NOSZ_ACHCY
ID NOSZ_ACHCY Reviewed; 642 AA.
AC P94127; O68477;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
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 Achromobacter cycloclastes.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chang W.C., Liu M.Y., Chang T., Payne W.J., Legall J., Chang W.C.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC 102459 / An-17;
RX PubMed=10048486; DOI=10.1093/dnares/5.6.365;
RA Inatomi K.;
RT "Analysis of the nitrous oxide reduction genes, nosZDFYL, of Achromobacter
RT cycloclastes.";
RL DNA Res. 5:365-371(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS OF
RP THE MATURE PROTEIN.
RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC
RC 102459 / An-17;
RX PubMed=9720302; DOI=10.1016/s0162-0134(98)10001-6;
RA McGuirl M.A., Nelson L.K., Bollinger J.A., Chan Y.-K., Dooley D.M.;
RT "The nos (nitrous oxide reductase) gene cluster from the soil bacterium
RT Achromobacter cycloclastes: cloning, sequence analysis, and expression.";
RL J. Inorg. Biochem. 70:155-169(1998).
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; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
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:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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; X94977; CAA64426.1; -; Genomic_DNA.
DR EMBL; Y15161; CAA75425.1; -; Genomic_DNA.
DR EMBL; AF047429; AAD09157.1; -; Genomic_DNA.
DR PDB; 2IWF; X-ray; 1.86 A; A/B=1-642.
DR PDB; 2IWK; X-ray; 1.70 A; A/B=1-642.
DR PDBsum; 2IWF; -.
DR PDBsum; 2IWK; -.
DR AlphaFoldDB; P94127; -.
DR SMR; P94127; -.
DR BRENDA; 1.7.2.4; 69.
DR UniPathway; UPA00652; UER00709.
DR EvolutionaryTrace; P94127; -.
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; 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; 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; Copper; Direct protein sequencing; Metal-binding;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..46
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:9720302"
FT CHAIN 47..642
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019822"
FT REGION 544..642
FT /note="COX2-like"
FT BINDING 135
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="H -> L (in Ref. 1; CAA64426)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..163
FT /note="AR -> GA (in Ref. 1; CAA64426)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="T -> S (in Ref. 1; CAA64426)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..294
FT /note="AIKA -> PLRR (in Ref. 1; CAA64426)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="W -> S (in Ref. 1; CAA64426)"
FT /evidence="ECO:0000305"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 482..491
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 545..553
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 569..576
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:2IWK"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:2IWK"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:2IWK"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:2IWK"
SQ SEQUENCE 642 AA; 70922 MW; 76C9049FF5E712AB CRC64;
MESKEHKGLS RRALFSATAG SAILAGTVGP AALSLGAAGL ATPARAATGA DGSVAPGKLD
DYYGFWSSGQ TGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESIRIHQ RTMTEKTKKQ
LAANGKKIHD NGDLHHVHMS FTDGKYDGRY LFMNDKANTR VARVRCDVMK TDAILEIPNA
KGIHGMRPQK WPRSNYVFCN GEDEAPLVND GSTMTDVATY VNIFTAVDAD KWEVAWQVKV
SGNLDNCDAD YEGKWAFSTS YNSEMGMTLE EMTKSEMDHV VVFNIAEIEK AIKAGQYEEI
NGVKVVDGRK EAKSLFTRYI PIANNPHGCN MAPDRKHLCV AGKLSPTVTV LDVTKFDALF
YDNAEPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIDEAI RAYAGEKINP
IKDKLDVQYQ PGHLKTVMGE TLDAANDWLV CLCKFSKDRF LNVGPLKPEN DQLIDISGDK
MVLVHDGPTF AEPHDAIAVS PSILPNIRSV WDRKDPLWAE TRKQAEADEV DIDEWTEAVI
RDGNKVRVYM TSVAPSFSQP SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG NHGVAMEVGP
QQTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMFVEPK GA
