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Conserved domains on  [gi|517056601|ref|WP_018245419|]
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MULTISPECIES: D-amino acid dehydrogenase [Rhizobium]

Protein Classification

D-amino acid dehydrogenase( domain architecture ID 11479161)

D-amino acid dehydrogenase catalyzes the oxidative deamination of D-amino acids to yield the corresponding 2-oxo acids; also able to oxidize D-amino acid analogs

EC:  1.4.99.-
SCOP:  3000055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-415 0e+00

D-amino acid dehydrogenase;


:

Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 825.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPK 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  81 LDMAMLSWMARMLSNCTSERYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAAD 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRHVRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITDASRAPESTVMDETYKIAITRLGDRIRVGGMAEISGY 320
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 321 TNDLGLARRSTLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGDLVS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGgGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400
                        410
                 ....*....|....*.
gi 517056601 400 GRQPEIDARDLAISRY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
 
Name Accession Description Interval E-value
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-415 0e+00

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 825.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPK 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  81 LDMAMLSWMARMLSNCTSERYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAAD 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRHVRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITDASRAPESTVMDETYKIAITRLGDRIRVGGMAEISGY 320
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 321 TNDLGLARRSTLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGDLVS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGgGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400
                        410
                 ....*....|....*.
gi 517056601 400 GRQPEIDARDLAISRY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 5.72e-110

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 327.63  E-value: 5.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQsGPALETSFANAGEVSFGycspWAAPGIPmkamkwlfmkhaplilrpk 80
Cdd:COG0665    3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPG----LAALADR------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  81 ldmamlswmarmlsnctseryainksRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAAD 160
Cdd:COG0665   59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRhvRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD 240
Cdd:COG0665  113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITDAsrAPESTVMDETyKIAITRLGD-RIRVGGMAEISG 319
Cdd:COG0665  191 RGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPLPD--LPLRPVLDDT-GVYLRPTADgRLLVGGTAEPAG 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 320 YTNDLGLARRSTLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPT-KVAGLFLNTGHGTLGWTMSTGSARLIGDL 397
Cdd:COG0665  268 FDRAPTPERLEALLRRLRRLFPAlADAEIVRAWAGLRPMTPDGLPIIGRLpGAPGLYVATGHGGHGVTLAPAAGRLLADL 347
                        410
                 ....*....|....*..
gi 517056601 398 VSGRQPEIDARDLAISR 414
Cdd:COG0665  348 ILGGEPPLDLAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
2-397 2.06e-74

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 235.76  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601    2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYcspwaapgipmkamkwlfmkhaplilrpkl 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGL------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   82 dmamlswmarmlsnctserYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQlEASAKDVKALAADG 161
Cdd:pfam01266  51 -------------------RYLEPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  162 IPYEVLDRDGCVRFEPALrhvrDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGrVRGVITDR 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLL----PGLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVVTTG 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  242 ErmsAEAVVIALGSYSPLLLKPlGIRLPVYPVKGYSLTI-PITDASRAPE--STVMDETYKIAITRLGDRIRVGGMAEIS 318
Cdd:pfam01266 186 E---ADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLePLPEALLILPvpITVDPGRGVYLRPRADGRLLLGGTDEED 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  319 GY-TNDLGLARRSTLEHSVTDLFPG-GDIskASFWSGLRPMtPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGD 396
Cdd:pfam01266 262 GFdDPTPDPEEIEELLEAARRLFPAlADI--ERAWAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAE 338

                  .
gi 517056601  397 L 397
Cdd:pfam01266 339 L 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
17-402 1.68e-31

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


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 122.47  E-value: 1.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   17 YQLAKAGHDVTVVDRQSgpaletsfaNAGEVSfgycspWAAPGipmkamkwlfmkhaplilrpkldmaMLSwmarMLSNC 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRDP---------MGGGAS------WAAAG-------------------------MLA----PHAEC 36
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   97 TSERyainkSRMLRLADYSR----IALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAADGIPYEVLDRDGC 172
Cdd:TIGR02352  37 EYAE-----DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRAL 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  173 VRFEPALRhvrDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAVVIA 252
Cdd:TIGR02352 112 RRLEPYLS---GGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGDVQADQVVLA 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  253 LGSYSPLLLKplgirLPVYPVKGYSLTIPITDASRAP---ESTVMDETYKIaITRLGDRIRVGGMAEISGY--TNDLGLA 327
Cdd:TIGR02352 189 AGAWAGELLP-----LPLRPVRGQPLRLEAPAVPLLNrplRAVVYGRRVYI-VPRRDGRLVVGATMEESGFdtTPTLGGI 262
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517056601  328 RRstLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPTKVA-GLFLNTGHGTLGWTMSTGSARLIGDLVSGRQ 402
Cdd:TIGR02352 263 KE--LLRDAYTILPAlKEARLLETWAGLRPGTPDNLPYIGEHPEDrRLLIATGHYRNGILLAPATAEVIADLILGKE 337
 
Name Accession Description Interval E-value
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-415 0e+00

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 825.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPK 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  81 LDMAMLSWMARMLSNCTSERYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAAD 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRHVRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITDASRAPESTVMDETYKIAITRLGDRIRVGGMAEISGY 320
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 321 TNDLGLARRSTLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGDLVS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGgGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400
                        410
                 ....*....|....*.
gi 517056601 400 GRQPEIDARDLAISRY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 5.72e-110

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 327.63  E-value: 5.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQsGPALETSFANAGEVSFGycspWAAPGIPmkamkwlfmkhaplilrpk 80
Cdd:COG0665    3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPG----LAALADR------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  81 ldmamlswmarmlsnctseryainksRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAAD 160
Cdd:COG0665   59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRhvRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD 240
Cdd:COG0665  113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITDAsrAPESTVMDETyKIAITRLGD-RIRVGGMAEISG 319
Cdd:COG0665  191 RGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPLPD--LPLRPVLDDT-GVYLRPTADgRLLVGGTAEPAG 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 320 YTNDLGLARRSTLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPT-KVAGLFLNTGHGTLGWTMSTGSARLIGDL 397
Cdd:COG0665  268 FDRAPTPERLEALLRRLRRLFPAlADAEIVRAWAGLRPMTPDGLPIIGRLpGAPGLYVATGHGGHGVTLAPAAGRLLADL 347
                        410
                 ....*....|....*..
gi 517056601 398 VSGRQPEIDARDLAISR 414
Cdd:COG0665  348 ILGGEPPLDLAPFSPDR 364
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
2-398 8.22e-105

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 316.19  E-value: 8.22e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPKL 81
Cdd:PRK12409   3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAAMETSFANGGQLSASNAEVWNHWATVLKGLKWMLRKDAPLLLNPKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  82 DMAMLSWMARMLSNCtsERYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAADG 161
Cdd:PRK12409  83 SWHKYSWLAEFLAHI--PNYRANTIETVRLAIAARKHLFDIAEREGIDFDLERRGILHIYHDKAGFDHAKRVNALLAEGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 162 IPYEVLDRDGCVRFEPALRhvrDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITD- 240
Cdd:PRK12409 161 LERRAVTPEEMRAIEPTLT---GEYYGGYYTPSDSTGDIHKFTTGLAAACARLGVQFRYGQEVTSIKTDGGGVVLTVQPs 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 241 ----RERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVKGYSLTIPITD-ASR--APESTVMDETYKIAITRLG-DRIRVG 312
Cdd:PRK12409 238 aehpSRTLEFDGVVVCAGVGSRALAAMLGDRVNVYPVKGYSITVNLDDeASRaaAPWVSLLDDSAKIVTSRLGaDRFRVA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 313 GMAEISGYTNDLGLARRSTLEHSVTDLFPGGDISKASFWSGLRPMTPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSAR 392
Cdd:PRK12409 318 GTAEFNGYNRDIRADRIRPLVDWVRRNFPDVSTRRVVPWAGLRPMMPNMMPRVGRGRRPGVFYNTGHGHLGWTLSAATAD 397

                 ....*.
gi 517056601 393 LIGDLV 398
Cdd:PRK12409 398 LVAQVV 403
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
2-397 2.06e-74

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 235.76  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601    2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYcspwaapgipmkamkwlfmkhaplilrpkl 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGL------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   82 dmamlswmarmlsnctserYAINKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQlEASAKDVKALAADG 161
Cdd:pfam01266  51 -------------------RYLEPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  162 IPYEVLDRDGCVRFEPALrhvrDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGrVRGVITDR 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLL----PGLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVVTTG 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  242 ErmsAEAVVIALGSYSPLLLKPlGIRLPVYPVKGYSLTI-PITDASRAPE--STVMDETYKIAITRLGDRIRVGGMAEIS 318
Cdd:pfam01266 186 E---ADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLePLPEALLILPvpITVDPGRGVYLRPRADGRLLLGGTDEED 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  319 GY-TNDLGLARRSTLEHSVTDLFPG-GDIskASFWSGLRPMtPDGTPVIGPTKVAGLFLNTGHGTLGWTMSTGSARLIGD 396
Cdd:pfam01266 262 GFdDPTPDPEEIEELLEAARRLFPAlADI--ERAWAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAE 338

                  .
gi 517056601  397 L 397
Cdd:pfam01266 339 L 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
17-402 1.68e-31

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


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 122.47  E-value: 1.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   17 YQLAKAGHDVTVVDRQSgpaletsfaNAGEVSfgycspWAAPGipmkamkwlfmkhaplilrpkldmaMLSwmarMLSNC 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRDP---------MGGGAS------WAAAG-------------------------MLA----PHAEC 36
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   97 TSERyainkSRMLRLADYSR----IALAELRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAADGIPYEVLDRDGC 172
Cdd:TIGR02352  37 EYAE-----DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRAL 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  173 VRFEPALRhvrDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAVVIA 252
Cdd:TIGR02352 112 RRLEPYLS---GGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGDVQADQVVLA 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  253 LGSYSPLLLKplgirLPVYPVKGYSLTIPITDASRAP---ESTVMDETYKIaITRLGDRIRVGGMAEISGY--TNDLGLA 327
Cdd:TIGR02352 189 AGAWAGELLP-----LPLRPVRGQPLRLEAPAVPLLNrplRAVVYGRRVYI-VPRRDGRLVVGATMEESGFdtTPTLGGI 262
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517056601  328 RRstLEHSVTDLFPG-GDISKASFWSGLRPMTPDGTPVIGPTKVA-GLFLNTGHGTLGWTMSTGSARLIGDLVSGRQ 402
Cdd:TIGR02352 263 KE--LLRDAYTILPAlKEARLLETWAGLRPGTPDNLPYIGEHPEDrRLLIATGHYRNGILLAPATAEVIADLILGKE 337
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
3-275 9.31e-25

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 105.23  E-value: 9.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   3 VIVLGAGIVGVTSAYQLAKA-GHDVTVVDRQSGPALETSFANAGEVsfgycspwaapgipmkamkwlfmkHAPLILRPKl 81
Cdd:COG0579    7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVI------------------------HAGLYYTPG- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  82 dmamlSWMARMlsnCTseryAINKsrmlRLADYSRialaelraETGIAYDERmqGTLQLFRTQQQLEASAKDVKALAADG 161
Cdd:COG0579   62 -----SLKARL---CV----EGNE----LFYELCR--------ELGIPFKRC--GKLVVATGEEEVAFLEKLYERGKANG 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 162 IPY-EVLDRDGCVRFEPalrHVRDKIVGGLLTPkdETGDC--FKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRgVI 238
Cdd:COG0579  116 VPGlEILDREELRELEP---LLSDEGVAALYSP--STGIVdpGALTRALAENAEANGVELLLNTEVTGIEREGDGWE-VT 189
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 517056601 239 TDRERMSAEAVVIALGSYSPLLLKPLGIRLPV--YPVKG 275
Cdd:COG0579  190 TNGGTIRARFVINAAGLYADRLAQMAGIGKDFgiFPVKG 228
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
2-401 1.95e-09

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


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 59.47  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSfgycspwaapgipmkamkwlfmkhaPLILRPkl 81
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALY-------------------------PLLSKD-- 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  82 DMAMlswmarmlsnctseryainkSRMLRLA-DYSRIALAELRAE-----------TGIAYDERMQGTLQ---------- 139
Cdd:PRK01747 315 DNAL--------------------SRFFRAAfLFARRFYDALPAAgvafdhdwcgvLQLAWDEKSAEKIAkmlalglpae 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 140 LFRTQQQLEASAKDVKALAADGIPYevldrdgcvrfePAlrhvrdkivGGLLTPKDetgdcfkFTNALAAKAEAlGVRFA 219
Cdd:PRK01747 375 LARALDAEEAEELAGLPVPCGGIFY------------PQ---------GGWLCPAE-------LCRALLALAGQ-QLTIH 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 220 YGTTIKALDVEAGRVRGVITDRERMSAEAVVIALGSYSPLLlkPLGIRLPVYPVKGYSLTIPITDASRAPESTVMDETYK 299
Cdd:PRK01747 426 FGHEVARLEREDDGWQLDFAGGTLASAPVVVLANGHDAARF--AQTAHLPLYSVRGQVSHLPTTPALSALKQVLCYDGYL 503
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 300 IAITRLG--------DRirvggmaeisgytNDLGLARRSTlEH-----SVTDLFPGG------DISKASFWSGLRPMTPD 360
Cdd:PRK01747 504 TPQPANGthcigasyDR-------------DDTDTAFREA-DHqenleRLAECLPQAlwakevDVSALQGRVGFRCASRD 569
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517056601 361 GTPVIGP------TKVA-----------------GLFLNTGHGTLGWTMSTGSARLIGDLVSGR 401
Cdd:PRK01747 570 RLPMVGNvpdeaaTLAEyaalanqqpardaprlpGLYVAGALGSRGLCSAPLGAELLASQIEGE 633
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
16-400 2.27e-09

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 58.82  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   16 AYQLAKAGHDVTVVDRQSGPALETSfanagevsfgycspwaapGIPMKAMKwlfmkhaPLILRPKLDMAMLSwmarMLSN 95
Cdd:TIGR03197   2 AYSLARRGWQVTLYEQDEAPAQGAS------------------GNPQGALY-------PLLSADDNPLSRFF----LAAF 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   96 ctseRYAinKSRMLRLADYSRIALAELRAETGIAYDERMQGTLQLFRTQQQLEA------SAKDVKALAADGIPYEVLdr 169
Cdd:TIGR03197  53 ----LYA--RRFYRQLAEAGFPFDHEWCGVLQLAYDEKEAERLQKLLEQLGFPEelarwvDAEQASQLAGIPLPYGGL-- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  170 dgcvrFEPAlrhvrdkivGGLLTPKDetgdcfkFTNALAAKAEAlGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAV 249
Cdd:TIGR03197 125 -----FFPQ---------GGWLSPPQ-------LCRALLAHAGI-RLTLHFNTEITSLERDGEGWQLLDANGEVIAASVV 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  250 VIALGSYSPLLLKPLgiRLPVYPVKGYSLTIPITDASRAPESTVMDETYkiaITRLGDRIRVGGmaeiSGYT-NDLGLAR 328
Cdd:TIGR03197 183 VLANGAQAPQLAQTA--HLPLRPVRGQVSHLPATEALSALKTVLCYDGY---LTPANNGEHCIG----ASYDrNDDDLAL 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  329 RsTLEHS-----VTDLFP------GGDISKASFWSGLRPMTPDGTPVIGP--------------------------TKVA 371
Cdd:TIGR03197 254 R-EADHAenlerLAECLPalawasEVDISALQGRVGVRCASPDHLPLVGAvpdfeaikeayaelakdknrpiaepaPYYP 332
                         410       420
                  ....*....|....*....|....*....
gi 517056601  372 GLFLNTGHGTLGWTMSTGSARLIGDLVSG 400
Cdd:TIGR03197 333 GLYVLGGLGSRGLTSAPLAAEILAAQICG 361
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-250 8.69e-08

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 54.09  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPaletsfanaGevsfGYCSPWAAPG---------IPM-KAMKWLF- 69
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP---------G----GRARTFERPGfrfdvgpsvLTMpGVLERLFr 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  70 ----MKHAPLIlrpKLDMAMlswmarmlsnctseRYAINKSRMLRL-ADYSRIA--LAELRAETGIAYDERMQGTLQLFr 142
Cdd:COG1233   71 elglEDYLELV---PLDPAY--------------RVPFPDGRALDLpRDLERTAaeLERLFPGDAEAYRRFLAELRRLY- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 143 tqqqlEASAKDVKALAADGIPyEVLDRDGCVRFEPAL---------RHVRDKIVGGLLT--------PKDET-------- 197
Cdd:COG1233  133 -----DALLEDLLYRPLLSLR-DLLRPLALARLLRLLlrslrdllrRYFKDPRLRALLAgqalylglSPDRTpalyalia 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517056601 198 ------------GDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVIT-DRERMSAEAVV 250
Cdd:COG1233  207 yleyaggvwypkGGMGALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLaDGEEIRADAVV 272
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
173-256 1.20e-07

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 53.73  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 173 VRFEPALrhvrdkivGGLLTPKDET----GDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVIT-----DRER 243
Cdd:PRK08274 107 VRFQPPL--------SGALHVARTNaffwGGGKALVNALYRSAERLGVEIRYDAPVTALELDDGRFVGARAgsaagGAER 178
                         90
                 ....*....|...
gi 517056601 244 MSAEAVVIALGSY 256
Cdd:PRK08274 179 IRAKAVVLAAGGF 191
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
202-280 6.57e-07

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 50.35  E-value: 6.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517056601 202 KFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAVVIALGSYSPlLLKPLGIRLPVYPVKGYSLTI 280
Cdd:COG0644   87 RFDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGARSL-LARKLGLKRRSDEPQDYALAI 164
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
1-36 8.05e-07

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


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 50.71  E-value: 8.05e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPA 36
Cdd:COG0654    4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
3-266 1.33e-06

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 50.21  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   3 VIVLGAGIVGVTSAYQLAKAGHD--VTVVDRQSGPALETSFANAGEVSFG--YcspwaAPGiPMKAmkwlfmkhaplilr 78
Cdd:PRK11728   5 FVIIGGGIVGLSTAMQLQERYPGarIAVLEKESGPARHQTGHNSGVIHAGvyY-----TPG-SLKA-------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  79 pkldmamlswmarmlsnctseryainksrmlRLADYSRIALAELRAETGIAYDErmQGTLQLFRTQQQLEASAKDVKALA 158
Cdd:PRK11728  65 -------------------------------RFCRRGNEATKAFCDQHGIPYEE--CGKLLVATSELELERMEALYERAR 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 159 ADGIPYEVLDRDGCVRFEPalrHVRDkiVGGLLTPkdETG--DCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRg 236
Cdd:PRK11728 112 ANGIEVERLDAEELREREP---NIRG--LGAIFVP--STGivDYRAVAEAMAELIQARGGEIRLGAEVTALDEHANGVV- 183
                        250       260       270
                 ....*....|....*....|....*....|
gi 517056601 237 VITDRERMSAEAVVIALGSYSPLLLKPLGI 266
Cdd:PRK11728 184 VRTTQGEYEARTLINCAGLMSDRLAKMAGL 213
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
1-253 3.04e-06

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 49.08  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTV--------------VDRQSGPALETSFanagEVSFGYCSpwAAPGipmkamk 66
Cdd:COG3349    4 PRVVVVGGGLAGLAAAVELAEAGFRVTLlearprlggrarsfPDPDTGLPIDNGQ----HVLLGCYR--NTLD------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  67 wlFMKHAP----LILRPKLDMAM---LSWMARM---------LSnctseryAINKSRMLRLADYSRIALAeLRAETGIAY 130
Cdd:COG3349   71 --LLRRIGaadnLVGPEPLQFPLpggRRWTLRAprlpaplhlLR-------ALLRAPGLSLADRLALLRL-LTACRERRW 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 131 DERMQGTL-QLFRTQQQLEASAKD------VKALAADGipyevldRDGCVRfePALRHVRDKIVGG-----LLTPKDETG 198
Cdd:COG3349  141 RELDDISVaDWLRRHGQSPRLIRRlwepllLAALNTPP-------EQASAR--LALTVLRETLLAGpaasdLLVPRGPLS 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517056601 199 DCfkFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVIT-DRERMSAEAVVIAL 253
Cdd:COG3349  212 EL--FVDPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLaDGETVPADAVVLAV 265
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
5-68 3.48e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 44.44  E-value: 3.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517056601    5 VLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWL 68
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLL 64
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
3-274 4.57e-06

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


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 48.29  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601    3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDRqsgpaletsfanagevsfgycspwaapgipmkamkwLFMKHaplilrpkld 82
Cdd:TIGR01377   3 VIVVGAGIMGCFAAYHLAKHGKKTLLLEQ------------------------------------FDLPH---------- 36
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   83 mamlswmarmlSNCTSEryaiNKSRMLRLA----DYSRIAL------AELRAETGIaydermqgtlQLFRTQQQLEASAK 152
Cdd:TIGR01377  37 -----------SRGSSH----GQSRIIRKAypedFYTPMMLecyqlwAQLEKEAGT----------KLHRQTGLLLLGPK 91
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  153 D-------VKALAADGIPYEVLDRDGCVRFEPALRHVRDKIvgGLLtpkDETGDCFKFTNALAA---KAEALGVRFAYGT 222
Cdd:TIGR01377  92 EnqflktiQATLSRHGLEHELLSSKQLKQRFPNIRVPRNEV--GLL---DPNGGVLYAEKALRAlqeLAEAHGATVRDGT 166
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517056601  223 TIKALDVEAGRVRgVITDRERMSAEAVVIALGSYSPLLLKPLGIRLPVYPVK 274
Cdd:TIGR01377 167 KVVEIEPTELLVT-VKTTKGSYQANKLVVTAGAWTSKLLSPLGIEIPLQPLR 217
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-35 5.78e-06

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 47.95  E-value: 5.78e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGV 38
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
1-33 6.92e-06

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


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 47.90  E-value: 6.92e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQS 33
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASD 34
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
2-28 7.26e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 47.99  E-value: 7.26e-06
                         10        20
                 ....*....|....*....|....*..
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTV 28
Cdd:COG1231    9 DVVIVGAGLAGLAAARELRKAGLDVTV 35
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
1-36 1.77e-05

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 46.38  E-value: 1.77e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPA 36
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHL 36
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
3-257 1.83e-05

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601   3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDRQS---GpaleTSFANAGEVsfgycspwAAPGIPMkamkwlfmkhaplilrp 79
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPprgG----HTAAAQGGI--------NAAGTNV----------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601  80 kldmamlswmarmlsnctseryainksrMLRLADYSR-IALAELRAETGIAYDERMQGTLqlfrtqqqLEASAKDVKALA 158
Cdd:COG1053   57 ----------------------------QKAAGEDSPeEHFYDTVKGGDGLADQDLVEAL--------AEEAPEAIDWLE 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 159 ADGIPYEVLDrdgcvrfEPALRHVRDKIVGGLLTPKDETGdcFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVI 238
Cdd:COG1053  101 AQGVPFSRTP-------DGRLPQFGGHSVGRTCYAGDGTG--HALLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVV 171
                        250       260
                 ....*....|....*....|....
gi 517056601 239 T-----DRERMSAEAVVIALGSYS 257
Cdd:COG1053  172 ArdrtgEIVRIRAKAVVLATGGFG 195
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
1-31 2.06e-05

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 46.00  E-value: 2.06e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVAR 31
PRK07233 PRK07233
hypothetical protein; Provisional
2-31 2.13e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 46.42  E-value: 2.13e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEA 30
trkA PRK09496
Trk system potassium transporter TrkA;
1-31 2.70e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 46.27  E-value: 2.70e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDT 31
PRK06753 PRK06753
hypothetical protein; Provisional
1-45 3.50e-05

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 45.45  E-value: 3.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSgpalETSFANAG 45
Cdd:PRK06753   1 MKIAIIGAGIGGLTAAALLQEQGHEVKVFEKNE----SVKEVGAG 41
PRK12921 PRK12921
oxidoreductase;
1-32 4.36e-05

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 45.23  E-value: 4.36e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQ 32
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFLVRP 32
solA PRK11259
N-methyl-L-tryptophan oxidase;
161-270 8.06e-05

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 44.44  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056601 161 GIPYEVLDRDGCVRFEPALRhVRDKIVG------GLLTPKDetgdCFKftnALAAKAEALGVRFAYGTTIKALDVEAGRV 234
Cdd:PRK11259 111 GLPHEVLDAAEIRRRFPQFR-LPDGYIAlfepdgGFLRPEL----AIK---AHLRLAREAGAELLFNEPVTAIEADGDGV 182
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517056601 235 RgVITDRERMSAEAVVIALGSYSPLLLKPLGIRLPV 270
Cdd:PRK11259 183 T-VTTADGTYEAKKLVVSAGAWVKDLLPPLELPLTP 217
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
2-32 1.53e-04

