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Conserved domains on  [gi|736057464|ref|WP_034200850|]
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MULTISPECIES: D-amino acid dehydrogenase [Burkholderia]

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: 861.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPWAAPGVPLKAVKWMFEKHAPLAIRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  81 GTRFQLQWMYQMLRNCTAERYAVNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 161 NVPFELLSPAELKKAEPALAAVSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 241 SETVRADAYVVALGSYSTSFISNL-MKIPVYPLKGYSITAPIVNEAAAPVSTVLDETYKIAITRFDQRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 320 DKKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADLIS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 736057464 400 GKMPAIQADDLSVHRY 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: 861.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPWAAPGVPLKAVKWMFEKHAPLAIRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  81 GTRFQLQWMYQMLRNCTAERYAVNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 161 NVPFELLSPAELKKAEPALAAVSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 241 SETVRADAYVVALGSYSTSFISNL-MKIPVYPLKGYSITAPIVNEAAAPVSTVLDETYKIAITRFDQRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 320 DKKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADLIS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 736057464 400 GKMPAIQADDLSVHRY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 3.41e-110

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 328.79  E-value: 3.41e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAgPALETSFANAGQISPGYAAPWAApgvplkavkwmfekhaplairld 80
Cdd:COG0665    3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGR-PGSGASGRNAGQLRPGLAALADR----------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  81 gtrfqlqwmyqmlrnctaeryavnkgRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEA 160
Cdd:COG0665   59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 161 NVPFELLSPAELKKAEPALAavSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCG 240
Cdd:COG0665  113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 241 SETVRADAYVVALGSYSTSFISNL-MKIPVYPLKGYSITAPIVneAAAPVSTVLDETyKIAITRF-DQRIRVGGMAEIVG 318
Cdd:COG0665  191 RGTVRADAVVLAAGAWSARLLPMLgLRLPLRPVRGYVLVTEPL--PDLPLRPVLDDT-GVYLRPTaDGRLLVGGTAEPAG 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 319 FDKKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTP-VSNLFLNTGHGTLGWTMSCGSGQLLADL 397
Cdd:COG0665  268 FDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPgAPGLYVATGHGGHGVTLAPAAGRLLADL 347

                        410
                 ....*....|....*..
gi 736057464 398 ISGKMPAIQADDLSVHR 414
Cdd:COG0665  348 ILGGEPPLDLAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-397 1.80e-76

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: 241.15  E-value: 1.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464    2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPwaapgvplkavkwmfekhaplairldg 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYL--------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   82 trfqlqwmyqmlrnctaeryavNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQlDGAAKDIAVLQEAN 161
Cdd:pfam01266  54 ----------------------EPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  162 VPFELLSPAELKKAEPALAavshKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGkIAGVQcgs 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLLP----GLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVV--- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  242 ETVRADAYVVALGSYSTSFISNLMKIPVYPLKGYSI-TAPIV-NEAAAPVS-TVLDETYKIAITRFDQRIRVGGMAEIVG 318
Cdd:pfam01266 183 TTGEADAVVNAAGAWADLLALPGLRLPVRPVRGQVLvLEPLPeALLILPVPiTVDPGRGVYLRPRADGRLLLGGTDEEDG 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  319 FDK-KLRAARRETLEMCVNDLFPGGGDTSKAtfWTGLRPMtPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADL 397
Cdd:pfam01266 263 FDDpTPDPEEIEELLEAARRLFPALADIERA--WAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
 17-401 5.64e-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: 132.49  E-value: 5.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   17 YYLARAGHEVTVIDREagpaletsfanagqiSPGYAAPWAAPGvplkavkwMFEKHAPlairldgtrfqlQWMYQmlrnc 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRD---------------PMGGGASWAAAG--------MLAPHAE------------CEYAE----- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   97 taeryavnkGRMVRLAEYSR----DCLQALRADTGIQYEGRTGGTLQL---------FRTQQQLDGAAKdiavlqeanVP 163
Cdd:TIGR02352  41 ---------DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVafdeddvehLRQLADLQSATG---------ME 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  164 FELLSPAELKKAEPALaavSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCGSET 243
Cdd:TIGR02352 103 VEWLSGRALRRLEPYL---SGGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGD 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  244 VRADAYVVALGSYSTSfisnLMKIPVYPLKGYSI--TAPIVNEAAAPV-STVLDETYKIaITRFDQRIRVGGMAEIVGFD 320
Cdd:TIGR02352 180 VQADQVVLAAGAWAGE----LLPLPLRPVRGQPLrlEAPAVPLLNRPLrAVVYGRRVYI-VPRRDGRLVVGATMEESGFD 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  321 KKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTP-VSNLFLNTGHGTLGWTMSCGSGQLLADLIS 399
Cdd:TIGR02352 255 TTPTLGGIKELLRDAYTILPALKEARLLETWAGLRPGTPDNLPYIGEHPeDRRLLIATGHYRNGILLAPATAEVIADLIL 334


