Trk system potassium transporter TrkA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909708613   1 MRFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATAKRARNQG-FTVVDGDGSQETLLEQARVEDADAVGALTGDLNTNF 79
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLdVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909708613  80 SACLIADH-YGC-RTVLRI-DEEYRE--EIYRKYADVVDEVIYPERLGAMGAKNALLGGTIRAIADIAQ-HLQVVELTIT 153
Cdd:PRK09496  81 VACQIAKSlFGApTTIARVrNPEYAEydKLFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADgRVQLVEVKVY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 909708613 154 DEAPINGYTISELQ--LPADATVLAFGKIDGDLEIPTADESLESGDRLVVLAD 204
Cdd:PRK09496 161 EGSPLVGKPLSDLRehFPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGA 213

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909708613   2 RFVLIGA-GRVGLRTARVLHEEGHDVTLIERDEATAKrARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:cd05244    1 KIAIIGAtGRTGSAIVREALARGHEVTALVRDPAKLP-AEHEKLKVVQGDVLDLEDVKEA-LEGQDAV 66

Trk system potassium transporter TrkA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909708613   1 MRFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATAKRARNQG-FTVVDGDGSQETLLEQARVEDADAVGALTGDLNTNF 79
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLdVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909708613  80 SACLIADH-YGC-RTVLRI-DEEYRE--EIYRKYADVVDEVIYPERLGAMGAKNALLGGTIRAIADIAQ-HLQVVELTIT 153
Cdd:PRK09496  81 VACQIAKSlFGApTTIARVrNPEYAEydKLFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADgRVQLVEVKVY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 909708613 154 DEAPINGYTISELQ--LPADATVLAFGKIDGDLEIPTADESLESGDRLVVLAD 204
Cdd:PRK09496 161 EGSPLVGKPLSDLRehFPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGA 213

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 909708613    3 FVLIGAGRVGLRTARVLHEeGHDVTLIERDEATAKRARNQGFTVVDGDGSQETLLEQARVEDADAVGALTGDLNTNFSAC 82
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 909708613   83 LIAD--HYGCRTVLRIDEEYREEIYRKyaDVVDEVIYP 118
Cdd:pfam02254  80 LLARelNPDKKIIARANDPEHAELLRR--LGADHVISP 115

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 909708613  147 VVELTITDEAPINGYTISELQLPA--DATVLAFGKiDGDLEIPTADESLESGDRLVVLADFAVLSDVRQI 214
Cdd:pfam02080   1 LVEVTVPENSPLVGKTLKELNLPErfGVRIVAIRR-GGRLIIPSGDTVLEAGDRLLVIGTPDDLAALREL 69

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909708613   2 RFVLIGA-GRVGLRTARVLHEEGHDVTLIERDEATAKrARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:COG2910    1 KIAVIGAtGRVGSLIVREALARGHEVTALVRNPEKLP-DEHPGLTVVVGDVLDPAAVAEA-LAGADAV 66

NAD(P)H-binding;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909708613    7 GAGRVGLRTARVLHEEGHDVTLIERDEATAKR-ARNQGFTVVDGDGSQETLLEQArVEDADAV-GALTGDLNTNFSACLI 84
Cdd:pfam13460   2 ATGKIGRLLVKQLLARGHEVTALVRNPEKLADlEDHPGVEVVDGDVLDPDDLAEA-LAGQDAViSALGGGGTDETGAKNI 80

                  ..
gi 909708613   85 AD 86
Cdd:pfam13460  81 ID 82

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 909708613     2 RFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATAKRARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAELLEEA-VKEADLV 87

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909708613   2 RFVLIGA-GRVGLRTARVLHEEGHDVTLIERDEATAKRARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:COG0702    1 KILVTGAtGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGVEVVQGDLDDPESLAAA-LAGVDAV 67

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909708613   4 VLIGAGRVGLRTARVLHEEGHDVTLIERDEatAKRARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:cd05229    4 VLGASGPIGREVARELRRRGWDVRLVSRSG--SKLAWLPGVEIVAADAMDASSVIAA-ARGADVI 65

D-amino acid dehydrogenase;

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 909708613   1 MRFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATA 36
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPGPA 36

potassium/proton antiporter;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 909708613 146 QVVELTITDEAPINGYTISELQLPADATVLAFgKIDGDLEIPTADESLESGDRLVVLA 203
Cdd:PRK05326 415 ELLEYRVPAGSWLVGKALRDLRLPRGALIALI-IRDGKLLVPTGSTRLKAGDVLLVLG 471

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 909708613    6 IGAGRVGLRTARVLHEEGHDVTLIERDEATAKRA--RNQGF 44
Cdd:pfam01266   5 IGGGIVGLSTAYELARRGLSVTLLERGDDPGSGAsgRNAGL 45

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909708613   1 MRFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATAKRARNQGFTVVDGDGSQETLLEQARVEDA 65
Cdd:cd08242  157 DKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPDEAESEGGGFDVVVEA 221

NADP-dependent phosphogluconate dehydrogenase;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 909708613   1 MRFVLIGAGRVGLRTARVLHEEGHDVTLIERDEATAKRARNQGFTVVD 48
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGAD 48

voltage-gated potassium channel protein;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 909708613   3 FVLIGAGRVGLRTARVLHEEGHDVTLIERDEatAKRARNQGFTVVDGDGSQETLLEQARVEDADAVGALTGD 74
Cdd:PRK10537 243 FIICGHSPLAINTYLGLRQRGQAVTVIVPLG--LEHRLPDDADLIPGDSSDSAVLKKAGAARARAILALRDN 312

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909708613   2 RFVLIGA-GRVGLRTARVLHEEGHDVTLIERDEATAKRARNQGFTVVDGDGSQETLLEQArVEDADAV 68
Cdd:cd05243    1 KVLVVGAtGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAESLAAA-LEGIDAV 67