R2-like ligand binding oxidase

NameR2-like ligand binding oxidase
Synonyms
  • 1.-.-.-
  • Ribonucleotide reductase R2 subunit homolog
  • Ribonucleotide reductase small subunit homolog
Gene NamenrdB
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051266|R2-like ligand binding oxidase
MTRTRSGSLAAGGLNWASLPLKLFAGGNAKFWHPADIDFTRDRADWEKLSDDERDYATRL
CTQFIAGEEAVTEDIQPFMSAMRAEGRLADEMYLTQFAFEEAKHTQVFRMWLDAVGISED
LHRYLDDLPAYRQIFYAELPECLNALSADPSPAAQVRASVTYNHIVEGMLALTGYYAWHK
ICVERAILPGMQELVRRIGDDERRHMAWGTFTCRRHVAADDANWTVFETRMNELIPLALR
LIEEGFALYGDQPPFDLSKDDFLQYSTDKGMRRFGTISNARGRPVAEIDVDYSPAQLEDT
FADEDRRTLAAASA
Number of residues314
Molecular Weight35655.635
Theoretical pINot Available
GO Classification
Functions
  • oxidoreductase activity
  • iron ion binding
  • manganese ion binding
Processes
  • oxidation-reduction process
Components
  • cytosol
General FunctionProbable oxidase that might be involved in lipid metabolism.
Specific FunctionIron ion binding
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP9WH69
UniProtKB Entry NameRIR2H_MYCTU
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0051267|R2-like ligand binding oxidase (nrdB)
ATGACACGCACACGTTCGGGCTCGCTCGCCGCGGGCGGACTCAACTGGGCGAGCCTGCCA
CTGAAGCTGTTCGCCGGGGGCAACGCAAAGTTCTGGCATCCGGCCGACATCGACTTCACG
CGCGACCGGGCGGACTGGGAGAAGTTGTCGGACGACGAACGTGACTACGCCACCCGATTG
TGCACCCAGTTCATTGCCGGCGAGGAGGCGGTGACCGAGGACATCCAGCCGTTCATGTCC
GCGATGCGGGCCGAGGGACGGCTGGCCGACGAGATGTATCTGACGCAGTTCGCGTTCGAG
GAAGCCAAACACACCCAGGTGTTTCGCATGTGGCTGGATGCCGTCGGAATCAGCGAAGAC
TTGCATCGCTATCTCGACGACTTGCCCGCCTACCGCCAAATCTTCTACGCGGAGTTGCCG
GAGTGCCTCAACGCATTGTCGGCCGATCCCTCACCGGCCGCCCAGGTCCGGGCGTCGGTC
ACCTACAACCACATCGTGGAAGGCATGCTGGCGCTCACGGGCTACTACGCCTGGCACAAG
ATCTGTGTGGAACGCGCAATCCTTCCCGGCATGCAGGAGCTGGTCCGGCGCATCGGTGAC
GACGAGCGACGCCACATGGCTTGGGGCACCTTCACCTGTCGGCGCCACGTCGCCGCCGAC
GACGCCAATTGGACGGTGTTCGAAACACGGATGAACGAGCTCATCCCGCTGGCGCTGCGC
CTCATCGAGGAGGGCTTTGCGCTGTACGGCGACCAGCCCCCATTCGACCTGTCCAAGGAC
GATTTCCTGCAATACTCGACCGACAAGGGAATGCGCCGGTTCGGCACCATCAGCAACGCC
CGCGGCCGGCCGGTCGCCGAAATCGACGTCGACTACTCGCCCGCGCAGCTGGAGGACACC
TTCGCCGACGAGGACCGGCGCACCCTGGCAGCGGCCTCGGCCTAG
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. 9634230
  2. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. 21969609
  3. Andersson CS, Hogbom M: A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold. Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5633-8. doi: 10.1073/pnas.0812971106. Epub 2009 Mar 24. 19321420