PETC_NITEU
ID PETC_NITEU Reviewed; 234 AA.
AC Q82W83;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ammonia monooxygenase gamma subunit {ECO:0000303|PubMed:19453274};
DE Short=AMO {ECO:0000303|PubMed:19453274};
DE AltName: Full=Cytochrome c1 {ECO:0000303|PubMed:19453274};
DE AltName: Full=Heterotrimeric Cu-heme enzyme {ECO:0000303|PubMed:19453274};
DE Flags: Precursor;
GN Name=petC {ECO:0000312|EMBL:CAD84722.1};
GN OrderedLocusNames=NE0811 {ECO:0000312|EMBL:CAD84722.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC {ECO:0000312|Proteomes:UP000001416};
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [2]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=19453274; DOI=10.1515/bc.2009.085;
RA Gilch S., Meyer O., Schmidt I.;
RT "A soluble form of ammonia monooxygenase in Nitrosomonas europaea.";
RL Biol. Chem. 390:863-873(2009).
RN [3]
RP COFACTOR.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=20204476; DOI=10.1007/s10534-010-9308-2;
RA Gilch S., Meyer O., Schmidt I.;
RT "Electron paramagnetic studies of the copper and iron containing soluble
RT ammonia monooxygenase from Nitrosomonas europaea.";
RL BioMetals 23:613-622(2010).
CC -!- FUNCTION: Part of the ammonia monooxygenase complex, which catalyzes
CC the oxidation of ammonia to hydroxylamine, the first reaction in the
CC process of ammonia oxidation to nitrite. {ECO:0000269|PubMed:19453274}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:20204476};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:20204476};
CC -!- SUBUNIT: The soluble ammonia monooxygenase is a nonamer composed of
CC three alpha subunits (AmoA), three beta subunits (AmoB) and three gamma
CC subunits (Cytochrome c1 PetC). {ECO:0000269|PubMed:19453274}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19453274};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:19453274}. Note=Ammonia monooxygenase is active and
CC distributed approximately equally in both subcellular fractions.
CC {ECO:0000269|PubMed:19453274}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- CAUTION: Substoichiometric amounts of non-heme iron (about 1 iron atom
CC per ammonia monooxygenase complex) have been found, however it does not
CC seem to function as a cofactor. {ECO:0000305|PubMed:19453274}.
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DR EMBL; AL954747; CAD84722.1; -; Genomic_DNA.
DR RefSeq; WP_011111423.1; NC_004757.1.
DR AlphaFoldDB; Q82W83; -.
DR SMR; Q82W83; -.
DR STRING; 228410.NE0811; -.
DR DNASU; 1081750; -.
DR EnsemblBacteria; CAD84722; CAD84722; NE0811.
DR KEGG; neu:NE0811; -.
DR eggNOG; COG2857; Bacteria.
DR HOGENOM; CLU_078597_0_0_4; -.
DR OMA; MPHVLWE; -.
DR OrthoDB; 1426747at2; -.
DR PhylomeDB; Q82W83; -.
DR Proteomes; UP000001416; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 GO; GO:0004497; F:monooxygenase activity; 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 InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; PTHR10266; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Heme; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..234
FT /note="Ammonia monooxygenase gamma subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_5004297614"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..193
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 55
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 234 AA; 26870 MW; 8A7E976E5B2303FE CRC64;
MRMIKFLLLA ILLAPFVAHS SGQEVKLDKA PIDRADKESL QRGAKGFVEY CLTCHGANFM
RFNRHHDIGM SEDDIRADLI HTGQKTGDLM EAAMRKKEAE GWFGVVPPDL SVIARARGAD
WLYTYLRTFY QDTSTYSGWN NLIFDKVAMP HVLHHLQGWQ VLEPGTGNLV QTKPGTMTKE
EYDRFVADLV NYMVYLGEPH APYRRELGIT VLLFLFGMLG LTYLLKKEYW RDIH
