Trk system potassium transporter TrkA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   1 MRIVIVGAGNVGRSIARELTAHGHQILLIDKNPKAmkpdtVPEAEW------LCADACELATLEEARIDNCDIAISATGD 74
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEER-----LRRLQDrldvrtVVGNGSSPDVLREAGAEDADLLIAVTDS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918  75 DKVNLVHSLLAKTEFGVPRTVARVNHPG----NEWMFDQVWGVDVAVSTPRLMAALVEEAVTVGELVRLFTFQKGRANLV 150
Cdd:PRK09496  76 DETNMVACQIAKSLFGAPTTIARVRNPEyaeyDKLFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADGRVQLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488471918 151 ELTLPDNSPRVGDRIRDISM---PGDAVLVAIIRDGQGRAPEREAALEAGDELLFMISPNYEPDLVDLLAPR 219
Cdd:PRK09496 156 EVKVYEGSPLVGKPLSDLREhfpDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGAREHIRAVMSEFGRL 227

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   1 MRIVIVGAGNVGRSIARELTAHGHQILLIDKNPKamKPDTVPEAEWLCADACELATLEEArIDNCDIAISATGDDK---V 77
Cdd:cd05229    1 TAHVLGASGPIGREVARELRRRGWDVRLVSRSGS--KLAWLPGVEIVAADAMDASSVIAA-ARGADVIYHCANPAYtrwE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488471918  78 NLVHSLLAKTEFGVPRTVARVNHPGNEWMFDQVWGVDVAVSTPR 121
Cdd:cd05229   78 ELFPPLMENVVAAAEANGAKLVLPGNVYMYGPQAGSPITEDTPF 121

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.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 488471918    1 MRIVIVGAGNVGRSIARELTAHGHQILLIDKNPK 34
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQE 34

Trk system potassium transporter TrkA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   1 MRIVIVGAGNVGRSIARELTAHGHQILLIDKNPKAmkpdtVPEAEW------LCADACELATLEEARIDNCDIAISATGD 74
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEER-----LRRLQDrldvrtVVGNGSSPDVLREAGAEDADLLIAVTDS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918  75 DKVNLVHSLLAKTEFGVPRTVARVNHPG----NEWMFDQVWGVDVAVSTPRLMAALVEEAVTVGELVRLFTFQKGRANLV 150
Cdd:PRK09496  76 DETNMVACQIAKSLFGAPTTIARVRNPEyaeyDKLFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADGRVQLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488471918 151 ELTLPDNSPRVGDRIRDISM---PGDAVLVAIIRDGQGRAPEREAALEAGDELLFMISPNYEPDLVDLLAPR 219
Cdd:PRK09496 156 EVKVYEGSPLVGKPLSDLREhfpDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGAREHIRAVMSEFGRL 227

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918    3 IVIVGAGNVGRSIARELTAhGHQILLIDKNPKAMKPDTVPEAEWLCADACELATLEEARIDNCDIAISATGDDKVNLVHS 82
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 488471918   83 LLAKTEFGVPRTVARVNHPGNEWMFDQVwGVDVAVS 118
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRL-GADHVIS 114

potassium/proton antiporter;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471918 144 KGRANLVELTLPDNSPRVGDRIRDISMPGDAVLVAIIRDGQGRAPEREAALEAGDELLFMISPNYEPDLVDLLA 217
Cdd:PRK05326 411 ESDAELLEYRVPAGSWLVGKALRDLRLPRGALIALIIRDGKLLVPTGSTRLKAGDVLLVLGPERDLPALERLFS 484

Putative NADH-flavin reductase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   2 RIVIVGA-GNVGRSIARELTAHGHQILLIDKNPKAMkPDTVPEAEWLCADACELATLEEArIDNCDIAISATGDDKVNLV 80
Cdd:COG2910    1 KIAVIGAtGRVGSLIVREALARGHEVTALVRNPEKL-PDEHPGLTVVVGDVLDPAAVAEA-LAGADAVVSALGAGGGNPT 78

                 ....*
gi 488471918  81 HSLLA 85
Cdd:COG2910   79 TVLSD 83

TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918  149 LVELTLPDNSPRVGDRIRDISMP--GDAVLVAIIRDGQGRAPEREAALEAGDELLFMISPNYEPDLVDLL 216
Cdd:pfam02080   1 LVEVTVPENSPLVGKTLKELNLPerFGVRIVAIRRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALRELL 70

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   2 RIVIVGAGNVGRSIARELTAHGHQILLIDKNpkamkPDTVPEA-----EWLCADACELATLEEARIDNCDIAISATGDDK 76
Cdd:COG1226  126 HVIIAGFGRVGQIVARLLRAEGIPFVVIDLD-----PERVEELrrfgiKVYYGDATRPDVLEAAGIERARALVVAIDDPE 200

                 ...
gi 488471918  77 VNL 79
Cdd:COG1226  201 AAL 203

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   2 RIVIVGA-GNVGRSIARELTAHGHQILLID-KNPKAMKPDTVPEAEWLCADACELATLEEArIDNCDIAI 69
Cdd:COG0451    1 RILVTGGaGFIGSHLARRLLARGHEVVGLDrSPPGAANLAALPGVEFVRGDLRDPEALAAA-LAGVDAVV 69

