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Reviewed, UniProtKB/Swiss-Prot Q9ZRA2 (HGD_ARATH)

Last modified November 4, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Homogentisate 1,2-dioxygenase
    EC=1.13.11.5
Alternative name(s):
    Homogentisic acid oxidase
    Homogentisate oxygenase
    Homogentisicase
Gene names
Name: HGO
Ordered Locus Names: At5g54080
ORF Names: MJP23.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Homogentisate + O(2) = 4-maleylacetoacetate.

Cofactor

Iron.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 4/6.

Sequence similarities

Belongs to the homogentisate dioxygenase family.

Ontologies

Keywords

   Biological processPhenylalanine catabolism
Tyrosine catabolism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Homogentisate 1,2-dioxygenase
PRO_0000220244

Sites

Metal binding3411Iron By similarity
Metal binding3471Iron By similarity
Metal binding3771Iron By similarity

Experimental info

Sequence conflict71E → K in AAM65958. Ref.5
Sequence conflict691V → I in AAM65958. Ref.5
Sequence conflict1161I → T in AAM65958. Ref.5
Sequence conflict1461T → K in AAM65958. Ref.5
Sequence conflict1811T → S in AAM65958. Ref.5
Sequence conflict2311S → P in AAM65958. Ref.5
Sequence conflict4281D → E in AAD00360. Ref.1
Sequence conflict4521S → P in AAM65958. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9ZRA2-1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: CD90DD9638014D31

FASTA46151,455
        10         20         30         40         50         60 
MEEKKKELEE LKYQSGFGNH FSSEAIAGAL PLDQNSPLLC PYGLYAEQIS GTSFTSPRKL 

        70         80         90        100        110        120 
NQRSWLYRVK PSVTHEPFKP RVPAHKKLVS EFDASNSRTN PTQLRWRPED IPDSEIDFVD 

       130        140        150        160        170        180 
GLFTICGAGS SFLRHGFAIH MYVANTGMKD SAFCNADGDF LLVPQTGRLW IETECGRLLV 

       190        200        210        220        230        240 
TPGEIAVIPQ GFRFSIDLPD GKSRGYVAEI YGAHFQLPDL GPIGANGLAA SRDFLAPTAW 

       250        260        270        280        290        300 
FEDGLRPEYT IVQKFGGELF TAKQDFSPFN VVAWHGNYVP YKYDLKKFCP YNTVLLDHGD 

       310        320        330        340        350        360 
PSINTVLTAP TDKPGVALLD FVIFPPRWLV AEHTFRPPYY HRNCMSEFMG LIYGAYEAKA 

       370        380        390        400        410        420 
DGFLPGGASL HSCMTPHGPD TTTYEATIAR VNAMAPSKLT GTMAFMFESA LIPRVCHWAL 

       430        440        450        460 
ESPFLDHDYY QCWIGLKSHF SRISLDKTNV ESTEKEPGAS E 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the homogentisate 1,2-dioxygenase gene in A. thaliana and C. elegans."
Schmidt S.R., Werner E., Mueller C.R., Kress W.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]Schmidt S.R.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

U80668 mRNA. Translation: AAD00360.1.
AF130845 Genomic DNA. Translation: AAF36499.1.
AB018115 Genomic DNA. Translation: BAA97130.1.
AY140075 mRNA. Translation: AAM98216.1.
BT010329 mRNA. Translation: AAQ55280.1.
AY088421 mRNA. Translation: AAM65958.1.
RefSeqNP_200219.1.
NP_851187.1.
UniGeneAt.23160

3D structure databases

HSSPHSSP built from PDB template 1EYB based on UniProtKB Q93099.
ModBaseSearch...

Genome annotation databases

GeneID835494.
GenomeReviewsGene locus AT5G54080 in contig BA000015_GR.
KEGGath:AT5G54080.
NMPDRfig|3702.1.peg.27312.

Organism-specific databases

TAIRAt5g54080.

Gene expression databases

ArrayExpressQ9ZRA2.
GermOnlineAT5G54080. Arabidopsis thaliana.

Family and domain databases

InterProIPR005708. Homogentis_dOase.
[Graphical view]
PANTHERPTHR11056. Homogentis_dOase. 1 hit.
PfamPF04209. HgmA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01015. hmgA. 1 hit.
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameHGD_ARATH
AccessionPrimary (citable) accession number: Q9ZRA2
Secondary accession number(s): Q8L9I0, Q9LDB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 27, 2001
Last modified: November 4, 2008
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents