NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1502504201|ref|WP_122257309|]
View 

FAD-dependent oxidoreductase, partial [Pseudomonas salomonii]

Protein Classification

FAD dependent oxidoreductase family protein( domain architecture ID 1750071)

FAD dependent oxidoreductase family protein may catalyze the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Gene Ontology:  GO:0071949|GO:0016491
PubMed:  27714222

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DAO super family cl40741
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 4-234 4.16e-86

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.


The actual alignment was detected with superfamily member PRK00711:

Pssm-ID: 477422 [Multi-domain]  Cd Length: 416  Bit Score: 261.27  E-value: 4.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLSYRYVAPLADKGVPLQAIGWLLRGDSPLKLRPRL 83
Cdd:PRK00711    2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  84 DPQQWRWMAAFIGACRGSVNKRNAAHLLRLASLSQATLEQWREGDRLEgFDWRRNGKLVTFRNAASFEHARS--KVINS- 160
Cdd:PRK00711   82 DPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQ-YEGRQGGTLQLFRTQQQLDAAAKdiAVLEEa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 161 -VQQQVMSAADCAQVEPALMGA--DFLGGIYTPNEEVADCHAFCQRLAARLQASG-RCRF------LL--GRKVTRIRHA 228
Cdd:PRK00711  161 gVPYELLDRDELAAVEPALAGVrhKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGvKFRFntpvdgLLveGGRITGVQTG 240


                  ....*.
gi 1502504201 229 DGAVQA 234
Cdd:PRK00711  241 GGVITA 246
 
Name Accession Description Interval E-value
PRK00711 PRK00711
D-amino acid dehydrogenase;
4-234 4.16e-86

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 261.27  E-value: 4.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLSYRYVAPLADKGVPLQAIGWLLRGDSPLKLRPRL 83
Cdd:PRK00711    2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  84 DPQQWRWMAAFIGACRGSVNKRNAAHLLRLASLSQATLEQWREGDRLEgFDWRRNGKLVTFRNAASFEHARS--KVINS- 160
Cdd:PRK00711   82 DPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQ-YEGRQGGTLQLFRTQQQLDAAAKdiAVLEEa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 161 -VQQQVMSAADCAQVEPALMGA--DFLGGIYTPNEEVADCHAFCQRLAARLQASG-RCRF------LL--GRKVTRIRHA 228
Cdd:PRK00711  161 gVPYELLDRDELAAVEPALAGVrhKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGvKFRFntpvdgLLveGGRITGVQTG 240


                  ....*.
gi 1502504201 229 DGAVQA 234
Cdd:PRK00711  241 GGVITA 246
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-234 2.47e-32

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 120.40  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEaRDSLGSETSFANGGQLSYRYVAPLADkgvplqaigwllrgdsplklr 80
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSGASGRNAGQLRPGLAALADR--------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  81 prldpqqwrwmaafigacrgsvnkrnaahllRLASLSQATLEQWREGDRLEG--FDWRRNGKLVTFRNAASFEHARsKVI 158
Cdd:COG0665    59 -------------------------------ALVRLAREALDLWRELAAELGidCDFRRTGVLYLARTEAELAALR-AEA 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 159 NSVQQ-----QVMSAADCAQVEPALMGADFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAVQ 233
Cdd:COG0665   107 EALRAlglpvELLDAAELREREPGLGSPDYAGGLYDPDDGHVDPAKLVRALARAARAAG-VRIREGTPVTGLEREGGRVT 185


                  .
gi 1502504201 234 A 234
Cdd:COG0665   186 G 186
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 4-233 4.54e-27

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: 105.94  E-value: 4.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLS--YRYVAPladkgvplqaigwllrgdsplklrp 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHpgLRYLEP------------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  82 rldpqqwrwmaafigacrgsvnkrnaahlLRLASLSQATLEQWREGDRLEG--FDWRRNGKLVTFRNAAS---FEHARSK 156
Cdd:pfam01266  56 -----------------------------SELARLALEALDLWEELEEELGidCGFRRCGVLVLARDEEEealEKLLAAL 106

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502504201 157 VINSVQQQVMSAADCAQVEPALmgADFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAVQ 233
Cdd:pfam01266 107 RRLGVPAELLDAEELRELEPLL--PGLRGGLFYPDGGHVDPARLLRALARAAEALG-VRIIEGTEVTGIEEEGGVWG 180
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 3-37 7.07e-05

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 43.40  E-value: 7.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:TIGR01350 171 ESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRI 205
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-32 1.49e-03

