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Conserved domains on  [gi|18044345|gb|AAH19856|]
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Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAD_lactone_ox super family cl36950
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-433 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


The actual alignment was detected with superfamily member TIGR01678:

Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 723.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345     7 GVQFQNWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    87 VEAGILLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMKADGTVLECSESSKADVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   167 ARVHLGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEPSSASNWF 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKELLDNWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   247 WDYAIGFYLLEFLLWTSTYLPRLVGWINRFFFWLLFN----CKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLE 322
Cdd:TIGR01678 241 WDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGekssTKKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   323 LKAMLEAHPK---VVAHYPVEVRFTRG---DDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHW 396
Cdd:TIGR01678 321 LKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPCFQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHW 400
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 18044345   397 AKAHN-CTRKDFEKMYPAFHKFCDIREKLDPTGMFLNS 433
Cdd:TIGR01678 401 AKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLNS 438
 
Name Accession Description Interval E-value
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-433 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 723.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345     7 GVQFQNWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    87 VEAGILLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMKADGTVLECSESSKADVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   167 ARVHLGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEPSSASNWF 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKELLDNWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   247 WDYAIGFYLLEFLLWTSTYLPRLVGWINRFFFWLLFN----CKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLE 322
Cdd:TIGR01678 241 WDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGekssTKKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   323 LKAMLEAHPK---VVAHYPVEVRFTRG---DDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHW 396
Cdd:TIGR01678 321 LKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPCFQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHW 400
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 18044345   397 AKAHN-CTRKDFEKMYPAFHKFCDIREKLDPTGMFLNS 433
Cdd:TIGR01678 401 AKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLNS 438
ALO pfam04030
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
180-438 1.49e-121

D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.


Pssm-ID: 397924  Cd Length: 259  Bit Score: 353.88  E-value: 1.49e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   180 VTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKE--PSSASNWFWDYAIGFYLLE 257
Cdd:pfam04030   1 VTLRVVPAFTLHSTQEPISFDTLLENWDELLTSSEHFRFWWFPYTDRAVVWRANKTDEPeqPSRPRKSLYDEWLGNGVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   258 FLLWTSTYLPRLVGWINRFFFWLLFNcKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLELKAMLEAHPKVVaHY 337
Cdd:pfam04030  81 ALLWLSRIFPSLTPWVERFSFRLQYG-GDEAVDDSYKVFNMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAALRV-HF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   338 PVEVRFTRGDDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHWAKAHNCTRKDFEKMYPAFHKF 417
Cdd:pfam04030 159 PIEVRCSAADDIWLSPAYGRDTCYINAHMYRPYGRNVPYQKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRF 238
                         250       260
                  ....*....|....*....|.
gi 18044345   418 CDIREKLDPTGMFLNSYLEKV 438
Cdd:pfam04030 239 LQVRKKLDPEGVFLNEYLRRV 259
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
12-439 1.07e-65

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 220.49  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   12 NWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVTVEAGI 91
Cdd:PLN02465  88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDKEKKRVTVQAGA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   92 LLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMK-ADGTvLECSESSKADVFQAARVH 170
Cdd:PLN02465 168 RVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTpAKGT-IELSKEDDPELFRLARCG 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  171 LGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEP----------- 239
Cdd:PLN02465 247 LGGLGVVAEVTLQCVPAHRLVEHTFVSNRKEIKKNHKKWLSENKHIRYMWIPYTDTVVVVTCNPLSKWKeppkikpkyse 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  240 ------------------SSASNWFWDYAIGF-YLLEFLLWTSTYLPRLVGWINRF--FFWllfnckKESSNL----SHK 294
Cdd:PLN02465 327 dervqplrdlykesagtkSSENPEPDIQEMGFgELRDKLLALDPLDPDHVKRVNAAeaEFW------RRSEGYrvgwSDE 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  295 IFSYECRFKQHVQDWAIP-------REKTKEALLELKAMLEAHpKVVAHYPVEVRFTRGDDILLSPCFQ----RDSCYMN 363
Cdd:PLN02465 401 ILGFDCGGQQWVSEVCFPagtlakpSMKDLEFMEELLALIEKE-GIPAPAPIEQRWTASSSSPMSPASSpspdDLHSWVG 479
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  364 IIMYRPYG-----KDVPRL--DYWLAYET-IMKKFGGRPHWAK--------AHNCTRKDFEKMYP--AFHKfcdIREKLD 425
Cdd:PLN02465 480 IIMYLPTEderqrKEITEEffHYRKKTQRnLWDKYSAYEHWAKievpkdkeELEALRERLRKRFPvdAFNK---ARKELD 556
                        490
                 ....*....|....
gi 18044345  426 PTGMFLNSYLEKVF 439
Cdd:PLN02465 557 PKGILSNNLLEKLF 570
GlcD COG0277
FAD/FMN-containing dehydrogenase [Energy production and conversion];
27-435 7.61e-38

