ID Q30R05_SULDN Unreviewed; 865 AA.
AC Q30R05;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=NosZ Nitrous oxide reductase {ECO:0000313|EMBL:ABB44576.1};
DE EC=1.7.2.4 {ECO:0000313|EMBL:ABB44576.1};
GN OrderedLocusNames=Suden_1298 {ECO:0000313|EMBL:ABB44576.1};
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:ABB44576.1, ECO:0000313|Proteomes:UP000002714};
RN [1] {ECO:0000313|EMBL:ABB44576.1, 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; ABB44576.1; -; Genomic_DNA.
DR RefSeq; WP_011372928.1; NC_007575.1.
DR AlphaFoldDB; Q30R05; -.
DR STRING; 326298.Suden_1298; -.
DR KEGG; tdn:Suden_1298; -.
DR eggNOG; COG2010; Bacteria.
DR eggNOG; COG4263; Bacteria.
DR HOGENOM; CLU_016420_1_0_7; -.
DR OrthoDB; 9781261at2; -.
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 CDD; cd04223; N2OR_C; 1.
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; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR034205; N2OR_C.
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; PF13473; Cupredoxin_1; 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 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:ABB44576.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000002714};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..865
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004219843"
FT DOMAIN 501..653
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 767..859
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 865 AA; 96497 MW; 3428D49227842A52 CRC64;
MTKHSKILVS LLVGASVAVS VSSADGELQK VMKARGLSEV DVVRAAKTYN PSGVKDEFVV
FSSAGQAGQV IVYGVPSMRI LKYIGVFTPE PWQGYGFDEE SKKVLRQGNI RGREINWGDT
HHPALSEKDG KYDGKWLAIN DKANPRIAII DLADFETKQI VVNPVFKSAH GGAFFTQNSD
YIIEACQYAA PLDNNYHPIE DYKEAYRGGA TMWRFDPAKG KINVKESFTI EMPPYMQDLS
DSGKGVSDGW GFTNSFNSEM YTGGIEVGMP PNEAGMSRND TDFLHVYNWK KLAELAKDSK
NVKIINDHKV IPMDIAVKNN ALFLIPEPKS PHGVDVSPDG EYITVCGKLD THASVYKWSN
IKKLIDAKEY AGKDPYGIPI LDMKKSLHGQ AELGLGPLHN QYSNIDGEIY TSLYVDSQIV
KWNYKTLKVI DKVNVHYNVG HLCGMEGKSA DPQGKYIISL NKLAIDRFQN VGPLHPQNHQ
LIDISGKKMD LLVDMPLPLG EPHQAVAIRA EKLHGHVRYP MGTNTRTDEI HEGKTLAGQE
RIERNGNKVT VYATVVRSHI NPERITVNKG DEVTFYLTNL ERAQDEAHGF TVDHYNIHAS
LEPGKTASLK FIADIEGVFP YYCTEFCSAL HLEMMGYMMV KDPNKKYESA QKMKMQTMTP
EQLKAEYDKT VATNAATDAV IQSVVKFLKE NKYEKHKVVA DLVADAFVQY GQIPDQKKLA
DKSLKDGDIE KAILFENMIW QLMVKTADVG IRAKDALVRL VATKQSAAAS AGEKAFGEGG
CGGCHVIGKV SSGPDLTGVL QRHGANGEKW VKDFIMNPEK MYDEPYVKGM IDYFNLRMPN
QHMDEKETKN IIEYLKWVDD NANLF
//
