Database Retrieval System V1.0

Name ddhA
Function
2 [Fe(III)-cytochrome c2] + dimethyl sulfide + H2O = 2 [Fe(II)-cytochrome c2] + dimethyl sulfoxide + 2 H+
Definition dimethylsulfide dehydrogenase subunit alpha [EC:1.8.2.4]
AA seq
MLRTTRRTLMQGASLVGAGLFAAGRGWALNRLEPIGDTLAEEYPYRDWEDLYRNEFTWDY VGKAAHCINCLGNCAFDIYVKDGIVIREEQLAKYPQISPDIPDANPRGCQKGAIHSTSMY EADRLRYPMKRVGARGEGKWQRISWDQATEEIADKIIDIYEKYGPGKLMTHTGSGNMSMM RMAAPYRFASLVGGVQLDIFTDVGDLNTGAHLAYGNALESFTSDAWFGADYIMFLLFNPV ATRIPDAHFLWEAKWNGARVVSVAPDYNPSSIHSDLWMPIKQGADPFLAMSMVNVIIEGK LYNEAFMKEQTDLPILVRSDNGMLLREADLEEGGSDQVFYHWDSRTGAAVKVKGSMGSEE KTLVLGDVDPALEGSFEVGGIPVTTVFEKVRAEAAKYPPEETAAITGIGPGVVRAEAETF ARAKKALLMTGFNIGRYSNGIYTSWALTLMLALTGHGGRTGGLDTSWIAWNQPALLELAF FDFKKLPRLEAGGLGEFVRGGMMEHSRQHYDNDKLKARTGFDLDELQEMIDESIDAGWMP YYGDMKGLISIADNKFRRNKNAEAYRERILEEVEELFVDINVRMDSTAQWADYLLPAAAH YEAWDLRSIAFHRFVNVFSRPVPPIGEAKSDWEIMEILTRKIQERAIARGITGYEDGDVT RDFATIHDDYTMDGTLMTDHDVVSWLVENGPEFAGATLEEGVERGFFVMGEDAGPTQKLR PSEPYHAFLQQTEGKEPYKTMTGRITFFVDHPRFVRLGATVPTARHHAGRDASNYPLNFF SPHTRWGIHSNWRSNKFMLRLQRGEPNIYISPQLAAAKGIADGAQVRVFNELSFFFAQAK FYPSLPPDTIMMEHGWEPHQFPNWRPMNVCMATLLQPLELVGGWGHLNFSLWHWNANQLA HESSVDIEPA925
Structure
Reference
PMIDTitle & AuthorAbstractYear
012903308Design of an artificial restriction enzyme having simultaneous DNA cleavage activity. T Inui , H Ikeda, Y NakamuraWe designed dimeric distamycin linked hydroxamic acid (DDHA)-metal complexes and investigated double strand simultaneous cleavage. Compared as distamycin linked hydroxamic acid (DHA)-metal complex, DDHA-metal complex cleaved DNA at the same level of DHA-metal complex without double strand simultaneous cleavage.2000
112957948A gene cluster for chlorate metabolism in Ideonella dechloratans. Helena Danielsson Thorell , Katarina Stenklo, Jan Karlsson, Thomas NilssonChlorate reductase has been isolated from the chlorate-respiring bacterium Ideonella dechloratans, and the genes encoding the enzyme have been sequenced. The enzyme is composed of three different subunits and contains molybdopterin, iron, probably in iron-sulfur clusters, and heme b. The genes (clr) encoding chlorate reductase are arranged as clrABDC, where clrA, clrB, and clrC encode the subunits and clrD encodes a specific chaperone. Judging from the subunit composition, cofactor content, and sequence comparisons, chlorate reductase belongs to class II of the dimethyl sulfoxide reductase family. The clr genes are preceded by a novel insertion sequence (transposase gene surrounded by inverted repeats), denoted ISIde1. Further upstream, we find the previously characterized gene for chlorite dismutase (cld), oriented in the opposite direction. Chlorate metabolism in I. dechloratans starts with the reduction of chlorate, which is followed by the decomposition of the resulting chlorite to chloride and molecular oxygen. The present work reveals that the genes encoding the enzymes catalyzing both these reactions are in close proximity.2003

Mcdevitt C H P , Hanson G R , Mcewan A G . Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes[J]. Molecular Microbiology, 2010, 44(6):1575-1587.