NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.;
"Complete sequence of chromosome 2 of Ochrobactrum anthropi ATCC 49188.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate (By similarity).
CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O₂ = 2-amino-3-carboxymuconate semialdehyde.
COFACTOR: Binds 2 Fe(2+) ions per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the 3-HAO 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

CP000759; ABS17102.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001372931.1; -.

3D structure databases

ModBase

A6X798.

Ontologies

GO:0000334;	Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0008198;	Molecular function: ferrous iron binding (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00825; -; 1.
PBIL [Tree]

InterPro

IPR010329; 3hydroanth_dOase.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.

Pfam

PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR03037; anthran_nbaC; 1.

BLOCKS

A6X798.

Genome annotation databases

GeneID

5382663; -.

GenomeReviews

CP000759_GR; Oant_4402.

KEGG

oan:Oant_4402; -.

CMR

A6X798; Oant_4402.

Other

ProtoNet

A6X798.

UniRef

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

Keywords

Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 182`	`182`	`3-hydroxyanthranilate 3,4-dioxygenase.`	`PRO_0000309576`
`METAL`	`50 50`		`Iron 1; catalytic (By similarity).`
`METAL`	`56 56`		`Iron 1; catalytic (By similarity).`
`METAL`	`96 96`		`Iron 1; catalytic (By similarity).`
`METAL`	`126 126`		`Iron 2 (By similarity).`
`METAL`	`129 129`		`Iron 2 (By similarity).`
`METAL`	`163 163`		`Iron 2 (By similarity).`
`METAL`	`166 166`		`Iron 2 (By similarity).`
`BINDING`	`46 46`		`Dioxygen (By similarity).`
`BINDING`	`56 56`		`Substrate (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`111 111`		`Substrate (By similarity).`

Sequence information

Length: 182 AA [This is the length of the unprocessed precursor]

Molecular weight: 20693 Da [This is the MW of the unprocessed precursor]

CRC64: 2E0B4D684E611342 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKLSAFNFQ KWIDEHKHLL KPPVGNQLVF KDADLMVTVV GGPNKRTDYH DDPVEEFFYQ 

        70         80         90        100        110        120 
LKGDMLLKLH DTSTGEFYDV PIREGDIFLL PAHIRHSPQR PQEGSIGLVI EPARPEGVLD 

       130        140        150        160        170        180 
AVEWYCFECS GLVHRAEVDL ESIVDDLPPL YAAFYNDEKL RTCPHCNTVH PGKNPPEGWV 


AL

A6X798 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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