FAD/FMN-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 223354 [Multi-domain]  Cd Length: 459  Bit Score: 143.11  E-value: 7.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  27 PTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTD-GFMIHMGKMNRVLQVDKEKKQVTVEAGILLTDLHPQLDKHGL 105
Cdd:COG0277  38 PKSEEEVAAILRLANENGIPVVPRGGGTSLSGGAVPDgGVVLDLSRLNRILEIDPEDGTATVQAGVTLEDLEKALAPHGL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 106 ALSNLGAVSD-VTVGGVIGSGTHNT-GIKHGILATQVVALTLMKADGTVLECSESSKADVFQ----AARVH-LGCLGVIL 178
Cdd:COG0277 118 FLPVDPSSSGtATIGGNIATNAGGLrSLRYGLTRDNVLGLRVVLPDGEILRLGRKLRKDNAGydltALFVGsEGTLGIIT 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 179 TVTLQCVP---QFHLLETSFPSTLKEVLDNLDSHLKKSEY------FRFLWFPHSENVSIIYQDHTNKEPsSASNWFWDY 249
Cdd:COG0277 198 EATLKLLPlpeTKATAVAGFPSIEAAARLAVAAIALLEALgvipaaLEFMDRPIKAAEAYLGGGALPLEA-PARLLVEVE 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 250 AIGFYLLEFLLWT-STYLPRLVGWINRFF---------FWllfnckKESSNLSHKIFSYECRFKQHvqDWAIPREKTKEA 319
Cdd:COG0277 277 GSDEAAVDEALEAlGELLLEHGLARDLVVaqdlaeaarLW------LARKGALAAAGALGPGVIQE--DVVVPLEALPEF 348
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 320 LLELKAMLEAHPKVVahyPVEVRFTRGDDILLSPcfqrdscymniIMYRPYGKDVPRLDYWLAYETIMK---KFGGRPHW 396
Cdd:COG0277 349 LREILALLDKAGLAL---RVALFGHAGDGNLHLN-----------ILYDVGDEAEELARAEALNEAIEAlavELGGSISG 414
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 18044345 397 AKAHNCTRKDFEKMYP--AFHKFCDIREKLDPTGMFLNSYL 435
Cdd:COG0277 415 EHGIGRTKAEFLELEPgeAWALLRAIKRAFDPNGIFNPGKL 455
 
Name Accession Description Interval E-value
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
7-433 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 723.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345     7 GVQFQNWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    87 VEAGILLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMKADGTVLECSESSKADVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   167 ARVHLGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEPSSASNWF 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKELLDNWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   247 WDYAIGFYLLEFLLWTSTYLPRLVGWINRFFFWLLFN----CKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLE 322
Cdd:TIGR01678 241 WDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGekssTKKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   323 LKAMLEAHPK---VVAHYPVEVRFTRG---DDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHW 396
Cdd:TIGR01678 321 LKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPCFQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHW 400
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 18044345   397 AKAHN-CTRKDFEKMYPAFHKFCDIREKLDPTGMFLNS 433
Cdd:TIGR01678 401 AKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLNS 438
ALO pfam04030
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
180-438 1.49e-121

D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.


