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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
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 sitei293 – 2931Proton acceptorUniRule annotation
Metal bindingi336 – 3361IronUniRule annotation
Metal bindingi342 – 3421IronUniRule annotation
Binding sitei351 – 3511homogentisateUniRule annotation
Metal bindingi372 – 3721IronUniRule annotation
Binding sitei372 – 3721homogentisateUniRule 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

BioCyciCPIN264198:GIW3-3997-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:Reut_B3923
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002697 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Homogentisate 1,2-dioxygenasePRO_0000225794Add
BLAST

Interactioni

Subunit structurei

Hexamer; dimer of trimers.UniRule annotation

Protein-protein interaction databases

STRINGi264198.Reut_B3923.

Structurei

3D structure databases

ProteinModelPortaliQ46UA4.
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.

Q46UA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLTHTQLAE HGYMSGFANE FATEALPGAL PVGQNSPQRA PYGLYAEQLS
60 70 80 90 100
GTAFTAPRAH NRRSWLYRIR PGAVHKPFTL VEQSRFLSRF DEVPPSPNQM
110 120 130 140 150
RWSPPAMPTT PTDFIDGIVT MAGNGGPDAM TGCGIHLYLA NQSMQDRFFY
160 170 180 190 200
NADGEMLIVP QQGRVRFVTE MGRLDVEPQE IVVIPRGVRF RVELPDGEAR
210 220 230 240 250
GYICENYGAL FKLPDLGVIG SNGLANPRDF MTPVAAYEDR EGDFELVAKF
260 270 280 290 300
QGNLWRADIG HSPLDVVAWH GNFAPYKYDL RRFNTIGSIS FDHPDPSIFL
310 320 330 340 350
VLQSPSDTPG VDTIDFVIFG PRWLAMENSF RPPWFHRNIA SEFMGLITGV
360 370 380 390 400
YDAKADGFAP GGASLHNCMS GHGPDADTFA KATSADTSTP HHITDTMAFM
410 420 430
FETPGVIRPT PYAARSASLQ QDYYTCWQGL KKHFNPNVR
Length:439
Mass (Da):48,732
Last modified:March 7, 2006 - v2
Checksum:i293FAF36EFC3752D
GO

Sequence cautioni

The sequence AAZ63280.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000091 Genomic DNA. Translation: AAZ63280.1. Different initiation.
RefSeqiWP_041680146.1. NC_007348.1.

Genome annotation databases

EnsemblBacteriaiAAZ63280; AAZ63280; Reut_B3923.
KEGGireu:Reut_B3923.
PATRICi20233659. VBIRalEut24049_4633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000091 Genomic DNA. Translation: AAZ63280.1. Different initiation.
RefSeqiWP_041680146.1. NC_007348.1.

3D structure databases

ProteinModelPortaliQ46UA4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264198.Reut_B3923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ63280; AAZ63280; Reut_B3923.
KEGGireu:Reut_B3923.
PATRICi20233659. VBIRalEut24049_4633.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciCPIN264198:GIW3-3997-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 2 of Ralstonia eutropha JMP134."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JMP134 / LMG 1197.

Entry informationi

Entry nameiHGD_CUPPJ
AccessioniPrimary (citable) accession number: Q46UA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: July 22, 2015
This is version 63 of the entry and version 2 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.