NORC_PSEST
ID NORC_PSEST Reviewed; 146 AA.
AC Q52527;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nitric oxide reductase subunit C;
DE AltName: Full=NOR small subunit;
DE AltName: Full=Nitric oxide reductase cytochrome c subunit;
GN Name=norC;
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 PROTEIN SEQUENCE OF 2-21.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=1551856; DOI=10.1128/jb.174.7.2394-2397.1992;
RA Braun C., Zumft W.G.;
RT "The structural genes of the nitric oxide reductase complex from
RT Pseudomonas stutzeri are part of a 30-kilobase gene cluster for
RT denitrification.";
RL J. Bacteriol. 174:2394-2397(1992).
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=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 [4]
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).
CC -!- SUBUNIT: Heterodimer of cytochromes b (large subunit) and c (small
CC subunit).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Note=May be attached to the membrane by a signal-anchor.
CC -!- INDUCTION: By nitric oxide. {ECO:0000305}.
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DR EMBL; X53676; CAA82228.1; -; Genomic_DNA.
DR PIR; S41116; S41116.
DR RefSeq; WP_058065565.1; NZ_POUM01000011.1.
DR AlphaFoldDB; Q52527; -.
DR SMR; Q52527; -.
DR STRING; 32042.PstZobell_00282; -.
DR TCDB; 3.D.4.10.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR eggNOG; COG2010; Bacteria.
DR BioCyc; MetaCyc:MON-242; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Respiratory chain; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1551856"
FT CHAIN 2..146
FT /note="Nitric oxide reductase subunit C"
FT /id="PRO_0000108425"
FT TRANSMEM 13..29
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 65
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 146 AA; 16639 MW; BBD733EE361E7A32 CRC64;
MSETFTKGMA RNIYFGGSVF FFLVFLGLTY HTEQTFPERT NESEMTEAVV RGKEVWENNN
CIGCHSLLGE GAYFAPELGN VFVRRGGEET FKPFLHAWMK AQPLGAPGRR AMPQFNLSEQ
QVDDMAEFLK WTSKIDTNDW PPNKEG
