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Conserved domains on  [gi|16129152|ref|NP_415707|]
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D-amino acid dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

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.-
Gene Ontology:  GO:0071949|GO:0016491|GO:0008718|GO:0055130
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: 869.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   81 GTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  161 GVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  241 DEVIKADAYVMAFGSYSTAMLKGI-VDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  320 NTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 16129152  400 GRTPAIPYEDLSVARY 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: 869.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   81 GTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  161 GVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  241 DEVIKADAYVMAFGSYSTAMLKGI-VDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  320 NTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 16129152  400 GRTPAIPYEDLSVARY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 1.83e-106

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 319.16  E-value: 1.83e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREpGAALETSAANAGQISPGYAAPWAApgvplkaikwmfqrhaplavrld 80
Cdd:COG0665   3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPGLAALADR----------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  81 gtqfqlkwmwqmlrncdtshymenkgRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDA 160
Cdd:COG0665  59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 161 GVPYQLLESSRLAEVEPALAevAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCG 240
Cdd:COG0665 113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 241 DEVIKADAYVMAFGSYSTAMLKGI-VDIPVYPLKGYSLTIPIaqEDGAPVSTILDETyKIAITRF-DNRIRVGGMAEIVG 318
Cdd:COG0665 191 RGTVRADAVVLAAGAWSARLLPMLgLRLPLRPVRGYVLVTEP--LPDLPLRPVLDDT-GVYLRPTaDGRLLVGGTAEPAG 267

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 319 FNTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTR-FKNLWLNTGHGTLGWTMACGSGQLLSDL 397
Cdd:COG0665 268 FDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPgAPGLYVATGHGGHGVTLAPAAGRLLADL 347

                       410
                ....*....|....*..
gi 16129152 398 LSGRTPAIPYEDLSVAR 414
Cdd:COG0665 348 ILGGEPPLDLAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-397 1.07e-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: 236.91  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152     2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYaapwaapgvplkaikwmfqrhaplavrldg 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGL------------------------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    82 tqfqlkwmwqmlrncdtshYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQyENATRDIAVLEDAG 161
Cdd:pfam01266  51 -------------------RYLEPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   162 VPYQLLESSRLAEVEPALAEVAhkltGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEqIYGVKCGD 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLLPGLR----GGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVVTTG 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   242 EvikADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTI--PIAQEDGAPVS-TILDETYKIAITRFDNRIRVGGMAEIVG 318
Cdd:pfam01266 186 E---ADAVVNAAGAWADLLALPGLRLPVRPVRGQVLVLepLPEALLILPVPiTVDPGRGVYLRPRADGRLLLGGTDEEDG 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   319 FNTELLQP-RRETLEMVVRDLYPRGGHVEQAtfWTGLRPMtPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDL 397
Cdd:pfam01266 263 FDDPTPDPeEIEELLEAARRLFPALADIERA--WAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
 17-402 6.84e-35

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: 132.10  E-value: 6.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    17 WYLNQAGHEVTVIDREPGAAlETSAANAGQISPgyaapwaapgvplkaikwmfqrHAPlavrldgtqfqlkwmWQMLRnc 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRDPMGG-GASWAAAGMLAP----------------------HAE---------------CEYAE-- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    97 dtshymenkGRMVRLAEYSR----DCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAGVPYQLLESSRL 172
Cdd:TIGR02352  41 ---------DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRAL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   173 AEVEPALAEvahKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMA 252
Cdd:TIGR02352 112 RRLEPYLSG---GIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGDVQADQVVLA 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   253 FGSYSTAMLKGivdiPVYPLKGYSL--TIPIAQEDGAPV-STILDETYKIaITRFDNRIRVGGMAEIVGFNTellQPRRE 329
Cdd:TIGR02352 189 AGAWAGELLPL----PLRPVRGQPLrlEAPAVPLLNRPLrAVVYGRRVYI-VPRRDGRLVVGATMEESGFDT---TPTLG 260

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129152   330 TLEMVVRDLY---PRGGHVEQATFWTGLRPMTPDGTPVVGRTRF-KNLWLNTGHGTLGWTMACGSGQLLSDLLSGRT 402
Cdd:TIGR02352 261 GIKELLRDAYtilPALKEARLLETWAGLRPGTPDNLPYIGEHPEdRRLLIATGHYRNGILLAPATAEVIADLILGKE 337
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-47 1.15e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 45.19  E-value: 1.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129152      2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP----------GAALETSAANAGQI 47
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRParlrqlesllGARFTTLYSQAELL 77
 