                  ..
gi 736057464  400 GK 401
Cdd:TIGR02352 335 GK 336
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-47 5.88e-04

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: 40.18  E-value: 5.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 736057464     2 RVVILGSGVVGVASAYYLARAGHEVTVIDREA----------GPALETSFANAGQI 47
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRParlrqlesllGARFTTLYSQAELL 77
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 2-89 2.91e-03

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 39.52  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   2 RVVILG-SGVVGVASAYYLARAGHEVTVIDREAGPALET-------SFANAGQISPGYAAPWAAPGVPLKAVKWMFE-KH 72
Cdd:cd05242    1 KIVITGgTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLaevitwdGLSLGPWELPGADAVINLAGEPIACRRWTEAnKK 80

                         90
                 ....*....|....*..
gi 736057464  73 APLAIRLDGTRFQLQWM 89
Cdd:cd05242   81 EILSSRIESTRVLVEAI 97
 
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: 861.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPWAAPGVPLKAVKWMFEKHAPLAIRLD 80
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  81 GTRFQLQWMYQMLRNCTAERYAVNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEA 160
Cdd:PRK00711  81 GDPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQYEGRQGGTLQLFRTQQQLDAAAKDIAVLEEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 161 NVPFELLSPAELKKAEPALAAVSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCG 240
Cdd:PRK00711 161 GVPYELLDRDELAAVEPALAGVRHKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 241 SETVRADAYVVALGSYSTSFISNL-MKIPVYPLKGYSITAPIVNEAAAPVSTVLDETYKIAITRFDQRIRVGGMAEIVGF 319
Cdd:PRK00711 241 GGVITADAYVVALGSYSTALLKPLgVDIPVYPLKGYSLTVPITDEDRAPVSTVLDETYKIAITRFDDRIRVGGMAEIVGF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 320 DKKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADLIS 399
Cdd:PRK00711 321 DLRLDPARRETLEMVVRDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATRYKNLWLNTGHGTLGWTMACGSGQLLADLIS 400

                        410
                 ....*....|....*.
gi 736057464 400 GKMPAIQADDLSVHRY 415
Cdd:PRK00711 401 GRKPAIDADDLSVARY 416
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-414 3.41e-110

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 328.79  E-value: 3.41e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAgPALETSFANAGQISPGYAAPWAApgvplkavkwmfekhaplairld 80
Cdd:COG0665    3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGR-PGSGASGRNAGQLRPGLAALADR----------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  81 gtrfqlqwmyqmlrnctaeryavnkgRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEA 160
Cdd:COG0665   59 --------------------------ALVRLAREALDLWRELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRAL 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 161 NVPFELLSPAELKKAEPALAavSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCG 240
Cdd:COG0665  113 GLPVELLDAAELREREPGLG--SPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTE 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 241 SETVRADAYVVALGSYSTSFISNL-MKIPVYPLKGYSITAPIVneAAAPVSTVLDETyKIAITRF-DQRIRVGGMAEIVG 318
Cdd:COG0665  191 RGTVRADAVVLAAGAWSARLLPMLgLRLPLRPVRGYVLVTEPL--PDLPLRPVLDDT-GVYLRPTaDGRLLVGGTAEPAG 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 319 FDKKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTP-VSNLFLNTGHGTLGWTMSCGSGQLLADL 397
Cdd:COG0665  268 FDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPgAPGLYVATGHGGHGVTLAPAAGRLLADL 347

