Q8PAD3 (KMO_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynurenine 3-monooxygenase
EC=1.14.13.9

Alternative name(s):
Kynurenine 3-hydroxylase

Gene names

Name:	kmo
Ordered Locus Names:	XCC1552

Organism

Xanthomonas campestris pv. campestris

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid By similarity.
Catalytic activity	L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.
Cofactor	FAD By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kynurenine 3-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 456	456	Kynurenine 3-monooxygenase		PRO_0000361950

Sequences

	Sequence		Length	Mass (Da)
	Q8PAD3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 265B933209C490EA	FASTA	456	50,945
	10 20 30 40 50 60 MSAAASPRSL TLIGAGLAGC LLAILLSRRG WQITLYERRG DPRIKGYESG RSINLALAER 70 80 90 100 110 120 GRHALRQAGA EDAVMAKAVM MRGRMIHPVS GEPQLQRYGR DDSEVIWSIH RAALNVTLLD 130 140 150 160 170 180 LAEQAGARVH FYRRLHTVDF DAGYARFIDD RDDQPHEIHF QALVGSDGAG SALRAAMQRK 190 200 210 220 230 240 APVGEHIAFL DHSYKELEIP PRADGGFRIE RNALHIWPRG RYMCIALPND GGTFTVTLFL 250 260 270 280 290 300 PNEGMPSFAT TRSGDEALAL FARDFPDALP LIPQLKEHWE EHPPGLLGTL TRERWHLDGR 310 320 330 340 350 360 AVLLGDAAHA MVPFHGQGMN CAFEDCVALA EQLDAHSDLS EAFAAFEAAR RDDAAAIQQM 370 380 390 400 410 420 ALENYLEMRD RVGDAQFLLQ RALEQQLQAR WPTRFVPHYT MVTFLRTRYA IALARSEIQR 430 440 450 EILLEATHGH TDLSRIDWVA LETVVHARLE PLEGAH

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40847.1.
RefSeq	NP_636923.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PAD3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	998940.
GenomeReviews	Gene locus XCC1552 in contig AE008922_GR.
KEGG	xcc:XCC1552.
PATRIC	24073902. VBIXanCam115730_1665.
Phylogenomic databases
HOGENOM	HBG430104.
OMA	YFPDAIP.
ProtClustDB	CLSK903475.
Enzyme and pathway databases
BioCyc	XCAM190485:XCC1552-MONOMER.
Family and domain databases
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
KO	K00486.
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

KMO_XANCP

Accession

Primary (citable) accession number: Q8PAD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program