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488471918     1 MRIVIVGAGNVGRSIARELTAHGHQILLIDKNP-KAMkpdtvpEAewlCADACELATLEEArIDNCDIAISATGDDKV 77
Cdd:smart00997  24 KNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPiRAL------EA---AMDGFEVMKMEEA-AKRADIFVTATGNKDV 91

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488471918   2 RIVIVGA-GNVGRSIARELTAHGHQILLIDKNPKAmKPDTVPEAEWlcaDACELATLEearIDNCDIAISATG 73
Cdd:cd05242    1 KIVITGGtGFIGRALTRRLTAAGHEVVVLSRRPGK-AEGLAEVITW---DGLSLGPWE---LPGADAVINLAG 66

p-hydroxybenzoic acid--AMP ligase FadD22;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918  45 EWLCADACELATLEEARIDNCDIAISATGDDK---VNLVHSLLAKTEFGVPRTVA--RVNHPG-NEWMFDQVWGVDVAVS 118
Cdd:PRK06060 548 DAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSqmtVTLCKRLAAVTGLRLPETVGwdYGSISGlAQYLEAELAGGHGRLK 627

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918 119 TP-------RLMAALVEEAVTVGELVRLFTfqkgranlveltlPDNSPRVGDRIRdismpgdaVLVAIIRDGQGRAPERE 191
Cdd:PRK06060 628 SAgpvnsgaTGLWAIEEQLNKVEELVAVIA-------------DGEKQRVADRLR--------ALLGTIAGSEAGLGKLI 686

                        170
                 ....*....|...
gi 488471918 192 AALEAGDELLFMI 204
Cdd:PRK06060 687 QAASTPDEIFQLI 699

Predicted dinucleotide-binding enzyme [General function prediction only];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   3 IVIVGAGNVGRSIARELTAHGHQILLIDKNpkamkPDTVPEAEWLCADACELATLEEArIDNCDIAISAT 72
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRD-----PEKAAALAAELGPGARAGTNAEA-AAAADVVVLAV 64

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488471918    1 MRIVIVGAGNVGRSIARELTAHGHQILLIDknpkamkpdtvPEAEWLCADACELATLE-EARIDNCDIAISATGDDKVN 78
Cdd:pfam13241   8 KRVLVVGGGEVAARKARKLLEAGAKVTVVS-----------PEITPFLEGLLDLIRREfEGDLDGADLVIAATDDPELN 75

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   2 RIVIVGAGNVGRSIARELTAHGHQILLIDKNpkamkpdTVPEAEWLC----ADACELATLEEArIDNCDIAISATGddkv 77
Cdd:cd05213  180 KVLVIGAGEMGELAAKHLAAKGVAEITIANR-------TYERAEELAkelgGNAVPLDELLEL-LNEADVVISATG---- 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471918  78 nlvHSLLAKTefgVPRTVARVNHpgnewmFDQVWgVDVAVstPRlmaaLVEEAVTVGELVRLFT 141
Cdd:cd05213  248 ---APHYAKI---VERAMKKRSG------KPRLI-VDLAV--PR----DIEPEVGELEGVRLYT 292

NAD(P)H-binding;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488471918    7 GA-GNVGRSIARELTAHGHQILLIDKNPKAMKPDT-VPEAEWLCADACELATLEEArIDNCDIAISATGDDK 76
Cdd:pfam13460   1 GAtGKIGRLLVKQLLARGHEVTALVRNPEKLADLEdHPGVEVVDGDVLDPDDLAEA-LAGQDAVISALGGGG 71

3-hydroxyacyl-CoA dehydrogenase;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488471918   2 RIVIVGAGNVGRSIARELTAHGHQILLIDKNPKAMKpDTVPEAEWLCADACELATLEEA 60
Cdd:PRK09260   3 KLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLE-SAQQEIASIFEQGVARGKLTEA 60

NAD(P)-binding Rossmann-like domain;

                          10        20
                  ....*....|....*....|....*....
gi 488471918    5 IVGAGNVGRSIARELTAHGHQILLIDKNP 33
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRD 29

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471918   2 RIVIVGA-GNVGRSIARELTAHGHQILLIDKNPKAMKPDTVPeAEWLCADACELATLEEArIDNCDIAISATGDDKVNLV 80
Cdd:cd05244    1 KIAIIGAtGRTGSAIVREALARGHEVTALVRDPAKLPAEHEK-LKVVQGDVLDLEDVKEA-LEGQDAVISALGTRNDLSP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488471918  81 HSLLAKT---------EFGVPRTVArVNHPGNEWMFDQVWGVDVAVSTPRLMAALVEEAVTVGELVR 138
Cdd:cd05244   79 TTLHSEGtrnivsamkAAGVKRLIV-VGGAGSLDDRPKVTLVLDTLLFPPALRRVAEDHARMLKVLR 144

FAD-dependent hydroxylase;

                         10        20        30
                 ....*....|....*....|....*....|...
gi 488471918   3 IVIVGAGNVGRSIARELTAHGHQILLIDKNPKA 35
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPLA 38

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

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488471918   1 MRIVIVGAGNVGRSIAREL---TAHGHQILLIDKNP 33
Cdd:COG1252    2 KRIVIVGGGFAGLEAARRLrkkLGGDAEVTLIDPNP 37

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

                         10        20        30
                 ....*....|....*....|....*....|...
gi 488471918   3 IVIVGAGNVGRSIARELT-AHGHQILLIDKNPK 34
Cdd:COG0579    7 VVIIGAGIVGLALARELSrYEDLKVLVLEKEDD 39