIDLSTTFLGQKLSAPIIIAPMTGGGLAH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPealrwMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:COG1304  80 PEGEVINAKLAAAAGEPFILSTVGSQRIEEVAAAPP-----FQLYFSKDREFAPNLVDRAANAGAKQLVLTVDSPVGGER 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  168 IDDVRNRFKLPPQLRMKNFEtnDLAFSPKGN---FGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDA 244
Cdd:COG1304 155 ERDAVNGISAPALAIHLNVL--QEATQPEGDrdgKGGLDSIAEYVSALSVPVISKEDGAGISKEWAGPLVLKGILAPEDA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  245 KEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQ 324
Cdd:COG1304 233 AGAGGTGADGIEVSNHGGRQLDWGISTADSLPEIVEAVGDRIEVIADGGIRSGLDVAKALALGADAVGIGRPFLYGLAAG 312
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 6754156  325 GEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 313 GEAGVERVLEIIRKELKIAMALTGAKNIEELKRVPLV 349
L_lactate_LldD NF033901
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ...
9-361 3.08e-80

FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.


Pssm-ID: 411463  Cd Length: 377  Bit Score: 250.12  E-value: 3.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:NF033901   7 TDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYAR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRI 168
Cdd:NF033901  87 RGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPM-WFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   169 DDVRNRFKLP--PQLRMKNFETN-----DLAFSPK----GNF----GDNSGLAEYV---AQAIDPSLSWDDITWLRRLTS 230
Cdd:NF033901 166 RDAHSGMSGPnaALRRMLQAVTHpqwawDVGLLGRphdlGNIsayrGKPTGLEDYIgwlGNNFDPSISWKDLEWIREFWD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   231 LPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKA 310
Cdd:NF033901 246 GPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGADS 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6754156   311 VFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK-TLVR 361
Cdd:NF033901 326 VLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRdSLVQ 377
 
Name Accession Description Interval E-value
FMN_dh pfam01070
FMN-dependent dehydrogenase;
16-362 0e+00

FMN-dependent dehydrogenase;


Pssm-ID: 395850  Cd Length: 350  Bit Score: 512.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     16 RSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATV 95
Cdd:pfam01070   2 RKRLPRFAFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQTLSLPFGIAPVGMQGLAHPDGELALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     96 RACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRF 175
Cdd:pfam01070  82 RAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    176 KLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKH 250
Cdd:pfam01070 161 TLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    251 GVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQ 330
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
                         330       340       350
                  ....*....|....*....|....*....|..
gi 6754156    331 DVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 319 HALEILRDELERTMALLGCTSIADLTPSLLRR 350
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
9-357 2.23e-169

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203  Cd Length: 299  Bit Score: 474.24  E-value: 2.23e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02809   1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRi 168
Cdd:cd02809  81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  169 ddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqaidpsLSWDDITWLRRLTSLPIVVKGILRGDDAKEAV 248
Cdd:cd02809 159 ------------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  249 KHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
                       330       340
                ....*....|....*....|....*....
gi 6754156  329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
8-357 4.51e-140

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134  Cd Length: 367  Bit Score: 402.57  E-value: 4.51e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     8 ISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:PLN02493   6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493  86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   168 IDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   248 VKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
                        330       340       350
                 ....*....|....*....|....*....|
gi 6754156   328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
PLN02535 PLN02535
glycolate oxidase
1-361 2.46e-138

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 398.05  E-value: 2.46e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     1 MLPRLVCISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGAT 80
Cdd:PLN02535   1 MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    81 AMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAeAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVD 160
Cdd:PLN02535  81 AMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVA-SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   161 TPYLGNRIDDVRNRFKLPpqlRMKNFETndlAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILR 240
Cdd:PLN02535 160 VPRLGRREADIKNKMISP---QLKNFEG---LLSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   241 GDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWG 320
Cdd:PLN02535 234 REDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYG 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 6754156   321 LAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:PLN02535 314 LAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
9-353 1.41e-130

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238  Cd Length: 344  Bit Score: 377.32  E-value: 1.41e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02922   1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPE-ALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:cd02922  81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  168 IDDVRNRFKlppqlrmknfETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEA 247
Cdd:cd02922 161 ERDERLKAE----------EAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  248 VKHGVDGILVSNHGARQLDGVPATIDVLPEIVE---AVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQ 324
Cdd:cd02922 231 AEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAY 310
                       330       340
                ....*....|....*....|....*....
gi 6754156  325 GEKGVQDVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02922 311 GEEGVEKAIQILKDEIETTMRLLGVTSLD 339
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
9-360 2.50e-128

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448  Cd Length: 383  Bit Score: 373.16  E-value: 2.50e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd03332  22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRI 168
Cdd:cd03332 102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  169 DDVRNRFKlpPQLRMKNFE--TNDLAF------SPKGNFGDNSGLAEYVAQAI----DPSLSWDDITWLRRLTSLPIVVK 236
Cdd:cd03332 182 RDLDLGYL--PFLRGIGIAnyFSDPVFrkklaePVGEDPEAPPPMEAAVARFVsvfsGPSLTWEDLAFLREWTDLPIVLK 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  237 GILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRP 316
Cdd:cd03332 260 GILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRP 339
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 6754156  317 IIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV 360
Cdd:cd03332 340 YAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
PLN02979 PLN02979
glycolate oxidase
51-357 1.60e-126

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 368.28  E-value: 1.60e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    51 PRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQ 130
Cdd:PLN02979  48 PRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQ 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   131 LYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVA 210
Cdd:PLN02979 127 LYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVA 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   211 QAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFL 290
Cdd:PLN02979 204 GQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFL 283
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754156   291 DGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02979 284 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
8-361 3.20e-124

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only];


Pssm-ID: 224223  Cd Length: 360  Bit Score: 361.99  E-value: 3.20e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    8 ISDYEQHVRSVLQKsVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:COG1304   1 VADLRRAAQRRLPK-AFHYIDGGAEDEVTLRRNREAFEDIALRPRVLPEVDDIDLSTTFLGQKLSAPIIIAPMTGGGLAH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPealrwMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNR 167
Cdd:COG1304  80 PEGEVINAKLAAAAGEPFILSTVGSQRIEEVAAAPP-----FQLYFSKDREFAPNLVDRAANAGAKQLVLTVDSPVGGER 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  168 IDDVRNRFKLPPQLRMKNFEtnDLAFSPKGN---FGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDA 244
Cdd:COG1304 155 ERDAVNGISAPALAIHLNVL--QEATQPEGDrdgKGGLDSIAEYVSALSVPVISKEDGAGISKEWAGPLVLKGILAPEDA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  245 KEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQ 324
Cdd:COG1304 233 AGAGGTGADGIEVSNHGGRQLDWGISTADSLPEIVEAVGDRIEVIADGGIRSGLDVAKALALGADAVGIGRPFLYGLAAG 312
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 6754156  325 GEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 313 GEAGVERVLEIIRKELKIAMALTGAKNIEELKRVPLV 349
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
10-358 2.73e-118

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088  Cd Length: 351  Bit Score: 346.74  E-value: 2.73e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   10 DYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04737  10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRID 169
Cdd:cd04737  90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  170 DVRNRFKLPpqLRMKNFEtNDLAFSPKGnfgdnSGLAEYVAQAiDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVK 249
Cdd:cd04737 170 DIRNKFQFP--FGMPNLN-HFSEGTGKG-----KGISEIYAAA-KQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAIN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  250 HGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGV 329
Cdd:cd04737 241 AGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGV 320
                       330       340
                ....*....|....*....|....*....
gi 6754156  330 QDVLEILKEEFRLAMALSGCQNVKVIDKT 358
Cdd:cd04737 321 ASVLEHLNKELKIVMQLAGTRTIEDVKRT 349
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
10-357 4.01e-92

