3GKE,1Z03,2DE7,2DE7,3GCF,3GKQ,3GOB,3GB4,3GTE


Conserved Protein Domain Family
RHO_alpha_C_DMO-like

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cd08878: RHO_alpha_C_DMO-like 
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C-terminal catalytic domain of the oxygenase alpha subunit of dicamba O-demethylase and related aromatic ring hydroxylating dioxygenases
C-terminal catalytic domain of the oxygenase alpha subunit of Stenotrophomonas maltophilia dicamba O-demethylase (DMO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of carbazole 1,9a-dioxygenase, phthalate dioxygenase, vanillate O-demethylase, Pseudomonas putida 2-oxoquinoline 8-monooxygenase, and Comamonas testosteroni T-2 p-toluenesulfonate dioxygenase. It also includes the C-terminal domain of the lignin biphenyl-specific O-demethylase (LigX) of the 5,5'-dehydrodivanillic acid O- demethylation system of Sphingomonas paucimobilis SYK-6. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.
Statistics
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PSSM-Id: 176887
View PSSM: cd08878
Aligned: 46 rows
Threshold Bit Score: 99.8097
Threshold Setting Gi: 15644093
Created: 31-Jul-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 19 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:based on substrate and Fe(II) binding sites of various RHO_alpha_C_DMO-like domains
  • Structure:2DE7_C; Janthinobacterium oxygenase component of carbazole 1,9a-dioxygenase binds carbazole (contacts at 4A) and Fe (II).
    View structure with Cn3D
  • Structure:1Z03_A; Pseudomonas putida oxygenase component of 2-oxoquinoline 8-monooxygenase binds 2-oxoquinoline (contacts at 4A) and Fe(II).
    View structure with Cn3D
  • Structure:3GOB_A; Stenotrophomonas maltophilia oxygenase component of dicamba monooxygenase binds 3,6-dichlorosalicylic acid (the reaction product, contacts at 4A) and Co(II).
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                # ## ##   #                                             
3GKE_A       137 TVGGYGHVDC------NYKLLVDNLMDLGHAqYVHRANAQtdaf-----------drleREVIVG------DGEIQALMK 193 Stenotrophomona...
2DE7_C       160 ILGKNQIIKS------NWRLAVENGFDPSHI-YIHKDSILvkdndlalplgfapggdrkQQTRVVdddvvgRKGVYDLIG 232 Janthinobacterium
YP_299968    157 NAVPFKVLEDc-----NYAQAVEGTIDSAHAgVLHREQPWsapakydh---erdlqpkiEVEYTK------YGLRYAGVR 222 Ralstonia eutro...
YP_001415952 166 EHPDDKLVPYcvtypcNWLQVLENVMDPAHAvFLHTRVTFshfsdtw------gelpvmDFVETP------TGMIYVTTR 233 Xanthobacter au...
NP_890824    165 DIPGDRLVPYcitypcNWLQVHENVMDPAHAvFLHTRISFtqfaeaw------gelpemDFVPTP------TGMIYVTSR 232 Bordetella bron...
YP_002943603 158 AQAVFAEIPC------NWFQCQENSIDPVHFeWTHNNWTTrlqgdegp---yvpthlklAFDEFE------HGFVYRRLR 222 Variovorax para...
YP_001263550 159 VQVVLAEIPC------NWLQCQENSIDPVHFeWMHMNWGRrlrapdsa---hgprhlavAFDEFD------HGFVYRRHR 223 Sphingomonas wi...
ZP_03265574  154 WQNGFCQIVTsvi-ncNWLQCQENSIDPIHFeWQHSNYSVrrmggtkek--yvpkhtalDFTEFQ------FGYQYRRQR 224 Burkholderia sp...
ZP_05069914  173 NTSSPYRIDYn----cNWIQVLDAIMDPLHTsFLHGQSSGlqfs-----------egfaEVGEIEfy---eRGIQYLGCN 234 Candidatus Pela...
BAA36168     152 WKNGFRQIVIsvl-pcNWLQGQENSMDPIHFeWMHANWSKrlrgetgp---ygpkhlkiDFREYD------YGFTYNRIR 221 Sphingomonas pa...
Feature 1                                  ## #       # #                  # #                   
3GKE_A       194 Ipggtpsvlma---kflrgantpvDAWNDIRWNKVSAMLNFiavapegtpkeqsihsRGTHILTPET-EASCHYFFGSSR 269 Stenotrophomona...
2DE7_C       233 EhgvpvfegtiggevvregaygekIVANDISIWLPGVLKVNpfpn---------pdmMQFEWYVPID-ENTHYYFQTLGK 302 Janthinobacterium
YP_299968    223 Nfre-----------------egkLHARVTEVVLPFFTLIPpdgfg------vrknrRMANAFVPRDdESTWHVQWFFDD 279 Ralstonia eutro...
YP_001415952 234 Rwk-------------------dkVWVRSNDILMPNLAQVGhiwedgqe-akqfgrvGITRWTTPIDnQTCRVIGWRHFH 293 Xanthobacter au...
NP_890824    233 Rwe-------------------dkVWVRSNDIVLPNLAQVGhiwedglt-pkefarvAITRWTTPIDdHTCRIIGWRHMH 292 Bordetella bron...
YP_002943603 223 Ggese----------------dnvMWTTGRVTLWPNGFFLG----------------HHFEWRVPIDdHNTLSVLWVLSR 270 Variovorax para...
YP_001263550 224 Edlge----------------ahgMWTVGRVCLWPNAFFLG----------------DHFEYRVPIDdENTLSVAWMFNR 271 Sphingomonas wi...
ZP_03265574  225 Tdtna----------------ehpLWTTGRVCLYPNGFFLG----------------EHFEWRVPVDdEHTLSISWFYLP 272 Burkholderia sp...
ZP_05069914  235 Trri-----------------ndnVWVRVNELILPNFTQAGaafaadgtkskyfgrsSFTRWVVPIDdHHCVALAWANFG 297 Candidatus Pela...
BAA36168     222 Edtde----------------tnpLWTIGRACLWPNAMFTG----------------DHFEYRVPIDdETMMSVGWFFTP 269 Sphingomonas pa...
Feature 1                                                 #   ##  ##   #                         
3GKE_A       270 Nfgid-----------------------------dpeMDGVLRS-WQAQALvKEDKVVVEAIERRRAyveangiRPAMLS 319 Stenotrophomona...
2DE7_C       303 Pcandeer-----------------------kkyeqeFESKWKPmALEGFN-NDDIWAREAMVDFYAddk-gwvNEILFE 357 Janthinobacterium
YP_299968    280 TqpvdvayrieegghwvdenfrkklnidnwyqqdrewMKTGSMS-GIKGIL-TQDHAVSETQGRILDr-----tKEHLGT 352 Ralstonia eutro...
YP_001415952 294 Pdvdprglakee--------------ecgvekvdfygQGIGASF-EERQRL-PGDYDAIVSQRPIAVh-----aLEHLTY 352 Xanthobacter au...
NP_890824    293 Pdadprglades--------------lcgvetvdffgQNGERPY-ADRQRM-PGDYDAQISQRPIAVh-----aMENLTR 351 Bordetella bron...
YP_002943603 271 Vpteqepyvqe----------------ripswygpikDPATGRW-ITSHVA-NQDFVVWVGQGTVTDr-----tREKLGQ 327 Variovorax para...
YP_001263550 272 Vptesepfvqe----------------tipawrgpiaDPATGKW-ISSHVM-NQDFVAWVGQGRIADr-----tKENLGT 328 Sphingomonas wi...
ZP_03265574  273 Vpaevrpyvqd-----------------qiptwespvMDANGKY-HDSHIL-NQDFMAWVGQGTIADr-----tKEVLGS 328 Burkholderia sp...
ZP_05069914  298 Ergdpieynnq-----------------egyerieagEISNRTK-EEKQKS-PGDAEAVEGMGSISGh-----kGEHLMP 353 Candidatus Pela...
BAA36168     270 Crampspmcr-------------------spspsgmaRSRTRKA-SGSPAMmNQDFVAWIGQGNISDr-----tQENLGL 324 Sphingomonas pa...
Feature 1                        
3GKE_A       320 CDEAAVRVSREIEKLE 335 Stenotrophomonas maltophilia
2DE7_C       358 SDEAIVAWRKLASEHN 373 Janthinobacterium
YP_299968    353 SDVAVVAWRRQMIRTA 368 Ralstonia eutropha JMP134
YP_001415952 353 CDKGVVMLRKLLRRDI 368 Xanthobacter autotrophicus Py2
NP_890824    352 CDRGVAMLRQLLRRES 367 Bordetella bronchiseptica RB50
YP_002943603 328 SDKGIVMMRRRFFEEL 343 Variovorax paradoxus S110
YP_001263550 329 SDRGIGLLRRRFTSEM 344 Sphingomonas wittichii RW1
ZP_03265574  329 SDKGVVMLRRRFESDL 344 Burkholderia sp. H160
ZP_05069914  354 TDKGVMIYRRRTRKLI 369 Candidatus Pelagibacter sp. HTCC7211
BAA36168     325 SDKGIGMMRRQFLRDM 340 Sphingomonas paucimobilis

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