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Protein

Homogentisate 1,2-dioxygenase

Gene

hmgA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Homogentisate + O2 = 4-maleylacetoacetate.

Cofactori

Pathway: L-phenylalanine degradation

This protein is involved in step 4 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
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. Maleylacetoacetate isomerase (maiA)
  6. Fumarylacetoacetase (fahA)
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
Metal bindingi340 – 3401IronBy similarity
Metal bindingi346 – 3461IronBy similarity
Metal bindingi377 – 3771IronBy similarity

GO - Molecular functioni

  • homogentisate 1,2-dioxygenase activity Source: ASPGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • L-phenylalanine catabolic process Source: ASPGD
  • tyrosine catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12040.
BRENDAi1.13.11.5. 517.
UniPathwayiUPA00139; UER00339.

Names & Taxonomyi

Protein namesi
Recommended name:
Homogentisate 1,2-dioxygenase (EC:1.13.11.5)
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene namesi
Name:hmgA
ORF Names:AN1897
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VII

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Homogentisate 1,2-dioxygenasePRO_0000220245Add
BLAST

Expressioni

Inductioni

During growth with phenylacetate and phenylalanine.

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00008553.

Structurei

3D structure databases

ProteinModelPortaliQ00667.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the homogentisate dioxygenase family.Curated

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
InParanoidiQ00667.
KOiK00451.
OMAiPRGIRYR.
OrthoDBiEOG72NS04.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR005708. Homogentis_dOase.
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.

Q00667-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVTEFSFKD PYTYQNGFDS YHESEAIEGA LPVGHNSPQK APYGLYAEKL
60 70 80 90 100
SGTAFTAPRH ENKQTWVYRI LPAAAHENFV EEDASSYHTL SDAKKLQHIP
110 120 130 140 150
NQLRWDPFDL DETVDWVHGL HLVAGSGDPT VKQGLGILLY AAGKDMGKEA
160 170 180 190 200
FYSADGDFLI VAQHGVLDIQ TELGRLLVRP NEICVIPRGV RYRVTLPDGP
210 220 230 240 250
VRGYICELYQ GHYQLPELGP IGSNGLANAR DFQAPVAAFD DEEGPTEYRL
260 270 280 290 300
YSKFNNHLFS ARQDHTPFDI VAWHGNYYPY KYDLGRFNTM GSVSFDHPDP
310 320 330 340 350
SIYTVLTGPS DHVGTAIADF VIFPPRWLVA EKTFRPPWYH RNTMSEFMGL
360 370 380 390 400
ITGNYDAKTG GGFQPAGASL HNIMSAHGPD MHAFEGASNA DLKPTKIGDG
410 420 430 440
SMAFMFESSL MVGVSEWGLK TCQKVQEEYN EHSWQPLKRH FKDPRKAQ
Length:448
Mass (Da):50,168
Last modified:November 1, 1996 - v1
Checksum:i4AE6414823A04C0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30797 Genomic DNA. Translation: AAC49071.1.
AJ001836 Genomic DNA. Translation: CAA05042.1.
AACD01000029 Genomic DNA. Translation: EAA65062.1.
BN001307 Genomic DNA. Translation: CBF85779.1.
PIRiA57435.
RefSeqiXP_659501.1. XM_654409.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008553; CADANIAP00008553; CADANIAG00008553.
GeneIDi2874820.
KEGGiani:AN1897.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30797 Genomic DNA. Translation: AAC49071.1.
AJ001836 Genomic DNA. Translation: CAA05042.1.
AACD01000029 Genomic DNA. Translation: EAA65062.1.
BN001307 Genomic DNA. Translation: CBF85779.1.
PIRiA57435.
RefSeqiXP_659501.1. XM_654409.1.

3D structure databases

ProteinModelPortaliQ00667.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00008553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00008553; CADANIAP00008553; CADANIAG00008553.
GeneIDi2874820.
KEGGiani:AN1897.2.

Phylogenomic databases

eggNOGiCOG3508.
HOGENOMiHOG000139824.
InParanoidiQ00667.
KOiK00451.
OMAiPRGIRYR.
OrthoDBiEOG72NS04.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00339.
BioCyciMetaCyc:MONOMER-12040.
BRENDAi1.13.11.5. 517.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR005708. Homogentis_dOase.
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

« Hide 'large scale' publications
  1. "Molecular characterization of a gene encoding a homogentisate dioxygenase from Aspergillus nidulans and identification of its human and plant homologues."
    Fernandez-Canon J.M., Penalva M.A.
    J. Biol. Chem. 270:21199-21205(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: biA1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiHGD_EMENI
AccessioniPrimary (citable) accession number: Q00667
Secondary accession number(s): C8VKJ8, Q5BC33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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.