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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
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:iL-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 sitei298 – 2981Proton acceptorUniRule annotation
Metal bindingi341 – 3411IronUniRule annotation
Metal bindingi347 – 3471IronUniRule annotation
Binding sitei356 – 3561homogentisateUniRule annotation
Metal bindingi377 – 3771IronUniRule annotation
Binding sitei377 – 3771homogentisateUniRule 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

BioCyciBMUL395019:GIYO-675-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:Bmul_2563, BMULJ_00675
OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
Taxonomic identifieri395019 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000008815 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Homogentisate 1,2-dioxygenasePRO_1000119843Add
BLAST

Interactioni

Subunit structurei

Hexamer; dimer of trimers.UniRule annotation

Protein-protein interaction databases

STRINGi395019.BMULJ_00675.

Structurei

3D structure databases

ProteinModelPortaliA9AFM6.
ModBaseiSearch...
MobiDBiSearch...

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.

A9AFM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLDLSKPAT AGYLSGFANE FATEALPGAL PHGRNSPQRA PYGLYAEQLS
60 70 80 90 100
GTAFTAPRGH NRRSWLYRIR PAAVHRPFEP FAGAQRLVSD FADSADVPPT
110 120 130 140 150
PPNQLRWNPL PMPSEPTDFV EGLVTMAGNG SAAAMSGCAI HLYAANRSMR
160 170 180 190 200
DRFFYSADGE LLIVPQQGRL FIATELGRLD VEPFEIAVIP RGVRFTVALP
210 220 230 240 250
DGDARGYICE NFGALLRLPD LGPIGSNGLA NPRDFLTPQA AYEDREGAFE
260 270 280 290 300
LVAKLNGRLW RADIGHSPLD VVAWHGNYAP YKYDLRLFNT IGSISFDHPD
310 320 330 340 350
PSIFLVLHSQ TDTPGVDAID FVIFPPRWLA AEDTFRPPWF HRNVASEFMG
360 370 380 390 400
LVHGAYDAKA EGFVPGGASL HNCMSGHGPD ADTFEKASAS DTTKPHKVDN
410 420 430 440
TMAFMFETRT LIRPTRYALD TAQLQANYFE CWQGIRKHFN PEQR
Length:444
Mass (Da):49,008
Last modified:January 15, 2008 - v1
Checksum:i7E2FF16ADA189980
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000868 Genomic DNA. Translation: ABX16247.1.
AP009385 Genomic DNA. Translation: BAG42638.1.
RefSeqiWP_012214028.1. NC_010804.1.

Genome annotation databases

EnsemblBacteriaiABX16247; ABX16247; Bmul_2563.
BAG42638; BAG42638; BMULJ_00675.
KEGGibmj:BMULJ_00675.
bmu:Bmul_2563.
PATRICi19163055. VBIBurMul203716_1626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000868 Genomic DNA. Translation: ABX16247.1.
AP009385 Genomic DNA. Translation: BAG42638.1.
RefSeqiWP_012214028.1. NC_010804.1.

3D structure databases

ProteinModelPortaliA9AFM6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395019.BMULJ_00675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX16247; ABX16247; Bmul_2563.
BAG42638; BAG42638; BMULJ_00675.
KEGGibmj:BMULJ_00675.
bmu:Bmul_2563.
PATRICi19163055. VBIBurMul203716_1626.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciBMUL395019:GIYO-675-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 chromosome 1 of Burkholderia multivorans ATCC 17616."
    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., Kim E., Tiedje J., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.
  2. "Complete genome sequence of Burkholderia multivorans ATCC 17616."
    Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.

Entry informationi

Entry nameiHGD_BURM1
AccessioniPrimary (citable) accession number: A9AFM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: July 22, 2015
This is version 57 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.