[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 25618 / H37Rv; DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan] Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."; Nature 393:537-544(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CDC 1551 / Oshkosh; DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan] Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.; "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."; J. Bacteriol. 184:5479-5490(2002).
[3]	ROLE IN MYCOBACTIN BIOSYNTHESIS. STRAIN=CDC 1551 / Oshkosh; DOI=10.1016/S1074-5521(98)90291-5; PubMed=9831524 [NCBI, ExPASy, EBI, Israel, Japan] Quadri L.E.N., Sello J., Keating T.A., Weinreb P.H., Walsh C.T.; "Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin."; Chem. Biol. 5:631-645(1998).
[4]	FUNCTION, AND COFACTOR. STRAIN=ATCC 25618 / H37Rv; DOI=10.1073/pnas.0507924103; PubMed=16461464 [NCBI, ExPASy, EBI, Israel, Japan] Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.; "A genetic locus required for iron acquisition in Mycobacterium tuberculosis."; Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).

Comments

FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation of the two acylated lysine residues during mycobactin assembly, thus producing the hydroxamate groups necessary for iron sequestration. Is also able, but less efficiently, to hydroxylate L-lysine (non acylated) in vitro.
CATALYTIC ACTIVITY: L-lysine + NADPH + O₂ = N⁶-hydroxy-L-lysine + NADP⁺ + H₂O.
COFACTOR: FAD.
PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis .
INDUCTION: Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by ideR and iron (By similarity).
SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX842579; CAB08475.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK46741.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A70588; A70588.

RefSeq

NP_216894.1; -.
NP_336927.1; -.

3D structure databases

ModBase

O05820.

Organism-specific databases

TubercuList

Rv2378c; -.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047091;	Molecular function: L-lysine 6-monooxygenase (NADPH) activity (inferred from electronic annotation from EC).
GO:0006826;	Biological process: iron ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Genome annotation databases

GeneID

885648; -.
925901; -.

GenomeReviews

AE000516_GR; MT2446.
AL123456_GR; Rv2378c.

KEGG

mtc:MT2446; -.
mtu:Rv2378c; -.

TIGR

MT2446; -.

Phylogenomic databases

HOGENOM

O05820; -.

Other

ProtoNet

O05820.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; Flavoprotein; Ion transport; Iron; Iron transport; Monooxygenase; NADP; Oxidoreductase; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 431`	`410`	`L-lysine 6-monooxygenase mbtG.`	`PRO_0000261312`

Sequence information

Length: 431 AA [This is the length of the unprocessed precursor]

Molecular weight: 46944 Da [This is the MW of the unprocessed precursor]

CRC64: 8D200693CB6D4EB0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPTLAVLGA GAKAVAVAAK ASVLRDMGVD VPDVIAVERI GVGANWQASG GWTDGAHRLG 

        70         80         90        100        110        120 
TSPEKDVGFP YRSALVPRRN AELDERMTRY SWQSYLIATA SFAEWIDRGR PAPTHRRWSQ 

       130        140        150        160        170        180 
YLAWVADHIG LKVIHGEVER LAVTGDRWAL CTHETTVQAD ALMITGPGQA EKSLLPGNPR 

       190        200        210        220        230        240 
VLSIAQFWDR AAGHDRINAE RVAVIGGGET AASMLNELFR HRVSTITVIS PQVTLFTRGE 

       250        260        270        280        290        300 
GFFENSLFSD PTDWAALTFD ERRDALARTD RGVFSATVQE ALLADDRIHH LRGRVAHAVG 

       310        320        330        340        350        360 
RQGQIRLTLS TNRGSENFET VHGFDLVIDG SGADPLWFTS LFSQHTLDLL ELGLGGPLTA 

       370        380        390        400        410        420 
DRLQEAIGYD LAVTDVTPKL FLPTLSGLTQ GPGFPNLSCL GLLSDRVLGA GIFTPTKHND 

       430 
TRRSGEHQSF R

O05820 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools