2JL1,2ZCU,3E48


Conserved Protein Domain Family
TMR_SDR_a

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cd05269: TMR_SDR_a 
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triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs
TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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.
Statistics
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PSSM-Id: 187578
Aligned: 38 rows
Threshold Bit Score: 225.227
Created: 22-Sep-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
NADP binding
Conserved site includes 20 residues -Click on image for an interactive view with Cn3D
Feature 1:NADP binding site [chemical binding site]
Evidence:
  • Structure:2JL1_A: Citrobacter sp. triphenylmethane reductase binds NADP, contacts at 4A

cd05269 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd05269 is a member of the superfamily cl21454
Sub-family Hierarchy
cd02266SDRcd05226SDR_e_acd05229SDR_a3cd05242SDR_a8cd05243SDR_a5cd05244BVR-B_like_SDR_acd05245SDR_a2cd05250CC3_like_SDR_acd05259PCBER_SDR_acd05262SDR_a7cd05265SDR_a1cd05266SDR_a4cd05267SDR_a6cd05271NDUFA9_like_SDR_acd08946SDR_ecd05193AR_like_SDR_ecd05227AR_SDR_ecd05228AR_FR_like_1_SDR_ecd08958FR_SDR_ecd05230UGD_SDR_ecd05232UDP_G4E_4_SDR_ecd05234UDP_G4E_2_SDR_ecd05235SDR_e1cd05236FAR-N_SDR_ecd05237UDP_invert_4-6DH_SDR_ecd05238Gne_like_SDR_ecd05239GDP_FS_SDR_ecd05240UDP_G4E_3_SDR_ecd052413b-HSD-like_SDR_ecd098113b-HSD_HSDB1_like_SDR_ecd098123b-HSD_like_1_SDR_ecd098133b-HSD-NSDHL-like_SDR_ecd05246dTDP_GD_SDR_ecd05247UDP_G4E_1_SDR_ecd05248ADP_GME_SDR_ecd05252CDP_GD_SDR_ecd05253UDP_GE_SDE_ecd05254dTDP_HR_like_SDR_ecd05255SQD1_like_SDR_ecd05256UDP_AE_SDR_ecd05257Arna_like_SDR_ecd05258CDP_TE_SDR_ecd05260GDP_MD_SDR_ecd05261CAPF_like_SDR_ecd05263MupV_like_SDR_ecd05264UDP_G4E_5_SDR_ecd05272TDH_SDR_ecd05273GME-like_SDR_ecd08957WbmH_like_SDR_ecd08947NmrA_TMR_like_SDR_acd05231NmrA_TMR_like_1_SDR_acd05251NmrA_like_SDR_acd05269TMR_SDR_acd089485beta-POR_like_SDR_acd05233SDR_ccd05322SDH_SDR_c_likecd05323ADH_SDR_c_likecd05324carb_red_PTCR-like_SDR_ccd05325carb_red_sniffer_like_SDR_ccd05326secoisolariciresinol-DH_like_SDR_ccd05327retinol-DH_like_SDR_c_likecd09807retinol-DH_like_SDR_ccd09808DHRS-12_like_SDR_c-likecd09809human_WWOX_like_SDR_c-likecd09810LPOR_like_SDR_c_likecd053283alpha_HSD_SDR_ccd05329TR_SDR_ccd05330cyclohexanol_reductase_SDR_ccd05331DH-DHB-DH_SDR_ccd0533211beta-HSD1_like_SDR_ccd05333BKR_SDR_ccd05334DHPR_SDR_c_likecd05337BKR_1_SDR_ccd05338DHRS1_HSDL2-like_SDR_ccd09762HSDL2_SDR_ccd09763DHRS1-like_SDR_ccd0533917beta-HSDXI-like_SDR_ccd05340Ycik_SDR_ccd053413beta-17beta-HSD_like_SDR_ccd05343Mgc4172-like_SDR_ccd05344BKR_like_SDR_likecd05345BKR_3_SDR_ccd05346SDR_c5cd05347Ga5DH-like_SDR_ccd05348BphB-like_SDR_ccd05349BKR_2_SDR_ccd05350SDR_c6cd05351XR_like_SDR_ccd05352MDH-like_SDR_ccd05353hydroxyacyl-CoA-like_DH_SDR_c-likecd05354SDR_c7cd05355SDR_c1cd0535617beta-HSD1_like_SDR_ccd05357PR_SDR_ccd05358GlcDH_SDR_ccd05359ChcA_like_SDR_ccd05360SDR_c3cd05361haloalcohol_DH_SDR_c-likecd05362THN_reductase-like_SDR_ccd05363SDH_SDR_ccd05364SDR_c11cd053657_alpha_HSDH_SDR_ccd05366meso-BDH-like_SDR_ccd05367SPR-like_SDR_ccd05368DHRS6_like_SDR_ccd05369TER_DECR_SDR_acd05370SDR_c2cd05371HSD10-like_SDR_ccd05372ENR_SDRcd05373SDR_c10cd0537417beta-HSD-like_SDR_ccd09805type2_17beta_HSD-like_SDR_ccd09806type1_17beta-HSD-like_SDR_ccd08929SDR_c4cd08930SDR_c8cd08931SDR_c9cd08932HetN_like_SDR_ccd08933RDH_SDR_ccd08934CAD_SDR_ccd08935mannonate_red_SDR_ccd08936CR_SDR_ccd08937DHB_DH-like_SDR_ccd08939KDSR-like_SDR_ccd08940HBDH_SDR_ccd089413KS_SDR_ccd08942RhlG_SDR_ccd08943R1PA_ADH_SDR_ccd08944SDR_c12cd08945PKR_SDR_ccd09761A3DFK9-like_SDR_ccd11730Tthb094_like_SDR_ccd11731Lin1944_like_SDR_ccd05274KR_FAS_SDR_xcd08952KR_1_SDR_xcd08953KR_2_SDR_xcd08954KR_1_FAS_SDR_xcd08955KR_2_FAS_SDR_xcd08956KR_3_FAS_SDR_xcd08928KR_fFAS_like_SDR_c_likecd08950KR_fFAS_SDR_c_likecd08951DR_C-13_KR_SDR_c_like
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1         # ####                       ##  #             ####                  ####   
2JL1_A      3 IAVTGATGQLGGLVIQHLLkkvp--asqIIAIVRNveKASTLADQGVEVRHGDYNqpeSLQKAFa-GVSKLLFISGPhyd 79  Citrobacter sp. MY-5
3E48_A      3 IXLTGATGHLGTHITNQAIanh---idhFHIGVRNveKVPDDWRGKVSVRQLDYFnqeSXVEAFk-GXDTVVFIPSIihp 78  Staphylococcus aur...
YP_521565   5 LLVTGASGHLGQRVIHHLLetlkvapqrIIATTRKpeTLKDLAAKGITVRGADFDdaaSLRSAFa-GADRLLLISTDald 83  Rhodoferax ferrire...
BAB48794    5 LLVTGAAGQLGRGVIRYLMdthkvppakIIATTRNpeNVADLAARGVVVRAADFNdatSLENAFk-GADRVLIISTSdld 83  Mesorhizobium loti...
EAL84494    5 IGIFPASGGLGTSIINHLVklvp--asqLILIARNpeKLASFSRDGATIRRADYDdraSLERVFd-GVGVLMLISYAsfe 81  Aspergillus fumiga...
NP_866435   4 IAITSASGQLGAAIVEASVklv---ggdNVIGLAR--TPEKASSLGIEIRPGDYNspaDLENSLq-GIDYLLLVSGMda- 76  Rhodopirellula bal...
BAC68593    2 IIVTGATGKLGRRIVERLLervp--adrVGVSVRDprKAQDLADRGVRVRQGSFDdpaSLVHAFe-GAEQLLLVSLDrt- 77  Streptomyces averm...
YP_468565   3 IGINGASGKLGAAIIEELSsrg----ggHHIVAIS--RSPEKACSGIEARKGDYDqpeTLQDAYa-GLDRLVLIPSAdlr 75  Rhizobium etli CFN 42
CAD65380    3 YAITGATGHLGQQIVAAMRplva--tteLYLGVHTlsKAQVYQQQGLHIAAIDYQq-pEQLRAFfqDSDVLIYIPSKshd 79  Lactobacillus plan...
CAG42155    3 IMLTGATGHLGTHITNQAIanh---idhFHIGVRNveKVPEDWRGKVPVRQLDYFnpeSMVEVFk-GMDTVVFIPSIihp 78  Staphylococcus aur...
Feature 1                                                                          ###        
2JL1_A     80 --ntLLIVQHANVVKAARDAGVKHIAYTGYafaee----siipLAHVHLATEYAIRTTNIP--YTFLRNALYTDFFvneg 151 Citrobacter sp. MY-5
3E48_A     79 --sfKRIPEVENLVYAAKQSGVAHIIFIGYyadqh---nnpfhXSPYFGYASRLLSTSGID--YTYVRXAXYXDPLkpyl 151 Staphylococcus aur...
YP_521565  84 -rpgRRLAQQQAAVAAAQQAGVAHVVYTSMplpen----spllIAPDHAGTEKALASSALKg-WTLLRNHWYFENLfmwl 157 Rhodoferax ferrire...
BAB48794   84 lktgRRLKQHEAAVAAAKKAGVSHLLYTSMpnpep---vspvlFAGDHYGTEQAIKASGIA--YTIFRNGWYQENLfial 158 Mesorhizobium loti...
EAL84494   82 --iqHRVEAHKAAIDAARRSGVKHIFYSSLafagdlgesslahVMGAHLATEKYLAELPGHftYTAIREGLYSESFpiyt 159 Aspergillus fumiga...
NP_866435  77 --peKRIQQHRNVIEAAKRAGVSKIVYTSIqgaeqg--tafspVVQSNRQTESDVRDSGLA--WVIGRNGIYIEPDveyi 150 Rhodopirellula bal...
BAC68593   78 --gqECVSGHRAAIDAAVKAGVGRILYTSQmgaah---dsrfqACRDHAQTEDLLRATGLP--WTALRNGFYASSAlqfl 150 Streptomyces averm...
YP_468565  76 --pgVRGAQLKSAIDVAVESGVQHIVLLSAagtre---aaipaLGESYWTAEQHLIRSAPH--WTILRMNYFAQSMidev 148 Rhizobium etli CFN 42
CAD65380   80 --sySRVQEFENVLAAVQQANVHHFLVMGFiadqv---nnpfaLSAFYGYVPRRLAGSDIN--YTIVRNALYADPLvpyl 152 Lactobacillus plan...
CAG42155   79 --sfKRIPEVENLVYAAKQSGVAHIIFIGYyadqh---nnpfhMSPYFGYAARLLATSGID--YTYVRMAMYMDPLkpyl 151 Staphylococcus aur...
Feature 1                                #                                                    
2JL1_A    152 lr--astesGAIVTn--aGSGIVNSVTRNELALAAATVLTeeg-------heNKTYNLvSNQPWTFdELAQILSEVSGKK 220 Citrobacter sp. MY-5
3E48_A    152 p---elxnxHKLIYp--aGDGRINYITRNDIARGVIAIIKnpd-------twGKRYLL-SGYSYDXkELAAILSEASGTE 218 Staphylococcus aur...
YP_521565 158 p---salasGQWYSa--aEQGKVAHIARDDLARAAAAALLkd--------tgKNTYTLsGAEAFTTeQIAQQVSQATGKP 224 Rhodoferax ferrire...
BAB48794  159 p---haiasGQWYTs--aGDGRIAHGSRDDMAAAIAAGLAsgs-------tdSKTYTLtGPQAYTTaEIAALVSEVTGKP 226 Mesorhizobium loti...
EAL84494  160 awfdphqpvEEITIphpgTGPGVAWAKRDELGEATAKMIYayakntagfpylNRVVLLsGPREVSLaETAEVLGRAVGKP 239 Aspergillus fumiga...
NP_866435 151 d---qykerGEVANc--aGDGKCGYTTRSELADAYAKMLTesk-------hnGQVYNL-HGEAITQqQLTTYLNETFGTD 217 Rhodopirellula bal...
BAC68593  151 e---sarhtGDIALp---ADGPVAWTGHDDLAEATAAILAeeh------rfeGPTPPLtGPAALDFdTVAEIASQTTGRP 218 Streptomyces averm...
YP_468565 149 m---msqsqGMLAGl---GEGRVAYVSRNDVAGATAGAVLgeg-------haGAIYNLtGPDALTGhDVAAIASEALGKP 215 Rhizobium etli CFN 42
CAD65380  153 pe--lierhNVVYPm---ADQALSFISQADSAAAFAKVATtpdl-----lqrGRIYTLtQSRAYTMpELATVLSQVSGQL 222 Lactobacillus plan...
CAG42155  152 pe--lmnmhKLIYPa---GDGRINYITRNDIARGVIAIIKnpd-------twGKRYLL-SGYSYDMkELAAILSEASGTE 218 Staphylococcus aur...
Feature 1                                                                     
2JL1_A    221 VVHQPVsfEEEKNFLvna-gvPEPFTEITAAiyda-----iskGEASKTSDDlqkLIGSLTPLK 278 Citrobacter sp. MY-5
3E48_A    219 IKYEPVslETFAEXYd----ePKGFGALLASxyha-----garGLLDQESNDfkqLVNDQPQTL 273 Staphylococcus aureus subsp. aureus
YP_521565 225 LQVVPVplAGLIQGMvsa-gfPEPLAAVFASfdtn-----taaGRVAEVTGDfqkLTGVAPQPF 282 Rhodoferax ferrireducens T118
BAB48794  227 LEVIQLp-DEALTEGvkaagvPEEFARVIVSfdan-----trsGRIAMATDAvetLSGRKPRTL 284 Mesorhizobium loti MAFF303099
EAL84494  240 VRIREIsvDEYVALPqi--gdKHTYHGLNLSrewatawaairaGETAVVSPLlgeILGREPEDF 301 Aspergillus fumigatus Af293
NP_866435 218 LRYRPMsvDEYRADRta--elGEFLGEIIAGiyeg-----irnGAVDNESHFa-qASGREHLDW 273 Rhodopirellula baltica SH 1
BAC68593  219 FTRTVVp-DDAFREQvlahgaPAPIGNLMLSifaa-----arnGEFTAVDSTlaeLIGREPATF 276 Streptomyces avermitilis MA-4680
YP_468565 216 IVFASVt-EEQLRGGl----gQAGLPDLVVNaimdik-ktfveGHFDVLTHDverLSGRAPISF 273 Rhizobium etli CFN 42
CAD65380  223 IGYRPVs-LQAFSNMy----nQNGEGPMLASmyag-----garGLLATVSDDyqlIMDRPAQSL 276 Lactobacillus plantarum WCFS1
CAG42155  219 IKYEPVs-LETFAEMyd---ePKGFGALLASmyda-----garGLLDQESNDfqqLVNDQPQTL 273 Staphylococcus aureus subsp. aureu...

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