P21394 (XYLA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xylene monooxygenase electron transfer component

Including the following 2 domains:

1. Ferredoxin
2. Ferredoxin--NAD(+) reductase
   EC=1.18.1.3

Gene names

Name:

xylA

Encoded on

Plasmid TOL pWW0

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Oxidizes toluene and xylenes to (methyl)benzyl alcohols. The enzyme has a broad specificity and also oxidizes (methyl)benzyl alcohols to (methyl)benzaldehydes and indole to indoxyl.
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.
Cofactor	FAD. Binds 1 2Fe-2S cluster per subunit By similarity.
Subunit structure	Composed of two subunits: xylA and xylM.
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	Xylene monooxygenase electron transfer component		PRO_0000167660
Regions
	Domain	16 – 108	93	2Fe-2S ferredoxin-type
	Domain	114 – 213	100	FAD-binding FR-type
	Region	109 – 350	242	Ferredoxin--NADH reductase
Sites
	Metal binding	52	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	57	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	60	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	92	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21394 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 26828AC2226C1DDD	FASTA	350	38,455
	10 20 30 40 50 60 MNEFFKKISG LFVPPPESTV SVRGQGFQFK VPRGQTILES ALHQGIAFPH DCKVGSCGTC 70 80 90 100 110 120 KYKLISGRVN ELTSSAMGLS GDLYQSGYRL GCQCIPKEDL EIELDTVLGQ ALVPIETSAL 130 140 150 160 170 180 ISKQKRLAHD IVEMEVVPDK QIAFYPGQYA DVECAECSAV RSYSFSAPPQ PDGSLSFHVR 190 200 210 220 230 240 LVPGGVFSGW LFGGDRTGAT LTLRAPYGQF GLHESNATMV CVAGGTGLAP IKCVLQSMTQ 250 260 270 280 290 300 AQRERDVLLF FGARQQRDLY CLDEIEALQL DWGGRFELIP VLSEESSTSS WKGKRGMVTE 310 320 330 340 350 YFKEYLTGQP YEGYLCGPPP MVDAAETELV RLGVARELVF ADRFYNRPPC

References

[1]	"Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system." Suzuki M., Hayakawa T., Shaw J.P., Rekik M., Harayama S. J. Bacteriol. 173:1690-1695(1991) [PubMed: 1999388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-16.
[2]	"Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2." Shaw J.P., Harayama S. Eur. J. Biochem. 209:51-61(1992) [PubMed: 1327782] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M37480 Genomic DNA. Translation: AAA26027.1. D63341 Genomic DNA. Translation: BAA09663.1.
PIR	B37316.
RefSeq	NP_542886.1. NC_003350.1.
3D structure databases
ProteinModelPortal	P21394.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1218743.
Phylogenomic databases
ProtClustDB	CLSK862333.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2941.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR017927. Fd_Rdtase_FAD-bd. IPR001041. Ferredoxin. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYLA_PSEPU

Accession

Primary (citable) accession number: P21394

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program