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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Bordetella avium (strain 197N)
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 sitei286 – 2861Proton acceptorUniRule annotation
Metal bindingi329 – 3291IronUniRule annotation
Metal bindingi335 – 3351IronUniRule annotation
Binding sitei344 – 3441homogentisateUniRule annotation
Metal bindingi365 – 3651IronUniRule annotation
Binding sitei365 – 3651homogentisateUniRule 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

BioCyciBAVI360910:GCKI-538-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:BAV0528
OrganismiBordetella avium (strain 197N)
Taxonomic identifieri360910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001977 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Homogentisate 1,2-dioxygenasePRO_1000019520Add
BLAST

Interactioni

Subunit structurei

Hexamer; dimer of trimers.UniRule annotation

Protein-protein interaction databases

STRINGi360910.BAV0528.

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.

Q2KYC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLNYQSGFG NACATEALPG ALPQGRNSPQ QCPYGLYAEQ LSGTAFTAPR
60 70 80 90 100
SENRRSWLYR IRPGVVHRPF EPYAGAPHWL ADFGTGPVTP NQLRWSPLPL
110 120 130 140 150
PATPTDFIDG VHTWGGNGGP DEQSGVGIHL YAANQSMKGR FFYNADAEML
160 170 180 190 200
LVPQLGRLRL ATEMGLLDLE PLEIAVLPRG VRFRVELLDA EARGYLLENF
210 220 230 240 250
GTALRPPELG PIGSNGLANA RDFQTPVAWY EDVEGDFELI AKFTGGFWRA
260 270 280 290 300
PLTHSPLDVV AWHGTHAPYK YDLRHFNTIG SISYDHPDPS IFTVLTSPSD
310 320 330 340 350
TPGTANLDFA IFPPRILAME NTFRPPWFHR NIASEFMGLI QGVYDAKAEG
360 370 380 390 400
FAPGGASLHN CMSGHGPDAD TFEKASVADT SKAHYIRDTM AFMFETRRVI
410 420 430
RPTRQALASA QLQGDYYQCW QDLKKHFNPE KA
Length:432
Mass (Da):47,808
Last modified:March 7, 2006 - v1
Checksum:i2CEC82ACE2DE950E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ48133.1.
RefSeqiWP_012416224.1. NC_010645.1.

Genome annotation databases

EnsemblBacteriaiCAJ48133; CAJ48133; BAV0528.
KEGGibav:BAV0528.
PATRICi21127210. VBIBorAvi43433_0541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ48133.1.
RefSeqiWP_012416224.1. NC_010645.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi360910.BAV0528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ48133; CAJ48133; BAV0528.
KEGGibav:BAV0528.
PATRICi21127210. VBIBorAvi43433_0541.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciBAVI360910:GCKI-538-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. "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
    Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
    J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 197N.

Entry informationi

Entry nameiHGD_BORA1
AccessioniPrimary (citable) accession number: Q2KYC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: July 22, 2015
This is version 62 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, Reference 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.