NORB_PSEAE
ID NORB_PSEAE Reviewed; 466 AA.
AC Q59647;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nitric oxide reductase subunit B;
DE EC=1.7.2.5;
DE AltName: Full=NOR large subunit;
DE AltName: Full=Nitric oxide reductase cytochrome b subunit;
GN Name=norB; OrderedLocusNames=PA0524;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7711073; DOI=10.1016/0167-4781(95)00018-c;
RA Arai H., Igarashi Y., Kodama T.;
RT "The structural genes for nitric oxide reductase from Pseudomonas
RT aeruginosa.";
RL Biochim. Biophys. Acta 1261:279-284(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Component of the anaerobic respiratory chain that transforms
CC nitrate to dinitrogen (denitrification). NorB is the catalytic subunit
CC of the enzyme complex. Shows proton pump activity across the membrane
CC in denitrifying bacterial cells. The mononitrogen reduction is probably
CC coupled to electron transport phosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + nitrous oxide = 2 Fe(II)-
CC [cytochrome c] + 2 H(+) + 2 nitric oxide; Xref=Rhea:RHEA:30211,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16480, ChEBI:CHEBI:17045,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.5;
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 3/4.
CC -!- SUBUNIT: Heterodimer of cytochromes b (large subunit) and c (small
CC subunit).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; D38133; BAA07330.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03913.1; -; Genomic_DNA.
DR PIR; S53713; S53713.
DR RefSeq; NP_249215.1; NC_002516.2.
DR RefSeq; WP_003113237.1; NZ_QZGE01000010.1.
DR PDB; 3O0R; X-ray; 2.70 A; B=1-466.
DR PDB; 3WFB; X-ray; 2.70 A; B=1-466.
DR PDB; 3WFC; X-ray; 2.50 A; B=1-466.
DR PDB; 3WFD; X-ray; 2.30 A; B=1-466.
DR PDB; 3WFE; X-ray; 2.49 A; B=1-466.
DR PDB; 5GUW; X-ray; 3.20 A; B/D=1-466.
DR PDB; 5GUX; X-ray; 3.30 A; B=1-466.
DR PDBsum; 3O0R; -.
DR PDBsum; 3WFB; -.
DR PDBsum; 3WFC; -.
DR PDBsum; 3WFD; -.
DR PDBsum; 3WFE; -.
DR PDBsum; 5GUW; -.
DR PDBsum; 5GUX; -.
DR AlphaFoldDB; Q59647; -.
DR SMR; Q59647; -.
DR STRING; 287.DR97_3492; -.
DR TCDB; 3.D.4.10.3; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; Q59647; -.
DR PRIDE; Q59647; -.
DR ABCD; Q59647; 1 sequenced antibody.
DR EnsemblBacteria; AAG03913; AAG03913; PA0524.
DR GeneID; 882193; -.
DR KEGG; pae:PA0524; -.
DR PATRIC; fig|208964.12.peg.554; -.
DR PseudoCAP; PA0524; -.
DR HOGENOM; CLU_021582_1_0_6; -.
DR InParanoid; Q59647; -.
DR OMA; LDKMYWW; -.
DR PhylomeDB; Q59647; -.
DR BioCyc; PAER208964:G1FZ6-529-MON; -.
DR BRENDA; 1.7.2.5; 5087.
DR UniPathway; UPA00652; UER00708.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016966; F:nitric oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..466
FT /note="Nitric oxide reductase subunit B"
FT /id="PRO_0000183472"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 60
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 348
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2; high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 350
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 16..40
FT /evidence="ECO:0007829|PDB:3WFD"
FT TURN 44..50
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 53..84
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 141..163
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 234..255
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3WFD"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 343..368
FT /evidence="ECO:0007829|PDB:3WFD"
FT TURN 369..374
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 381..416
FT /evidence="ECO:0007829|PDB:3WFD"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 435..456
FT /evidence="ECO:0007829|PDB:3WFD"
SQ SEQUENCE 466 AA; 52336 MW; DFB379172C86D5B7 CRC64;
MMSPNGSLKF ASQAVAKPYF VFALILFVGQ ILFGLIMGLQ YVVGDFLFPA IPFNVARMVH
TNLLIVWLLF GFMGAAYYLV PEESDCELYS PKLAWILFWV FAAAGVLTIL GYLLVPYAGL
ARLTGNELWP TMGREFLEQP TISKAGIVIV ALGFLFNVGM TVLRGRKTAI SMVLMTGLIG
LALLFLFSFY NPENLTRDKF YWWWVVHLWV EGVWELIMGA ILAFVLVKIT GVDREVIEKW
LYVIIAMALI SGIIGTGHHY FWIGVPGYWL WLGSVFSALE PLPFFAMVLF AFNTINRRRR
RDYPNRAVAL WAMGTTVMAF LGAGVWGFMH TLAPVNYYTH GTQLTAAHGH MAFYGAYAMI
VMTIISYAMP RLRGIGEAMD NRSQVLEMWG FWLMTVAMVF ITLFLSAAGV LQVWLQRMPA
DGAAMTFMAT QDQLAIFYWL REGAGVVFLI GLVAYLLSFR RGKAAA