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: 869.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   81 GTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  161 GVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  241 DEVIKADAYVMAFGSYSTAMLKGI-VDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  320 NTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 16129152  400 GRTPAIPYEDLSVARY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 1.83e-106

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 319.16  E-value: 1.83e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREpGAALETSAANAGQISPGYAAPWAApgvplkaikwmfqrhaplavrld 80
Cdd:COG0665   3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPGLAALADR----------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  81 gtqfqlkwmwqmlrncdtshymenkgRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDA 160
Cdd:COG0665  59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 161 GVPYQLLESSRLAEVEPALAevAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCG 240
Cdd:COG0665 113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 241 DEVIKADAYVMAFGSYSTAMLKGI-VDIPVYPLKGYSLTIPIaqEDGAPVSTILDETyKIAITRF-DNRIRVGGMAEIVG 318
Cdd:COG0665 191 RGTVRADAVVLAAGAWSARLLPMLgLRLPLRPVRGYVLVTEP--LPDLPLRPVLDDT-GVYLRPTaDGRLLVGGTAEPAG 267

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 319 FNTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTR-FKNLWLNTGHGTLGWTMACGSGQLLSDL 397
Cdd:COG0665 268 FDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPgAPGLYVATGHGGHGVTLAPAAGRLLADL 347

                       410
                ....*....|....*..
gi 16129152 398 LSGRTPAIPYEDLSVAR 414
Cdd:COG0665 348 ILGGEPPLDLAPFSPDR 364
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 2-404 3.83e-86

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 268.82  E-value: 3.83e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLDG 81
Cdd:PRK12409   3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAAMETSFANGGQLSASNAEVWNHWATVLKGLKWMLRKDAPLLLNPKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   82 TQFQLKWMWQMLRNcdTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAG 161
Cdd:PRK12409  83 SWHKYSWLAEFLAH--IPNYRANTIETVRLAIAARKHLFDIAEREGIDFDLERRGILHIYHDKAGFDHAKRVNALLAEGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  162 VPYQLLESSRLAEVEPALAEVAHkltGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYgVKCGD 241
Cdd:PRK12409 161 LERRAVTPEEMRAIEPTLTGEYY---GGYYTPSDSTGDIHKFTTGLAAACARLGVQFRYGQEVTSIKTDGGGVV-LTVQP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  242 ------EVIKADAYVMAFGSYSTAMLKGIVD-IPVYPLKGYSLTIPIAQED---GAPVSTILDETYKIAITRF-DNRIRV 310
Cdd:PRK12409 237 saehpsRTLEFDGVVVCAGVGSRALAAMLGDrVNVYPVKGYSITVNLDDEAsraAAPWVSLLDDSAKIVTSRLgADRFRV 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  311 GGMAEIVGFNTELLQPRRETLEMVVRDLYPrGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGS 390
Cdd:PRK12409 317 AGTAEFNGYNRDIRADRIRPLVDWVRRNFP-DVSTRRVVPWAGLRPMMPNMMPRVGRGRRPGVFYNTGHGHLGWTLSAAT 395

                        410
                 ....*....|....
gi 16129152  391 GQLLSDLLSGRTPA 404
Cdd:PRK12409 396 ADLVAQVVAQKLPA 409
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-397 1.07e-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: 236.91  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152     2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYaapwaapgvplkaikwmfqrhaplavrldg 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGL------------------------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    82 tqfqlkwmwqmlrncdtshYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQyENATRDIAVLEDAG 161
Cdd:pfam01266  51 -------------------RYLEPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   162 VPYQLLESSRLAEVEPALAEVAhkltGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEqIYGVKCGD 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLLPGLR----GGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVVTTG 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   242 EvikADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTI--PIAQEDGAPVS-TILDETYKIAITRFDNRIRVGGMAEIVG 318
Cdd:pfam01266 186 E---ADAVVNAAGAWADLLALPGLRLPVRPVRGQVLVLepLPEALLILPVPiTVDPGRGVYLRPRADGRLLLGGTDEEDG 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   319 FNTELLQP-RRETLEMVVRDLYPRGGHVEQAtfWTGLRPMtPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDL 397
Cdd:pfam01266 263 FDDPTPDPeEIEELLEAARRLFPALADIERA--WAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
 17-402 6.84e-35