Pssm-ID: 397924  Cd Length: 259  Bit Score: 353.88  E-value: 1.49e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   180 VTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKE--PSSASNWFWDYAIGFYLLE 257
Cdd:pfam04030   1 VTLRVVPAFTLHSTQEPISFDTLLENWDELLTSSEHFRFWWFPYTDRAVVWRANKTDEPeqPSRPRKSLYDEWLGNGVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   258 FLLWTSTYLPRLVGWINRFFFWLLFNcKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLELKAMLEAHPKVVaHY 337
Cdd:pfam04030  81 ALLWLSRIFPSLTPWVERFSFRLQYG-GDEAVDDSYKVFNMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAALRV-HF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   338 PVEVRFTRGDDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHWAKAHNCTRKDFEKMYPAFHKF 417
Cdd:pfam04030 159 PIEVRCSAADDIWLSPAYGRDTCYINAHMYRPYGRNVPYQKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRF 238
                         250       260
                  ....*....|....*....|.
gi 18044345   418 CDIREKLDPTGMFLNSYLEKV 438
Cdd:pfam04030 239 LQVRKKLDPEGVFLNEYLRRV 259
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
12-439 1.07e-65

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 220.49  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   12 NWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVTVEAGI 91
Cdd:PLN02465  88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDKEKKRVTVQAGA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   92 LLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMK-ADGTvLECSESSKADVFQAARVH 170
Cdd:PLN02465 168 RVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTpAKGT-IELSKEDDPELFRLARCG 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  171 LGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEP----------- 239
Cdd:PLN02465 247 LGGLGVVAEVTLQCVPAHRLVEHTFVSNRKEIKKNHKKWLSENKHIRYMWIPYTDTVVVVTCNPLSKWKeppkikpkyse 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  240 ------------------SSASNWFWDYAIGF-YLLEFLLWTSTYLPRLVGWINRF--FFWllfnckKESSNL----SHK 294
Cdd:PLN02465 327 dervqplrdlykesagtkSSENPEPDIQEMGFgELRDKLLALDPLDPDHVKRVNAAeaEFW------RRSEGYrvgwSDE 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  295 IFSYECRFKQHVQDWAIP-------REKTKEALLELKAMLEAHpKVVAHYPVEVRFTRGDDILLSPCFQ----RDSCYMN 363
Cdd:PLN02465 401 ILGFDCGGQQWVSEVCFPagtlakpSMKDLEFMEELLALIEKE-GIPAPAPIEQRWTASSSSPMSPASSpspdDLHSWVG 479
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  364 IIMYRPYG-----KDVPRL--DYWLAYET-IMKKFGGRPHWAK--------AHNCTRKDFEKMYP--AFHKfcdIREKLD 425
Cdd:PLN02465 480 IIMYLPTEderqrKEITEEffHYRKKTQRnLWDKYSAYEHWAKievpkdkeELEALRERLRKRFPvdAFNK---ARKELD 556
                        490
                 ....*....|....
gi 18044345  426 PTGMFLNSYLEKVF 439
Cdd:PLN02465 557 PKGILSNNLLEKLF 570
GLDHase TIGR01676
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ...
12-439 7.50e-46

galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.


Pssm-ID: 130737  Cd Length: 541  Bit Score: 166.39  E-value: 7.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    12 NWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVTVEAGI 91
Cdd:TIGR01676  53 NWSGTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGLSRAGMVNLALMDKVLEVDEEKKRVRVQAGI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    92 LLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMKADGTVLECSESSKADVFQAARVHL 171
Cdd:TIGR01676 133 RVQQLVDAIKEYGITLQNFASIREQQIGGIIQVGAHGTGAKLPPIDEQVIAMKLVTPAKGTIEISKDKDPELFFLARCGL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   172 GCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNK---EPSSASNWFWD 248
Cdd:TIGR01676 213 GGLGVVAEVTLQCVERQELVEHTFISNMKDIKKNHKKFLADNKHVKYLHIPYTDAIVVVTCNPISKsrgPPKFKPKYTSE 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   249 YAIGFYLLEFLLWTSTYLPRLVGW------INRFFFWLL------------------------FNCKKESSNL--SHKIF 296
Cdd:TIGR01676 293 EAIQHVRDLYRESLKKYRGQVADSaseepdIDEFSFTELrdkllaldplnkehvieinkaeaeFWRKSEGYKVgwSDEIL 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   297 SYECRFKQHVQD-------WAIPREKTKEALLELKAMLEAHpKVVAHYPVEVRFTRGDDILLSPCFQRDS----CYMNII 365
Cdd:TIGR01676 373 GFDCGGHQWVSEtcfpagtLAKPNMKDIEYIEELKQLIEKE-NIPAPAPIEQRWTACSKSPMSPASSSADddifSWVGII 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   366 MYRPYGKDVPR---LDYWLAYETIMK-----KFGGRPHWAKAHNCTRKD--------FEKMYPAfHKFCDIREKLDPTGM 429
Cdd:TIGR01676 452 MYLPTMDARQRkeiTEEFFHYRHLTQallwdHFSAFEHWAKIEVPKDKDelaalqarLKKKFPV-DASNKARKALDPNKI 530
                         490
                  ....*....|
gi 18044345   430 FLNSYLEKVF 439
Cdd:TIGR01676 531 LSNNKLEKLF 540
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
21-156 9.18e-40