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 280.18  E-value: 4.01e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   10 DYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04736   2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKdREISRQIVKRAEKQGYKAIFVTVDTPYLGNRID 169
Cdd:cd04736  82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  170 DVRNRFKLP--------------PQLRMKNFETNDLAfspKGNFG--DNSGLAEYVA---QAIDPSLSWDDITWLRRLTS 230
Cdd:cd04736 160 DLRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQ---LANFAsdDAIDVEVQAAlmsRQMDASFNWQDLRWLRDLWP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  231 LPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKA 310
Cdd:cd04736 237 HKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANA 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 6754156  311 VFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
lldD PRK11197
L-lactate dehydrogenase; Provisional
7-366 2.78e-89

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 273.44  E-value: 2.78e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     7 CISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPIC---VGATAMq 83
Cdd:PRK11197   5 AASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVAlapVGLTGM- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    84 cMAHvDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPY 163
Cdd:PRK11197  84 -YAR-RGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   164 LGNRIDDVRNRFKLPP-------QLRMKNFETNDLAFSPK----GN----FGDNSGLAEYVAQA---IDPSLSWDDITWL 225
Cdd:PRK11197 161 PGARYRDAHSGMSGPNaamrrylQAVTHPQWAWDVGLNGRphdlGNisayLGKPTGLEDYIGWLgnnFDPSISWKDLEWI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   226 RRLTSLPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALA 305
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754156   306 LGAKAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLA 366
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGNAA 381
L_lactate_LldD NF033901
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ...
9-361 3.08e-80

FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.


Pssm-ID: 411463  Cd Length: 377  Bit Score: 250.12  E-value: 3.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156     9 SDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:NF033901   7 TDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYAR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRI 168
Cdd:NF033901  87 RGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPM-WFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   169 DDVRNRFKLP--PQLRMKNFETN-----DLAFSPK----GNF----GDNSGLAEYV---AQAIDPSLSWDDITWLRRLTS 230
Cdd:NF033901 166 RDAHSGMSGPnaALRRMLQAVTHpqwawDVGLLGRphdlGNIsayrGKPTGLEDYIgwlGNNFDPSISWKDLEWIREFWD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   231 LPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKA 310
Cdd:NF033901 246 GPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGADS 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6754156   311 VFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK-TLVR 361
Cdd:NF033901 326 VLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRdSLVQ 377
PRK05437 PRK05437
isopentenyl pyrophosphate isomerase; Provisional
56-353 9.30e-18

isopentenyl pyrophosphate isomerase; Provisional


Pssm-ID: 235465  Cd Length: 352  Bit Score: 83.28  E-value: 9.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    56 NVADIDLSTSVLGQRVSMPICVGAtamqcM-------AHVDGELAtvRACQTMGTGMMLSSwatSSIeevaeagpeALRw 128
Cdd:PRK05437  44 DLDDIDLSTEFLGKKLSAPFLINA-----MtggsekaKEINRKLA--EAAEELGIAMGVGS---QRA---------ALK- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   129 mqlyiYKDREISRQIVKRaekqgykaifVTVDTPYLGNriddvrnrfkL-PPQLRMKNFE-----------------TND 190
Cdd:PRK05437 104 -----DPELADSFSVVRK----------VAPDGLLFAN----------LgAVQLYGYGVEeaqravemieadalqihLNP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   191 L--AFSPKG--NFgdnSGLAEYVAQaidpslswdditwLRRLTSLPIVVK----GILRgDDAKEAVKHGVDGILVSNHG- 261
Cdd:PRK05437 159 LqeLVQPEGdrDF---RGWLDNIAE-------------IVSALPVPVIVKevgfGISK-ETAKRLADAGVKAIDVAGAGg 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   262 --------ARQLD----------GVPaTIDVLPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAF 323
Cdd:PRK05437 222 tswaaienYRARDdrlasyfadwGIP-TAQSLLEARSLLP-DLPIIASGGIRNGLDIAKALALGADAVGMAGPFLKAALE 299
                        330       340       350
                 ....*....|....*....|....*....|
gi 6754156   324 QGEKGVQDVLEILKEEFRLAMALSGCQNVK 353
Cdd:PRK05437 300 GGEEAVIELIEQWIEELKIAMFLTGAKNIA 329
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
56-353 2.00e-17