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: 37.87  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 1502504201    4 RVCIIGGGVIGLASAYALVRAGHEVTVIE 32
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 3-31 4.41e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 37.27  E-value: 4.41e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGG-GVIGLASAYALVRAGHEVTVI 31
Cdd:cd05265     1 MKILIIGGtRFIGKALVEELLAAGHDVTVF 30
 
Name Accession Description Interval E-value
PRK00711 PRK00711
D-amino acid dehydrogenase;
4-234 4.16e-86

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 261.27  E-value: 4.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLSYRYVAPLADKGVPLQAIGWLLRGDSPLKLRPRL 83
Cdd:PRK00711    2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPALETSFANAGQISPGYAAPWAAPGVPLKAIKWLFQRHAPLAIRPDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  84 DPQQWRWMAAFIGACRGSVNKRNAAHLLRLASLSQATLEQWREGDRLEgFDWRRNGKLVTFRNAASFEHARS--KVINS- 160
Cdd:PRK00711   82 DPFQLRWMWQMLRNCTASRYAVNKSRMVRLAEYSRDCLKALRAETGIQ-YEGRQGGTLQLFRTQQQLDAAAKdiAVLEEa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 161 -VQQQVMSAADCAQVEPALMGA--DFLGGIYTPNEEVADCHAFCQRLAARLQASG-RCRF------LL--GRKVTRIRHA 228
Cdd:PRK00711  161 gVPYELLDRDELAAVEPALAGVrhKLVGGLRLPNDETGDCQLFTQRLAAMAEQLGvKFRFntpvdgLLveGGRITGVQTG 240


                  ....*.
gi 1502504201 229 DGAVQA 234
Cdd:PRK00711  241 GGVITA 246
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 3-232 1.46e-38

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 137.85  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLSYRYVAPLADKGVPLQAIGWLLRGDSPLKLRPR 82
Cdd:PRK12409    2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYAAMETSFANGGQLSASNAEVWNHWATVLKGLKWMLRKDAPLLLNPK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  83 LDPQQWRWMAAFIGACRGSvnKRNAAHLLRLASLSQATLEQWREGDRLEgFDWRRNGKLVTFRNAASFEHAR--SKVINS 160
Cdd:PRK12409   82 PSWHKYSWLAEFLAHIPNY--RANTIETVRLAIAARKHLFDIAEREGID-FDLERRGILHIYHDKAGFDHAKrvNALLAE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502504201 161 --VQQQVMSAADCAQVEPALMGaDFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAV 232
Cdd:PRK12409  159 ggLERRAVTPEEMRAIEPTLTG-EYYGGYYTPSDSTGDIHKFTTGLAAACARLG-VQFRYGQEVTSIKTDGGGV 230
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-234 2.47e-32

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 120.40  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEaRDSLGSETSFANGGQLSYRYVAPLADkgvplqaigwllrgdsplklr 80
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSGASGRNAGQLRPGLAALADR--------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  81 prldpqqwrwmaafigacrgsvnkrnaahllRLASLSQATLEQWREGDRLEG--FDWRRNGKLVTFRNAASFEHARsKVI 158
Cdd:COG0665    59 -------------------------------ALVRLAREALDLWRELAAELGidCDFRRTGVLYLARTEAELAALR-AEA 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 159 NSVQQ-----QVMSAADCAQVEPALMGADFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAVQ 233
Cdd:COG0665   107 EALRAlglpvELLDAAELREREPGLGSPDYAGGLYDPDDGHVDPAKLVRALARAARAAG-VRIREGTPVTGLEREGGRVT 185


                  .
gi 1502504201 234 A 234
Cdd:COG0665   186 G 186
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 4-233 4.54e-27

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: 105.94  E-value: 4.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGGQLS--YRYVAPladkgvplqaigwllrgdsplklrp 81
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHpgLRYLEP------------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  82 rldpqqwrwmaafigacrgsvnkrnaahlLRLASLSQATLEQWREGDRLEG--FDWRRNGKLVTFRNAAS---FEHARSK 156
Cdd:pfam01266  56 -----------------------------SELARLALEALDLWEELEEELGidCGFRRCGVLVLARDEEEealEKLLAAL 106

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502504201 157 VINSVQQQVMSAADCAQVEPALmgADFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAVQ 233
Cdd:pfam01266 107 RRLGVPAELLDAEELRELEPLL--PGLRGGLFYPDGGHVDPARLLRALARAAEALG-VRIIEGTEVTGIEEEGGVWG 180
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
5-232 1.08e-11

