AMOA_NITEU
ID AMOA_NITEU Reviewed; 276 AA.
AC Q04507;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ammonia monooxygenase alpha subunit {ECO:0000303|PubMed:19453274};
DE Short=AMO {ECO:0000303|PubMed:19453274};
DE EC=1.14.99.39 {ECO:0000269|PubMed:19453274, ECO:0000305|PubMed:8468301};
DE AltName: Full=Acetylene-binding polypeptide {ECO:0000303|PubMed:8468301};
DE AltName: Full=Heterotrimeric Cu-heme enzyme {ECO:0000303|PubMed:19453274};
GN Name=amoA1 {ECO:0000303|PubMed:8468301};
GN Synonyms=amoA {ECO:0000303|PubMed:8468301}; OrderedLocusNames=NE0944;
GN and
GN Name=amoA2 {ECO:0000303|PubMed:8468301};
GN Synonyms=amoA {ECO:0000303|PubMed:8468301}; OrderedLocusNames=NE2063;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=8468301; DOI=10.1128/jb.175.8.2436-2444.1993;
RA McTavish H.E., Fuchs J.A., Hooper A.B.;
RT "Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas
RT europaea.";
RL J. Bacteriol. 175:2436-2444(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
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 [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=8458839; DOI=10.1128/jb.175.7.1971-1980.1993;
RA Ensign S.A., Hyman M.R., Arp D.J.;
RT "In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by
RT copper.";
RL J. Bacteriol. 175:1971-1980(1993).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9642187; DOI=10.1128/jb.180.13.3353-3359.1998;
RA Hommes N.G., Sayavedra-Soto L.A., Arp D.J.;
RT "Mutagenesis and expression of amo, which codes for ammonia monooxygenase
RT in Nitrosomonas europaea.";
RL J. Bacteriol. 180:3353-3359(1998).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11064189; DOI=10.1111/j.1574-6968.2000.tb09376.x;
RA Stein L.Y., Sayavedra-Soto L.A., Hommes N.G., Arp D.J.;
RT "Differential regulation of amoA and amoB gene copies in Nitrosomonas
RT europaea.";
RL FEMS Microbiol. Lett. 192:163-168(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY 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 [7]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=19118368; DOI=10.1099/mic.0.023721-0;
RA Gilch S., Vogel M., Lorenz M.W., Meyer O., Schmidt I.;
RT "Interaction of the mechanism-based inactivator acetylene with ammonia
RT monooxygenase of Nitrosomonas europaea.";
RL Microbiology 155:279-284(2009).
RN [8]
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:11064189,
CC ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:8468301,
CC ECO:0000269|PubMed:9642187, ECO:0000305|PubMed:8458839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + NH4(+) + O2 = A + H(+) + H2O + hydroxylamine;
CC Xref=Rhea:RHEA:27341, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15429,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938; EC=1.14.99.39;
CC Evidence={ECO:0000269|PubMed:19453274, ECO:0000305|PubMed:8468301};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:20204476,
CC ECO:0000305|PubMed:8458839};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:19453274,
CC ECO:0000269|PubMed:20204476};
CC -!- ACTIVITY REGULATION: In vitro, inhibited by acetylene
CC (PubMed:19453274). In fact, acetylene is oxidized to ketene which binds
CC irreversibly to His-191 of ammonia monooxygenase alpha subunit (AmoA)
CC (PubMed:19118368). {ECO:0000269|PubMed:19118368,
CC ECO:0000269|PubMed:19453274}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 20 sec(-1) for ammonia. {ECO:0000269|PubMed:8468301};
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 Multi-pass membrane protein {ECO:0000305|PubMed:8468301}. 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 -!- DISRUPTION PHENOTYPE: Cells lacking amoA1 grow more slowly than wild-
CC type cells, while cells lacking amoA2 grow at rates similar to wild-
CC type. {ECO:0000269|PubMed:11064189, ECO:0000269|PubMed:9642187}.
CC -!- MISCELLANEOUS: The physiological significance of the two gene copies is
CC still unknown. {ECO:0000305|PubMed:11064189}.
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DR EMBL; L08050; AAA66194.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD84855.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD85974.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04507; -.
DR SMR; Q04507; -.
DR STRING; 228410.NE0944; -.
DR EnsemblBacteria; CAD84855; CAD84855; NE0944.
DR EnsemblBacteria; CAD85974; CAD85974; NE2063.
DR KEGG; neu:NE0944; -.
DR KEGG; neu:NE2063; -.
DR eggNOG; ENOG502Z9FM; Bacteria.
DR HOGENOM; CLU_1123603_0_0_4; -.
DR OMA; MHFMLLA; -.
DR BioCyc; MetaCyc:MON-3741; -.
DR BRENDA; 1.14.99.39; 3654.
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:0018597; F:ammonia monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IDA:CACAO.
DR Gene3D; 1.20.1450.10; -; 1.
DR InterPro; IPR037001; NH3/CH4_mOase_suA_sf.
DR InterPro; IPR003393; NH3_CH4_mOase_A.
DR Pfam; PF02461; AMO; 1.
DR TIGRFAMs; TIGR03080; CH4_NH3mon_ox_A; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Cytoplasm; Direct protein sequencing; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8468301"
FT CHAIN 2..276
FT /note="Ammonia monooxygenase alpha subunit"
FT /id="PRO_0000064589"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 187
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:19453274"
FT BINDING 191
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:19453274"
FT BINDING 204
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:19453274"
SQ SEQUENCE 276 AA; 31991 MW; CE4CF5879DE3682A CRC64;
MSIFRTEEIL KAAKMPPEAV HMSRLIDAVY FPILIILLVG TYHMHFMLLA GDWDFWMDWK
DRQWWPVVTP IVGITYCSAI MYYLWVNYRQ PFGATLCVVC LLIGEWLTRY WGFYWWSHYP
INFVTPGIML PGALMLDFTL YLTRNWLVTA LVGGGFFGLL FYPGNWPIFG PTHLPIVVEG
TLLSMADYMG HLYVRTGTPE YVRHIEQGSL RTFGGHTTVI AAFFSAFVSM LMFTVWWYLG
KVYCTAFFYV KGKRGRIVHR NDVTAFGEEG FPEGIK