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205  Cd Length: 326  Bit Score: 82.16  E-value: 2.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   56 NVADIDLSTSVLGQRVSMPICVGAtamqcM-------AHVDGELAtvRACQTMGTGMMLSS----------WATSSIeeV 118
Cdd:cd02811  36 DLDDIDLSTEFLGKRLSAPLLISA-----MtggsekaKEINRNLA--EAAEELGIAMGVGSqraaledpelAESFTV--V 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  119 AEAGPEALRWMQLYIYKDREISRQIVKRA-EKQGYKAIFVTVdtpylgnriddvrNrfklPPQlrmknfEtndlAFSPKG 197
Cdd:cd02811 107 REAPPNGPLIANLGAVQLNGYGVEEARRAvEMIEADALAIHL-------------N----PLQ------E----AVQPEG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  198 --NFgdnSGLAEYVAQaidpslswdditwLRRLTSLPIVVK----GILRgDDAKEAVKHGVDGILVSNHG---------A 262
Cdd:cd02811 160 drDF---RGWLERIEE-------------LVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGgtswarvenY 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  263 RQLD------------GVPaTIDVLPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIwGLAFQGEKGVQ 330
Cdd:cd02811 223 RAKDsdqrlaeyfadwGIP-TAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVI 299
                       330       340
                ....*....|....*....|...
gi 6754156  331 DVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02811 300 ETIEQIIEELRTAMFLTGAKNLA 322
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
204-315 1.44e-09

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 57.21  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  204 GLAEYVAQAIDPSLSWDDITWLR-RLTSLPIVVKGILRG-DDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEA 281
Cdd:cd04722  87 GVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGeLAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
                        90       100       110
                ....*....|....*....|....*....|....
gi 6754156  282 VEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
242-314 7.40e-08

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 52.49  E-value: 7.40e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6754156  242 DDAKEAVKHGVDGILVSN-----HGARQLDGvpaTIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:cd04730 113 EEARKAEAAGADALVAQGaeaggHRGTFDIG---TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
232-316 8.17e-08

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organisms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287  Cd Length: 367  Bit Score: 53.49  E-value: 8.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    232 PIVVK---GILRGDDAKEAVKHGVDGILVSNH----GA-----RQLDGVPaTIDVLPEIVEAV--EG---KVEVFLDGGV 294
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYdggtGAspktsIKHAGLP-WELALAEAHQTLkeNGlrdRVSLIADGGL 282
                          90       100
                  ....*....|....*....|..
gi 6754156    295 RKGTDVLKALALGAKAVFVGRP 316
Cdd:pfam01645 283 RTGADVAKAAALGADAVYIGTA 304
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
222-315 1.86e-07

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202  Cd Length: 392  Bit Score: 52.54  E-value: 1.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  222 ITWLRRLT-SLPIVVK---GILRGDDAkEAVKHG-VDGILVSNH----GARQLD-----GVPaTIDVLPEIVEA-----V 282
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaGHGEGDIA-AGVAAAgADFITIDGAeggtGAAPLTfidhvGLP-TELGLARAHQAlvkngL 282
                        90       100       110
                ....*....|....*....|....*....|...
gi 6754156  283 EGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd02808 283 RDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism];
225-315 7.93e-07

Glutamate synthase domain 2 [Amino acid transport and metabolism];


