Methane monooxygenase component A alpha chain
Details
- Name
- Methane monooxygenase component A alpha chain
- Synonyms
- 1.14.13.25
- Methane hydroxylase
- Gene Name
- mmoX
- UniProtKB Entry
- P22869Swiss-Prot
- Organism
- Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
- NCBI Taxonomy ID
- 243233
- Amino acid sequence
>lcl|BSEQ0012329|Methane monooxygenase component A alpha chain MALSTATKAATDALAANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQF KLIAKEYARMEAVKDERQFGSLQDALTRLNAGVRVHPKWNETMKVVSNFLEVGEYNAIAA TGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPAGHNDARRTRTIGPL WKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAVTEWAAANGDEITPTVFLSIE TDELRHMANGYQTVVSIANDPASAKYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEP WVKTWNRWVYEDWGGIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFR LALPDQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIYIDRV SQVPFCPSLAKGASTLRVHEYNGQMHTFSDQWGERMWLAEPERYECQNIFEQYEGRELSE VIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLNCVFKNPVKAFN
- Number of residues
- 527
- Molecular Weight
- 60645.97
- Theoretical pI
- 6.29
- GO Classification
- Functionsmetal ion binding / methane monooxygenase activityProcessescellular aromatic compound metabolic process / one-carbon metabolic process
- General Function
- Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
- Specific Function
- metal ion binding
- Pfam Domain Function
- Phenol_Hydrox (PF02332)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012330|Methane monooxygenase component A alpha chain (mmoX) ATGGCACTTAGCACCGCAACCAAGGCCGCGACGGACGCGCTGGCTGCCAATCGGGCACCC ACCAGCGTGAATGCACAGGAAGTGCACCGTTGGCTCCAGAGCTTCAACTGGGATTTCAAG AACAACCGGACCAAGTACGCCACCAAGTACAAGATGGCGAACGAGACCAAGGAACAGTTC AAGCTGATCGCCAAGGAATATGCGCGCATGGAGGCAGTCAAGGACGAAAGGCAGTTCGGT AGCCTGCAGGATGCGCTGACCCGCCTCAACGCCGGTGTTCGCGTTCATCCGAAGTGGAAC GAGACCATGAAAGTGGTTTCGAACTTCCTGGAAGTGGGCGAATACAACGCCATCGCCGCT ACCGGGATGCTGTGGGATTCCGCCCAGGCGGCGGAACAGAAGAACGGCTATCTGGCCCAG GTGTTGGATGAAATCCGCCACACCCACCAGTGTGCCTACGTCAACTACTACTTCGCGAAG AACGGCCAGGACCCGGCCGGTCACAACGATGCTCGCCGCACCCGTACCATCGGTCCGCTG TGGAAGGGCATGAAGCGCGTGTTTTCCGACGGCTTCATTTCCGGCGACGCCGTGGAATGC TCCCTCAACCTGCAGCTGGTGGGTGAGGCCTGCTTCACCAATCCGCTGATCGTCGCAGTG ACCGAATGGGCTGCCGCCAACGGCGATGAAATCACCCCGACGGTGTTCCTGTCGATCGAG ACCGACGAACTGCGCCACATGGCCAACGGTTACCAGACCGTCGTTTCCATCGCCAACGAT CCGGCTTCCGCCAAGTATCTCAACACGGACCTGAACAACGCCTTCTGGACCCAGCAGAAG TACTTCACGCCGGTGTTGGGCATGCTGTTCGAGTATGGCTCCAAGTTCAAGGTCGAGCCG TGGGTCAAGACGTGGAACCGCTGGGTGTACGAGGACTGGGGCGGCATCTGGATCGGCCGT CTGGGCAAGTACGGGGTGGAGTCGCCGCGCAGCCTCAAGGACGCCAAGCAGGACGCTTAC TGGGCTCACCACGACCTGTATCTGCTGGCTTATGCGCTGTGGCCGACCGGCTTCTTCCGT CTGGCGCTGCCGGATCAGGAAGAAATGGAGTGGTTCGAGGCCAACTACCCCGGCTGGTAC GACCACTACGGCAAGATCTACGAGGAATGGCGCGCCCGCGGTTGCGAGGATCCGTCCTCG GGCTTCATCCCGCTGATGTGGTTCATCGAAAACAACCATCCCATCTACATCGATCGCGTG TCGCAAGTGCCGTTCTGCCCGAGCTTGGCCAAGGGCGCCAGCACCCTGCGCGTGCACGAG TACAACGGCCAGATGCACACCTTCAGCGACCAGTGGGGCGAGCGCATGTGGCTGGCCGAG CCGGAGCGCTACGAGTGCCAGAACATCTTCGAACAGTACGAAGGACGCGAACTGTCGGAA GTGATCGCCGAACTGCACGGGCTGCGCAGTGATGGCAAGACCCTGATCGCCCAGCCGCAT GTCCGTGGCGACAAGCTGTGGACGTTGGACGATATCAAACGCCTGAACTGCGTCTTCAAG AACCCGGTGAAGGCATTCAATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P22869 UniProtKB Entry Name MEMA_METCA GenBank Gene ID M90050 PDB ID(s) 1FYZ, 1FZ0, 1FZ1, 1FZ2, 1FZ3, 1FZ4, 1FZ5, 1FZ6, 1FZ7, 1FZ8, 1FZ9, 1FZH, 1FZI, 1MMO, 1MTY, 1XMF, 1XMG, 1XMH, 1XU3, 1XU5, 1XVB, 1XVC, 1XVD, 1XVE, 1XVF, 1XVG, 4GAM KEGG ID mca:MCA1194 - General References
- Stainthorpe AC, Lees V, Salmond GP, Dalton H, Murrell JC: The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene. 1990 Jul 2;91(1):27-34. [Article]
- Ward N, Larsen O, Sakwa J, Bruseth L, Khouri H, Durkin AS, Dimitrov G, Jiang L, Scanlan D, Kang KH, Lewis M, Nelson KE, Methe B, Wu M, Heidelberg JF, Paulsen IT, Fouts D, Ravel J, Tettelin H, Ren Q, Read T, DeBoy RT, Seshadri R, Salzberg SL, Jensen HB, Birkeland NK, Nelson WC, Dodson RJ, Grindhaug SH, Holt I, Eidhammer I, Jonasen I, Vanaken S, Utterback T, Feldblyum TV, Fraser CM, Lillehaug JR, Eisen JA: Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath). PLoS Biol. 2004 Oct;2(10):e303. Epub 2004 Sep 21. [Article]
- Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P: Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature. 1993 Dec 9;366(6455):537-43. [Article]
- Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ: Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chem Biol. 1995 Sep;2(9):409-18. [Article]
- Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA: Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins. 1997 Oct;29(2):141-52. [Article]
- Whittington DA, Lippard SJ: Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site. J Am Chem Soc. 2001 Feb 7;123(5):827-38. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Methane monooxygenase component A alpha chain (Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 3-Bromo-3-buten-1-ol experimental unknown target Details 6-Bromo-1-hexanol experimental unknown target Details