                        410
                 ....*....|....*..
gi 736057464 398 ISGKMPAIQADDLSVHR 414
Cdd:COG0665  348 ILGGEPPLDLAPFSPDR 364
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 2-404 1.11e-99

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 303.48  E-value: 1.11e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPWAAPGVPLKAVKWMFEKHAPLAIRLDG 81
Cdd:PRK12409   3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAAMETSFANGGQLSASNAEVWNHWATVLKGLKWMLRKDAPLLLNPKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  82 TRFQLQWMYQMLRNCtaERYAVNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQLDGAAKDIAVLQEAN 161
Cdd:PRK12409  83 SWHKYSWLAEFLAHI--PNYRANTIETVRLAIAARKHLFDIAEREGIDFDLERRGILHIYHDKAGFDHAKRVNALLAEGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 162 VPFELLSPAELKKAEPALAAVSHkltGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIA-----G 236
Cdd:PRK12409 161 LERRAVTPEEMRAIEPTLTGEYY---GGYYTPSDSTGDIHKFTTGLAAACARLGVQFRYGQEVTSIKTDGGGVVltvqpS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 237 VQCGSETVRADAYVVALGSYSTSFISNLM-KIPVYPLKGYSITAPIVNE---AAAPVSTVLDETYKIAITRF-DQRIRVG 311
Cdd:PRK12409 238 AEHPSRTLEFDGVVVCAGVGSRALAAMLGdRVNVYPVKGYSITVNLDDEasrAAAPWVSLLDDSAKIVTSRLgADRFRVA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 312 GMAEIVGFDKKLRAARRETLEMCVNDLFPGGGdTSKATFWTGLRPMTPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSG 391
Cdd:PRK12409 318 GTAEFNGYNRDIRADRIRPLVDWVRRNFPDVS-TRRVVPWAGLRPMMPNMMPRVGRGRRPGVFYNTGHGHLGWTLSAATA 396

                        410
                 ....*....|...
gi 736057464 392 QLLADLISGKMPA 404
Cdd:PRK12409 397 DLVAQVVAQKLPA 409
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-397 1.80e-76