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 43.59  E-value: 1.53e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQ 32
Cdd:COG0493  123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEAL 153
gltD PRK12810
glutamate synthase subunit beta; Reviewed
2-31 2.13e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 43.23  E-value: 2.13e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFER 174
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
3-31 2.97e-04

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 40.68  E-value: 2.97e-04
                          10        20
                  ....*....|....*....|....*....
gi 517056601    3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILR 29
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
3-36 3.35e-04

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 42.54  E-value: 3.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPA 36
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG 42
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
2-33 3.46e-04

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


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 39.11  E-value: 3.46e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 517056601    2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQS 33
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRD 32
PRK07208 PRK07208
hypothetical protein; Provisional
2-31 3.58e-04

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 42.57  E-value: 3.58e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK07208   6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
2-35 3.61e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.55  E-value: 3.61e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKL 172
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
1-31 4.11e-04

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 41.98  E-value: 4.11e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDK 126
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
3-33 4.74e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 42.47  E-value: 4.74e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDRQS 33
Cdd:COG3573    8 VIVVGAGLAGLVAAAELADAGRRVLLLDQEP 38
PRK07588 PRK07588
FAD-binding domain;
1-31 8.26e-04

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 41.26  E-value: 8.26e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIER 31
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
1-31 8.28e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 41.32  E-value: 8.28e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEA 171
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-33 8.30e-04

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 41.27  E-value: 8.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAK---AGHDVTVVDRQS 33
Cdd:COG1252    2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNP 37
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
1-30 8.68e-04

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 39.92  E-value: 8.68e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 517056601    1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVD 30
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVD 30
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
2-31 1.01e-03

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 39.83  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 517056601    2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDI 30
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-30 1.19e-03

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 40.78  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVD 30
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVD 30
PRK05868 PRK05868
FAD-binding protein;
2-35 1.27e-03

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 40.74  E-value: 1.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:PRK05868   3 TVVVSGASVAGTAAAYWLGRHGYSVTMVERHPGL 36
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
1-31 1.77e-03

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 40.09  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDR 31
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDI 33
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
1-30 1.80e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 40.29  E-value: 1.80e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 517056601    1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVD 30
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVD 30
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
2-35 2.39e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 39.79  E-value: 2.39e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:COG0446  126 RAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
1-44 2.69e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 39.59  E-value: 2.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGPALETSFANA 44
Cdd:PRK14619   5 KTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGLSLAAVLADA 48
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
1-47 2.76e-03

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.61  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517056601    1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQS-----GPALETSFANAGEV 47
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcpygGCVLSKALLGAAEA 52
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
1-34 4.21e-03

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 38.87  E-value: 4.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSG 34
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPA 36
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
2-34 4.22e-03

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 38.74  E-value: 4.22e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 517056601    2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSG 34
Cdd:pfam13738 157 KVVVIGGYNSAVDAALELVRKGARVTVLYRGSE 189
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
1-27 4.80e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 38.97  E-value: 4.80e-03
                         10        20
                 ....*....|....*....|....*..
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVT 27
Cdd:PRK05335   3 KPVNVIGAGLAGSEAAWQLAKRGVPVE 29
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
2-30 4.97e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 39.33  E-value: 4.97e-03
                         10        20
                 ....*....|....*....|....*....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVD 30
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFD 223
PRK08401 PRK08401
L-aspartate oxidase; Provisional
1-45 6.54e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 38.63  E-value: 6.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVdrqsGPALETS---FANAG 45
Cdd:PRK08401   2 MKVGIVGGGLAGLTAAISLAKKGFDVTII----GPGIKKSnsyLAQAG 45
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-35 6.58e-03

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 38.58  E-value: 6.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:COG1251  144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
1-61 6.77e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 38.52  E-value: 6.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056601   1 MKVIVLGAGIVGVTSAYQLAKAGHDVTVVD-RQSGPALETSFANAG-EVSFG--YCSPWAA-------PGIP 61
Cdd:COG0771    5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDdRPAPELAAAELEAPGvEVVLGehPEELLDGadlvvksPGIP 76
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
2-35 8.90e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 37.97  E-value: 8.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056601   2 KVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:PRK04965 143 RVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-35 9.14e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 38.35  E-value: 9.14e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 517056601   3 VIVLGAGIVGVTSAYQLAKAGHDVTVVDRQSGP 35
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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