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Q9RPU5

- HPAG_SALDU

UniProt

Q9RPU5 - HPAG_SALDU

Protein

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase

Gene

hpaG

Organism
Salmonella dublin
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).

    Catalytic activityi

    5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate.
    5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi276 – 2761Divalent metal cationBy similarity
    Metal bindingi278 – 2781Divalent metal cationBy similarity
    Metal bindingi307 – 3071Divalent metal cationBy similarity

    GO - Molecular functioni

    1. 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity Source: UniProtKB-EC
    2. 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. 4-hydroxyphenylacetate catabolic process Source: InterPro

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00208; UER00419.
    UPA00208; UER00420.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase
    Including the following 2 domains:
    2-hydroxyhepta-2,4-diene-1,7-dioate isomerase (EC:5.3.3.10)
    Short name:
    HHDD isomerase
    Alternative name(s):
    5-carboxymethyl-2-hydroxymuconate Delta-isomerase
    5-carboxymethyl-2-oxo-hex-3-ene-1,7-dioate decarboxylase (EC:4.1.1.68)
    Alternative name(s):
    5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
    Short name:
    OPET decarboxylase
    Gene namesi
    Name:hpaG
    OrganismiSalmonella dublin
    Taxonomic identifieri98360 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4294294-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylasePRO_0000156834Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RPU5.
    SMRiQ9RPU5. Positions 1-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 215215ApproximateAdd
    BLAST
    Repeati216 – 429214ApproximateAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FAH family.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.90.850.10. 2 hits.
    InterProiIPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR012684. HPA_isomer/decarb_C.
    IPR012686. HPA_isomer/decarb_N.
    [Graphical view]
    PfamiPF01557. FAA_hydrolase. 2 hits.
    [Graphical view]
    SUPFAMiSSF56529. SSF56529. 2 hits.
    TIGRFAMsiTIGR02303. HpaG-C-term. 1 hit.
    TIGR02305. HpaG-N-term. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9RPU5-1 [UniParc]FASTAAdd to Basket

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    MKGTVFAVAL NHRSQLDAWQ EAFSQPPYNA PPKTAVWFIK PRNTVIRHGE    50
    PILYPQGEKV LSGATVALIV GKTASRKRSE AAAEYIAGYA LANEVSLPEE 100
    SFYRPAIKAK CRDGFCPLGE MAPLSDVDNL TIITEINGRE ADHWNTADLQ 150
    RSAAQLLSAL SEFATLNPGD AILLGTPQNR VALRPGDRVR ILAKGLPALE 200
    NPVVAEDEFA RNQTFTWPLS ATGTLFALGL NYADHASELA FTPPKEPLVF 250
    IKAPNTFTEH HQTSVRPNNV EYMHYEAELV VVIGKTARKV SEAEAMEYVA 300
    GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPIGPWIVDK EAVSDPHNLT 350
    LRTFVNGELR QEGTTADLIF SIPFLISYLS EFMTLQPGDM IATGTPKGLS 400
    DVVPGDEVVL EIKGVGRLVN QIVCEESAN 429
    Length:429
    Mass (Da):47,186
    Last modified:May 1, 2000 - v1
    Checksum:iD32723999AC4084E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144422 Genomic DNA. Translation: AAD53501.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144422 Genomic DNA. Translation: AAD53501.1 .

    3D structure databases

    ProteinModelPortali Q9RPU5.
    SMRi Q9RPU5. Positions 1-428.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00208 ; UER00419 .
    UPA00208 ; UER00420 .

    Family and domain databases

    Gene3Di 3.90.850.10. 2 hits.
    InterProi IPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR012684. HPA_isomer/decarb_C.
    IPR012686. HPA_isomer/decarb_N.
    [Graphical view ]
    Pfami PF01557. FAA_hydrolase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56529. SSF56529. 2 hits.
    TIGRFAMsi TIGR02303. HpaG-C-term. 1 hit.
    TIGR02305. HpaG-N-term. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the hpa genetic locus from Salmonella dublin."
      Galyov E.E., Wood M.W., Hedges S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 2229.

    Entry informationi

    Entry nameiHPAG_SALDU
    AccessioniPrimary (citable) accession number: Q9RPU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 52 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

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3