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: 132.10  E-value: 6.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    17 WYLNQAGHEVTVIDREPGAAlETSAANAGQISPgyaapwaapgvplkaikwmfqrHAPlavrldgtqfqlkwmWQMLRnc 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRDPMGG-GASWAAAGMLAP----------------------HAE---------------CEYAE-- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    97 dtshymenkGRMVRLAEYSR----DCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAGVPYQLLESSRL 172
Cdd:TIGR02352  41 ---------DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRAL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   173 AEVEPALAEvahKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMA 252
Cdd:TIGR02352 112 RRLEPYLSG---GIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGDVQADQVVLA 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   253 FGSYSTAMLKGivdiPVYPLKGYSL--TIPIAQEDGAPV-STILDETYKIaITRFDNRIRVGGMAEIVGFNTellQPRRE 329
Cdd:TIGR02352 189 AGAWAGELLPL----PLRPVRGQPLrlEAPAVPLLNRPLrAVVYGRRVYI-VPRRDGRLVVGATMEESGFDT---TPTLG 260

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129152   330 TLEMVVRDLY---PRGGHVEQATFWTGLRPMTPDGTPVVGRTRF-KNLWLNTGHGTLGWTMACGSGQLLSDLLSGRT 402
Cdd:TIGR02352 261 GIKELLRDAYtilPALKEARLLETWAGLRPGTPDNLPYIGEHPEdRRLLIATGHYRNGILLAPATAEVIADLILGKE 337
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
3-274 8.28e-16

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 78.65  E-value: 8.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   3 VVILGSGVVGVASAWYLNQA-GHEVTVIDREPGAALETSAANAGQISPGYAAPwaaPGVpLKAIKwmfqrhaplAVRldG 81
Cdd:COG0579   7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYT---PGS-LKARL---------CVE--G 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  82 TQfqlkwmwqmlrncdtshymenkgrmvRLAEYSRdclkalraETNIQYegRQGGTLQLFRTEQQ-------YENATRDi 154
Cdd:COG0579  72 NE--------------------------LFYELCR--------ELGIPF--KRCGKLVVATGEEEvafleklYERGKAN- 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 155 avledaGVPY-QLLESSRLAEVEPALAEVAHkltGGLQLPndETGDC--QLFTQNLARMAEQAGVKFRFNTPVDQLLCDG 231
Cdd:COG0579 115 ------GVPGlEILDREELRELEPLLSDEGV---AALYSP--STGIVdpGALTRALAENAEANGVELLLNTEVTGIEREG 183

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 16129152 232 EQiYGVKCGDEVIKADAYVMAFGSYSTAMLK--GIV-DIPVYPLKG 274
Cdd:COG0579 184 DG-WEVTTNGGTIRARFVINAAGLYADRLAQmaGIGkDFGIFPVKG 228
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 2-33 3.62e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 49.01  E-value: 3.62e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFERAD 176
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-36 7.87e-06

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: 47.54  E-value: 7.87e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAA 36
Cdd:COG1893   1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGAHAE 36
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 1-252 8.76e-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: 47.93  E-value: 8.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVidrepgaaLEtSAANAGqispGYAAPW--AAPGVPL------------KAIK 66
Cdd:COG3349   4 PRVVVVGGGLAGLAAAVELAEAGFRVTL--------LE-ARPRLG----GRARSFpdPDTGLPIdngqhvllgcyrNTLD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  67 WM--------FQRHAPLAVRL-DGTQFQLK--------WMWQMLRNCdtshymenkgRMVRLAEYsrdcLKALRAETNIq 129
Cdd:COG3349  71 LLrrigaadnLVGPEPLQFPLpGGRRWTLRaprlpaplHLLRALLRA----------PGLSLADR----LALLRLLTAC- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 130 yegrqggtlqLFRTEQQYENAT-RDiaVLEDAGVPYQLLEssRLAEV----------EPALAEVAHK-----LTGG---- 189
Cdd:COG3349 136 ----------RERRWRELDDISvAD--WLRRHGQSPRLIR--RLWEPlllaalntppEQASARLALTvlretLLAGpaas 201

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129152 190 -LQLPNDETGDcqLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGD-EVIKADAYVMA 252
Cdd:COG3349 202 dLLVPRGPLSE--LFVDPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADgETVPADAVVLA 264
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-47 1.15e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 45.19  E-value: 1.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129152      2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP----------GAALETSAANAGQI 47
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRParlrqlesllGARFTTLYSQAELL 77
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 148-257 1.89e-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: 1.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 148 ENATRDIAVLEDAGVPYQLLESSRLAEVEPALAE--VAHKLTGGLQLpndetgdcqlfTQNLARMAEQAGVKFRFNTPVD 225
Cdd:COG1053  90 EEAPEAIDWLEAQGVPFSRTPDGRLPQFGGHSVGrtCYAGDGTGHAL-----------LATLYQAALRLGVEIFTETEVL 158

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16129152 226 QLLCDGEQIYGVKCGD-----EVIKADAYVMAFGSYS 257
Cdd:COG1053 159 DLIVDDGRVVGVVARDrtgeiVRIRAKAVVLATGGFG 195
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-33 2.19e-05

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: 46.36  E-value: 2.19e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:COG1232   2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASD 34
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 2-33 4.05e-05

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: 45.51  E-value: 4.05e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 16129152   2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEALD 154
PRK07588 PRK07588
FAD-binding domain;
1-33 5.35e-05

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 45.11  E-value: 5.35e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAP 33
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-94 7.18e-05

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: 44.54  E-value: 7.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAAlETSAANAgqISP---------GYAAPWAAPGVPLKAIKWMFQR 71
Cdd:COG0654   4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR-PDGRGIA--LSPrslellrrlGLWDRLLARGAPIRGIRVRDGS 80

                        90       100
                ....*....|....*....|...
gi 16129152  72 HAPLAVRLDGTQFQLKWMWQMLR 94
Cdd:COG0654  81 DGRVLARFDAAETGLPAGLVVPR 103
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-33 1.01e-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: 40.65  E-value: 1.01e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 16129152     2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRD 32
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
5-63 1.73e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 39.44  E-value: 1.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129152     5 ILGSGVVGVASAWYLNQAGHEVTVIDREPGAAletsaanagqispGYAAPWAAPGVPLK 63
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG-------------GNAYSYRVPGYVFD 46
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 1-64 2.23e-04

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: 43.15  E-value: 2.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQIS----PGYAAPWAA-------PGVPLKA 64
Cdd:COG0771   5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEvvlgEHPEELLDGadlvvksPGIPPDH 79
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 2-34 2.25e-04

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: 42.88  E-value: 2.25e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 16129152   2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPG 34
Cdd:COG0446 126 RAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-254 2.62e-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: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.69  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152     1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALetsaanaGQISPGYAAP-WAAPGVPLKAIKWMFQRHAPLAVRL 79
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPY-------GGCVLSKALLgAAEAPEIASLWADLYKRKEEVVKKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    80 D-GTQFQLKwmwqmlRNCDTshyMENKGRMVRLAEYSRDclkalrAETNIQYEgrQ-----GGTLQLFRTEQQYENATRD 153
Cdd:pfam07992  74 NnGIEVLLG------TEVVS---IDPGAKKVVLEELVDG------DGETITYD--RlviatGARPRLPPIPGVELNVGFL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   154 IAVLEDAGVPYQLLESSRLA-------EVEpaLAEVAHKLtgGLQLPNDETGDCQL------FTQNLARMAEQAGVKFRF 220
Cdd:pfam07992 137 VRTLDSAEALRLKLLPKRVVvvgggyiGVE--LAAALAKL--GKEVTLIEALDRLLrafdeeISAALEKALEKNGVEVRL 212

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 16129152   221 NTPVDQLLcDGEQIYGVKCGDE-VIKADAYVMAFG 254
Cdd:pfam07992 213 GTSVKEII-GDGDGVEVILKDGtEIDADLVVVAIG 246
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 2-35 2.65e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 43.18  E-value: 2.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGA 35
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQA 228
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-250 3.01e-04

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.91  E-value: 3.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDR--EPGaaletsaanagqispGYAAPWAAPGV-----PlkAIKWMFQRHA 73
Cdd:COG1233   4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKndTPG---------------GRARTFERPGFrfdvgP--SVLTMPGVLE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  74 PLAVRLdGTQFQLKWmwqmlRNCDTS--HYMENkGRMVRLaeySRDcLKALRAEtNIQYEGRQGGTLQLF--RTEQQYEN 149
Cdd:COG1233  67 RLFREL-GLEDYLEL-----VPLDPAyrVPFPD-GRALDL---PRD-LERTAAE-LERLFPGDAEAYRRFlaELRRLYDA 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152 150 ATRDIAV-----LEDAGVPYQLLESSRLAeVEPALAEVAHKLTGG------------LQLPNDET--------------- 197
Cdd:COG1233 135 LLEDLLYrpllsLRDLLRPLALARLLRLL-LRSLRDLLRRYFKDPrlrallagqalyLGLSPDRTpalyaliayleyagg 213

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129152 198 -----GDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGD-EVIKADAYV 250
Cdd:COG1233 214 vwypkGGMGALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLADgEEIRADAVV 272
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-36 3.29e-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: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 16129152     3 VVILGSGVVGVASAWYLNQAGHEVTVIDREPGAA 36
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA 34
trkA PRK09496
Trk system potassium transporter TrkA;
1-33 4.25e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 42.42  E-value: 4.25e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDE 33
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
1-33 7.73e-04

