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Database: UniProt
Entry: P98008
LinkDB: P98008
Original site: P98008 
ID   NORB_STUST              Reviewed;         474 AA.
AC   P98008;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 124.
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;
OS   Stutzerimonas stutzeri (Pseudomonas stutzeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / Baumann 218 / ZoBell 632;
RX   PubMed=7508388; DOI=10.1111/j.1432-1033.1994.tb19962.x;
RA   Zumft W.G., Braun C., Cuypers H.;
RT   "Nitric oxide reductase from Pseudomonas stutzeri. Primary structure and
RT   gene organization of a novel bacterial cytochrome bc complex.";
RL   Eur. J. Biochem. 219:481-490(1994).
RN   [2]
RP   EPR SPECTROSCOPY, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / Baumann 218 / ZoBell 632;
RX   PubMed=2542222; DOI=10.1128/jb.171.6.3288-3297.1989;
RA   Heiss B., Frunzke K., Zumft W.G.;
RT   "Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome
RT   bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri.";
RL   J. Bacteriol. 171:3288-3297(1989).
RN   [3]
RP   EPR SPECTROSCOPY.
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / Baumann 218 / ZoBell 632;
RX   PubMed=9521721; DOI=10.1021/bi972437y;
RA   Cheesman M.R., Zumft W.G., Thomson A.J.;
RT   "The MCD and EPR of the heme centers of nitric oxide reductase from
RT   Pseudomonas stutzeri: evidence that the enzyme is structurally related to
RT   the heme-copper oxidases.";
RL   Biochemistry 37:3994-4000(1998).
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.
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         Evidence={ECO:0000269|PubMed:2542222};
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   -!- INDUCTION: By nitric oxide. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X53676; CAA82229.1; -; Genomic_DNA.
DR   PIR; S41117; S41117.
DR   RefSeq; WP_003279682.1; NZ_POUM01000011.1.
DR   AlphaFoldDB; P98008; -.
DR   SMR; P98008; -.
DR   TCDB; 3.D.4.10.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   eggNOG; COG3256; Bacteria.
DR   BioCyc; MetaCyc:MONOMER-241; -.
DR   UniPathway; UPA00652; UER00708.
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; IMP:CACAO.
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; Cytochrome c oxidase-like, subunit I domain; 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   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF43; NITRIC OXIDE REDUCTASE SUBUNIT B; 1.
DR   Pfam; PF00115; COX1; 1.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7508388"
FT   CHAIN           2..474
FT                   /note="Nitric oxide reductase subunit B"
FT                   /id="PRO_0000183473"
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        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
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        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
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         347
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         349
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"
SQ   SEQUENCE   474 AA;  53137 MW;  6455FC53DCB27896 CRC64;
     MSSFNPHLKF QSQAVAKPYF VFALILFVGQ VLFGLIMGLQ YVVGDFLFPL LPFNVARMVH
     TNLLIVWLLF GFMGAAYYLI PEESDCELHS PKLAIILFWV FAAAGVLTIL GYLFVPYAAL
     AEMTRNDLLP TMGREFLEQP TITKIGIVVV ALGFLYNIGM TMLKGRKTVV STVMMTGLIG
     LAVFFLFAFY NPENLSRDKF YWWFVVHLWV EGVWELIMGA MLAFVLIKVT GVDREVIEKW
     LYVIIAMALI TGIIGTGHHF FWIGAPTVWL WVGSIFSALE PLPFFAMVLF ALNMVNRRRR
     EHPNKAASLW AIGTTVTAFL GAGVWGFMHT LAPVNYYTHG SQLTAAHGHL AFYGAYAMIV
     MTMISYAMPR LRGLGEAPDA RAQRIEVWGF WLMTISMIAI TLFLTAAGVV QIWLQRIPAD
     GAAMSFMNTA DQLAIFFWLR FIAGVFFLIG LVCYLYSFRQ RGRVPVVVAA PAAA
//
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