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: 241.15  E-value: 1.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464    2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPGYAAPwaapgvplkavkwmfekhaplairldg 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYL--------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   82 trfqlqwmyqmlrnctaeryavNKGRMVRLAEYSRDCLQALRADTGIQYEGRTGGTLQLFRTQQQlDGAAKDIAVLQEAN 161
Cdd:pfam01266  54 ----------------------EPSELARLALEALDLWEELEEELGIDCGFRRCGVLVLARDEEE-EALEKLLAALRRLG 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  162 VPFELLSPAELKKAEPALAavshKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGkIAGVQcgs 241
Cdd:pfam01266 111 VPAELLDAEELRELEPLLP----GLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEGG-VWGVV--- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  242 ETVRADAYVVALGSYSTSFISNLMKIPVYPLKGYSI-TAPIV-NEAAAPVS-TVLDETYKIAITRFDQRIRVGGMAEIVG 318
Cdd:pfam01266 183 TTGEADAVVNAAGAWADLLALPGLRLPVRPVRGQVLvLEPLPeALLILPVPiTVDPGRGVYLRPRADGRLLLGGTDEEDG 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  319 FDK-KLRAARRETLEMCVNDLFPGGGDTSKAtfWTGLRPMtPDGTPIVGRTPVSNLFLNTGHGTLGWTMSCGSGQLLADL 397
Cdd:pfam01266 263 FDDpTPDPEEIEELLEAARRLFPALADIERA--WAGLRPL-PDGLPIIGRPGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
 17-401 5.64e-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: 132.49  E-value: 5.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   17 YYLARAGHEVTVIDREagpaletsfanagqiSPGYAAPWAAPGvplkavkwMFEKHAPlairldgtrfqlQWMYQmlrnc 96
Cdd:TIGR02352   1 WELAKRGHSVTLFDRD---------------PMGGGASWAAAG--------MLAPHAE------------CEYAE----- 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   97 taeryavnkGRMVRLAEYSR----DCLQALRADTGIQYEGRTGGTLQL---------FRTQQQLDGAAKdiavlqeanVP 163
Cdd:TIGR02352  41 ---------DPLFDLALESLrlypEWLEALKELTGLDTGYHQCGTLVVafdeddvehLRQLADLQSATG---------ME 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  164 FELLSPAELKKAEPALaavSHKLTGGLRLPGDETGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCGSET 243
Cdd:TIGR02352 103 VEWLSGRALRRLEPYL---SGGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTPSGD 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  244 VRADAYVVALGSYSTSfisnLMKIPVYPLKGYSI--TAPIVNEAAAPV-STVLDETYKIaITRFDQRIRVGGMAEIVGFD 320
Cdd:TIGR02352 180 VQADQVVLAAGAWAGE----LLPLPLRPVRGQPLrlEAPAVPLLNRPLrAVVYGRRVYI-VPRRDGRLVVGATMEESGFD 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  321 KKLRAARRETLEMCVNDLFPGGGDTSKATFWTGLRPMTPDGTPIVGRTP-VSNLFLNTGHGTLGWTMSCGSGQLLADLIS 399
Cdd:TIGR02352 255 TTPTLGGIKELLRDAYTILPALKEARLLETWAGLRPGTPDNLPYIGEHPeDRRLLIATGHYRNGILLAPATAEVIADLIL 334


                  ..
gi 736057464  400 GK 401
Cdd:TIGR02352 335 GK 336
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
3-257 1.20e-15

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 78.26  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   3 VVILGSGVVGVASAYYLARA-GHEVTVIDREAGPALETSFANAGQISPGYAAPwaaPGVpLKAvkwmfekhaplairldg 81
Cdd:COG0579    7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSGVIHAGLYYT---PGS-LKA----------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  82 trfqlqwmyqmlrnctaeRYAVNKGRMvrLAEYSRdclqalraDTGIQYEgRTgGTLQLFRTQQQLDGAAKDIAVLQEAN 161
Cdd:COG0579   66 ------------------RLCVEGNEL--FYELCR--------ELGIPFK-RC-GKLVVATGEEEVAFLEKLYERGKANG 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 162 VP-FELLSPAELKKAEPalaAVSHKLTGGLRLPgdETGDC--QLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIaGVQ 238
Cdd:COG0579  116 VPgLEILDREELRELEP---LLSDEGVAALYSP--STGIVdpGALTRALAENAEANGVELLLNTEVTGIEREGDGW-EVT 189

                        250
                 ....*....|....*....
gi 736057464 239 CGSETVRADAYVVALGSYS 257
Cdd:COG0579  190 TNGGTIRARFVINAAGLYA 208
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 1-253 8.42e-09

