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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.UniRule annotation

Catalytic activityi

Homogentisate + O2 = 4-maleylacetoacetate.UniRule annotation

Cofactori

Fe cationUniRule annotation

Pathway: L-phenylalanine degradation

This protein is involved in step 4 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Homogentisate 1,2-dioxygenase (hmgA)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei306 – 3061Proton acceptorUniRule annotation
Metal bindingi349 – 3491IronUniRule annotation
Metal bindingi355 – 3551IronUniRule annotation
Binding sitei364 – 3641homogentisateUniRule annotation
Metal bindingi385 – 3851IronUniRule annotation
Binding sitei385 – 3851homogentisateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciSMED366394:GJAL-2876-MONOMER.
UniPathwayiUPA00139; UER00339.

Names & Taxonomyi

Protein namesi
Recommended name:
Homogentisate 1,2-dioxygenaseUniRule annotation (EC:1.13.11.5UniRule annotation)
Short name:
HGDOUniRule annotation
Alternative name(s):
Homogentisate oxygenaseUniRule annotation
Homogentisic acid oxidaseUniRule annotation
HomogentisicaseUniRule annotation
Gene namesi
Name:hmgAUniRule annotation
Ordered Locus Names:Smed_2833
OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
Taxonomic identifieri366394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001108 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Homogentisate 1,2-dioxygenasePRO_1000019544Add
BLAST

Interactioni

Subunit structurei

Hexamer; dimer of trimers.UniRule annotation

Protein-protein interaction databases

STRINGi366394.Smed_2833.

Family & Domainsi

Sequence similaritiesi

Belongs to the homogentisate dioxygenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
HAMAPiMF_00334. Homogentis_dioxygen.
InterProiIPR005708. Homogentis_dOase.
IPR022950. Homogentis_dOase_bac.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR11056. PTHR11056. 1 hit.
PfamiPF04209. HgmA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01015. hmgA. 1 hit.

Sequencei

Sequence statusi: Complete.

A6UDD3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEKAERQRK AAPDQQRSAG YMPGFGNDFE TESLPGSLPQ GQNSPQKCNY
60 70 80 90 100
GLYAEQLSGS PFTAPRGTNE RSWLYRIRPS VRHTGRFTKI DYPHWKTAPH
110 120 130 140 150
TPEHSLALGQ LRWSPLPAPS QSLTFLQGIR TMTTAGDALT QVGMAAHAYA
160 170 180 190 200
FNADMVDDYF FNADGELLIV PETGAFQVFT ELGRIDVEPS EICLVPRGMM
210 220 230 240 250
FKVTRLGDEK VWRGYICENY GAKFTLPDRG PIGANCLANP RDFKTPVAAY
260 270 280 290 300
EDKETPCRVQ VKWCGSFHTA EIAHSPLDVV AWHGNYAPYK YDLKTFSPVG
310 320 330 340 350
AILFDHPDPS IFTVLTAPSG EEGTANVDFV IFPPRWLVAE HTFRPPWYHR
360 370 380 390 400
NIMSEFMGLI HGRYDAKEEG FVPGGMSLHN MMLAHGPDFS GFEKASNGEL
410 420 430 440 450
KPVKLDNTMA FMFETRFPQQ LTTFAAELET LQDDYIDCWS GLERKFDGTP

GIK
Length:453
Mass (Da):50,785
Last modified:August 21, 2007 - v1
Checksum:i2C75617E743F9238
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000738 Genomic DNA. Translation: ABR61663.1.
RefSeqiWP_012067048.1. NC_009636.1.
YP_001328498.1. NC_009636.1.

Genome annotation databases

EnsemblBacteriaiABR61663; ABR61663; Smed_2833.
GeneIDi5323703.
KEGGismd:Smed_2833.
PATRICi23624831. VBISinMed134228_6043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000738 Genomic DNA. Translation: ABR61663.1.
RefSeqiWP_012067048.1. NC_009636.1.
YP_001328498.1. NC_009636.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi366394.Smed_2833.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR61663; ABR61663; Smed_2833.
GeneIDi5323703.
KEGGismd:Smed_2833.
PATRICi23624831. VBISinMed134228_6043.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciSMED366394:GJAL-2876-MONOMER.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
HAMAPiMF_00334. Homogentis_dioxygen.
InterProiIPR005708. Homogentis_dOase.
IPR022950. Homogentis_dOase_bac.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR11056. PTHR11056. 1 hit.
PfamiPF04209. HgmA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01015. hmgA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Sinorhizobium medicae WSM419 chromosome."
    US DOE Joint Genome Institute
    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., Reeve W.G., Richardson P.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM419.

Entry informationi

Entry nameiHGD_SINMW
AccessioniPrimary (citable) accession number: A6UDD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 27, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.