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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Xanthomonas axonopodis pv. citri (strain 306)
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 sitei308 – 3081Proton acceptorUniRule annotation
Metal bindingi351 – 3511IronUniRule annotation
Metal bindingi357 – 3571IronUniRule annotation
Binding sitei366 – 3661homogentisateUniRule annotation
Metal bindingi387 – 3871IronUniRule annotation
Binding sitei387 – 3871homogentisateUniRule 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

BioCyciXAXO190486:GH55-454-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:XAC0454
OrganismiXanthomonas axonopodis pv. citri (strain 306)
Taxonomic identifieri190486 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000000576 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Homogentisate 1,2-dioxygenasePRO_0000220257Add
BLAST

Interactioni

Subunit structurei

Hexamer; dimer of trimers.UniRule annotation

Protein-protein interaction databases

STRINGi190486.XAC0454.

Structurei

3D structure databases

ProteinModelPortaliQ8PQ74.
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.

Q8PQ74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQRDPNLLL SWRADQHPDA PMHNDQRYMT GFGNEFATEA VAGSLPIGQN
60 70 80 90 100
SPQRVAHGLY AEQLSGTAFT APRGQNRRSW LYRIRPAAVH GSFSLVEQSH
110 120 130 140 150
FHNDFGAGPV PPDQLRWSPL PLPSVPTDFV DGLYTMAGNG GPEAMSGVGV
160 170 180 190 200
HVYAANASMQ DRFFYDADGE LLLVPQQGRL RVHTELGVLA LEPQQIGVIP
210 220 230 240 250
RGMRFRVELL DAAARGYVCE NFGGLLRLPD LGPIGANGLA NPRDFETPHA
260 270 280 290 300
AFEQREGTFE LVAKFQGHLW RADIGHSPLD VVAWHGNYAP YRYDLRRFNT
310 320 330 340 350
IGSISFDHPD PSIFTVLTSP SDTHGTANMD FAIFPPRWLV AQHTFRPPWF
360 370 380 390 400
HRNVASEFMG LVHGVYDAKA EGFAPGGASL HNCMSGHGPD AATFDKASQA
410 420 430 440 450
DLTRPDVIAD TMAFMFETRA VLRPTQQALS AAHRQADYQQ CWSGLRAAFQ

PPITEDAT
Length:458
Mass (Da):50,450
Last modified:October 10, 2002 - v1
Checksum:iE2237A2256088FDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM35345.1.

Genome annotation databases

EnsemblBacteriaiAAM35345; AAM35345; XAC0454.
KEGGixac:XAC0454.
PATRICi24052775. VBIXanAxo33670_0489.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM35345.1.

3D structure databases

ProteinModelPortaliQ8PQ74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190486.XAC0454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM35345; AAM35345; XAC0454.
KEGGixac:XAC0454.
PATRICi24052775. VBIXanAxo33670_0489.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
KOiK00451.
OMAiRGYLCEN.
OrthoDBiEOG6D5FZK.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciXAXO190486:GH55-454-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 genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 306.

Entry informationi

Entry nameiHGD_XANAC
AccessioniPrimary (citable) accession number: Q8PQ74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: July 22, 2015
This is version 82 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.