NORC_HALHD
ID NORC_HALHD Reviewed; 150 AA.
AC O50651;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
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 Halomonas halodenitrificans (Paracoccus halodenitrificans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=28252;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13511 / DSM 735 / CIP 105456 / NBRC 14912 / NCIMB 700;
RX PubMed=9480821; DOI=10.1006/bbrc.1998.8106;
RA Sakurai N., Sakurai T.;
RT "Genomic DNA cloning of the region encoding nitric oxide reductase in
RT Paracoccus halodenitrificans and a structure model relevant to cytochrome
RT oxidase.";
RL Biochem. Biophys. Res. Commun. 243:400-406(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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=May be attached to the membrane by a
CC signal-anchor. {ECO:0000250}.
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DR EMBL; AB010889; BAA24700.1; -; Genomic_DNA.
DR PIR; JE0165; JE0165.
DR AlphaFoldDB; O50651; -.
DR SMR; O50651; -.
DR BRENDA; 1.7.2.5; 3346.
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 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Respiratory chain; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..150
FT /note="Nitric oxide reductase subunit C"
FT /id="PRO_0000108423"
FT TRANSMEM 13..29
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT BINDING 62
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 /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 66
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 150 AA; 16773 MW; 8D613ADE2367928A CRC64;
MADGLTKSAA RNIFYGGSLF FFLLFAALTA HSHWYMVNKS TDNEGLTESV VAGKHIWEKN
MCINCHSIMG EGAYFAPELS NVWERYGGHQ NPEAARAGLA AWIRAQPLGT QGRRQMPAYD
FTDEEMSSLI DFLEWTDGID DQDWPPHPAG