ID A0A370DMK4_9GAMM Unreviewed; 643 AA.
AC A0A370DMK4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Nitrous-oxide reductase {ECO:0000256|ARBA:ARBA00016560, ECO:0000256|HAMAP-Rule:MF_00716};
DE EC=1.7.2.4 {ECO:0000256|ARBA:ARBA00011896, ECO:0000256|HAMAP-Rule:MF_00716};
DE AltName: Full=N(2)OR {ECO:0000256|ARBA:ARBA00031077, ECO:0000256|HAMAP-Rule:MF_00716};
DE AltName: Full=N2O reductase {ECO:0000256|ARBA:ARBA00032847, ECO:0000256|HAMAP-Rule:MF_00716};
GN Name=nosZ {ECO:0000256|HAMAP-Rule:MF_00716};
GN ORFNames=DIZ80_01270 {ECO:0000313|EMBL:RDH86128.1};
OS endosymbiont of Galathealinum brachiosum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2200906 {ECO:0000313|EMBL:RDH86128.1, ECO:0000313|Proteomes:UP000254266};
RN [1] {ECO:0000313|EMBL:RDH86128.1, ECO:0000313|Proteomes:UP000254266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1464 {ECO:0000313|EMBL:RDH86128.1};
RX PubMed=30022157;
RA Li Y., Liles M.R., Halanych K.M.;
RT "Endosymbiont genomes yield clues of tubeworm success.";
RL ISME J. 0:0-0(2018).
CC -!- FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory
CC system which is activated under anaerobic conditions in the presence of
CC nitrate or nitrous oxide. {ECO:0000256|ARBA:ARBA00003034,
CC ECO:0000256|HAMAP-Rule:MF_00716}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c]
CC + 2 H(+) + nitrous oxide; Xref=Rhea:RHEA:43108, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.7.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00029370, ECO:0000256|HAMAP-
CC Rule:MF_00716};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00716};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00716};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00716};
CC Note=Binds 6 Cu cations per subunit. Each subunit contains 2 copper
CC centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought
CC to be the site of nitrous oxide reduction. {ECO:0000256|HAMAP-
CC Rule:MF_00716};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 4/4. {ECO:0000256|ARBA:ARBA00004779}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00716}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|HAMAP-Rule:MF_00716}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000256|HAMAP-Rule:MF_00716}.
CC -!- SIMILARITY: Belongs to the NosZ family. {ECO:0000256|ARBA:ARBA00010372,
CC ECO:0000256|HAMAP-Rule:MF_00716}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family. {ECO:0000256|ARBA:ARBA00006790,
CC ECO:0000256|HAMAP-Rule:MF_00716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDH86128.1}.
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DR EMBL; QFXC01000002; RDH86128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370DMK4; -.
DR UniPathway; UPA00652; UER00709.
DR Proteomes; UP000254266; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd04223; N2OR_C; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_00716; NosZ; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR034205; N2OR_C.
DR InterPro; IPR023644; NO_Rdtase.
DR InterPro; IPR041114; Nos_propeller.
DR InterPro; IPR041142; NOS_propeller_2.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR NCBIfam; TIGR04244; nitrous_NosZ_RR; 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; PF18764; nos_propeller; 1.
DR Pfam; PF18793; nos_propeller_2; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_00716};
KW Copper {ECO:0000256|HAMAP-Rule:MF_00716};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00716};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00716};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00716};
KW Reference proteome {ECO:0000313|Proteomes:UP000254266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00716}.
FT DOMAIN 540..643
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT REGION 547..643
FT /note="COX2-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 143
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 191
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 332
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 387
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 438
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 499
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 588
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 623
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 623
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 625
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 627
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 627
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 631
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
FT BINDING 634
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00716"
SQ SEQUENCE 643 AA; 71404 MW; 5E66F586D88EF0C0 CRC64;
MAIKKDNPEN EQLEEVGRSR RQLLGSSVKL AALAGFAGLT GAGVMTPKAA IAASKNSAHV
GPGDLDEYYG FWSSGQAGEL RILGMPSMRE LMRVPVFNRC SASGWGDTNE SRKILRDGLL
PETKEFLDSG NRGGVWLNGD LHHPHMSFTD GTYDGRYLFM NDKANTRVAR VRCDVMKCDK
IIEIPNASDI HGLRPQKYPR TGYVFANGEH RVPLPNDGSI LDEPEKYHAI FSAIDGDEME
VKWQVMVDGN LDNCDADYQG LYAFSTCYNS EEAINAGGMM SNERDWAVVF DIKAIEKAVK
TGDFKRIKGV PVIDGRKGSK YTRYIPVPNS PHGCNTAPDG KHVVFNGKLS PTVTVIDVRR
LPDLFKDKIK PRDTVVAEPE LGLGPLHTAF DGKGNAFTTL FLDSQAVKWN IQKAIDAYNG
KKVNPILEKI DVHYQPGHNH TSMGETKDAD GKWLVSLNKF SKDRFINVGP LKPENEQLID
ITGKKMKVVH DGPTYAEPHD VIIVRNDIVN PDSLWTKGDP MWAEASAQAK KDGVELGVDS
KIVREGKKVR IYMWSIAPNF SMEKFTVKQG DEVTVYVSNS DAIDDLTHGF TVANYGVAME
VGPQQTSSIT FTADRPGVHW FYCQWFCHAL HMEMRGRMMV EPA
//