Pssm-ID: 223147  Cd Length: 485  Bit Score: 50.72  E-value: 7.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  225 LRRLTSL-PIVVK-----GIlrGDDAKEAVKHGVDGILVSNH----GARQLD-----GVPaTIDVLPEIVEAVEG----- 284
Cdd:COG0069 297 LKEANPWaKISVKlvaehGV--GTIAAGVAKAGADVITIDGAdggtGASPLTsidhaGIP-WELGLAETHQTLVLnglrd 373
                        90       100       110
                ....*....|....*....|....*....|.
gi 6754156  285 KVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:COG0069 374 KVKLIADGGLRTGADVAKAAALGADAVGFGT 404
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
244-314 4.62e-06

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 224981 [Multi-domain]  Cd Length: 336  Bit Score: 47.71  E-value: 4.62e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754156  244 AKEAVKHGVDGILVsnHGAR------QLDGVPATIDVLPEIVEAVEGkVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:COG2070 140 ALKAERAGADAVIA--QGAEagghrgGVDLEVSTFALVPEVVDAVDG-IPVIAAGGIADGRGIAAALALGADGVQMG 213
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
222-316 1.09e-04

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 43.66  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  222 ITWLRRL-TSLPIVVKGILRGDDAKEAVKHGVDGILV-----SNHGARQLDGV--P---ATIDVlpeiVEAVEG-KVEVF 289
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvPqatAVADV----AAAARDyGVPVI 201
                        90       100
                ....*....|....*....|....*..
gi 6754156  290 LDGGVRKGTDVLKALALGAKAVFVGRP 316
Cdd:cd00381 202 ADGGIRTSGDIVKALAAGADAVMLGSL 228
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
220-315 2.37e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 43.03  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156   220 DDITWLRRLT-SLPIVVKGILRGDDAKEAVKHGVDGI-------------LVSNHGARQLDGVpatIDVLPEiveAVEGK 285
Cdd:PTZ00314 271 DMIKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAV---YHVARY---ARERG 344
                         90       100       110
                 ....*....|....*....|....*....|
gi 6754156   286 VEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:PTZ00314 345 VPCIADGGIKNSGDICKALALGADCVMLGS 374
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
266-354 4.50e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism];


Pssm-ID: 223184  Cd Length: 241  Bit Score: 38.33  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  266 DGVPATIDVLPEIVEAVEGKVEVflDGGVRKGTDVLKALALGAKAVfvgrpIIWGLAFQGEKGVQDVLEILKEefRLAMA 345
Cdd:COG0106  58 AGGPRNLEAIKEILEATDVPVQV--GGGIRSLEDVEALLDAGVARV-----IIGTAAVKNPDLVKELCEEYGD--RIVVA 128

                ....*....
gi 6754156  346 LSgCQNVKV 354
Cdd:COG0106 129 LD-ARDGKV 136
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
233-314 7.18e-03

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 37.88  E-value: 7.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156    233 IVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATID-----VLPEIVEAVEgkVEVFLDGGVRKGTDVLKALALG 307
Cdd:pfam03060 138 ALIPTISSAKEARIAEARGADALIVQGPEAGGHQGTPEYGDkglfrLVPQVPDAVD--IPVIAAGGIWDRRGVAAALALG 215

                  ....*..
gi 6754156    308 AKAVFVG 314
Cdd:pfam03060 216 ASGVQMG 222
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
237-319 9.53e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 37.58  E-value: 9.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754156  237 GILRGDDAKEAVKH----GVDGILVSNHGAR--QLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKA 310
Cdd:cd04735 230 PGIRMEDTLALVDKladkGLDYLHISLWDFDrkSRRGRDDNQTIMELVKERIAGRLPLIAVGSINTPDDALEALETGADL 309

                ....*....
gi 6754156  311 VFVGRPIIW 319
Cdd:cd04735 310 VAIGRGLLV 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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