NOSZ_PARDE
ID NOSZ_PARDE Reviewed; 652 AA.
AC Q51705;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nitrous-oxide reductase;
DE EC=1.7.2.4;
DE AltName: Full=N(2)OR;
DE AltName: Full=N2O reductase;
DE Flags: Precursor;
GN Name=nosZ;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NL1B8944;
RX PubMed=8243476; DOI=10.1111/j.1432-1033.1993.tb18350.x;
RA Hoeren F.U., Berks B.C., Ferguson S.J., McCarthy J.E.G.;
RT "Sequence and expression of the gene encoding the respiratory nitrous-oxide
RT reductase from Paracoccus denitrificans. New and conserved structural and
RT regulatory motifs.";
RL Eur. J. Biochem. 218:49-57(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pd 1222;
RX PubMed=10960107; DOI=10.1128/jb.182.18.5211-5217.2000;
RA Saunders N.F.W., Hornberg J.J., Reijnders W.N.M., Westerhoff H.V.,
RA de Vries S., van Spanning R.J.M.;
RT "The NosX and NirX proteins of Paracoccus denitrificans are functional
RT homologues: their role in maturation of nitrous oxide reductase.";
RL J. Bacteriol. 182:5211-5217(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 60-650, AND PROTEIN SEQUENCE OF
RP 58-63.
RC STRAIN=1657;
RX PubMed=12356332; DOI=10.1042/bj20020782;
RA Haltia T., Brown K., Tegoni M., Cambillau C., Saraste M., Mattila K.,
RA Djinovic-Carugo K.;
RT "Crystal structure of nitrous oxide reductase from Paracoccus denitrificans
RT at 1.6 A resolution.";
RL Biochem. J. 369:77-88(2003).
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.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 6 Cu cations. Each subunit contains 2 copper centers; Cu(A)
CC (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site
CC of nitrous oxide reduction.;
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 4/4.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the NosZ family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family. {ECO:0000305}.
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DR EMBL; X74792; CAA52798.1; -; Genomic_DNA.
DR EMBL; AJ010260; CAB53351.1; -; Genomic_DNA.
DR PIR; S39409; S39409.
DR PDB; 1FWX; X-ray; 1.60 A; A/B/C/D=58-652.
DR PDBsum; 1FWX; -.
DR AlphaFoldDB; Q51705; -.
DR SMR; Q51705; -.
DR DrugBank; DB03151; mu4-sulfido-quadro-tetracopper.
DR TCDB; 3.D.4.2.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR BRENDA; 1.7.2.4; 3341.
DR UniPathway; UPA00652; UER00709.
DR EvolutionaryTrace; Q51705; -.
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; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.420; -; 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 Pfam; PF13473; Cupredoxin_1; 1.
DR Pfam; PF18764; nos_propeller; 1.
DR Pfam; PF18793; nos_propeller_2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF50974; SSF50974; 1.
DR TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chloride; Copper; Direct protein sequencing;
KW Metal-binding; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..57
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:12356332"
FT CHAIN 58..652
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019827"
FT REGION 554..652
FT /note="COX2-like"
FT BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT BINDING 146
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT BINDING 197
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT BINDING 339
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 340
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 392
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 392
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT BINDING 443
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 504
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT BINDING 595
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 630
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 630
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 632
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 634
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT BINDING 634
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 638
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT BINDING 641
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 325..335
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 456..464
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 492..501
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 511..516
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:1FWX"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:1FWX"
FT TURN 600..603
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 613..619
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:1FWX"
FT STRAND 642..648
FT /evidence="ECO:0007829|PDB:1FWX"
SQ SEQUENCE 652 AA; 71414 MW; 40492A4FDE7EDEA8 CRC64;
MESKQEKGLS RRALLGATAG GAAVAGAFGG RLALGPAALG LGTAGVATVA GSGAALAASG
DGSVAPGQLD DYYGFWSSGQ SGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESVRIHE
RTMSERTKKF LAANGKRIHD NGDLHHVHMS FTEGKYDGRF LFMNDKANTR VARVRCDVMK
CDAILEIPNA KGIHGLRPQK WPRSNYVFCN GEDETPLVND GTNMEDVANY VNVFTAVDAD
KWEVAWQVLV SGNLDNCDAD YEGKWAFSTS YNSEKGMTLP EMTAAEMDHI VVFNIAEIEK
AIAAGDYQEL NGVKVVDGRK EASSLFTRYI PIANNPHGCN MAPDKKHLCV AGKLSPTATV
LDVTRFDAVF YENADPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIEDAI
RAYAGEKVDP IKDKLDVHYQ PGHLKTVMGE TLDATNDWLV CLSKFSKDRF LNVGPLKPEN
DQLIDISGDK MVLVHDGPTF AEPHDAIAVH PSILSDIKSV WDRNDPMWAE TRAQAEADGV
DIDNWTEEVI RDGNKVRVYM SSVAPSFSIE SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG
NYGVAMEIGP QMTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMLVEPK EA
