ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q2J1P2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HGD_RHOP2
Primary accession number Q2J1P2
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on March 7, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 19)
Name and origin of the protein
Protein name Homogentisate 1,2-dioxygenase
Synonyms EC 1.13.11.5
Homogentisicase
Homogentisate oxygenase
Homogentisic acid oxidase
Gene name
Name: hmgA
OrderedLocusNames: RPB_0907
From
Rhodopseudomonas palustris (strain HaA2) [TaxID: 316058] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Rhodopseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
"Complete sequence of Rhodopseudomonas palustris HaA2.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
Comments
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
CP000250; ABD05618.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_484529.1; -.
3D structure databases
ModBase Q2J1P2.
Enzyme and pathway databases
BioCyc RPAL316058:RPB_0907-MON; -.
Ontologies
GO
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 Q2J1P2.
Genome annotation databases
GeneID 3909087; -.
GenomeReviews CP000250_GR; RPB_0907.
KEGG rpb:RPB_0907; -.
Phylogenomic databases
HOGENOM Q2J1P2; -.
Genome annotation databases
CMR Q2J1P2; RPB_0907.
Other
ProtoNet Q2J1P2.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   448  448     Homogentisate 1,2-dioxygenase. PRO_1000019540
METAL   346   346        Iron (By similarity). 
METAL   352   352        Iron (By similarity). 
METAL   382   382        Iron (By similarity). 
Sequence information
Length: 448 AA [This is the length of the unprocessed precursor] Molecular weight: 49544 Da [This is the MW of the unprocessed precursor] CRC64: 55E2497583E035F0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNINAAPQII GHGSQGVTPG YMSGFGNSFE TEALPGALPI GRNSPQRAAY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGANE RSWLYRIRPS VKHSGRFTKA DMGLWRSAPC LEYDMPIAQL RWDAPSMPQE 

       130        140        150        160        170        180 
DLTFLQGVRT MTTAGDVNTQ AGMATHMYLI TQSMVDQHFY NADGELMFVP QQGSLRLVTE 

       190        200        210        220        230        240 
FGVISIEPAE IAVIPRGVKF RVELVDGPAR GYLCENYGGA FTLPERGPIG ANCLANSRDF 

       250        260        270        280        290        300 
LTPVAAYEDR DVPTELFVKW GGALWQTTLP HSPIDVVAWH GNYAPYKYDL RTFSPVGAIG 

       310        320        330        340        350        360 
FDHPDPSIFT VLTSPSETAG TANIDFVIFP ERWMVAENTF RPPWYHMNIM SEFMGLICGV 

       370        380        390        400        410        420 
YDAKPQGFVP GGASLHNMML PHGPDREAFD HASNGELKPV KLTGTMAFMF ETRYPQRVTE 

       430        440 
YAATAGTLQD DYADCWRGLE KRFDPSRP
Q2J1P2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!