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: 57.17  E-value: 8.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIdrEAGPALetsfanaGqispGYAAPW--AAPGVPL------------KAVK 66
Cdd:COG3349    4 PRVVVVGGGLAGLAAAVELAEAGFRVTLL--EARPRL-------G----GRARSFpdPDTGLPIdngqhvllgcyrNTLD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  67 WMfeKHAPLAIRLDGTRfQLQWMYQMLRNCTAER----------YAVNKGRMVRLAEYSRdCLQALRADTGIQYEGRTGG 136
Cdd:COG3349   71 LL--RRIGAADNLVGPE-PLQFPLPGGRRWTLRAprlpaplhllRALLRAPGLSLADRLA-LLRLLTACRERRWRELDDI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 137 TL-QLFRTQQQLDGAAKD------IAVLqeaNVPFELLSpaelkkAEPALAAVSHKLTGG-----LRLPGDETGDcqLFT 204
Cdd:COG3349  147 SVaDWLRRHGQSPRLIRRlwepllLAAL---NTPPEQAS------ARLALTVLRETLLAGpaasdLLVPRGPLSE--LFV 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 736057464 205 TRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCGS-ETVRADAYVVAL 253
Cdd:COG3349  216 DPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADgETVPADAVVLAV 265
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-252 1.87e-07

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 52.93  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPaletsfanaGqispGYAAPWAAPGV----------PLKAVKWMFE 70
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP---------G----GRARTFERPGFrfdvgpsvltMPGVLERLFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  71 ----------KHAPLAIRL---DGTRFQL-----QWMYQMLRNCTAERYAVNK--GRMVRLAEYS------------RDC 118
Cdd:COG1233   71 elgledylelVPLDPAYRVpfpDGRALDLprdleRTAAELERLFPGDAEAYRRflAELRRLYDALledllyrpllslRDL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 119 LQALRADTGIQYEGRTGGTL--QLF---RTQQQLDGAAKDIAVlqeanVPFEllSPAelkkAEPALAAVSHklTGGLRLP 193
Cdd:COG1233  151 LRPLALARLLRLLLRSLRDLlrRYFkdpRLRALLAGQALYLGL-----SPDR--TPA----LYALIAYLEY--AGGVWYP 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 194 gdeTGDCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQCGS-ETVRADAYVVA 252
Cdd:COG1233  218 ---KGGMGALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLADgEEIRADAVVSN 274
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-257 3.80e-07

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 51.75  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   1 MRVVILGSGVVGVASAYYLARA--GHEVTVIDREAGPALETSFANAGQISPG--YAapwaaPGvPLKAvkwmfekhapla 76
Cdd:PRK11728   3 YDFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPARHQTGHNSGVIHAGvyYT-----PG-SLKA------------ 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  77 irldgtrfqlqwmyqmlRNCTaeryavnkgRMVRLaeysrdcLQALRADTGIQYEgrTGGTLQLFRTQQQLDGAAKDIAV 156
Cdd:PRK11728  65 -----------------RFCR---------RGNEA-------TKAFCDQHGIPYE--ECGKLLVATSELELERMEALYER 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 157 LQEANVPFELLSPAELKKAEPALAAVshkltGGLRLPgdETG--DCQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKI 234
Cdd:PRK11728 110 ARANGIEVERLDAEELREREPNIRGL-----GAIFVP--STGivDYRAVAEAMAELIQARGGEIRLGAEVTALDEHANGV 182

                        250       260
                 ....*....|....*....|...
gi 736057464 235 AgVQCGSETVRADAYVVALGSYS 257
Cdd:PRK11728 183 V-VRTTQGEYEARTLINCAGLMS 204
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 2-400 6.09e-07

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: 51.77  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANAGQISPgyaapwaapgvplkavkwMFEKHAPLAIRLDG 81
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYP------------------LLSKDDNALSRFFR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  82 TRFQlqwmyqmlrnctaeryavnkgrmvrlaeYSRDCLQALrADTGIQYEGRTGGTLQLFRTqqqlDGAAKDIAVLQEAN 161
Cdd:PRK01747 324 AAFL----------------------------FARRFYDAL-PAAGVAFDHDWCGVLQLAWD----EKSAEKIAKMLALG 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 162 VPFEL---LSPAELkkAEPALAAVSHkltGGLRLPgdETG--DCQLFTTRLAALAESlGVKFRYNTPIDALAIAGGKIAG 236
Cdd:PRK01747 371 LPAELaraLDAEEA--EELAGLPVPC---GGIFYP--QGGwlCPAELCRALLALAGQ-QLTIHFGHEVARLEREDDGWQL 442

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 237 VQCGSETVRADAYVVALGSYSTSFiSNLMKIPVYPLKGYSITAPIVNEAAAPVSTVLDETYKIAITRfDQRIRVGGMAEI 316
Cdd:PRK01747 443 DFAGGTLASAPVVVLANGHDAARF-AQTAHLPLYSVRGQVSHLPTTPALSALKQVLCYDGYLTPQPA-NGTHCIGASYDR 520

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 317 VGFDKKLRAA----RRETLEMCVNDL-FPGGGDTSKATFWTGLRPMTPDGTPIVGRTP---------------------- 369
Cdd:PRK01747 521 DDTDTAFREAdhqeNLERLAECLPQAlWAKEVDVSALQGRVGFRCASRDRLPMVGNVPdeaatlaeyaalanqqpardap 600

                        410       420       430
                 ....*....|....*....|....*....|..
gi 736057464 370 -VSNLFLNTGHGTLGWTMSCGSGQLLADLISG 400
Cdd:PRK01747 601 rLPGLYVAGALGSRGLCSAPLGAELLASQIEG 632
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-33 8.84e-07

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: 50.24  E-value: 8.84e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA 33
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-36 4.45e-06

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


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 48.40  E-value: 4.45e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPA 36
Cdd:COG0654    4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-45 6.43e-06

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: 44.12  E-value: 6.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 736057464    2 RVVILGSGVVGVASAYYLARAGHEVTVI----------DREAGPALETSFANAG 45
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVerrdrllpgfDPEIAKILQEKLEKNG 54
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 2-34 7.20e-06

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: 47.82  E-value: 7.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDR--EAG 34
Cdd:COG0493  123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEAldKPG 157
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-33 1.11e-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: 47.52  E-value: 1.11e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASD 34
PRK07233 PRK07233
hypothetical protein; Provisional
 2-37 1.67e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 46.80  E-value: 1.67e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIdrEAGPAL 37
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVF--EADDQL 34
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 2-37 1.81e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 46.79  E-value: 1.81e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVidREAGPAL 37
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTI--FEAGPKL 172
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
5-63 1.96e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 42.13  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 736057464    5 ILGSGVVGVASAYYLARAGHEVTVIDREAGPAletsfanagqispGYAAPWAAPGVPLK 63
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG-------------GNAYSYRVPGYVFD 46
HI0933_like pfam03486
HI0933-like protein;
201-257 3.85e-05

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 45.65  E-value: 3.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736057464  201 QLFTTRLAAL---------AESLGVKFRYNTPIDALAIAGGKIAGVQCGSETVRADAYVVALGSYS 257
Cdd:pfam03486 100 RLFPDSDKASdivdallneLKELGVKIRLRTRVLSVEKDDDGRFRVKTGGEELEADSLVLATGGLS 165
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 2-32 4.39e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 45.54  E-value: 4.39e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDRE 32
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFERA 175
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-32 4.70e-05

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: 45.00  E-value: 4.70e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 736057464    1 MRVVILGSGVVGVASAYYLARAGHEVTVIDRE 32
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
PRK07588 PRK07588
FAD-binding domain;
1-39 7.57e-05

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 44.73  E-value: 7.57e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIdrEAGPALET 39
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLI--ERAPELRT 37
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 1-64 8.25e-05

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: 44.69  E-value: 8.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVID-REAGPALETSFANAG---QISPGYAAPWAA-------PGVPLKA 64
Cdd:COG0771    5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDdRPAPELAAAELEAPGvevVLGEHPEELLDGadlvvksPGIPPDH 79
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-36 1.07e-04

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 44.07  E-value: 1.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPA 36
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHL 36
trkA PRK09496
Trk system potassium transporter TrkA;
1-31 1.29e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 43.96  E-value: 1.29e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDR 31
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDT 31
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 193-257 1.59e-04

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: 43.67  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464 193 PGDETGdcQLFTTRLAALAESLGVKFRYNTPIDALAIAGGKIAGVQC-----GSETVRADAYVVALGSYS 257
Cdd:COG1053  128 AGDGTG--HALLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVVArdrtgEIVRIRAKAVVLATGGFG 195
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-33 1.61e-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: 41.83  E-value: 1.61e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 736057464    3 VVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGA 31
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 2-35 2.50e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 43.18  E-value: 2.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQA 228
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 2-35 2.82e-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: 42.49  E-value: 2.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:COG0446  126 RAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 1-36 2.89e-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: 42.93  E-value: 2.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPA 36
Cdd:COG2072    7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG 42
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-31 3.60e-04

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 42.43  E-value: 3.60e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   1 MRVVILGSGVVGVASAYYLAR---AGHEVTVIDR 31
Cdd:COG1252    2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDP 35
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-45 4.22e-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: 41.92  E-value: 4.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 736057464    2 RVVILGSGVVGVASAYYLARAGHEVTVI----------DREAGPALETSFANAG 45
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIealdrllrafDEEISAALEKALEKNG 207
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
209-256 4.25e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 42.55  E-value: 4.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736057464 209 ALAESLGVKFRYNTPIDALAIAGGKIAGVQCGS-----ETVRADAYVVALGSY 256
Cdd:PRK08274 139 RSAERLGVEIRYDAPVTALELDDGRFVGARAGSaaggaERIRAKAVVLAAGGF 191
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 1-34 4.61e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 42.47  E-value: 4.61e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDR--EAG 34
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEArdKAG 176
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
2-33 5.34e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 42.22  E-value: 5.34e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIdrEA 33
Cdd:COG1231    9 DVVIVGAGLAGLAAARELRKAGLDVTVL--EA 38
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-47 5.88e-04

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: 40.18  E-value: 5.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 736057464     2 RVVILGSGVVGVASAYYLARAGHEVTVIDREA----------GPALETSFANAGQI 47
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRParlrqlesllGARFTTLYSQAELL 77
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-34 6.46e-04

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 41.57  E-value: 6.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAG 34
Cdd:PRK06129   3 GSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPA 36
PRK05868 PRK05868
FAD-binding protein;
2-35 6.85e-04

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 41.51  E-value: 6.85e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:PRK05868   3 TVVVSGASVAGTAAAYWLGRHGYSVTMVERHPGL 36
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-33 9.81e-04

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 40.87  E-value: 9.81e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 736057464   3 VVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGE 33
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
1-35 1.02e-03

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 41.25  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 736057464   1 MRVVILGSGVVGVASAYYLARAgHEVTVIdrEAGP 35
Cdd:COG2907    4 MRIAVIGSGISGLTAAWLLSRR-HDVTLF--EAND 35
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-31 1.10e-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: 1.10e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDR 31
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDK 126
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-35 1.19e-03

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 41.05  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 736057464   3 VVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 16-400 1.33e-03

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: 40.71  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   16 AYYLARAGHEVTVIDREAGPALETSfanagqispgyaapwaapGVPLKAVKwmfekhaPLaIRLDGTRFqlqwmyqmlrn 95
Cdd:TIGR03197   2 AYSLARRGWQVTLYEQDEAPAQGAS------------------GNPQGALY-------PL-LSADDNPL----------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   96 ctaeryavnkGRMVRLA-EYSRDCLQALrADTGIQYEGRTGGTLQLFRT---QQQLDgaakdiAVLQEANVPFELLSPAE 171
Cdd:TIGR03197  45 ----------SRFFLAAfLYARRFYRQL-AEAGFPFDHEWCGVLQLAYDekeAERLQ------KLLEQLGFPEELARWVD 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  172 LKKAEPALAAVSHKltGGLRLPgdETG--DCQLFTTRLAALAEsLGVKFRYNTPIDALAIAGGKIAGVQCGSETVRADAY 249
Cdd:TIGR03197 108 AEQASQLAGIPLPY--GGLFFP--QGGwlSPPQLCRALLAHAG-IRLTLHFNTEITSLERDGEGWQLLDANGEVIAASVV 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  250 VVALGSYSTSFiSNLMKIPVYPLKGYSITAPiVNEAAAPVSTVLdeTYKIAIT-RFDQRIRVGGMAEIVGFDKKLR-AAR 327
Cdd:TIGR03197 183 VLANGAQAPQL-AQTAHLPLRPVRGQVSHLP-ATEALSALKTVL--CYDGYLTpANNGEHCIGASYDRNDDDLALReADH 258

