NORB_PSEST
ID NORB_PSEST Reviewed; 474 AA.
AC P98008;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
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 / 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 / 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 / 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 STRING; 32042.PstZobell_00287; -.
DR TCDB; 3.D.4.10.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR eggNOG; COG3256; Bacteria.
DR BioCyc; MetaCyc:MON-241; -.
DR UniPathway; UPA00652; UER00708.
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; 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; -; 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 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
