NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1021;
PubMed=10220173 [NCBI, ExPASy, EBI, Israel, Japan]
Milcamps A., de Bruijn F.J.;
"Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine.";
Microbiology 145:935-947(1999).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan]
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.";
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).

Comments

CATALYTIC ACTIVITY: Homogentisate + O₂ = 4-maleylacetoacetate.
COFACTOR: Iron (By similarity).
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 4/6 .
INDUCTION: By nitrogen and carbon deprivation as well as in the presence of tyrosine. Also induced by phenylalanine, but only in nitrogen-free medium.
SIMILARITY: Belongs to the homogentisate dioxygenase 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

AF109131; AAD29874.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC47518.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_387045.1; -.

3D structure databases

HSSP

Q93099; 1EYB. [HSSP ENTRY / PDB]

ModBase

Q9X4F5.

Enzyme and pathway databases

BioCyc

SMEL266834:SMC03208-MON; -.

Ontologies

GO:0004411;	Molecular function: homogentisate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0006559;	Biological process: L-phenylalanine catabolic process (inferred from electronic annotation from HAMAP).
GO:0006572;	Biological process: tyrosine catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00334; -; 1.
PBIL [Tree]

InterPro

IPR005708; Homogentis_dOase.
Graphical view of domain structure.

PANTHER

PTHR11056; Homogentis_dOase; 1.

Pfam

PF04209; HgmA; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01015; hmgA; 1.

BLOCKS

Q9X4F5.

Genome annotation databases

1234616; -.

AL591688_GR; R02939.

sme:SMc03208; -.

fig|266834.1.peg.4233; -.

Phylogenomic databases

HOGENOM

Q9X4F5; -.

Genome annotation databases

CMR

Q9X4F5; R02939.

Other

ProtoNet

Q9X4F5.

UniRef

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

Keywords

Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Tyrosine catabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 453`	`453`	`Homogentisate 1,2-dioxygenase.`	`PRO_0000220254`
`METAL`	`349 349`		`Iron (By similarity).`
`METAL`	`355 355`		`Iron (By similarity).`
`METAL`	`385 385`		`Iron (By similarity).`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 50756 Da [This is the MW of the unprocessed precursor]

CRC64: AC49AEFF0C783200 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLEKAEKQRR AGSGQQRAAG YMPGFGNDFE TESLPGALPQ GQNSPQKCNY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGTNE RSWLYRIRPS VRHTGRFRRV DYPHWKTAPH VGEHSLALGQ LRWSPLPAPS 

       130        140        150        160        170        180 
EALDFLQGIR TMTTAGDALT QAGMAAHAYA FNADMVDDYF FNADGELLIV PETGAIQVFT 

       190        200        210        220        230        240 
ELGRMDVEPS EICLIPRGMM FKVTRLGEEK VWRGYICENY GAKFTLPDRG PIGANCLANP 

       250        260        270        280        290        300 
RDFKTPVAAY EDKETPCRVQ VKWCGSFHMV EIGHSPLDVV AWHGNYAPYK YDLKTFSPVG 

       310        320        330        340        350        360 
AILFDHPDPS IFTVLTAPSG EEGTANVDFV IFPPRWLVAE HTFRPPWYHR NIMSEFMGLI 

       370        380        390        400        410        420 
YGRYDAKEEG FVPGGMSLHN MMLAHGPDFS GFEKASNGEL KPVKLDNTMA FMFETRFPQQ 

       430        440        450 
LTTFAAELDT LQDDYMDCWS GLERKFDGTP GIK

Q9X4F5 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