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 396238 [Multi-domain]  Cd Length: 139  Bit Score: 139.26  E-value: 9.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    21 PEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIAC-TDGFMIHMGKMNRVLQVDKEKKQVTVEAGILLTDLHPQ 99
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVqTGGVVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18044345   100 LDKHGLALS-NLGAVSDVTVGGVIGSGTHNTG-IKHGILATQVVALTLMKADGTVLECS 156
Cdd:pfam01565  81 LAAKGLLLGlDPGSGIPGTVGGAIATNAGGYGsEKYGLTRDNVLGLEVVLADGEVVRLS 139
GlcD COG0277
FAD/FMN-containing dehydrogenase [Energy production and conversion];
27-435 7.61e-38

FAD/FMN-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 223354 [Multi-domain]  Cd Length: 459  Bit Score: 143.11  E-value: 7.61e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  27 PTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTD-GFMIHMGKMNRVLQVDKEKKQVTVEAGILLTDLHPQLDKHGL 105
Cdd:COG0277  38 PKSEEEVAAILRLANENGIPVVPRGGGTSLSGGAVPDgGVVLDLSRLNRILEIDPEDGTATVQAGVTLEDLEKALAPHGL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 106 ALSNLGAVSD-VTVGGVIGSGTHNT-GIKHGILATQVVALTLMKADGTVLECSESSKADVFQ----AARVH-LGCLGVIL 178
Cdd:COG0277 118 FLPVDPSSSGtATIGGNIATNAGGLrSLRYGLTRDNVLGLRVVLPDGEILRLGRKLRKDNAGydltALFVGsEGTLGIIT 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 179 TVTLQCVP---QFHLLETSFPSTLKEVLDNLDSHLKKSEY------FRFLWFPHSENVSIIYQDHTNKEPsSASNWFWDY 249
Cdd:COG0277 198 EATLKLLPlpeTKATAVAGFPSIEAAARLAVAAIALLEALgvipaaLEFMDRPIKAAEAYLGGGALPLEA-PARLLVEVE 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 250 AIGFYLLEFLLWT-STYLPRLVGWINRFF---------FWllfnckKESSNLSHKIFSYECRFKQHvqDWAIPREKTKEA 319
Cdd:COG0277 277 GSDEAAVDEALEAlGELLLEHGLARDLVVaqdlaeaarLW------LARKGALAAAGALGPGVIQE--DVVVPLEALPEF 348
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345 320 LLELKAMLEAHPKVVahyPVEVRFTRGDDILLSPcfqrdscymniIMYRPYGKDVPRLDYWLAYETIMK---KFGGRPHW 396
Cdd:COG0277 349 LREILALLDKAGLAL---RVALFGHAGDGNLHLN-----------ILYDVGDEAEELARAEALNEAIEAlavELGGSISG 414
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 18044345 397 AKAHNCTRKDFEKMYP--AFHKFCDIREKLDPTGMFLNSYL 435
Cdd:COG0277 415 EHGIGRTKAEFLELEPgeAWALLRAIKRAFDPNGIFNPGKL 455
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
27-430 2.11e-36

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 140.38  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345    27 PTSVGEVREVLALARQQNKKVKVVGG-GHSPSDIACTDG----FMIHMGKMNRVLQVDKEKKQVTVEAGILLTDLHPQLD 101
Cdd:TIGR01677  38 PKTEAELVSVVAAATAAGRKMKVVTRySHSIPKLACPDGsdgaLLISTKRLNHVVAVDATAMTVTVESGMSLRELIVEAE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   102 KHGLALSNLGAVSDVTVGGVIGSGTHNTGI--KHGILATQVVALTLM----KADG--TVLECSESSKADVFQAARVHLGC 173
Cdd:TIGR01677 118 KAGLALPYAPYWWGLTVGGMMGTGAHGSSLwgKGSAVHDYVVGIRLVvpasAAEGfaKVRILSEGDTPNEFNAAKVSLGV 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   174 LGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDhtnKEPSSASnwfwdyaiGF 253
Cdd:TIGR01677 198 LGVISQVTLALQPMFKRSVTYTMRDDSDFEDQFVTFGKKHEFADITWYPSQGKAVYRRDD---RVPVNAS--------GN 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   254 YLLEFLLWTSTylPRLVGWINRFFFWLLFNCKKES--------------------SNLSHKIFS---------------- 297
Cdd:TIGR01677 267 GVNDFLGFRST--LIAAIAGIRALEETFERSRNANgkcvtatitsaalflpgyglTNSGGIIFTgypvvgsqgrmqtsgs 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   298 ------------------YECRFKQHVQDWAIPREKTKEALLELKAMLEAHPK----VVAHYPVEVRFTRGDDILLSPcf 355
Cdd:TIGR01677 345 cldspqdglltacawdprYKGLFFFHQTTLSVPVSRFRDFVLDVKRLRDMEPKslcgVELYNGILIRYVKASPAYLGK-- 422
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18044345   356 QRDSCYMNIIMYRPYGKDVPRL--DYWLAYETI-MKKFGGRPHWAKAHNCTRKDFEKMYPAFHKFCDIREKLDPTGMF 430
Cdd:TIGR01677 423 EEDAVDFDFTYYRAKDPLTPRLyeDVIEEIEQMaFFKYGALPHWGKNRNLAFDGVIRKYPNADKFLKVKDSYDPKGLF 500
PLN00107 PLN00107
FAD-dependent oxidoreductase; Provisional
310-439 3.24e-08

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 165679  Cd Length: 257  Bit Score: 54.21  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  310 AIPREKTKEALLELKAMLEAHPKVVA----HYPVEVRFTRGddillSPCFQR---DSCYMNIIMYRpyGKD---VPRL-- 377
Cdd:PLN00107  68 SVPLSGAAAFINDIKALRDIEPDALCglelNYGVLLRYVRA-----SPAHLGkeeDALDFDLTYYR--SKDdpaAPRLhe 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18044345  378 DYWLAYETI-MKKFGGRPHWAKAHNCTRKDFEKMYPAFHKFCDIREKLDPTGMFLNSYLEKVF 439
Cdd:PLN00107 141 DAMEEIEQMaILKYGALPHWGKNRNAAFDGAIAKYKKAGEFLKVKERLDPEGLFSSEWSDKIL 203
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis];
22-183 1.11e-05

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223882 [Multi-domain]  Cd Length: 291  Bit Score: 46.82  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  22 EMYYQPTSVGEVREVLALARQQNKKVKVVGGGhspSDIACTDGFM---IHMGKMNRVLQVDKEKKQVTVEAGILLTDLHP 98
Cdd:COG0812  22 EVLVEPRDIEELKAALKYAKAEDLPVLILGGG---SNLLVRDGGIggvVIKLGKLNFIEIEGDDGLIEAGAGAPWHDLVR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345  99 QLDKHGLA-LSNLGAVSDvTVGG--VIGSGTHNTGIKHGilatqVVALTLMKADGTVL-----ECSESSKADVFQAARvh 170
Cdd:COG0812  99 FALENGLSgLEFLAGIPG-SVGGavIMNAGAYGVEISDV-----LVSVEVLDRDGEVRwlsaeELGFGYRTSPFKKEY-- 170
                       170
                ....*....|...
gi 18044345 171 lgclGVILTVTLQ 183
Cdd:COG0812 171 ----LVVLSVEFK 179
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
24-106 2.41e-05

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 45.87  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18044345   24 YYQPTSVGEVREVLALARQQNKKVKVVGGGhspSDIACTD----GFMIHMGKMNRVLQVDKEkkQVTVEAGILLTDLHPQ 99
Cdd:PRK13905  34 LVEPADIEDLQEFLKLLKENNIPVTVLGNG---SNLLVRDggirGVVIRLGKGLNEIEVEGN--RITAGAGAPLIKLARF 108

                 ....*..
gi 18044345  100 LDKHGLA 106
Cdd:PRK13905 109 AAEAGLS 115
 
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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