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 63.63  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   5 VCIIGGGVIGLASAYALVRA-GHEVTVIEARDSLGSETSFANGGqlsyryVapladkgvplqaigwllrGDSPLKLRPrl 83
Cdd:COG0579     7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVAQESSGNNSG------V------------------IHAGLYYTP-- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  84 dpqqwrwmaafigacrGSVNkrnaahllrlASLSQATLEQWREGDRLEGFDWRRNGKLVTFRNAASFE-----HARSKVi 158
Cdd:COG0579    61 ----------------GSLK----------ARLCVEGNELFYELCRELGIPFKRCGKLVVATGEEEVAfleklYERGKA- 113

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502504201 159 NSVQQ-QVMSAADCAQVEPaLMGADFLGGIYTPNEEVADCHAFCQRLAARLQASGrCRFLLGRKVTRIRHADGAV 232
Cdd:COG0579   114 NGVPGlEILDREELRELEP-LLSDEGVAALYSPSTGIVDPGALTRALAENAEANG-VELLLNTEVTGIEREGDGW 186
PRK07233 PRK07233
hypothetical protein; Provisional
 4-38 4.39e-11

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 61.83  E-value: 4.39e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLG 35
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
3-233 2.91e-10

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 59.16  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG----SETSFAN------GGQL---SYRYVAPLADK-GVPL---- 64
Cdd:COG1231     8 KDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGgrvwTLRFGDDglyaelGAMRippSHTNLLALARElGLPLepfp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  65 QAIGWLLRGDSPLKLRPRLDPQQWRWMAAFIGACRGSVNKRNAAHLLRLASLSQATLEQWREGDRLEGFDWRRNGKLVTF 144
Cdd:COG1231    88 NENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAELDRESLAEWLRRNGASPSARRLLGLLGAG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 145 RNAASFEHarskvinsvqqqvMSAADCAQVEPALMGAD----FLGGIytpneevadcHAFCQRLAARLQAsgrcRFLLGR 220
Cdd:COG1231   168 EYGADPDE-------------LSLLDLLRYAASAGGGAqqfrIVGGM----------DQLPRALAAELGD----RIRLGA 220

                         250
                  ....*....|...
gi 1502504201 221 KVTRIRHADGAVQ 233
Cdd:COG1231   221 PVTRIRQDGDGVT 233
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 3-38 1.05e-09

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: 57.84  E-value: 1.05e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG0493   122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 1-38 1.93e-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: 56.79  E-value: 1.93e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG3349     2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLG 39
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 3-38 3.82e-09

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: 55.99  E-value: 3.82e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVG 37
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 3-38 9.17e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 54.88  E-value: 9.17e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK12771  138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLG 173
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-37 1.20e-07

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 51.30  E-value: 1.20e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:COG1251   142 GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-37 1.22e-07

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: 47.97  E-value: 1.22e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-65 1.64e-07

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: 50.78  E-value: 1.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETsfanGGQLSYRYVAPLADKGVPLQ 65
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAF----DEEISAALEKALEKNGVEVR 211
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
1-232 2.94e-07

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 50.21  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRA--GHEVTVIEARDSLGSETSFANGGQL-SYRYVAP------LADKGVplqaigwll 71
Cdd:PRK11728    1 AMYDFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPARHQTGHNSGVIhAGVYYTPgslkarFCRRGN--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201  72 rgdsplklrprldpqqwRWMAAFigaCrgsvnkrnAAHllrlaslsqatleqwregdrleGFDWRRNGKLVTFRNAASFE 151
Cdd:PRK11728   72 -----------------EATKAF---C--------DQH----------------------GIPYEECGKLLVATSELELE 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201 152 -----HARSKViNSVQQQVMSAADCAQVEPALMGadfLGGIYTPNEEVADCHAFCQRLAARLQASGRcRFLLGRKVTRIR 226
Cdd:PRK11728  102 rmealYERARA-NGIEVERLDAEELREREPNIRG---LGAIFVPSTGIVDYRAVAEAMAELIQARGG-EIRLGAEVTALD 176


                  ....*..
gi 1502504201 227 -HADGAV 232
Cdd:PRK11728  177 eHANGVV 183
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
7-38 3.04e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 46.37  E-value: 3.04e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1502504201   7 IIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG 32
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 3-38 3.30e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 50.16  E-value: 3.30e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK12810  144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIG 179
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 4-38 4.32e-07

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: 49.86  E-value: 4.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG2072     8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG 42
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-38 5.35e-07

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 49.46  E-value: 5.35e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG1233     2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPG 39
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 3-38 7.52e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 49.02  E-value: 7.52e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK11749  141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAG 176
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 2-37 1.12e-06

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: 48.27  E-value: 1.12e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:COG0446   124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-38 1.18e-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: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
PLN02576 PLN02576
protoporphyrinogen oxidase
 2-47 1.34e-06

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 48.47  E-value: 1.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRA-GHEVTVIEARDSLGSE-TSFANGG 47
Cdd:PLN02576   12 SKDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNiTSVSEDG 59
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 2-42 1.41e-06

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: 48.69  E-value: 1.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETS 42
Cdd:PRK01747  260 ARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGAS 300
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 3-41 2.39e-06

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 47.48  E-value: 2.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSET 41
Cdd:PRK06292  170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLE 208
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 3-38 2.76e-06

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 47.54  E-value: 2.76e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAG--HEVTVIEARDSLG 38
Cdd:PRK11883    1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLG 38
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
1-38 3.35e-06

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 47.03  E-value: 3.35e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAgHEVTVIEARDSLG 38
Cdd:COG2907     2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLG 38
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 3-37 3.86e-06

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: 47.00  E-value: 3.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1502504201   3 KRVCIIGGGVIG--LASAYAlvRAGHEVTVIEARDSL 37
Cdd:COG1249   169 KSLVVIGGGYIGleFAQIFA--RLGSEVTLVERGDRL 203
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 3-72 4.02e-06

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 47.03  E-value: 4.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDslgsetsfANGGQLSY-----RYVAPLADKGV-PLQAIGWLLR 72
Cdd:PRK12814  194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANE--------QAGGMMRYgiprfRLPESVIDADIaPLRAMGAEFR 261
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
1-38 4.78e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.78  E-value: 4.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG1148   139 VNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELG 176
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 1-37 1.03e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 45.91  E-value: 1.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1502504201   1 MAKRVCIIGGGVIG--LASAYALVraGHEVTVIEARDSL 37
Cdd:PRK06416  171 VPKSLVVIGGGYIGveFASAYASL--GAEVTIVEALPRI 207
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-38 1.24e-05

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 45.25  E-value: 1.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:COG3380     2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVG 39
PLN02268 PLN02268
probable polyamine oxidase
 5-38 2.18e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 44.68  E-value: 2.18e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PLN02268    3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIG 36
PRK07208 PRK07208
hypothetical protein; Provisional
 1-38 4.21e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 43.72  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK07208    3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVG 40
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 14-38 4.95e-05

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: 43.63  E-value: 4.95e-05
                          10        20
                  ....*....|....*....|....*
gi 1502504201  14 GLASAYALVRAGHEVTVIEARDSLG 38
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVG 27
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 3-37 7.07e-05

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 43.40  E-value: 7.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:TIGR01350 171 ESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRI 205
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-47 8.51e-05

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 43.05  E-value: 8.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGG 47
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGG 44
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 3-34 1.50e-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: 1.50e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEAR 34
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 4-31 1.68e-04

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: 41.77  E-value: 1.68e-04
                          10        20
                  ....*....|....*....|....*...
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVI 31
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLV 29
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
2-37 2.08e-04

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 41.83  E-value: 2.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:PRK04965  141 AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
1-38 2.15e-04

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 41.56  E-value: 2.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PRK08163    3 KVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
PRK06847 PRK06847
hypothetical protein; Provisional
 1-35 2.71e-04

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.40  E-value: 2.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARD 35
Cdd:PRK06847    3 AVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
PRK06753 PRK06753
hypothetical protein; Provisional
 4-37 3.12e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 41.21  E-value: 3.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSL 37
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 3-35 4.72e-04

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


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 40.48  E-value: 4.72e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARD 35
Cdd:COG1250     3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISP 35
PRK13984 PRK13984
putative oxidoreductase; Provisional
 3-68 6.01e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 40.52  E-value: 6.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFangGQLSYRYVAPLADKGVP-LQAIG 68
Cdd:PRK13984  284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRY---GIPSYRLPDEALDKDIAfIEALG 347
PRK07588 PRK07588
FAD-binding domain;
3-33 7.07e-04

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 40.10  E-value: 7.07e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEA 33
Cdd:PRK07588    1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIER 31
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-32 7.14e-04

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.05  E-value: 7.14e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIE 32
Cdd:COG0569    94 LKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 3-33 1.02e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 39.52  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEA 33
Cdd:PRK06327  184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEA 214
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 3-35 1.37e-03

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 39.25  E-value: 1.37e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARD 35
Cdd:PRK09564  150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLED 182
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-32 1.49e-03

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: 37.87  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*....
gi 1502504201    4 RVCIIGGGVIGLASAYALVRAGHEVTVIE 32
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
PLN02976 PLN02976
amine oxidase
 3-38 1.50e-03

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 39.47  E-value: 1.50e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1502504201    3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PLN02976   694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIG 729
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 3-35 1.63e-03

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


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 38.91  E-value: 1.63e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARD 35
Cdd:COG0771     5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRP 37
PLN02612 PLN02612
phytoene desaturase
 4-38 1.96e-03

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 39.06  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PLN02612   95 KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLG 129
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 5-47 1.99e-03

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: 38.66  E-value: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANGG 47
Cdd:COG1053     6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGG 48
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 3-38 2.01e-03

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 38.66  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGGGVIGLASAYALVR----AGHEVTVIEARDSLG 38
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAYYLEKeipeLPVELTLVEASDRVG 42
PRK07538 PRK07538
hypothetical protein; Provisional
 4-33 2.13e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 38.72  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEA 33
Cdd:PRK07538    2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEA 31
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-33 2.14e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 38.69  E-value: 2.14e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEA 33
Cdd:PRK06185    5 ETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEK 37
PLN03000 PLN03000
amine oxidase
 5-38 2.40e-03

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 38.85  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSLG 38
Cdd:PLN03000  187 VVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPG 220
trkA PRK09496
Trk system potassium transporter TrkA;
2-32 2.60e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 38.56  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1502504201   2 AKRVCIIGGGVIGLASAYALVRAGHEVTVIE 32
Cdd:PRK09496  231 VKRVMIVGGGNIGYYLAKLLEKEGYSVKLIE 261
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 5-57 2.88e-03

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 38.36  E-value: 2.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSLgsetsfanGGQLSYRYVAPL 57
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFL--------GGMLTSGLVGPD 46
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
3-35 3.02e-03

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 38.19  E-value: 3.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1502504201   3 KRVCIIGGGVIGLASAYAL---VRAGHEVTVIEARD 35
Cdd:COG1252     2 KRIVIVGGGFAGLEAARRLrkkLGGDAEVTLIDPNP 37
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 3-35 3.27e-03

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 38.05  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAG-HEVTVIEaRD 35
Cdd:PRK07688   25 KHVLIIGAGALGTANAEMLVRAGvGKVTIVD-RD 57
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 4-31 4.31e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 37.52  E-value: 4.31e-03
                          10        20
                  ....*....|....*....|....*...
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVI 31
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQAGHDVTLV 29
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 4-35 4.32e-03

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


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 36.75  E-value: 4.32e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARD 35
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISE 32
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 3-31 4.41e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 37.27  E-value: 4.41e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGG-GVIGLASAYALVRAGHEVTVI 31
Cdd:cd05265     1 MKILIIGGtRFIGKALVEELLAAGHDVTVF 30
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
1-38 4.55e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 37.85  E-value: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVI--EARDSLG 38
Cdd:COG3573     4 MDADVIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLG 43
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-40 4.64e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 37.41  E-value: 4.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSE 40
Cdd:COG0492   142 KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS 179
PLN02487 PLN02487
zeta-carotene desaturase
 4-42 6.16e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 37.47  E-value: 6.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETS 42
Cdd:PLN02487   77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVG 115
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-49 6.32e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 37.02  E-value: 6.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVIEARDSlgsetsfanGGQL 49
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP---------GGQL 38
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 5-31 6.40e-03

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: 36.06  E-value: 6.40e-03
                          10        20
                  ....*....|....*....|....*..
gi 1502504201   5 VCIIGGGVIGLASAYALVRAGHEVTVI 31
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLI 27
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 3-32 7.69e-03

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


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 36.82  E-value: 7.69e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1502504201   3 KRVCIIGGGVIGLASAYALVRAGHEVTVIE 32
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVD 30
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-94 8.96e-03

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


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 36.50  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502504201   1 MAKRVCIIGGGVIGLASAYALVRAGHEVTVIEARDSLGSETSFANG----GQLSYRYVAPLADKgvpLQAIGwllrgdsp 76
Cdd:PRK14619    3 QPKTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGLSLAAVLADAdvivSAVSMKGVRPVAEQ---VQALN-------- 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1502504201  77 lkLRPR---------LDPQQWR-----WMAAF 94
Cdd:PRK14619   72 --LPPEtiivtatkgLDPETTRtpsqiWQAAF 101
PRK08401 PRK08401
L-aspartate oxidase; Provisional
 4-31 9.23e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 36.70  E-value: 9.23e-03
                          10        20
                  ....*....|....*....|....*...
gi 1502504201   4 RVCIIGGGVIGLASAYALVRAGHEVTVI 31
Cdd:PRK08401    3 KVGIVGGGLAGLTAAISLAKKGFDVTII 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH