KEGG   ENZYME: 1.14.99.39
Entry
EC 1.14.99.39               Enzyme                                 
Name
ammonia monooxygenase;
AMO
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
Sysname
ammonia,donor:oxygen oxidoreductase (hydroxylamine-producing)
Reaction(IUBMB)
NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O [RN:R09519]
Reaction(KEGG)
R09519 > R00148;
(other) R09156
Substrate
NH3 [CPD:C00014];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
NH2OH [CPD:C00192];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper [1], iron [5] and possibly zinc [9]. The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.
History
EC 1.14.99.39 created 2010
Pathway
ec00910  Nitrogen metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K10944  methane/ammonia monooxygenase subunit A
Genes
MCAMCA1797(pmoA) MCA2854(pmoA2)
METUGNH96_03570 GNH96_09690
MMEOOOT43_00490 OOT43_14055
MMTMetme_0304
MDNJT25_004545 JT25_012445
MDHAYM39_18580 AYM39_19770
MKOMKLM6_3758 MKLM6_3997
METLU737_00525 U737_22530
MPADKEF85_05595 KEF85_15100
MELLIVG45_01190 IVG45_17415
MRPNM686_001765
MMOTQZJ86_01655(amoA)
MAHMEALZ_0515(pmoA)
MBUREQU24_19305
MPSYCEK71_17435
MMAIsS8_1788 sS8_3977
MSZEMSZNOR_3294(pmoA) MSZNOR_4515(pmoA)
MMOBF6R98_01475 F6R98_16060
MEINmethR_P0112
MOZMoryE10_29180 MoryE10_29210
MISZMishRS11D_20920 MishRS11D_40480 MishRS11D_42080
MESLKKZ03_06640
MEIYMIN45_P0548 MIN45_P2284
MCAUMIT9_P0452 MIT9_P0923
NOCNoc_2502
NHLNhal_0676
NWANwat_0632
NWRE3U44_00915
NTTTAO_1521(amoA)
NTGNSCAC_1278(amoA)
HPSEHPF_13160(pmoA1)
NEUNE0944(amoA1) NE2063(amoA2)
NETNeut_2077 Neut_2318
NITNAL212_0798 NAL212_1387 NAL212_2605
NIINit79A3_0472 Nit79A3_1080 Nit79A3_2885
NCOAAW31_01085 AAW31_05380
NURATY38_01310 ATY38_07255 ATY38_13755
NSTNstercoris_00328 Nstercoris_01426
NMUNmul_A0799 Nmul_A2325 Nmul_A2765
NLCEBAPG3_006230 EBAPG3_014830 EBAPG3_15005
NIZNNRS527_00820 NNRS527_02502 NNRS527_03102
AZRCJ010_10955
BAUTQA635_32490
MEDKQEV83_09615(amoA)
MSCBN69_0203(pmoA2) BN69_2827(pmoA) BN69_3534(pmoA)
MBRYB1812_00565 B1812_13465 B1812_14775 B1812_18680
MROSEHO51_01980 EHO51_08605
MHEYH2LOC_006300 H2LOC_011625 H2LOC_017530
MPARF7D14_03105 F7D14_11665 F7D14_16695
MIWASS37A_06920 SS37A_17860 SS37A_28170
MTWCQW49_01220 CQW49_10255
MECQMSC49_20790 MSC49_22310 MSC49_34660
MDXBTO20_38255
MCBMycch_5910
MRHMycrhN_3041
MINMinf_1507(pmoA) Minf_1510(pmoA) Minf_1590(pmoA)
MKCkam1_1359(pmoA3) kam1_1509(pmoA2) kam1_1512(pmoA1) kam1_1972(pmoA4)
MFHMFUM_1605(pmoA3) MFUM_1792(pmoA1) MFUM_1795(pmoA2)
MCAOIT6_09400 IT6_09940 IT6_09955
MEAPMTHMO_0894(pmoA1) MTHMO_0897(pmoA2)
NIONITINOP_1853(amoA)
NKFNkreftii_003170
MOXDAMO_2450(pmoA)
NMRNmar_1500
NIRNSED_08255
NKRNKOR_08170
NIDNPIRD3C_2147(amoA)
NINNADRNF5_0394(amoA)
NIWNisw_06415
NCLC5F47_07870
NOXC5F49_07755
NUEC5F50_11085
NIPNsoK4_00795
NZTNZOSNM25_000290
NCTNMSP_0259
NICDSQ20_08765
NGANgar_c25350(amoA)
NVNNVIE_027270(amoA)
NEVNTE_00961
TAANMY3_03280
NFNNFRAN_0675(amoA)
NCVNCAV_0492(amoA)
CSYCENSYa_0402
NBVT478_0302
TAHSU86_008325
NIUDSQ19_08460
NCKQVH35_01005
NDVNDEV_1777(amoA)
 » show all
Reference
1  [PMID:8458839]
  Authors
Ensign SA, Hyman MR, Arp DJ
  Title
In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper.
  Journal
J Bacteriol 175:1971-80 (1993)
DOI:10.1128/JB.175.7.1971-1980.1993
Reference
2  [PMID:8085841]
  Authors
Hyman MR, Page CL, Arp DJ
  Title
Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea.
  Journal
Appl Environ Microbiol 60:3033-5 (1994)
DOI:10.1128/AEM.60.8.3033-3035.1994
Reference
3  [PMID:7980540]
  Authors
Bergmann DJ, Hooper AB
  Title
Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea.
  Journal
Biochem Biophys Res Commun 204:759-62 (1994)
DOI:10.1006/bbrc.1994.2524
  Sequence
Reference
4  [PMID:7590173]
  Authors
Holmes AJ, Costello A, Lidstrom ME, Murrell JC
  Title
Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related.
  Journal
FEMS Microbiol Lett 132:203-8 (1995)
DOI:10.1111/j.1574-6968.1995.tb07834.x
Reference
5  [PMID:8941709]
  Authors
Zahn JA, Arciero DM, Hooper AB, DiSpirito AA
  Title
Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea.
  Journal
FEBS Lett 397:35-8 (1996)
DOI:10.1016/S0014-5793(96)01116-7
Reference
6  [PMID:8654570]
  Authors
Moir JW, Crossman LC, Spiro S, Richardson DJ
  Title
The purification of ammonia monooxygenase from Paracoccus denitrificans.
  Journal
FEBS Lett 387:71-4 (1996)
DOI:10.1016/0014-5793(96)00463-2
Reference
7  [PMID:11004450]
  Authors
Whittaker M, Bergmann D, Arciero D, Hooper AB
  Title
Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea.
  Journal
Biochim Biophys Acta 1459:346-55 (2000)
DOI:10.1016/S0005-2728(00)00171-7
Reference
8  [PMID:12209257]
  Authors
Arp DJ, Sayavedra-Soto LA, Hommes NG.
  Title
Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea.
  Journal
Arch Microbiol 178:250-5 (2002)
DOI:10.1007/s00203-002-0452-0
Reference
9  [PMID:19453274]
  Authors
Gilch S, Meyer O, Schmidt I
  Title
A soluble form of ammonia monooxygenase in Nitrosomonas europaea.
  Journal
Biol Chem 390:863-73 (2009)
DOI:10.1515/BC.2009.085
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.39
IUBMB Enzyme Nomenclature: 1.14.99.39
ExPASy - ENZYME nomenclature database: 1.14.99.39
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.99.39
BRENDA, the Enzyme Database: 1.14.99.39

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