3.D.4.2.2 Nitrous oxide reductase, NosZ, of 652 aas with one N-terminal TMS. The NosZ enzyme is the terminal reductase of anaerobic N2O
respiration. Electrons derived from a donor substrate are
transferred to NosZ by means of an electron transport chain (ETC) that
conserves energy through proton motive force generation (Hein and Simon 2019). In both clade I and clade II NosZs, proton motive quinol oxidation by N2O is thought to be catalyzed by the Q cycle mechanism of a membrane-bound Rieske/cytochrome bc complex (Hein and Simon 2019). Nitrous-oxide reductase is part of a bacterial
respiratory system which is activated under anaerobic conditions in the
presence of nitrate or nitrous oxide. NosZ is similar in sequence to cytochrome c oxidase component 2 only in the C-terminal 100 aa residues of both proteins which contains a pair of cysteyl residues.
|
Accession Number: | Q51705 |
Protein Name: | Nitrous-oxide reductase |
Length: | 652 |
Molecular Weight: | 71414.00 |
Species: | Paracoccus denitrificans [266] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Periplasm1 |
Substrate |
hydron, dinitrogen oxide |
---|
1: MESKQEKGLS RRALLGATAG GAAVAGAFGG RLALGPAALG LGTAGVATVA GSGAALAASG
61: DGSVAPGQLD DYYGFWSSGQ SGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESVRIHE
121: RTMSERTKKF LAANGKRIHD NGDLHHVHMS FTEGKYDGRF LFMNDKANTR VARVRCDVMK
181: CDAILEIPNA KGIHGLRPQK WPRSNYVFCN GEDETPLVND GTNMEDVANY VNVFTAVDAD
241: KWEVAWQVLV SGNLDNCDAD YEGKWAFSTS YNSEKGMTLP EMTAAEMDHI VVFNIAEIEK
301: AIAAGDYQEL NGVKVVDGRK EASSLFTRYI PIANNPHGCN MAPDKKHLCV AGKLSPTATV
361: LDVTRFDAVF YENADPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIEDAI
421: RAYAGEKVDP IKDKLDVHYQ PGHLKTVMGE TLDATNDWLV CLSKFSKDRF LNVGPLKPEN
481: DQLIDISGDK MVLVHDGPTF AEPHDAIAVH PSILSDIKSV WDRNDPMWAE TRAQAEADGV
541: DIDNWTEEVI RDGNKVRVYM SSVAPSFSIE SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG
601: NYGVAMEIGP QMTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMLVEPK EA