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-APR-2013, entry version 86.
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 / 218 / ZoBell;
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
RT and 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 / 218 / ZoBell;
RX PubMed=2542222;
RA Heiss B., Frunzke K., Zumft W.G.;
RT "Formation of the N-N bond from nitric oxide by a membrane-bound
RT cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas
RT stutzeri.";
RL J. Bacteriol. 171:3288-3297(1989).
RN [3]
RP EPR SPECTROSCOPY.
RC STRAIN=ATCC 14405 / 218 / ZoBell;
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
RT to the heme-copper oxidases.";
RL Biochemistry 37:3994-4000(1998).
CC -!- FUNCTION: Component of the anaerobic respiratory chain that
CC transforms nitrate to dinitrogen (denitrification). NorB is the
CC catalytic subunit of the enzyme complex. Shows proton pump
CC activity across the membrane in denitrifying bacterial cells. The
CC mononitrogen reduction is probably coupled to electron transport
CC phosphorylation.
CC -!- CATALYTIC ACTIVITY: Nitrous oxide + 2 ferricytochrome c + H(2)O =
CC 2 nitric oxide + 2 ferrocytochrome c + 2 H(+).
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; Multi-pass membrane protein
CC (Potential).
CC -!- INDUCTION: By nitric oxide (Probable).
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
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DR EMBL; X53676; CAA82229.1; -; Genomic_DNA.
DR PIR; S41117; S41117.
DR ProteinModelPortal; P98008; -.
DR TCDB; 3.D.4.10.2; proton-translocating cytochrome oxidase (COX) superfamily.
DR BioCyc; MetaCyc:MONOMER-241; -.
DR UniPathway; UPA00652; UER00708.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016966; F:nitric oxide reductase activity; IEA:EC.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR000883; Cyt_c_Oxase_su1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; COX1; 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;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 474 Nitric oxide reductase subunit B.
FT /FTId=PRO_0000183473.
FT TRANSMEM 19 39 Helical; (Potential).
FT TRANSMEM 61 81 Helical; (Potential).
FT TRANSMEM 95 115 Helical; (Potential).
FT TRANSMEM 145 165 Helical; (Potential).
FT TRANSMEM 169 189 Helical; (Potential).
FT TRANSMEM 207 227 Helical; (Potential).
FT TRANSMEM 243 263 Helical; (Potential).
FT TRANSMEM 270 290 Helical; (Potential).
FT TRANSMEM 308 328 Helical; (Potential).
FT TRANSMEM 348 368 Helical; (Potential).
FT TRANSMEM 390 410 Helical; (Potential).
FT TRANSMEM 433 453 Helical; (Potential).
FT METAL 60 60 Iron (low-spin heme axial ligand)
FT (Probable).
FT METAL 207 207 Iron B (Probable).
FT METAL 258 258 Iron B (Probable).
FT METAL 259 259 Iron B (Probable).
FT METAL 347 347 Iron (high-spin heme axial ligand)
FT (Probable).
FT METAL 349 349 Iron (low-spin heme axial ligand)
FT (Probable).
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
//
