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Database: UniProt
Entry: Q30PN7_SULDN
LinkDB: Q30PN7_SULDN
Original site: Q30PN7_SULDN 
ID   Q30PN7_SULDN            Unreviewed;       864 AA.
AC   Q30PN7;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   SubName: Full=Nitrous oxide reductase NosZ {ECO:0000313|EMBL:ABB45044.1};
DE            EC=1.7.2.4 {ECO:0000313|EMBL:ABB45044.1};
GN   OrderedLocusNames=Suden_1770 {ECO:0000313|EMBL:ABB45044.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB45044.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB45044.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR   EMBL; CP000153; ABB45044.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q30PN7; -.
DR   STRING; 326298.Suden_1770; -.
DR   KEGG; tdn:Suden_1770; -.
DR   eggNOG; COG2010; Bacteria.
DR   eggNOG; COG4263; Bacteria.
DR   HOGENOM; CLU_016420_1_0_7; -.
DR   OMA; HHNIHAS; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR026468; Nitrous_oxide_Rdtase_Sec-dep.
DR   InterPro; IPR041114; Nos_propeller.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   NCBIfam; TIGR04246; nitrous_NosZ_Gp; 1.
DR   PANTHER; PTHR42838; CYTOCHROME C OXIDASE SUBUNIT II; 1.
DR   PANTHER; PTHR42838:SF1; NITROUS-OXIDE REDUCTASE; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF18764; nos_propeller; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABB45044.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          534..652
FT                   /note="Cytochrome oxidase subunit II copper A binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50857"
FT   DOMAIN          767..858
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   COILED          660..723
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   864 AA;  98003 MW;  97569F0023121221 CRC64;
     MKKYLQIVYG ALLGVLVIVQ SATAESEFQK VMQKRGLSEK DALAALKVYN PSGKHDEYYA
     FVSGGQSGQV MVYGIPSMRI LKYIAVFAPE PWQGYGFDTD SKEILRQGNI RGREINWGDT
     HHPALSESDG KYDGKYLFIN DKANARIAVI DLKYFETSQI VVNPIFKSSH GGAFVTPNTD
     YILESCQYAA PFTNDYYPME AYEEVYRGGV TFWKFDKKNG KISQQDSFTL ELPPYMQDLT
     DAGKGISDGW AFTNSFNSEL YTGGIEKGLP PFEAGCSRND MDYLHVYNWK KLAELVKDDK
     NVKVINGHRV IPIEIAVKNN ALFLIPENKS PHGVDVNPDG QYIIVSGKLD THASVYDFKK
     ILKQIENKEF ASKDSYGIPI LDIKKSLHGQ LELGLGHLHN TFGKEDGTIY SSLYVDSQVV
     KWNYKQLKLL DRTNIHYNVG HLEAMEGKSA DPQGEYLIAL NKLSIDRFLP VGPLHPQNNQ
     LIDIGGKKME LLVDMPVPLG EPHQAASIRA SKIHTEVRYN MGTNSKTLKP HVGKTLAGQE
     RIERKGNHVY IYSTMVRSHI NPEHITLNKG DKVTMYITNL ERAQDETHGF TIDHHNIHAS
     VEPGESVQLD FVADIEGVFP YYCTEFCSAL HIEMLGYMLV KDPNKDYGWI QKTKIKGLSK
     EELQKEYEKI LANNEATNSV IDSLFKFFED RGYAKYPTVK NLVDDAKDQY TKIDSEREKA
     TKAYNEKNLE NAVLFENMVW QYMIKTADSA IRAKDLLVTN LATKKSAGAK KGEEVFHEGG
     CSGCHVVGRV SSGPDLIGVL KRHRNAEKWV AEYIKNPESK FKEPYMERLI KFFNLKMPNQ
     NMKDEEIKDI IEYFKWIDEN ADLF
//
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