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 41.64  E-value: 7.73e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAgHEVTVIDREP 33
Cdd:COG2907   4 MRIAVIGSGISGLTAAWLLSRR-HDVTLFEAND 35
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-36 1.04e-03

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: 40.82  E-value: 1.04e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAA 36
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERV 131
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-227 1.45e-03

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 40.58  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152    1 MRVVILGSGVVGVASAWYLNQA--GHEVTVIDREPGAALETSAANAGQISPG--YaapwaAPGvPLKAikwmfqrhapla 76
Cdd:PRK11728   3 YDFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPARHQTGHNSGVIHAGvyY-----TPG-SLKA------------ 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152   77 vrldgtqfqlkwmwqmlrncdtshymenkgrmvRLAEYSRDCLKALRAETNIQYEgrQGGTL-------QLFRTEQQYEN 149
Cdd:PRK11728  65 ---------------------------------RFCRRGNEATKAFCDQHGIPYE--ECGKLlvatselELERMEALYER 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129152  150 ATRDiavledaGVPYQLLESSRLAEVEPALAEVahkltGGLQLPndETG--DCQLFTQNLARMAEQAGVKFRFNTPVDQL 227
Cdd:PRK11728 110 ARAN-------GIEVERLDAEELREREPNIRGL-----GAIFVP--STGivDYRAVAEAMAELIQARGGEIRLGAEVTAL 175
PRK05868 PRK05868
FAD-binding protein;
2-34 1.73e-03

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 40.35  E-value: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPG 34
Cdd:PRK05868   3 TVVVSGASVAGTAAAYWLGRHGYSVTMVERHPG 35
PRK07233 PRK07233
hypothetical protein; Provisional
 2-33 1.76e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 40.26  E-value: 1.76e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADD 32
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-36 1.95e-03

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 40.03  E-value: 1.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAA 36
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAA 38
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-33 2.10e-03

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 40.12  E-value: 2.10e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16129152   1 MRVVILGSGVVGVASAWYLNQ---AGHEVTVIDREP 33
Cdd:COG1252   2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNP 37
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 2-49 2.35e-03

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: 40.21  E-value: 2.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISP 49
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYP 309
PRK10015 PRK10015
oxidoreductase; Provisional
 207-257 2.72e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 39.96  E-value: 2.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129152  207 LARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMAFGSYS 257
Cdd:PRK10015 114 LMEQAEQAGAQFIPGVRVDALVREGNKVTGVQAGDDILEANVVILADGVNS 164
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-34 2.80e-03

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: 39.85  E-value: 2.80e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 16129152   1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPG 34
Cdd:COG2072   7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADD 40
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 1-39 4.04e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 39.45  E-value: 4.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAG--HEVTVIDRE--PGAALET 39
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASdrLGGKIQT 43
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-33 4.26e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 39.35  E-value: 4.26e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 16129152   2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:COG1251 144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAP 175
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 2-35 4.96e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.09  E-value: 4.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPGA 35
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKL 172
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-33 6.53e-03

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 38.73  E-value: 6.53e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 16129152    3 VVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWP 43
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
203-279 7.46e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 38.02  E-value: 7.46e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129152 203 FTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYgVKCGD-EVIKADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTI 279
Cdd:COG0644  88 FDRWLAEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDgEEIRADYVVDADGARSLLARKLGLKRRSDEPQDYALAI 164
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 2-38 8.45e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 37.47  E-value: 8.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 16129152     2 RVVILGSGVVGVASAWYLNQAGHEVTVIDREPgAALE 38
Cdd:pfam01262  30 KVLVIGGGVAGLNAAATAKGLGAIVTILDVRP-ARLE 65
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 209-280 8.92e-03

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 38.24  E-value: 8.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129152   209 RMAEQA-GVKFRFNTPVDQLLCDGEqIYGVKCGD-EVIKADAYVMAfgsystamlkgivdIPVYPLKGYSLTIP 280
Cdd:pfam01593 211 ALAAQLlGGDVRLNTRVRSIDREGD-GVTVTLTDgEVIEADAVIVT--------------VPLGVLKRILFTPP 269
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-33 9.60e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 37.91  E-value: 9.60e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 16129152    1 MRVVILGSGVVGVASAWYLNQAGHEVTVIDREP 33
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRG 33
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 2-34 9.71e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 38.05  E-value: 9.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 16129152    2 RVVILGSGVVGVASAWYLNQAGHEVTVIDR--EPG 34
Cdd:PRK12770  20 KVAIIGAGPAGLAAAGYLACLGYEVHVYDKlpEPG 54
 
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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