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464  328 RETLEMCVNDL----FPGGGDTSKATFWTGLRPMTPDGTPIVGRTP--------------------------VSNLFLNT 377
Cdd:TIGR03197 259 AENLERLAECLpalaWASEVDISALQGRVGVRCASPDHLPLVGAVPdfeaikeayaelakdknrpiaepapyYPGLYVLG 338

                         410       420
                  ....*....|....*....|...
gi 736057464  378 GHGTLGWTMSCGSGQLLADLISG 400
Cdd:TIGR03197 339 GLGSRGLTSAPLAAEILAAQICG 361
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 2-89 2.91e-03

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 39.52  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736057464   2 RVVILG-SGVVGVASAYYLARAGHEVTVIDREAGPALET-------SFANAGQISPGYAAPWAAPGVPLKAVKWMFE-KH 72
Cdd:cd05242    1 KIVITGgTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLaevitwdGLSLGPWELPGADAVINLAGEPIACRRWTEAnKK 80

                         90
                 ....*....|....*..
gi 736057464  73 APLAIRLDGTRFQLQWM 89
Cdd:cd05242   81 EILSSRIESTRVLVEAI 97
solA PRK11259
N-methyl-L-tryptophan oxidase;
3-31 3.30e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 39.43  E-value: 3.30e-03
                         10        20
                 ....*....|....*....|....*....
gi 736057464   3 VVILGSGVVGVASAYYLARAGHEVTVIDR 31
Cdd:PRK11259   6 VIVIGLGSMGSAAGYYLARRGLRVLGLDR 34
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 1-38 4.08e-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: 38.94  E-value: 4.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGpALE 38
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPE-ALE 39
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 1-30 5.16e-03

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: 38.00  E-value: 5.16e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 736057464    1 MRVVILGSGVVGVASAYYLARAGHEVTVID 30
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVIGVD 30
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 2-38 5.31e-03

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 37.90  E-value: 5.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 736057464    2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGpALE 38
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEE-ALE 36
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 2-45 5.66e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.91  E-value: 5.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVI----------DREAGPALETSFANAG 45
Cdd:COG1249  170 SLVVIGGGYIGLEFAQIFARLGSEVTLVergdrllpgeDPEISEALEKALEKEG 223
PRK13984 PRK13984
putative oxidoreductase; Provisional
 2-35 6.47e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 38.98  E-value: 6.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:PRK13984 285 KVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKP 318
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-44 7.04e-03

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


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 38.43  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREAGPALETSFANA 44
Cdd:PRK14619   5 KTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGLSLAAVLADA 48
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-35 7.22e-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: 7.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 736057464   2 RVVILGSGVVGVASAYYLARAGHEVTVIDREAGP 35
Cdd:COG1251  144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177
PRK07045 PRK07045
putative monooxygenase; Reviewed
 3-33 8.06e-03

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 38.35  E-value: 8.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 736057464   3 VVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:PRK07045   8 VLINGSGIAGVALAHLLGARGHSVTVVERAA 38
PRK12921 PRK12921
oxidoreductase;
1-33 9.62e-03

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 37.92  E-value: 9.62e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 736057464   1 MRVVILGSGVVGVASAYYLARAGHEVTVIDREA 33
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPK 33
 
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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