AMOB_NITEU
ID AMOB_NITEU Reviewed; 420 AA.
AC Q04508;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ammonia monooxygenase beta 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=Heterotrimeric Cu-heme enzyme {ECO:0000303|PubMed:19453274};
DE Flags: Precursor;
GN Name=amoB1 {ECO:0000303|PubMed:8468301};
GN Synonyms=amoB {ECO:0000303|PubMed:8468301}; OrderedLocusNames=NE0943;
GN and
GN Name=amoB2 {ECO:0000303|PubMed:8468301};
GN Synonyms=amoB {ECO:0000303|PubMed:8468301}; OrderedLocusNames=NE2062;
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;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-267, PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR 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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-420.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=7980540; DOI=10.1006/bbrc.1994.2524;
RA Bergmann D.J., Hooper A.B.;
RT "Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia
RT monooxygenase of Nitrosomonas europaea.";
RL Biochem. Biophys. Res. Commun. 204:759-762(1994).
RN [4]
RP PROTEIN SEQUENCE OF 26-35, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, 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 [5]
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 [6]
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 [7]
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: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(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:20204476,
CC ECO:0000305|PubMed:8458839};
CC Note=Binds 2 copper ions per subunit (PubMed:19453274,
CC PubMed:20204476). The two coppers forms a binuclear cluster (By
CC similarity). {ECO:0000250|UniProtKB:G1UBD1,
CC ECO:0000269|PubMed:19453274, ECO:0000269|PubMed:20204476};
CC -!- ACTIVITY REGULATION: In vitro, inhibited by acetylene.
CC {ECO:0000269|PubMed:19453274}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 20 sec(-1) for ammonia as substrate.
CC {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 amoB1 grow more slowly than wild-
CC type cells, while cells lacking amoB2 grow at rates similar to wild-
CC type. {ECO:0000269|PubMed:11064189}.
CC -!- MISCELLANEOUS: The physiological significance of the two gene copies is
CC still unknown. {ECO:0000305|PubMed:11064189}.
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DR EMBL; AL954747; CAD84854.1; -; Genomic_DNA.
DR EMBL; AL954747; CAD85973.1; -; Genomic_DNA.
DR EMBL; L08050; AAA66195.1; -; Genomic_DNA.
DR PIR; B49853; B49853.
DR RefSeq; WP_011111552.1; NC_004757.1.
DR AlphaFoldDB; Q04508; -.
DR SMR; Q04508; -.
DR STRING; 228410.NE0943; -.
DR EnsemblBacteria; CAD84854; CAD84854; NE0943.
DR EnsemblBacteria; CAD85973; CAD85973; NE2062.
DR KEGG; neu:NE0943; -.
DR KEGG; neu:NE2062; -.
DR eggNOG; ENOG502Z96N; Bacteria.
DR HOGENOM; CLU_660275_0_0_4; -.
DR OMA; ERSQEPF; -.
DR OrthoDB; 650121at2; -.
DR BioCyc; MetaCyc:MON-3761; -.
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 Gene3D; 1.10.287.710; -; 1.
DR Gene3D; 2.60.120.570; -; 1.
DR Gene3D; 2.60.40.1580; -; 1.
DR InterPro; IPR006833; NH3_CH4_mOase_B.
DR InterPro; IPR023303; NH3_CH4_mOase_suB_C.
DR InterPro; IPR023141; NH3_CH4_mOase_suB_hlx_hairpin.
DR InterPro; IPR023301; NH3_CH4_mOase_suB_N.
DR Pfam; PF04744; Monooxygenase_B; 1.
DR TIGRFAMs; TIGR03079; CH4_NH3mon_ox_B; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Cytoplasm; Direct protein sequencing; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:19453274"
FT CHAIN 26..420
FT /note="Ammonia monooxygenase beta subunit"
FT /id="PRO_0000064590"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 38
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G1UBD1,
FT ECO:0000305|PubMed:19453274"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G1UBD1,
FT ECO:0000305|PubMed:19453274"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G1UBD1,
FT ECO:0000305|PubMed:19453274"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G1UBD1,
FT ECO:0000305|PubMed:19453274"
SQ SEQUENCE 420 AA; 46793 MW; 745E4A1A6ACF0AD8 CRC64;
MGIKNLYKRG VMGLYGVAYA VAALAMTVTL DVSTVAAHGE RSQEPFLRMR TVQWYDIKWG
PEVTKVNENA KITGKFHLAE DWPRAAAQPD FSFFNVGSPS PVFVRLSTKI NGHPWFISGP
LQIGRDYEFE VNLRARIPGR HHMHAMLNVK DAGPIAGPGA WMNITGSWDD FTNPLKLLTG
ETIDSETFNL SNGIFWHVVW MSIGIFWIGV FTARPMFLPR SRVLLAYGDD LLMDPMDKKI
TWVLAILTLA LVWGGYRYTE NKHPYTVPIQ AGQSKVAALP VAPNPVSIVI TDANYDVPGR
ALRVTMEVTN NGDIPVTFGE FTTAGIRFIN STGRKYLDPQ YPRELIAVGL NFDDESAIQP
GQTKELKMEA KDALWEIQRL MALLGDPESR FGGLLMSWDA EGNRHINSIA GPVIPVFTKL
